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Protein Page:
p53 (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
p53 a transcription factor and major tumor suppressor that plays a major role in regulating cellular responses to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis. More than 50 percent of human tumors contain a mutation or deletion of the TP53 gene. p53 is modified post-translationally at multiple sites. DNA damage induces phosphorylation of p53 at S15, S20 and S37, reducing its interaction with the oncoprotein MDM2. MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation. Phosphorylated by many kinases including Chk2 and Chk1 at S20, enhancing its tetramerization, stability and activity. The phosphorylation by CAK at S392 is increased in human tumors and has been reported to influence the growth suppressor function, DNA binding and transcriptional activation of p53. Phosphorylation of p53 at S46 regulates the ability of p53 to induce apoptosis. The acetylation of p53 appears to play a positive role in the accumulation of p53 during the stress response. Following DNA damage, p53 becomes acetylated at K382, enhancing its binding to DNA. Deacetylation of p53 can occur through interaction with SIRT1, a deacetylase that may be involved in cellular aging and the DNA damage response. p53 regulates the transcription of a set of genes encoding endosomal proteins that regulate endosomal functions. These include STEAP3 and CHMP4C, which enhance exosome production, and CAV1 and CHMP4C, which produce a more rapid endosomal clearance of the EGFR from the plasma membrane. DNA damage regulates a p53-mediated secretory pathway, increasing the secretion of some proteins such as Hsp90, SERPINE1, SERPINB5, NKEF-A, and CyPA, and inhibiting the secretion of others including CTSL and IGFBP-2. Two alternatively spliced human isoforms have been reported. Isoform 2 is expressed in quiescent lymphocytes. Seems to be non-functional. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; DNA-binding; Motility/polarity/chemotaxis; Activator; Transcription factor; Tumor suppressor
Cellular Component: chromatin; cytoplasm; cytosol; endoplasmic reticulum; mitochondrial matrix; mitochondrion; nuclear body; nuclear chromatin; nuclear matrix; nucleolus; nucleoplasm; nucleus; PML body; protein complex; replication fork; transcription factor complex; transcription factor TFIID complex
Molecular Function: ATP binding; chaperone binding; chromatin binding; copper ion binding; damaged DNA binding; DNA binding; enzyme binding; histone acetyltransferase binding; histone deacetylase regulator activity; identical protein binding; metal ion binding; p53 binding; protease binding; protein binding; protein C-terminus binding; protein heterodimerization activity; protein kinase binding; protein N-terminus binding; protein phosphatase 2A binding; protein phosphatase binding; protein self-association; receptor tyrosine kinase binding; sequence-specific DNA binding; transcription factor activity; transcription factor binding; ubiquitin protein ligase binding
Biological Process: apoptosis; B cell lineage commitment; cell aging; cell cycle; cell cycle arrest; cellular response to glucose starvation; cellular response to stress; central nervous system development; cerebellum development; chromatin assembly; chromosome breakage; chromosome organization and biogenesis; circadian behavior; determination of adult life span; DNA damage response, signal transduction by p53 class mediator; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; DNA strand renaturation; double-strand break repair; embryonic development ending in birth or egg hatching; embryonic organ development; entrainment of circadian clock by photoperiod; ER overload response; G1 DNA damage checkpoint; gastrulation; heart development; in utero embryonic development; mitochondrial DNA repair; multicellular organism growth; multicellular organismal development; negative regulation of apoptosis; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of DNA replication; negative regulation of fibroblast proliferation; negative regulation of mitotic cell cycle; negative regulation of neuroblast proliferation; negative regulation of proteolysis; negative regulation of smooth muscle cell proliferation; negative regulation of telomerase activity; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of transforming growth factor beta receptor signaling pathway; neuron apoptosis; nucleotide-excision repair; positive regulation of apoptosis; positive regulation of cell cycle; positive regulation of histone deacetylation; positive regulation of leukocyte migration; positive regulation of neuron apoptosis; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of protein oligomerization; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; programmed cell death; protein complex assembly; protein import into nucleus, translocation; protein localization; protein stabilization; protein tetramerization; regulation of apoptosis; regulation of cell cycle; regulation of cell proliferation; regulation of intracellular pH; regulation of neuron apoptosis; regulation of tissue remodeling; regulation of transcription from RNA polymerase II promoter; regulation of transcription, DNA-dependent; release of cytochrome c from mitochondria; response to DNA damage stimulus; response to drug; response to gamma radiation; response to oxidative stress; response to salt stress; response to UV; response to X-ray; rhythmic process; rRNA transcription; somitogenesis; T cell differentiation in the thymus; T cell lineage commitment; T cell proliferation during immune response; transcription from RNA polymerase II promoter; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; viral reproduction
Reference #:  P02340 (UniProtKB)
Alt. Names/Synonyms: bbl; bfy; bhy; Cellular tumor antigen p53; P53; p53 cellular tumor antigen; RP23-56I20.1; Tp53; transformation related protein 53; Trp53; Tumor suppressor p53; tumor supressor p53
Gene Symbols: Tp53
Molecular weight: 43,155 Da
Basal Isoelectric point: 6.83  Predict pI for various phosphorylation states
CST Pathways:  AMPK Signaling  |  Apoptosis Regulation  |  ErbB/HER Signaling  |  G1/S Checkpoint  |  G2/M DNA Damage Checkpoint  |  Mitochondrial Control of Apoptosis  |  PI3K/Akt Signaling  |  Protein Acetylation  |  Regulation of P38 MAPKs  |  SAPK/JNK Signaling Cascades  |  Warburg Effect
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

p53

Protein Structure Not Found.
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Sites Implicated In
apoptosis, altered: S15‑p, T18‑p, S20‑p, S386‑p
apoptosis, induced: S15‑p, S386‑p
apoptosis, inhibited: S15‑p, S55‑p, K314‑ac
carcinogenesis, altered: S309‑p
carcinogenesis, inhibited: S15‑p
cell cycle regulation: S15‑p, T18‑p, S20‑p, S386‑p
cell growth, altered: S15‑p, S20‑p, S386‑p
cell growth, inhibited: S15‑p
transcription, altered: S15‑p, T18‑p, S309‑p, K314‑ac, K364‑ub, K366‑ub, K367‑ub, K375‑ub, K376‑ub, K380‑ub, S386‑p
transcription, induced: S15‑p, S55‑p, S386‑p
acetylation: S309‑p, S370‑p, S372‑p
activity, induced: S15‑p, T18‑p, S20‑p, S386‑p
intracellular localization: S15‑p, T18‑p
molecular association, regulation: S15‑p, T18‑p, S20‑p
phosphorylation: S34‑p
protein stabilization: S15‑p, T18‑p, S20‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

► Hide Isoforms
 
6 0 S4‑p ____MEEsQsDIsLE
31 4 S6‑p __MEEsQsDIsLELP
34 3 S9‑p EEsQsDIsLELPLsQ
380 4 S15‑p IsLELPLsQEtFsGL
31 0 T18‑p ELPLsQEtFsGLWKL
115 1 S20‑p PLsQEtFsGLWKLLP
30 3 P33 LPPEDILPsPHCMDD
67 3 S34‑p PPEDILPsPHCMDDL
95 3 L43 HCMDDLLLPQDVEEF
18 0 - gap
2 0 S55‑p EEFFEGPsEALRVSG
8 2 G75 DPVTETPGPVAPAPA
0 2 S93 PLSSFVPSQKTYQGN
1 2 K95 SSFVPSQKTYQGNYG
1 0 N100 SQKTYQGNYGFHLGF
0 1 H104 YQGNYGFHLGFLQSG
0 1 Q109 GFHLGFLQSGTAkSV
28 1 K114‑ac FLQSGTAkSVMCTYS
1 19 K114 FLQSGTAKSVMCTYS
1 0 Y120 AkSVMCTYSPPLNKL
1 1 K126 TYSPPLNKLFCQLAK
1 0 K133 KLFCQLAKTCPVQLW
3 1 A143 PVQLWVSATPPAGsR
1 1 A143 PVQLWVSATPPAGsR
4 8 T144 VQLWVSATPPAGsRV
4 1 S149‑p SATPPAGsRVRAMAI
5 1 K158 VRAMAIYKKSQHMTE
1 1 K158 VRAMAIYKKSQHMTE
2 0 S177 CPHHERCSDGDGLAP
0 1 R203 YPEYLEDRQTFRHSV
1 0 T205 EYLEDRQTFRHSVVV
0 1 R207 LEDRQTFRHSVVVPY
5 0 S209 DRQTFRHSVVVPYEP
1 0 Y214 RHSVVVPYEPPEAGS
0 1 Y223‑p PPEAGSEyTTIHyKY
0 1 Y228‑p SEyTTIHyKYMCNSS
3 0 S263 GNLLGRDSFEVRVCA
1 0 T278 CPGRDRRTEEENFRK
1 0 K285 TEEENFRKkEVLCPE
1 3 K286 EEENFRKKEVLCPEL
1 6 K286‑ub EEENFRKkEVLCPEL
1 0 A298 PELPPGSAkRALPTC
2 15 K299‑ac ELPPGSAkRALPTCT
1 20 K299‑ub ELPPGSAkRALPTCT
0 1 T306 kRALPTCTsAsPPQk
1 5 S307‑p RALPTCTsAsPPQkk
1 7 A308 ALPTCTsAsPPQkkk
40 30 S309‑p LPTCTsAsPPQkkkP
0 4 K313‑ac TsAsPPQkkkPLDGE
1 0 K313 TsAsPPQKkkPLDGE
39 0 K314‑ac sAsPPQkkkPLDGEy
2 17 K314‑ub sAsPPQkkkPLDGEy
1 0 K314 sAsPPQkKkPLDGEy
2 10 K315‑ub AsPPQkkkPLDGEyF
1 0 K315 AsPPQkkKPLDGEyF
0 14 Y321‑p kkPLDGEyFTLKIRG
1 0 R327 EyFTLKIRGRKRFEM
1 0 R329 FTLKIRGRKRFEMFR
1 0 R331 LKIRGRKRFEMFREL
0 2 K345 LNEALELKDAHATEE
0 1 E351 LKDAHATEESGDSRA
0 3 E351 LKDAHATEESGDSRA
0 1 S356 ATEESGDSRAHSSYL
5 0 S360 SGDSRAHSSYLkTkk
15 3 K364 RAHSSYLKTkkGQsT
1 0 K364 RAHSSYLKTkkGQsT
4 0 K364 RAHSSYLKTkkGQsT
2 1 K364 RAHSSYLKTkkGQsT
2 0 K364 RAHSSYLKTkkGQsT
9 0 K364‑ub RAHSSYLkTkkGQsT
1 0 K364 RAHSSYLKTkkGQsT
4 0 T365 AHSSYLkTkkGQsTs
18 3 K366 HSSYLkTKkGQsTsR
3 0 K366‑me HSSYLkTkkGQsTsR
3 0 K366 HSSYLkTKkGQsTsR
9 0 K366‑ub HSSYLkTkkGQsTsR
1 0 K366 HSSYLkTKkGQsTsR
67 3 K367‑ac SSYLkTkkGQsTsRH
1 0 K367 SSYLkTkKGQsTsRH
1 0 K367 SSYLkTkKGQsTsRH
9 0 K367‑ub SSYLkTkkGQsTsRH
1 0 K367 SSYLkTkKGQsTsRH
12 0 S370‑p LkTkkGQsTsRHkkT
4 0 T371 kTkkGQsTsRHkkTM
15 1 S372‑p TkkGQsTsRHkkTMV
24 4 K375 GQsTsRHKkTMVkkV
9 0 K375‑ub GQsTsRHkkTMVkkV
128 4 K376‑ac QsTsRHkkTMVkkVG
1 0 K376 QsTsRHkKTMVkkVG
2 1 K376 QsTsRHkKTMVkkVG
9 0 K376‑ub QsTsRHkkTMVkkVG
6 3 K380‑ac RHkkTMVkkVGPDsD
0 1 K380 RHkkTMVKkVGPDsD
0 1 K380 RHkkTMVKkVGPDsD
9 1 K380‑ub RHkkTMVkkVGPDsD
12 0 K380 RHkkTMVKkVGPDsD
4 0 K381 HkkTMVkKVGPDsD_
2 0 K381‑ub HkkTMVkkVGPDsD_
0 1 - gap
93 11 S386‑p VkkVGPDsD______
9285 : Phospho-p53 (Ser6) Antibody
9284 : Phospho-p53 (Ser15) Antibody
9286 : Phospho-p53 (Ser15) (16G8) Mouse mAb
12571 : Phospho-p53 (Ser15) (D4S1H) XP(R) Rabbit mAb (Mouse Specific)
14789 : Phospho-p53 (Ser15) (D4S1H) XP(R) Rabbit mAb (Rodent Specific) (PE Conjugate)
9287 : Phospho-p53 (Ser20) Antibody
2570 : Acetyl-p53 (Lys379) Antibody
9281 : Phospho-p53 (Ser392) Antibody
  p53 iso2  
S7 _MTAMEESQSDISLE
S9 TAMEESQSDISLELP
S12 EESQSDISLELPLsQ
S18‑p ISLELPLsQETFSGL
T21 ELPLsQETFSGLWKL
S23 PLsQETFSGLWKLLP
P36 LPPEDILPSPHCMDD
S37 PPEDILPSPHCMDDL
L46 HCMDDLLLPQDVEEF
- gap
S58 EEFFEGPSEALRVSG
G78 DPVTETPGPVAPAPA
S96 PLSSFVPSQKTYQGN
K98 SSFVPSQKTYQGNYG
N103 SQKTYQGNYGFHLGF
H107 YQGNYGFHLGFLQSG
Q112 GFHLGFLQSGTAkSV
K117‑ac FLQSGTAkSVMCTYS
K117 FLQSGTAKSVMCTYS
Y123 AkSVMCTYSPPLNKL
K129 TYSPPLNKLFCQLAK
K136 KLFCQLAKTCPVQLW
A146 PVQLWVSATPPAGSR
A146 PVQLWVSATPPAGSR
T147 VQLWVSATPPAGSRV
S152 SATPPAGSRVRAMAI
K161 VRAMAIYKKSQHMTE
K161 VRAMAIYKKSQHMTE
S180 CPHHERCSDGDGLAP
R206 YPEYLEDRQTFRHSV
T208 EYLEDRQTFRHSVVV
R210 LEDRQTFRHSVVVPY
S212 DRQTFRHSVVVPYEP
Y217 RHSVVVPYEPPEAGS
Y226 PPEAGSEYTTIHYKY
Y231 SEYTTIHYKYMCNSS
S266 GNLLGRDSFEVRVCA
T281 CPGRDRRTEEENFRK
K288 TEEENFRKKEVLCPE
K289 EEENFRKKEVLCPEL
K289 EEENFRKKEVLCPEL
A301 PELPPGSAKRALPTC
K302 ELPPGSAKRALPTCT
K302 ELPPGSAKRALPTCT
T309 KRALPTCTSASPPQK
S310 RALPTCTSASPPQKk
A311 ALPTCTSASPPQKkK
S312 LPTCTSASPPQKkKP
K316 TSASPPQKkKPLDGE
K316 TSASPPQKkKPLDGE
K317‑ac SASPPQKkKPLDGEY
K317 SASPPQKKKPLDGEY
K317 SASPPQKKKPLDGEY
K318 ASPPQKkKPLDGEYF
K318 ASPPQKkKPLDGEYF
Y324 kKPLDGEYFTLKIRG
R330 EYFTLKIRGRKRFEM
R332 FTLKIRGRKRFEMFR
R334 LKIRGRKRFEMFREL
K348 LNEALELKDAHATEE
E354 LKDAHATEESGDSRA
E354 LKDAHATEESGDSRA
S359 ATEESGDSRAHSSLQ
S363 SGDSRAHSSLQPRAF
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K375‑sm RAFQALIkEEsPNC_
- gap
- gap
S378‑p QALIkEEsPNC____
- gap
14789 : Phospho-p53 (Ser15) (D4S1H) XP(R) Rabbit mAb (Rodent Specific) (PE Conjugate)
  human

► Hide Isoforms
 
P4 ____MEEPQsDPsVE
S6‑p __MEEPQsDPsVEPP
S9‑p EEPQsDPsVEPPLsQ
S15‑p PsVEPPLsQEtFsDL
T18‑p EPPLsQEtFsDLWKL
S20‑p PLsQEtFsDLWKLLP
S33‑p LPENNVLsPLPsQAM
S37‑p NVLsPLPsQAMDDLM
S46‑p AMDDLMLsPDDIEQW
T55‑p DDIEQWFtEDPGPDE
D61 FtEDPGPDEAPRMPE
T81‑p APAPAAPtPAAPAPA
S99‑p PLSSSVPsQkTYQGs
K101‑ub SSSVPsQkTYQGsYG
S106‑p sQkTYQGsYGFrLGF
R110‑m1 YQGsYGFrLGFLhSG
H115‑m1 GFrLGFLhSGTAkSV
K120‑ac FLhSGTAkSVTCTyS
K120‑ub FLhSGTAkSVTCTyS
Y126‑p AkSVTCTySPALNkM
K132‑ub TySPALNkMFCQLAk
K139‑ub kMFCQLAkTCPVQLW
S149‑p PVQLWVDstPPPGtR
S149‑gl PVQLWVDstPPPGtR
T150‑p VQLWVDstPPPGtRV
T155‑p DstPPPGtRVRAMAI
K164‑ac VRAMAIYkQSQHMTE
K164‑ub VRAMAIYkQSQHMTE
S183‑p CPHHERCsDSDGLAP
R209‑m1 RVEYLDDrNtFrHsV
T211‑p EYLDDrNtFrHsVVV
R213‑m1 LDDrNtFrHsVVVPy
S215‑p DrNtFrHsVVVPyEP
Y220‑p rHsVVVPyEPPEVGS
C229 PPEVGSDCTTIHYNY
Y234 SDCTTIHYNYMCNSS
S269‑p GNLLGRNsFEVRVCA
T284‑p CPGRDRRtEEENLRk
K291‑ub tEEENLRkkGEPHHE
K292‑ac EEENLRkkGEPHHEL
K292‑ub EEENLRkkGEPHHEL
T304‑p HELPPGStkRALPNN
K305‑ac ELPPGStkRALPNNt
K305‑ub ELPPGStkRALPNNt
T312‑p kRALPNNtsssPQPk
S313‑p RALPNNtsssPQPkk
S314‑p ALPNNtsssPQPkkk
S315‑p LPNNtsssPQPkkkP
K319‑ac tsssPQPkkkPLDGE
K319‑ub tsssPQPkkkPLDGE
K320‑ac sssPQPkkkPLDGEy
K320‑ub sssPQPkkkPLDGEy
K320‑ne sssPQPkkkPLDGEy
K321‑ub ssPQPkkkPLDGEyF
K321‑ne ssPQPkkkPLDGEyF
Y327‑p kkPLDGEyFTLQIrG
R333‑me EyFTLQIrGrErFEM
R335‑m2 FTLQIrGrErFEMFR
R337‑m2 LQIrGrErFEMFREL
K351‑ub LNEALELkDAQAGkE
K357 LkDAQAGKEPGGsRA
K357‑ub LkDAQAGkEPGGsRA
S362‑p AGkEPGGsRAHsSHL
S366‑p PGGsRAHsSHLkskk
K370‑ac RAHsSHLkskkGQst
K370‑me RAHsSHLkskkGQst
K370‑m1 RAHsSHLkskkGQst
K370‑m2 RAHsSHLkskkGQst
K370‑m3 RAHsSHLkskkGQst
K370‑ub RAHsSHLkskkGQst
K370‑ne RAHsSHLkskkGQst
S371‑p AHsSHLkskkGQsts
K372‑ac HsSHLkskkGQstsR
K372‑me HsSHLkskkGQstsR
K372‑m1 HsSHLkskkGQstsR
K372‑ub HsSHLkskkGQstsR
K372‑ne HsSHLkskkGQstsR
K373‑ac sSHLkskkGQstsRH
K373‑m1 sSHLkskkGQstsRH
K373‑m2 sSHLkskkGQstsRH
K373‑ub sSHLkskkGQstsRH
K373‑ne sSHLkskkGQstsRH
S376‑p LkskkGQstsRHkkL
T377‑p kskkGQstsRHkkLM
S378‑p skkGQstsRHkkLMF
K381‑ac GQstsRHkkLMFktE
K381‑ub GQstsRHkkLMFktE
K382‑ac QstsRHkkLMFktEG
K382‑m1 QstsRHkkLMFktEG
K382‑m2 QstsRHkkLMFktEG
K382‑ub QstsRHkkLMFktEG
K386‑ac RHkkLMFktEGPDsD
K386‑m1 RHkkLMFktEGPDsD
K386‑m2 RHkkLMFktEGPDsD
K386‑ub RHkkLMFktEGPDsD
K386‑sm RHkkLMFktEGPDsD
T387‑p HkkLMFktEGPDsD_
T387 HkkLMFkTEGPDsD_
- gap
S392‑p FktEGPDsD______
9285 : Phospho-p53 (Ser6) Antibody
9288 : Phospho-p53 (Ser9) Antibody
4030 : Phospho-p53 (Ser15) (16G8) Mouse mAb (Biotinylated)
8514 : Phospho-p53 (Ser15) (16G8) Mouse mAb (PE Conjugate)
8695 : Phospho-p53 (Ser15) (16G8) Mouse mAb (Alexa Fluor(R) 647 Conjugate)
9235 : Phospho-p53 (Ser15) (16G8) Mouse mAb (Alexa Fluor(R) 488 Conjugate)
9284 : Phospho-p53 (Ser15) Antibody
9286 : Phospho-p53 (Ser15) (16G8) Mouse mAb
9481 : Phospho-p53 (Ser15) (16G8) Mouse mAb (Alexa Fluor(R) 555 Conjugate)
2529 : Phospho-p53 (Thr18) Antibody
9287 : Phospho-p53 (Ser20) Antibody
2526 : Phospho-p53 (Ser33) Antibody
9289 : Phospho-p53 (Ser37) Antibody
2521 : Phospho-p53 (Ser46) Antibody
2676 : Phospho-p53 (Thr81) Antibody
2528 : Phospho-p53 (Ser315) Antibody
2525 : Acetyl-p53 (Lys382) Antibody
2570 : Acetyl-p53 (Lys379) Antibody
9281 : Phospho-p53 (Ser392) Antibody
  p53 iso4  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S7‑p _MDDLMLsPDDIEQW
T16 DDIEQWFTEDPGPDE
D22 FTEDPGPDEAPRMPE
T42 APAPAAPTPAAPAPA
S60 PLSSSVPSQKTYQGS
K62 SSSVPSQKTYQGSYG
S67 SQKTYQGSYGFRLGF
R71 YQGSYGFRLGFLHSG
H76 GFRLGFLHSGTAKSV
K81 FLHSGTAKSVTCTYS
K81 FLHSGTAKSVTCTYS
Y87 AKSVTCTYSPALNKM
K93 TYSPALNKMFCQLAK
K100 KMFCQLAKTCPVQLW
S110 PVQLWVDSTPPPGTR
S110 PVQLWVDSTPPPGTR
T111 VQLWVDSTPPPGTRV
T116 DSTPPPGTRVRAMAI
K125 VRAMAIYKQSQHMTE
K125 VRAMAIYKQSQHMTE
S144 CPHHERCSDSDGLAP
R170 RVEYLDDRNTFRHSV
T172 EYLDDRNTFRHSVVV
R174 LDDRNTFRHSVVVPY
S176 DRNTFRHSVVVPYEP
Y181 RHSVVVPYEPPEVGS
C190 PPEVGSDCTTIHYNY
Y195 SDCTTIHYNYMCNSS
S230 GNLLGRNSFEVRVCA
T245 CPGRDRRTEEENLRK
K252 TEEENLRKKGEPHHE
K253 EEENLRKKGEPHHEL
K253 EEENLRKKGEPHHEL
T265 HELPPGSTKRALPNN
K266 ELPPGSTKRALPNNT
K266 ELPPGSTKRALPNNT
T273 KRALPNNTSSSPQPK
S274 RALPNNTSSSPQPKK
S275 ALPNNTSSSPQPKKK
S276 LPNNTSSSPQPKKKP
K280 TSSSPQPKKKPLDGE
K280 TSSSPQPKKKPLDGE
K281 SSSPQPKKKPLDGEY
K281 SSSPQPKKKPLDGEY
K281 SSSPQPKKKPLDGEY
K282 SSPQPKKKPLDGEYF
K282 SSPQPKKKPLDGEYF
Y288 KKPLDGEYFTLQIRG
R294 EYFTLQIRGRERFEM
R296 FTLQIRGRERFEMFR
R298 LQIRGRERFEMFREL
K312 LNEALELKDAQAGKE
K318 LKDAQAGKEPGGSRA
K318 LKDAQAGKEPGGSRA
S323 AGKEPGGSRAHSSHL
S327 PGGSRAHSSHLKSKk
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
S332 AHSSHLKSKkGQSTS
K333 HSSHLKSKkGQSTSR
K333 HSSHLKSKkGQSTSR
K333 HSSHLKSKkGQSTSR
K333 HSSHLKSKkGQSTSR
K333 HSSHLKSKkGQSTSR
K334‑ac SSHLKSKkGQSTSRH
K334 SSHLKSKKGQSTSRH
K334 SSHLKSKKGQSTSRH
K334 SSHLKSKKGQSTSRH
K334 SSHLKSKKGQSTSRH
S337 LKSKkGQSTSRHKkL
T338 KSKkGQSTSRHKkLM
S339 SKkGQSTSRHKkLMF
K342 GQSTSRHKkLMFKTE
K342 GQSTSRHKkLMFKTE
K343‑ac QSTSRHKkLMFKTEG
K343 QSTSRHKKLMFKTEG
K343 QSTSRHKKLMFKTEG
K343 QSTSRHKKLMFKTEG
K347 RHKkLMFKTEGPDSD
K347 RHKkLMFKTEGPDSD
K347 RHKkLMFKTEGPDSD
K347 RHKkLMFKTEGPDSD
K347 RHKkLMFKTEGPDSD
T348 HKkLMFKTEGPDSD_
T348 HKkLMFKTEGPDSD_
- gap
S353 FKTEGPDSD______
  rat

 
S4‑p ____MEDsQsDMsIE
S6‑p __MEDsQsDMsIELP
S9‑p EDsQsDMsIELPLsQ
S15‑p MsIELPLsQEtFsCL
T18‑p ELPLsQEtFsCLWKL
S20‑p PLsQEtFsCLWKLLP
P33 LPPDDILPTTATGsP
S39‑p LPTTATGsPNSMEDL
L48 NSMEDLFLPQDVAEL
- gap
E60 AELLEGPEEALQVSA
A79 EPGTEAPAPVAPASA
S97 PLSSSVPSQKTYQGN
K99 SSSVPSQKTYQGNYG
N104 SQKTYQGNYGFHLGF
H108 YQGNYGFHLGFLQSG
Q113 GFHLGFLQSGTAkSV
K118‑ac FLQSGTAkSVMCTYS
K118 FLQSGTAKSVMCTYS
Y124 AkSVMCTYSISLNKL
K130 TYSISLNKLFCQLAK
K137 KLFCQLAKTCPVQLW
S147 PVQLWVTSTPPPGTR
S147 PVQLWVTSTPPPGTR
T148 VQLWVTSTPPPGTRV
T153 TSTPPPGTRVRAMAI
K162 VRAMAIYKKSQHMTE
K162 VRAMAIYKKSQHMTE
S181 CPHHERCSDGDGLAP
R207 YAEYLDDRQTFRHSV
T209 EYLDDRQTFRHSVVV
R211 LDDRQTFRHSVVVPY
S213 DRQTFRHSVVVPYEP
Y218 RHSVVVPYEPPEVGS
Y227 PPEVGSDYTTIHYKY
Y232 SDYTTIHYKYMCNSS
S267 GNLLGRDSFEVRVCA
T282 CPGRDRRTEEENFRK
K289 TEEENFRKKEEHCPE
K290 EEENFRKKEEHCPEL
K290 EEENFRKKEEHCPEL
A302 PELPPGSAKRALPTS
K303 ELPPGSAKRALPTST
K303 ELPPGSAKRALPTST
T310 KRALPTSTSSsPQQK
S311 RALPTSTSSsPQQKK
S312 ALPTSTSSsPQQKKK
S313‑p LPTSTSSsPQQKKKP
K317 TSSsPQQKKKPLDGE
K317 TSSsPQQKKKPLDGE
K318 SSsPQQKKKPLDGEY
K318 SSsPQQKKKPLDGEY
K318 SSsPQQKKKPLDGEY
K319 SsPQQKKKPLDGEYF
K319 SsPQQKKKPLDGEYF
Y325 KKPLDGEYFTLKIRG
R331 EYFTLKIRGRERFEM
R333 FTLKIRGRERFEMFR
R335 LKIRGRERFEMFREL
K349 LNEALELKDARAAEE
E355 LKDARAAEESGDSRA
E355 LKDARAAEESGDSRA
S360 AAEESGDSRAHSSYP
S364 SGDSRAHSSYPKTKk
K368 RAHSSYPKTKkGQST
K368 RAHSSYPKTKkGQST
K368 RAHSSYPKTKkGQST
K368 RAHSSYPKTKkGQST
K368 RAHSSYPKTKkGQST
K368 RAHSSYPKTKkGQST
K368 RAHSSYPKTKkGQST
T369 AHSSYPKTKkGQSTs
K370 HSSYPKTKkGQSTsR
K370 HSSYPKTKkGQSTsR
K370 HSSYPKTKkGQSTsR
K370 HSSYPKTKkGQSTsR
K370 HSSYPKTKkGQSTsR
K371‑ac SSYPKTKkGQSTsRH
K371 SSYPKTKKGQSTsRH