Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
FKBP4 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
FKBP4 Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. Note: This description may include information from UniProtKB.
Protein type: Isomerase; Chaperone; EC 5.2.1.8
Cellular Component: microtubule; endoplasmic reticulum membrane; mitochondrion; cell soma; perinuclear region of cytoplasm; cytoplasm; nucleolus; cytosol; nucleus
Molecular Function: protein binding, bridging; protein binding; peptidyl-prolyl cis-trans isomerase activity; FK506 binding; GTP binding; heat shock protein binding; phosphoprotein binding; tau protein binding; copper-dependent protein binding; ATP binding; glucocorticoid receptor binding
Biological Process: prostate gland development; male sex differentiation; steroid hormone receptor complex assembly; protein complex localization; protein peptidyl-prolyl isomerization; protein folding; negative regulation of microtubule polymerization; negative regulation of microtubule polymerization or depolymerization; androgen receptor signaling pathway; copper ion transport; embryo implantation
Reference #:  Q02790 (UniProtKB)
Alt. Names/Synonyms: 52 kD FK506 binding protein; 52 kDa FK506-binding protein; 52 kDa FKBP; 59 kDa immunophilin; FK506 binding protein 4, 59kDa; FK506 binding protein 52; FK506-binding protein 4; FK506-binding protein 4 (59kD); FKBP-4; FKBP-52; FKBP4; FKBP52; FKBP59; HBI; HSP binding immunophilin; HSP-binding immunophilin; Hsp56; Immunophilin FKBP52; p52; p59; p59 protein; Peptidyl-prolyl cis-trans isomerase FKBP4; Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; peptidylprolyl cis-trans isomerase; PPIase FKBP4; T-cell FK506-binding protein, 59kD
Gene Symbols: FKBP4
Molecular weight: 51,805 Da
Basal Isoelectric point: 5.35  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

FKBP4

Protein Structure Not Found.


STRING  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB


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


 SS 

SS: 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.


 MS 

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


       human

 
0 1 T9-p TAEEMKAtESGAQsA
0 1 S15-p AtESGAQsAPLPMEG
0 1 S26-p PMEGVDIsPkQDEGV
0 1 K28-ac EGVDIsPkQDEGVLk
0 76 K28-ub EGVDIsPkQDEGVLk
0 1 K35 kQDEGVLKVIKREGT
0 8 K35-ub kQDEGVLkVIKREGT
0 1 K38 EGVLkVIKREGTGTE
0 2 M46 REGTGTEMPMIGDRV
0 1 K74 FDSSLDRKDkFsFDL
0 2 K76-ub SSLDRKDkFsFDLGk
0 2 S78-p LDRKDkFsFDLGkGE
0 2 K83-ub kFsFDLGkGEVIkAW
0 1 K83-sc kFsFDLGkGEVIkAW
0 1 K88-ub LGkGEVIkAWDIAIA
0 2 S118-p YAYGSAGsPPKIPPN
1 0 T143 EFKGEDLTEEEDGGI
0 7 Y161-p IQTRGEGyAKPNEGA
0 2 K181-ub LEGYYKDkLFDQREL
0 3 S217-p RMEKGEHsIVyLkPS
0 232 Y220-p KGEHsIVyLkPSyAF
0 1 K222-ac EHsIVyLkPSyAFGs
0 2 K222-ub EHsIVyLkPSyAFGs
0 1 K222-sc EHsIVyLkPSyAFGs
0 2 Y225-p IVyLkPSyAFGsVGk
0 1 S229-p kPSyAFGsVGkEKFQ
0 2 K232-ac yAFGsVGkEKFQIPP
0 1 K232 yAFGsVGKEKFQIPP
0 1 K244-ub IPPNAELkYELHLkS
0 1 K250-ub LkYELHLkSFEKAKE
0 1 S258-p SFEKAKEsWEMNsEE
0 1 S263-p KEsWEMNsEEKLEQS
0 1 K274-ac LEQSTIVkERGTVYF
0 1 K274-ub LEQSTIVkERGTVYF
0 1 K274-sc LEQSTIVkERGTVYF
0 1 K282-ac ERGTVYFkEGKyKQA
0 1 K282-ub ERGTVYFkEGKyKQA
0 1 Y286-p VYFkEGKyKQALLQy
0 2 Y293-p yKQALLQykKIVSWL
0 1 K294-ac KQALLQykKIVSWLE
0 1 K294-sc KQALLQykKIVSWLE
0 1 S305-p SWLEYESsFSNEEAQ
0 1 S341-p AFSAAIEsCNKALEL
0 1 S350-p NKALELDsNNEkGLF
0 1 K354-ac ELDsNNEkGLFRRGE
0 4 K354-ub ELDsNNEkGLFRRGE
0 1 R373 VNDFELARADFQkVL
0 1 K378-ac LARADFQkVLQLYPN
0 1 K378-ub LARADFQkVLQLYPN
0 2 K387 LQLYPNNKAAkTQLA
0 4 K390-ub YPNNKAAkTQLAVCQ
0 2 K409-ub RQLAREKkLyANMFE
1 199 Y411-p LAREKkLyANMFERL
0 3 K424-ub RLAEEENkAkAEAss
0 1 K426-ub AEEENkAkAEAssGD
0 2 S430-p NkAkAEAssGDHPtD
0 4 S431-p kAkAEAssGDHPtDt
0 26 T436-p AssGDHPtDtEMkEE
0 6 T438-p sGDHPtDtEMkEEQK
0 6 K441-ub HPtDtEMkEEQKSNt
0 2 T448-p kEEQKSNtAGsQsQV
0 28 S451-p QKSNtAGsQsQVETE
0 16 S453-p SNtAGsQsQVETEA_
  mouse

 
A9 TAEEMKAAENGAQSA
S15 AAENGAQSAPLPLEG
S26 PLEGVDISPkQDEGV
K28 EGVDISPKQDEGVLk
K28-ub EGVDISPkQDEGVLk
K35-ac kQDEGVLkVIkREGT
K35-ub kQDEGVLkVIkREGT
K38-ac EGVLkVIkREGTGTE
T46-p REGTGTEtPMIGDRV
K74-ub FDSSLDRkDKFsFDL
K76 SSLDRkDKFsFDLGk
S78-p LDRkDKFsFDLGkGE
K83-ub KFsFDLGkGEVIKAW
K83 KFsFDLGKGEVIKAW
K88 LGkGEVIKAWDIAVA
S118 YAYGAAGSPPKIPPN
T143 EFKGEDLTEEEDGGI
Y161 IRTRGEGYARPNDGA
R181 LEGYHKDRLFDQREL
S217 RMEKGEHSIVyLkPS
Y220-p KGEHSIVyLkPSyAF
K222-ac EHSIVyLkPSyAFGS
K222-ub EHSIVyLkPSyAFGS
K222 EHSIVyLKPSyAFGS
Y225-p IVyLkPSyAFGSVGk
S229 kPSyAFGSVGkERFQ
K232 yAFGSVGKERFQIPP
K232-ub yAFGSVGkERFQIPP
R244 IPPHAELRYEVRLKS
K250 LRYEVRLKSFEKAKE
S258 SFEKAKESWEMSSAE
S263 KESWEMSSAEKLEQS
K274 LEQSNIVKERGTAYF
K274 LEQSNIVKERGTAYF
K274 LEQSNIVKERGTAYF
K282 ERGTAYFKEGKYKQA
K282 ERGTAYFKEGKYKQA
Y286 AYFKEGKYKQALLQY
Y293 YKQALLQYkKIVSWL
K294 KQALLQYKKIVSWLE
K294-sc KQALLQYkKIVSWLE
S305 SWLEYESSFSGEEMQ
S341 AFSAAIESCNKALEL
S350 NKALELDSNNEkGLF
K354 ELDSNNEKGLFRRGE
K354-ub ELDSNNEkGLFRRGE
R373-m1 VNDFDLArADFQKVL
K378 LArADFQKVLQLYPS
K378 LArADFQKVLQLYPS
K387-ub LQLYPSNkAAkTQLA
K390-ub YPSNkAAkTQLAVCQ
K409-ub RQLAREKkLyANMFE
Y411-p LAREKkLyANMFERL
K424-ub RLAEEEHkVKAEVAA
K426 AEEEHkVKAEVAAGD
A430 HkVKAEVAAGDHPTD
A431 kVKAEVAAGDHPTDA
T436 VAAGDHPTDAEMkGE
A438 AGDHPTDAEMkGERN
K441-ub HPTDAEMkGERNNVA
- gap
N450 ERNNVAENQSRVETE
S452 NNVAENQSRVETEA_
  rat

 
A9 TAEEMKVAENGAQSA
S15 VAENGAQSAPLPLEG
S26 PLEGVDISPKQDEGV
K28 EGVDISPKQDEGVLK
K28 EGVDISPKQDEGVLK
K35 KQDEGVLKVIKREGT
K35 KQDEGVLKVIKREGT
K38 EGVLKVIKREGTGTE
T46 REGTGTETAMIGDRV
K74 FDSSLDRKDKFSFDL
K76 SSLDRKDKFSFDLGK
S78 LDRKDKFSFDLGKGE
K83 KFSFDLGKGEVIKAW
K83 KFSFDLGKGEVIKAW
K88 LGKGEVIKAWDIAVA
S118 YAYGSAGSPPKIPPN
T143 EFKGEDLTEDEDGGI
Y161 IRTRGEGYARPNDGA
R181 LEGYYNDRLFDQREL
S217 RMEKGEHSIVYLKPS
Y220 KGEHSIVYLKPSYAF
K222 EHSIVYLKPSYAFGS
K222 EHSIVYLKPSYAFGS
K222 EHSIVYLKPSYAFGS
Y225 IVYLKPSYAFGSVGK
S229 KPSYAFGSVGKERFQ
K232 YAFGSVGKERFQIPP
K232 YAFGSVGKERFQIPP
R244 IPPHAELRYEVHLKS
K250 LRYEVHLKSFEKAKA
S258 SFEKAKASWEMNSEE
S263 KASWEMNSEEKLEQS
K274 LEQSNIVKERGTVYF
K274 LEQSNIVKERGTVYF
K274 LEQSNIVKERGTVYF
K282 ERGTVYFKEGKYKQA
K282 ERGTVYFKEGKYKQA
Y286 VYFKEGKYKQALLQY
Y293 YKQALLQYKKIVSWL
K294 KQALLQYKKIVSWLE
K294 KQALLQYKKIVSWLE
S305 SWLEYESSFSGEEMQ
S341 AFSAAIESCNKALEL
S350 NKALELDSNNEKGLF
K354 ELDSNNEKGLFRRGE
K354 ELDSNNEKGLFRRGE
R373 VNDFDLARADFQKVL
K378 LARADFQKVLQLYPS
K378 LARADFQKVLQLYPS
K387 LQLYPSNKAAKTQLA
K390 YPSNKAAKTQLAVCQ
K409 RQLAREKKLyANMFE
Y411-p LAREKKLyANMFERL
K424 RLAEEEHKAKTEVAA
K426 AEEEHKAKTEVAAGD
A430 HKAKTEVAAGDHPTD
A431 KAKTEVAAGDHPTDA
T436 VAAGDHPTDAEMKGE
A438 AGDHPTDAEMKGEPN
K441 HPTDAEMKGEPNNVA
- gap
N450 EPNNVAGNQAQVKTE
A452 NNVAGNQAQVKTEA_
  rabbit

 
A9 TAEEMKAAESGAQSA
S15 AAESGAQSAPLPLEG
S26 PLEGVDISPKQDEGV
K28 EGVDISPKQDEGVLK
K28 EGVDISPKQDEGVLK
K35 KQDEGVLKVIKREGT
K35 KQDEGVLKVIKREGT
K38 EGVLKVIKREGTGTE
T46 REGTGTETPMIGDRV
K74 FDSSLDRKDKFSFDL
K76 SSLDRKDKFSFDLGK
S78 LDRKDKFSFDLGKGE
K83 KFSFDLGKGEVIKAW
K83 KFSFDLGKGEVIKAW
K88 LGKGEVIKAWDIAVA
S118 YAYGSAGSPPKIPPN
T143-p EFKGEDLtDDEDGGI
Y161 IRTRGEGYARPNDGA
R181 LEGYYKDRLFDQREL
S217 RMEKGEHSILYLKPS
Y220 KGEHSILYLKPSYAF
K222 EHSILYLKPSYAFGN
K222 EHSILYLKPSYAFGN
K222 EHSILYLKPSYAFGN
Y225 ILYLKPSYAFGNAGK
N229 KPSYAFGNAGKEKFQ
K232 YAFGNAGKEKFQIPP
K232 YAFGNAGKEKFQIPP
K244 IPPYAELKYEVHLKS
K250 LKYEVHLKSFEKAKE
S258 SFEKAKESWEMSSEE
S263 KESWEMSSEEKLEQS
K274 LEQSAIVKERGTVYF
K274 LEQSAIVKERGTVYF
K274 LEQSAIVKERGTVYF
K282 ERGTVYFKEGKYKQA
K282 ERGTVYFKEGKYKQA
Y286 VYFKEGKYKQALLQY
Y293 YKQALLQYKKIVSWL
K294 KQALLQYKKIVSWLE
K294 KQALLQYKKIVSWLE
S305 SWLEYESSFSSEEVQ
S341 AFSAAVESCNKALEL
S350 NKALELDSNNEKGLF
K354 ELDSNNEKGLFRRGE
K354 ELDSNNEKGLFRRGE
R373 VNDFDLARADFQKVL
K378 LARADFQKVLQLYPS
K378 LARADFQKVLQLYPS
K387 LQLYPSNKAAKAQLA
K390 YPSNKAAKAQLAVCQ
K409 KQIAREKKLYANMFE
Y411 IAREKKLYANMFERL
K424 RLAEEENKAKAEVAA
K426 AEEENKAKAEVAAGD
A430 NKAKAEVAAGDHPMD
A431 KAKAEVAAGDHPMDT
M436 VAAGDHPMDTEMKDE
T438 AGDHPMDTEMKDERN
K441 HPMDTEMKDERNDVA
- gap
S450 ERNDVAGSQSQVETE
S452 NDVAGSQSQVETEA_
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.