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Protein Page:
PDIA1 (human)
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
PDIA1 This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. Belongs to the protein disulfide isomerase family. Note: This description may include information from UniProtKB.
Protein type: Isomerase; Oxidoreductase; EC 5.3.4.1; Endoplasmic reticulum; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 17q25
Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen; ER-Golgi intermediate compartment; external side of plasma membrane; extracellular region; focal adhesion; melanosome
Molecular Function: enzyme binding; integrin binding; procollagen-proline 4-dioxygenase activity; protein binding; protein disulfide isomerase activity; protein heterodimerization activity
Biological Process: cell redox homeostasis; lipoprotein biosynthetic process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; positive regulation of virion penetration into host cell; protein folding; response to reactive oxygen species
Disease: Cole-carpenter Syndrome 1
Reference #:  P07237 (UniProtKB)
Alt. Names/Synonyms: Cellular thyroid hormone-binding protein; collagen prolyl 4-hydroxylase beta; DSI; ERBA2L; GIT; glutathione-insulin transhydrogenase; P4HB; P4Hbeta; p55; PDI; PDIA1; PHDB; PO4DB; PO4HB; procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide; PROHB; Prolyl 4-hydroxylase subunit beta; prolyl 4-hydroxylase, beta polypeptide; protein disulfide isomerase family A, member 1; protein disulfide isomerase-associated 1; protein disulfide isomerase/oxidoreductase; Protein disulfide-isomerase; protocollagen hydroxylase; thyroid hormone-binding protein p55; v-erb-a avian erythroblastic leukemia viral oncogene homolog 2-like
Gene Symbols: P4HB
Molecular weight: 57,116 Da
Basal Isoelectric point: 4.76  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PDIA1

Protein Structure Not Found.


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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.


       human

 
0 1 K31 DHVLVLRKsNFAEAL
0 5 S32‑p HVLVLRKsNFAEALA
0 1 K65 ALAPEYAKAAGKLKA
0 1 K65 ALAPEYAKAAGKLKA
0 1 K65 ALAPEYAKAAGKLKA
0 1 K71 AKAAGKLKAEGSEIR
0 1 K71 AKAAGKLKAEGSEIR
0 1 K81 GSEIRLAKVDATEES
0 14 K81‑ub GSEIRLAkVDATEES
0 1 K81‑sc GSEIRLAkVDATEES
0 2 Y94‑p ESDLAQQyGVRGyPT
0 1 Y99‑p QQyGVRGyPTIkFFR
0 5 K103‑ac VRGyPTIkFFRNGDT
0 1 K103‑ub VRGyPTIkFFRNGDT
0 5 R106 yPTIkFFRNGDTASP
0 1 R106 yPTIkFFRNGDTASP
0 1 R106 yPTIkFFRNGDTASP
0 1 S112 FRNGDTASPKEYTAG
0 1 K114 NGDTASPKEYTAGRE
0 1 K114 NGDTASPKEYTAGRE
0 1 K130 DDIVNWLKKRTGPAA
0 1 K130 DDIVNWLKKRTGPAA
0 1 K130‑sc DDIVNWLkKRTGPAA
0 2 K200 FSKYQLDKDGVVLFK
0 2 K200‑ub FSKYQLDkDGVVLFK
0 1 K200‑sc FSKYQLDkDGVVLFK
0 1 K207 kDGVVLFKkFDEGRN
0 7 K208‑ac DGVVLFKkFDEGRNN
0 3 K222 NFEGEVTKENLLDFI
0 2 K222‑ub NFEGEVTkENLLDFI
0 1 K222 NFEGEVTKENLLDFI
0 1 N224 EGEVTkENLLDFIKH
0 1 N224 EGEVTkENLLDFIKH
0 1 N224 EGEVTkENLLDFIKH
0 1 T255 IFGGEIKTHILLFLP
0 1 K263 HILLFLPKSVsDyDG
0 1 K263‑sc HILLFLPkSVsDyDG
0 1 S266‑p LFLPkSVsDyDGkLs
0 2 Y268‑p LPkSVsDyDGkLsNF
0 1 K271 SVsDyDGKLsNFkTA
0 2 K271‑ub SVsDyDGkLsNFkTA
0 1 K271‑sc SVsDyDGkLsNFkTA
0 1 S273‑p sDyDGkLsNFkTAAE
0 6 K276 DGkLsNFKTAAEsFk
0 1 K276‑sc DGkLsNFkTAAEsFk
0 1 S281‑p NFkTAAEsFkGKILF
0 9 K283‑ac kTAAEsFkGKILFIF
0 21 K308‑ac ILEFFGLkKEECPAV
0 2 K308‑ub ILEFFGLkKEECPAV
0 1 K308‑sc ILEFFGLkKEECPAV
0 2 K326 TLEEEMTKyKPEsEE
0 1 Y327‑p LEEEMTKyKPEsEEL
0 1 K328 EEEMTKyKPEsEELT
0 1 S331‑p MTKyKPEsEELTAER
0 1 T340 ELTAERITEFCHRFL
0 1 K352 RFLEGKIKPHLMSQE
0 2 K366 ELPEDWDKQPVKVLV
0 17 K375‑ac PVKVLVGkNFEDVAF
0 1 K375‑ub PVKVLVGkNFEDVAF
0 7 K385‑ac EDVAFDEkKNVFVEF
0 1 K385 EDVAFDEKKNVFVEF
0 1 K385‑sc EDVAFDEkKNVFVEF
0 3 K409‑ac QLAPIWDkLGETYKD
0 1 K409 QLAPIWDKLGETYKD
0 1 K415 DkLGETYKDHENIVI
0 1 K415 DkLGETYKDHENIVI
0 2 S427‑p IVIAKMDstANEVEA
0 1 T428‑p VIAKMDstANEVEAV
0 1 K436 ANEVEAVKVHsFPtL
0 3 S439‑p VEAVKVHsFPtLkFF
0 1 T442 VKVHsFPTLkFFPAS
0 1 T442‑ga VKVHsFPtLkFFPAS
0 12 K444‑ac VHsFPtLkFFPASAD
0 2 K444‑ub VHsFPtLkFFPASAD
0 1 K444‑sc VHsFPtLkFFPASAD
0 3 Y457‑p ADRTVIDyNGERtLD
0 1 T462‑p IDyNGERtLDGFKKF
0 6 K467 ERtLDGFKKFLESGG
0 1 K467 ERtLDGFKKFLESGG
0 2 S472 GFKKFLESGGQDGAG
  mouse

 
K33‑ub DNVLVLKkSNFEEAL
S34 NVLVLKkSNFEEALA
K67 ALAPEYAKAAAKLkA
K67‑ub ALAPEYAkAAAKLkA
K67‑sc ALAPEYAkAAAKLkA
K73 AkAAAKLKAEGSEIR
K73‑sc AkAAAKLkAEGSEIR
K83 GSEIRLAKVDATEES
K83‑ub GSEIRLAkVDATEES
K83‑sc GSEIRLAkVDATEES
Y96 ESDLAQQYGVRGYPT
Y101 QQYGVRGYPTIKFFk
K105 VRGYPTIKFFkNGDT
K105 VRGYPTIKFFkNGDT
K108‑ac YPTIKFFkNGDTAsP
K108‑ub YPTIKFFkNGDTAsP
K108‑sc YPTIKFFkNGDTAsP
S114‑p FkNGDTAsPkEYTAG
K116‑ac NGDTAsPkEYTAGRE
K116‑sc NGDTAsPkEYTAGRE
K132‑ac DDIVNWLkKRTGPAA
K132‑ub DDIVNWLkKRTGPAA
K132‑sc DDIVNWLkKRTGPAA
K202‑ac FSKYQLDkDGVVLFk
K202‑ub FSKYQLDkDGVVLFk
K202‑sc FSKYQLDkDGVVLFk
K209‑ac kDGVVLFkkFDEGRN
K210‑ac DGVVLFkkFDEGRNN
K224‑ac NFEGEITkEkLLDFI
K224 NFEGEITKEkLLDFI
K224‑sc NFEGEITkEkLLDFI
K226 EGEITkEKLLDFIKH
K226‑ub EGEITkEkLLDFIKH
K226‑sc EGEITkEkLLDFIKH
T257‑p IFGGEIKtHILLFLP
K265‑ac HILLFLPkSVSDYDG
K265‑sc HILLFLPkSVSDYDG
S268 LFLPkSVSDYDGkLS
Y270 LPkSVSDYDGkLSSF
K273 SVSDYDGKLSSFkRA
K273‑ub SVSDYDGkLSSFkRA
K273‑sc SVSDYDGkLSSFkRA
S275 SDYDGkLSSFkRAAE
K278‑ac DGkLSSFkRAAEGFk
K278 DGkLSSFKRAAEGFk
G283 SFkRAAEGFkGKILF
K285‑ac kRAAEGFkGKILFIF
K310‑ac ILEFFGLkKEECPAV
K310‑ub ILEFFGLkKEECPAV
K310‑sc ILEFFGLkKEECPAV
K328‑ac TLEEEMTkYKPESDE
Y329 LEEEMTkYKPESDEL
K330 EEEMTkYKPESDELT
S333 MTkYKPESDELTAEK
T342 ELTAEKITEFCHRFL
K354 RFLEGKIKPHLMSQE
K368‑ac EVPEDWDkQPVKVLV
A377 PVKVLVGANFEEVAF
A377 PVKVLVGANFEEVAF
K387‑ac EEVAFDEkKNVFVEF
K387‑ub EEVAFDEkKNVFVEF
K387‑sc EEVAFDEkKNVFVEF
K411‑ac QLAPIWDkLGETYkD
K411‑sc QLAPIWDkLGETYkD
K417‑ac DkLGETYkDHENIII
K417‑sc DkLGETYkDHENIII
S429 IIIAKMDSTANEVEA
T430 IIAKMDSTANEVEAV
K438 ANEVEAVKVHsFPtL
S441‑p VEAVKVHsFPtLkFF
T444‑p VKVHsFPtLkFFPAS
T444 VKVHsFPTLkFFPAS
K446 VHsFPtLKFFPASAD
K446‑ub VHsFPtLkFFPASAD
K446‑sc VHsFPtLkFFPASAD
Y459 ADRTVIDYNGERtLD
T464‑p IDYNGERtLDGFkKF
K469‑ac ERtLDGFkKFLEsGG
K469‑sc ERtLDGFkKFLEsGG
S474‑p GFkKFLEsGGQDGAG
  rat

 
K33 DNVLVLKKSNFAEAL
S34 NVLVLKKSNFAEALA
K67‑ac ALAPEYAkAAAKLkA
K67 ALAPEYAKAAAKLkA
K67 ALAPEYAKAAAKLkA
K73‑ac AkAAAKLkAEGSEIR
K73 AkAAAKLKAEGSEIR
K83‑ac GSEIRLAkVDATEES
K83 GSEIRLAKVDATEES
K83 GSEIRLAKVDATEES
Y96 ESDLAQQYGVRGYPT
Y101 QQYGVRGYPTIkFFk
K105‑ac VRGYPTIkFFkNGDT
K105 VRGYPTIKFFkNGDT
K108‑ac YPTIkFFkNGDTASP
K108 YPTIkFFKNGDTASP
K108 YPTIkFFKNGDTASP
S114 FkNGDTASPKEYTAG
K116 NGDTASPKEYTAGRE
K116 NGDTASPKEYTAGRE
K132 DDIVNWLKKRTGPAA
K132 DDIVNWLKKRTGPAA
K132 DDIVNWLKKRTGPAA
K202‑ac FSKYQLDkDGVVLFK
K202 FSKYQLDKDGVVLFK
K202 FSKYQLDKDGVVLFK
K209 kDGVVLFKkFDEGRN
K210‑ac DGVVLFKkFDEGRNN
K224‑ac NFEGEITkEkLLDFI
K224 NFEGEITKEkLLDFI
K224 NFEGEITKEkLLDFI
K226‑ac EGEITkEkLLDFIKH
K226 EGEITkEKLLDFIKH
K226 EGEITkEKLLDFIKH
T257 IFGGEIKTHILLFLP
K265 HILLFLPKSVSDYDG
K265 HILLFLPKSVSDYDG
S268 LFLPKSVSDYDGkLS
Y270 LPKSVSDYDGkLSNF
K273‑ac SVSDYDGkLSNFkKA
K273 SVSDYDGKLSNFkKA
K273 SVSDYDGKLSNFkKA
S275 SDYDGkLSNFkKAAE
K278‑ac DGkLSNFkKAAEGFK
K278 DGkLSNFKKAAEGFK
G283 NFkKAAEGFKGKILF
K285 kKAAEGFKGKILFIF
K310 ILEFFGLKKEECPAV
K310 ILEFFGLKKEECPAV
K310 ILEFFGLKKEECPAV
K328‑ac TLEEEMTkYkPESDE
Y329 LEEEMTkYkPESDEL
K330‑ac EEEMTkYkPESDELT
S333 MTkYkPESDELTAEK
T342‑p ELTAEKItQFCHHFL
K354‑ac HFLEGKIkPHLMSQE
K368‑ac ELPEDWDkQPVKVLV
K377‑ac PVKVLVGkNFEEVAF
K377 PVKVLVGKNFEEVAF
K387 EEVAFDEKKNVFVEF
K387 EEVAFDEKKNVFVEF
K387 EEVAFDEKKNVFVEF
K411‑ac QLAPIWDkLGETYKD
K411 QLAPIWDKLGETYKD
K417 DkLGETYKDHENIVI
K417 DkLGETYKDHENIVI
S429 IVIAKMDSTANEVEA
T430 VIAKMDSTANEVEAV
K438‑ac ANEVEAVkVHSFPTL
S441 VEAVkVHSFPTLKFF
T444 VkVHSFPTLKFFPAS
T444 VkVHSFPTLKFFPAS
K446 VHSFPTLKFFPASAD
K446 VHSFPTLKFFPASAD
K446 VHSFPTLKFFPASAD
Y459 ADRTVIDYNGERTLD
T464 IDYNGERTLDGFKKF
K469 ERTLDGFKKFLESGG
K469 ERTLDGFKKFLESGG
S474 GFKKFLESGGQDGAG
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