Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

PIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, PubMed:23623683). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (PubMed:22608923). May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (PubMed:23623683, PubMed:27561354).8 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • GTPase activating protein binding Source: BHF-UCL
  • mitogen-activated protein kinase kinase binding Source: BHF-UCL
  • motor activity Source: ParkinsonsUK-UCL
  • peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL
  • phosphoprotein binding Source: ARUK-UCL
  • phosphoserine residue binding Source: BHF-UCL
  • phosphothreonine residue binding Source: BHF-UCL

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase
Biological processCell cycle

Enzyme and pathway databases

BRENDAi5.2.1.8 2681
ReactomeiR-HSA-1169408 ISG15 antiviral mechanism
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6811555 PI5P Regulates TP53 Acetylation
R-HSA-936440 Negative regulators of DDX58/IFIH1 signaling
SignaLinkiQ13526
SIGNORiQ13526

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8)
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase Pin1
Short name:
PPIase Pin1
Rotamase Pin1
Gene namesi
Name:PIN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000127445.13
HGNCiHGNC:8988 PIN1
MIMi601052 gene
neXtProtiNX_Q13526

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23Y → A: Reduced affinity for KIF20B. 1 Publication1
Mutagenesisi34W → A: Loss of binding to phosphorylated target proteins, including to phosphorylated RBBP8/CtIP; decrease in DNA repair of double-strand breaks by homologous recombination less efficient than that observed with wild-type protein. 2 Publications1
Mutagenesisi63K → A: Loss of peptidyl-prolyl cis/trans isomerase activity. 1 Publication1
Mutagenesisi71S → D or E: Loss of peptidyl-prolyl cis/trans isomerase activity, nuclear localization and cellular function. 1 Publication1
Mutagenesisi113C → A: Loss of peptidyl-prolyl cis/trans isomerase activity; decrease in DNA repair of double-strand breaks by homologous recombination slightly less efficient than that observed with wild-type protein. No effect on RBBP8/CtIP. 1 Publication1

Organism-specific databases

DisGeNETi5300
OpenTargetsiENSG00000127445
PharmGKBiPA33320

Chemistry databases

ChEMBLiCHEMBL2288
DrugBankiDB01766 Beta-(2-Naphthyl)-Alanine

Polymorphism and mutation databases

BioMutaiPIN1
DMDMi3024406

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001934351 – 163Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1Add BLAST163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43PhosphoserineCombined sources1
Modified residuei46N6-acetyllysineCombined sources1
Modified residuei71Phosphoserine; by DAPK11 Publication1
Modified residuei108PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13526
MaxQBiQ13526
PaxDbiQ13526
PeptideAtlasiQ13526
PRIDEiQ13526
ProteomicsDBi59519

PTM databases

iPTMnetiQ13526
PhosphoSitePlusiQ13526

Expressioni

Tissue specificityi

The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.2 Publications

Gene expression databases

BgeeiENSG00000127445 Expressed in 221 organ(s), highest expression level in anterior cingulate cortex
CleanExiHS_PIN1
ExpressionAtlasiQ13526 baseline and differential
GenevisibleiQ13526 HS

Organism-specific databases

HPAiCAB004528
CAB009326
HPA068650

Interactioni

Subunit structurei

Interacts with STIL. Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX. Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML (isoform PML-4) and BCL-6. Interacts with FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (PubMed:22608923). Directly interacts with RBBP8/CtIP; this interaction depends upon RBBP8 phosphorylation (PubMed:23623683).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI2Q9NYB93EBI-714158,EBI-743598
ADAMTSL4Q6UY14-33EBI-714158,EBI-10173507
ADARB1P7856312EBI-714158,EBI-2967304
AMOTQ4VCS5-23EBI-714158,EBI-3891843
ANKRD40Q6AI125EBI-714158,EBI-2838246
APPP05067-42EBI-714158,EBI-302641
ARHGAP8P85298-425EBI-714158,EBI-9523517
ARHGEF15D3DTR73EBI-714158,EBI-10176602
CBSP355203EBI-714158,EBI-740135
CCDC184Q52MB25EBI-714158,EBI-10179526
CCDC6Q162044EBI-714158,EBI-1045350
CDK10Q151315EBI-714158,EBI-1646959
CEP55Q53EZ43EBI-714158,EBI-747776
CEP76Q8TAP65EBI-714158,EBI-742887
CNKSR1Q969H45EBI-714158,EBI-741671
DAB1O755533EBI-714158,EBI-7875264
FOXP2O154095EBI-714158,EBI-983612
GOLGA2Q083795EBI-714158,EBI-618309
Grm5P31424-23EBI-714158,EBI-8830305From a different organism.
Grm5Q3UVX52EBI-714158,EBI-8795045From Mus musculus.
HEXIM2Q96MH27EBI-714158,EBI-5460660
HOMEZQ8IX15-33EBI-714158,EBI-10172004
IKZF1Q134223EBI-714158,EBI-745305
IKZF3Q9UKT95EBI-714158,EBI-747204
IRAK1P5161710EBI-714158,EBI-358664
JAKMIP2Q96AA83EBI-714158,EBI-752007
KRT31Q153235EBI-714158,EBI-948001
KRT38O760155EBI-714158,EBI-1047263
KRT40Q6A1623EBI-714158,EBI-10171697
KRTAP10-7P604093EBI-714158,EBI-10172290
KRTAP10-9P604113EBI-714158,EBI-10172052
KRTAP4-2Q9BYR53EBI-714158,EBI-10172511
MAP2K1Q027505EBI-714158,EBI-492564
Map2k1P319384EBI-714158,EBI-298860From Mus musculus.
Map2k2Q6393212EBI-714158,EBI-397724From Mus musculus.
MAP3K8P412798EBI-714158,EBI-354900
MDFIQ997506EBI-714158,EBI-724076
MEOX2P502223EBI-714158,EBI-748397
MTUS2Q5JR593EBI-714158,EBI-742948
MYCP011065EBI-714158,EBI-447544
NAB2Q157425EBI-714158,EBI-8641936
NanogQ80Z64-12EBI-714158,EBI-15699014From a different organism.
NEK6Q9HC983EBI-714158,EBI-740364
NONOQ152334EBI-714158,EBI-350527
NONOQ15233-23EBI-714158,EBI-10203843
NOTCH1P465319EBI-714158,EBI-636374
NUP62P371985EBI-714158,EBI-347978
PNMA1Q8ND903EBI-714158,EBI-302345
PRRC1Q96M273EBI-714158,EBI-2560879
RAF1P040492EBI-714158,EBI-365996
RAI1Q7Z5J44EBI-714158,EBI-743815
RBBP8Q99708-23EBI-714158,EBI-10203615
RBPMSQ930624EBI-714158,EBI-740322
RUNX2Q139507EBI-714158,EBI-976402
SP140Q133424EBI-714158,EBI-2865100
SPERTQ8NA613EBI-714158,EBI-741724
SSBP3Q9BWW45EBI-714158,EBI-2902395
SSBP4Q9BWG43EBI-714158,EBI-744719
SULT4A1Q9BR014EBI-714158,EBI-6690555
SUPT5HO002673EBI-714158,EBI-710464
TAB3Q8N5C83EBI-714158,EBI-359964
TCF4P158843EBI-714158,EBI-533224
THAP7Q9BT493EBI-714158,EBI-741350
TNIP1Q150256EBI-714158,EBI-357849
TP53P0463712EBI-714158,EBI-366083
TRAF1Q130773EBI-714158,EBI-359224
TRAF2Q129336EBI-714158,EBI-355744
TRIP6Q156543EBI-714158,EBI-742327
TSC22D4Q9Y3Q86EBI-714158,EBI-739485
ZBTB14O438293EBI-714158,EBI-10176632
ZBTB22O152093EBI-714158,EBI-723574
ZBTB7BO151563EBI-714158,EBI-740434
ZBTB9Q96C005EBI-714158,EBI-395708
ZMIZ2Q8NF644EBI-714158,EBI-745786
ZMIZ2Q8NF64-23EBI-714158,EBI-10182121
ZNF446Q9NWS9-25EBI-714158,EBI-740232

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111317, 247 interactors
CORUMiQ13526
DIPiDIP-29306N
ELMiQ13526
IntActiQ13526, 200 interactors
MINTiQ13526
STRINGi9606.ENSP00000247970

Chemistry databases

BindingDBiQ13526

Structurei

Secondary structure

1163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ13526
SMRiQ13526
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13526

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 39WWPROSITE-ProRule annotationAdd BLAST35
Domaini52 – 163PpiCPROSITE-ProRule annotationAdd BLAST112

Domaini

The WW domain is required for the interaction with STIL and KIF20B.

Phylogenomic databases

eggNOGiKOG3259 Eukaryota
COG0760 LUCA
GeneTreeiENSGT00640000091578
HOGENOMiHOG000275331
HOVERGENiHBG002101
InParanoidiQ13526
KOiK09578
OMAiDEVQCLH
OrthoDBiEOG091G0RO7
PhylomeDBiQ13526
TreeFamiTF101101

Family and domain databases

CDDicd00201 WW, 1 hit
InterProiView protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR001202 WW_dom
IPR036020 WW_dom_sf
PfamiView protein in Pfam
PF00639 Rotamase, 1 hit
PF00397 WW, 1 hit
SMARTiView protein in SMART
SM00456 WW, 1 hit
SUPFAMiSSF51045 SSF51045, 1 hit
PROSITEiView protein in PROSITE
PS01096 PPIC_PPIASE_1, 1 hit
PS50198 PPIC_PPIASE_2, 1 hit
PS01159 WW_DOMAIN_1, 1 hit
PS50020 WW_DOMAIN_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q13526-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG
60 70 80 90 100
EPARVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE
110 120 130 140 150
EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV
160
FTDSGIHIIL RTE
Length:163
Mass (Da):18,243
Last modified:November 1, 1996 - v1
Checksum:i35391AF40B7D1E13
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EMU7K7EMU7_HUMAN
Peptidyl-prolyl cis-trans isomerase
PIN1
145Annotation score:
K7EN45K7EN45_HUMAN
Peptidyl-prolyl cis-trans isomerase
PIN1
90Annotation score:
K7EP26K7EP26_HUMAN
Peptidyl-prolyl cis-trans isomerase...
PIN1
50Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49070 mRNA Translation: AAC50492.1
CR407654 mRNA Translation: CAG28582.1
BT019331 mRNA Translation: AAV38138.1
AK291074 mRNA Translation: BAF83763.1
CH471106 Genomic DNA Translation: EAW84057.1
BC002899 mRNA Translation: AAH02899.1
CCDSiCCDS12220.1
PIRiS68520
RefSeqiNP_006212.1, NM_006221.3
UniGeneiHs.465849

Genome annotation databases

EnsembliENST00000247970; ENSP00000247970; ENSG00000127445
ENST00000588695; ENSP00000466962; ENSG00000127445
GeneIDi5300
KEGGihsa:5300
UCSCiuc002mml.3 human

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49070 mRNA Translation: AAC50492.1
CR407654 mRNA Translation: CAG28582.1
BT019331 mRNA Translation: AAV38138.1
AK291074 mRNA Translation: BAF83763.1
CH471106 Genomic DNA Translation: EAW84057.1
BC002899 mRNA Translation: AAH02899.1
CCDSiCCDS12220.1
PIRiS68520
RefSeqiNP_006212.1, NM_006221.3
UniGeneiHs.465849

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F8AX-ray1.84B1-163[»]
1I6CNMR-A6-44[»]
1I8GNMR-B6-44[»]
1I8HNMR-B6-44[»]
1NMVNMR-A1-163[»]
1NMWNMR-A50-163[»]
1PINX-ray1.35A1-163[»]
1ZCNX-ray1.90A1-161[»]
2F21X-ray1.50A1-162[»]
2ITKX-ray1.45A1-163[»]
2KBUNMR-A6-39[»]
2KCFNMR-A6-39[»]
2LB3NMR-A6-41[»]
2M8INMR-A1-39[»]
2M8JNMR-A1-39[»]
2M9ENMR-A6-15[»]
A22-39[»]
2M9FNMR-A6-15[»]
A22-39[»]
2M9INMR-A6-39[»]
2M9JNMR-A6-39[»]
2N1ONMR-A7-39[»]
2Q5AX-ray1.50A1-163[»]
2RUCNMR-A51-163[»]
2RUDNMR-A51-163[»]
2RUQNMR-A51-163[»]
2RURNMR-A51-163[»]
2XP3X-ray2.00A1-163[»]
2XP4X-ray1.80A1-163[»]
2XP5X-ray1.90A1-163[»]
2XP6X-ray1.90A1-163[»]
2XP7X-ray2.00A1-163[»]
2XP8X-ray2.10A1-163[»]
2XP9X-ray1.90A1-163[»]
2XPAX-ray1.90A1-163[»]
2XPBX-ray2.00A1-163[»]
2ZQSX-ray1.90A1-163[»]
2ZQTX-ray1.46A1-163[»]
2ZQUX-ray2.50A1-163[»]
2ZQVX-ray2.50A1-163[»]
2ZR4X-ray2.00A1-163[»]
2ZR5X-ray2.60A1-163[»]
2ZR6X-ray3.20A1-163[»]
3I6CX-ray1.30A/B45-163[»]
3IK8X-ray1.85A/B45-163[»]
3IKDX-ray2.00A/B45-163[»]
3IKGX-ray1.86A/B45-163[»]
3JYJX-ray1.87A/B45-163[»]
3KABX-ray2.19A1-163[»]
3KACX-ray2.00A/B45-163[»]
3KADX-ray1.95A1-163[»]
3KAFX-ray2.30A1-163[»]
3KAGX-ray1.90A1-163[»]
3KAHX-ray2.30A1-163[»]
3KAIX-ray1.90A1-163[»]
3KCEX-ray1.90A1-163[»]
3NTPX-ray1.76A1-163[»]
3ODKX-ray2.30A1-163[»]
3OOBX-ray1.89A1-163[»]
3TC5X-ray1.40A1-163[»]
3TCZX-ray2.10A6-163[»]
3TDBX-ray2.27A6-163[»]
3WH0X-ray1.60A1-163[»]
4GWTX-ray2.25A6-39[»]
4GWVX-ray3.05A6-39[»]
4QIBX-ray1.86A7-163[»]
4TNSX-ray1.33A/B43-163[»]
4TYOX-ray1.75A/B45-163[»]
4U84X-ray1.78A1-163[»]
4U85X-ray1.70A1-163[»]
4U86X-ray1.60A1-163[»]
5B3WX-ray2.40A/B5-15[»]
5B3XX-ray2.40A5-15[»]
5B3YX-ray1.90A5-23[»]
5B3ZX-ray2.30A/B/C/D5-39[»]
5BMYX-ray2.00A5-29[»]
5GPHNMR-A51-163[»]
5UY9X-ray1.85A1-163[»]
5VTIX-ray1.80A6-39[»]
5VTJX-ray1.50A6-39[»]
5VTKX-ray1.99A6-39[»]
ProteinModelPortaliQ13526
SMRiQ13526
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111317, 247 interactors
CORUMiQ13526
DIPiDIP-29306N
ELMiQ13526
IntActiQ13526, 200 interactors
MINTiQ13526
STRINGi9606.ENSP00000247970

Chemistry databases

BindingDBiQ13526
ChEMBLiCHEMBL2288
DrugBankiDB01766 Beta-(2-Naphthyl)-Alanine

PTM databases

iPTMnetiQ13526
PhosphoSitePlusiQ13526

Polymorphism and mutation databases

BioMutaiPIN1
DMDMi3024406

Proteomic databases

EPDiQ13526
MaxQBiQ13526
PaxDbiQ13526
PeptideAtlasiQ13526
PRIDEiQ13526
ProteomicsDBi59519

Protocols and materials databases

DNASUi5300
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247970; ENSP00000247970; ENSG00000127445
ENST00000588695; ENSP00000466962; ENSG00000127445
GeneIDi5300
KEGGihsa:5300
UCSCiuc002mml.3 human

Organism-specific databases

CTDi5300
DisGeNETi5300
EuPathDBiHostDB:ENSG00000127445.13
GeneCardsiPIN1
HGNCiHGNC:8988 PIN1
HPAiCAB004528
CAB009326
HPA068650
MIMi601052 gene
neXtProtiNX_Q13526
OpenTargetsiENSG00000127445
PharmGKBiPA33320
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3259 Eukaryota
COG0760 LUCA
GeneTreeiENSGT00640000091578
HOGENOMiHOG000275331
HOVERGENiHBG002101
InParanoidiQ13526
KOiK09578
OMAiDEVQCLH
OrthoDBiEOG091G0RO7
PhylomeDBiQ13526
TreeFamiTF101101

Enzyme and pathway databases

BRENDAi5.2.1.8 2681
ReactomeiR-HSA-1169408 ISG15 antiviral mechanism
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6811555 PI5P Regulates TP53 Acetylation
R-HSA-936440 Negative regulators of DDX58/IFIH1 signaling
SignaLinkiQ13526
SIGNORiQ13526

Miscellaneous databases

ChiTaRSiPIN1 human
EvolutionaryTraceiQ13526
GeneWikiiPIN1
GenomeRNAii5300
PROiPR:Q13526
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000127445 Expressed in 221 organ(s), highest expression level in anterior cingulate cortex
CleanExiHS_PIN1
ExpressionAtlasiQ13526 baseline and differential
GenevisibleiQ13526 HS

Family and domain databases

CDDicd00201 WW, 1 hit
InterProiView protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR001202 WW_dom
IPR036020 WW_dom_sf
PfamiView protein in Pfam
PF00639 Rotamase, 1 hit
PF00397 WW, 1 hit
SMARTiView protein in SMART
SM00456 WW, 1 hit
SUPFAMiSSF51045 SSF51045, 1 hit
PROSITEiView protein in PROSITE
PS01096 PPIC_PPIASE_1, 1 hit
PS50198 PPIC_PPIASE_2, 1 hit
PS01159 WW_DOMAIN_1, 1 hit
PS50020 WW_DOMAIN_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPIN1_HUMAN
AccessioniPrimary (citable) accession number: Q13526
Secondary accession number(s): A8K4V9, Q53X75
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 10, 2018
This is version 190 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again