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Protein

Caspase-9

Gene

CASP9

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

Functioni

Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).
Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.

Catalytic activityi

Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.1 Publication

Activity regulationi

Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei237By similarity1
Active sitei287By similarity1

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: UniProtKB
  • cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
  • cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: UniProtKB
  • enzyme activator activity Source: ProtInc
  • identical protein binding Source: IntAct
  • peptidase activity Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • SH3 domain binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processApoptosis

Enzyme and pathway databases

BRENDAi3.4.22.62 2681
ReactomeiR-HSA-111458 Formation of apoptosome
R-HSA-111459 Activation of caspases through apoptosome-mediated cleavage
R-HSA-111463 SMAC binds to IAPs
R-HSA-111464 SMAC-mediated dissociation of IAP:caspase complexes
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-198323 AKT phosphorylates targets in the cytosol
R-HSA-418889 via Dependence Receptors in the absence of ligand
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
SABIO-RKiP55211
SIGNORiP55211

Protein family/group databases

MEROPSiC14.010

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-9 (EC:3.4.22.621 Publication)
Short name:
CASP-9
Alternative name(s):
Apoptotic protease Mch-6
Apoptotic protease-activating factor 3
Short name:
APAF-3
ICE-like apoptotic protease 6
Short name:
ICE-LAP6
Cleaved into the following 2 chains:
Gene namesi
Name:CASP9
Synonyms:MCH6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000132906.17
HGNCiHGNC:1511 CASP9
MIMi602234 gene
neXtProtiNX_P55211

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi153Y → F: Inhibits tyrosine phosphorylation. Reduces caspase-9 subunit p35 formation in response to genotoxic stress. Attenuates ABL1/c-Abl-mediated caspase-3 activation, DNA fragmentation and UV irradiation-induced apoptosis. 1 Publication1

Organism-specific databases

DisGeNETi842
OpenTargetsiENSG00000132906
PharmGKBiPA26094

Chemistry databases

ChEMBLiCHEMBL2273
GuidetoPHARMACOLOGYi1625

Polymorphism and mutation databases

DMDMi28558771

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000004641? – 315Caspase-9 subunit p35
PropeptideiPRO_00000046401 – ?Sequence analysis
PropeptideiPRO_0000004642316 – 330Add BLAST15
ChainiPRO_0000004643331 – 416Caspase-9 subunit p10Add BLAST86

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei125Phosphothreonine; by MAPK1Combined sources1 Publication1
Modified residuei153Phosphotyrosine; by ABL11 Publication1
Modified residuei302PhosphoserineCombined sources1
Modified residuei307PhosphoserineCombined sources1
Modified residuei310PhosphoserineCombined sources1

Post-translational modificationi

Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events.
Phosphorylated at Thr-125 by MAPK1/ERK2. Phosphorylation at Thr-125 is sufficient to block caspase-9 processing and subsequent caspase-3 activation. Phosphorylation on Tyr-153 by ABL1/c-Abl; occurs in the response of cells to DNA damage.2 Publications

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

EPDiP55211
MaxQBiP55211
PaxDbiP55211
PeptideAtlasiP55211
PRIDEiP55211
ProteomicsDBi56814
56815 [P55211-2]
56816 [P55211-3]

PTM databases

iPTMnetiP55211
PhosphoSitePlusiP55211

Miscellaneous databases

PMAP-CutDBiP55211

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in the heart, moderate expression in liver, skeletal muscle, and pancreas. Low levels in all other tissues. Within the heart, specifically expressed in myocytes.1 Publication

Developmental stagei

Expressed at low levels in fetal heart, at moderate levels in neonate heart, and at high levels in adult heart.1 Publication

Gene expression databases

BgeeiENSG00000132906 Expressed in 232 organ(s), highest expression level in adrenal tissue
CleanExiHS_CASP9
ExpressionAtlasiP55211 baseline and differential
GenevisibleiP55211 HS

Organism-specific databases

HPAiCAB004348
HPA001473
HPA046488

Interactioni

Subunit structurei

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 35 kDa (p35) and a 10 kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome C and ATP. Interacts (inactive form) with EFHD2. Interacts with HAX1. Interacts with BIRC2/c-IAP1, XIAP/BIRC4, BIRC5/survivin, BIRC6/bruce and BIRC7/livin. Interacts with ABL1 (via SH3 domain); the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation. Interacts with NleF from pathogenic E.coli.7 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107292, 35 interactors
CORUMiP55211
DIPiDIP-27625N
ELMiP55211
IntActiP55211, 18 interactors
MINTiP55211
STRINGi9606.ENSP00000330237

Chemistry databases

BindingDBiP55211

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP55211
SMRiP55211
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55211

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 92CARDPROSITE-ProRule annotationAdd BLAST92

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Phylogenomic databases

eggNOGiKOG3573 Eukaryota
ENOG410ZQIE LUCA
GeneTreeiENSGT00760000118912
HOVERGENiHBG059022
InParanoidiP55211
KOiK04399
PhylomeDBiP55211
TreeFamiTF102023

Family and domain databases

CDDicd00032 CASc, 1 hit
InterProiView protein in InterPro
IPR001315 CARD
IPR033171 Caspase-9
IPR029030 Caspase-like_dom_sf
IPR033139 Caspase_cys_AS
IPR016129 Caspase_his_AS
IPR011029 DEATH-like_dom_sf
IPR002398 Pept_C14
IPR002138 Pept_C14_p10
IPR001309 Pept_C14_p20
IPR015917 Pept_C14A
PANTHERiPTHR10454 PTHR10454, 2 hits
PTHR10454:SF157 PTHR10454:SF157, 2 hits
PfamiView protein in Pfam
PF00619 CARD, 1 hit
PRINTSiPR00376 IL1BCENZYME
SMARTiView protein in SMART
SM00114 CARD, 1 hit
SM00115 CASc, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
SSF52129 SSF52129, 1 hit
PROSITEiView protein in PROSITE
PS50209 CARD, 1 hit
PS01122 CASPASE_CYS, 1 hit
PS01121 CASPASE_HIS, 1 hit
PS50207 CASPASE_P10, 1 hit
PS50208 CASPASE_P20, 1 hit

Sequences (4+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P55211-1) [UniParc]FASTAAdd to basket
Also known as: 9L, Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MDEADRRLLR RCRLRLVEEL QVDQLWDALL SRELFRPHMI EDIQRAGSGS
60 70 80 90 100
RRDQARQLII DLETRGSQAL PLFISCLEDT GQDMLASFLR TNRQAAKLSK
110 120 130 140 150
PTLENLTPVV LRPEIRKPEV LRPETPRPVD IGSGGFGDVG ALESLRGNAD
160 170 180 190 200
LAYILSMEPC GHCLIINNVN FCRESGLRTR TGSNIDCEKL RRRFSSLHFM
210 220 230 240 250
VEVKGDLTAK KMVLALLELA QQDHGALDCC VVVILSHGCQ ASHLQFPGAV
260 270 280 290 300
YGTDGCPVSV EKIVNIFNGT SCPSLGGKPK LFFIQACGGE QKDHGFEVAS
310 320 330 340 350
TSPEDESPGS NPEPDATPFQ EGLRTFDQLD AISSLPTPSD IFVSYSTFPG
360 370 380 390 400
FVSWRDPKSG SWYVETLDDI FEQWAHSEDL QSLLLRVANA VSVKGIYKQM
410
PGCFNFLRKK LFFKTS
Length:416
Mass (Da):46,281
Last modified:February 22, 2003 - v3
Checksum:i78E0180DF2A3BDD2
GO
Isoform 2 (identifier: P55211-2) [UniParc]FASTAAdd to basket
Also known as: 9S, Beta

The sequence of this isoform differs from the canonical sequence as follows:
     140-289: Missing.

Show »
Length:266
Mass (Da):30,184
Checksum:iA12848BEBDC35A64
GO
Isoform 3 (identifier: P55211-3) [UniParc]FASTAAdd to basket
Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     152-154: AYI → TVL
     155-416: Missing.

Note: May function as an endogenous apoptotic inhibitor, inhibits the BAX-mediated cleavage of procaspase-3.
Show »
Length:154
Mass (Da):17,397
Checksum:iB23A46C92AC6AA11
GO
Isoform 4 (identifier: P55211-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Show »
Length:333
Mass (Da):36,564
Checksum:i2B62F8CFD1FF3145
GO

Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8VVS7F8VVS7_HUMAN
Caspase-9
CASP9
421Annotation score:
Q5JRU8Q5JRU8_HUMAN
Caspase-9
CASP9
254Annotation score:
Q5JRU2Q5JRU2_HUMAN
Caspase-9
CASP9
266Annotation score:
H0Y6Y2H0Y6Y2_HUMAN
Caspase-9
CASP9
198Annotation score:
F8VWA5F8VWA5_HUMAN
Caspase-9
CASP9
95Annotation score:
H0Y3S8H0Y3S8_HUMAN
Caspase-9
CASP9
152Annotation score:
A0A087WX72A0A087WX72_HUMAN
Caspase-9
CASP9
47Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32R → S in AAC50776 (PubMed:8900201).Curated1
Sequence conflicti32R → S in BAA82697 (PubMed:10384055).Curated1
Sequence conflicti32R → S in BAA87905 (Ref. 6) Curated1
Sequence conflicti96A → G in AAC50640 (PubMed:8663294).Curated1
Sequence conflicti197L → P in AAC50776 (PubMed:8900201).Curated1
Sequence conflicti197L → P in BAA82697 (PubMed:10384055).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01541528A → V4 PublicationsCorresponds to variant dbSNP:rs1052571Ensembl.1
Natural variantiVAR_01541699S → L1 PublicationCorresponds to variant dbSNP:rs4646008Ensembl.1
Natural variantiVAR_015417102T → I1 PublicationCorresponds to variant dbSNP:rs2308941Ensembl.1
Natural variantiVAR_015418106L → V1 PublicationCorresponds to variant dbSNP:rs2308938Ensembl.1
Natural variantiVAR_015419114E → D1 PublicationCorresponds to variant dbSNP:rs2020897Ensembl.1
Natural variantiVAR_059198136F → L. Corresponds to variant dbSNP:rs1132312Ensembl.1
Natural variantiVAR_015420173R → H1 PublicationCorresponds to variant dbSNP:rs2308950Ensembl.1
Natural variantiVAR_016131176G → R. Corresponds to variant dbSNP:rs2308949Ensembl.1
Natural variantiVAR_022053185I → M. Corresponds to variant dbSNP:rs9282624Ensembl.1
Natural variantiVAR_016132192R → C. Corresponds to variant dbSNP:rs2308939Ensembl.1
Natural variantiVAR_015421221Q → R2 PublicationsCorresponds to variant dbSNP:rs1052576Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0442561 – 83Missing in isoform 4. 1 PublicationAdd BLAST83
Alternative sequenceiVSP_000818140 – 289Missing in isoform 2. 4 PublicationsAdd BLAST150
Alternative sequenceiVSP_043910152 – 154AYI → TVL in isoform 3. 1 Publication3
Alternative sequenceiVSP_043911155 – 416Missing in isoform 3. 1 PublicationAdd BLAST262

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56390 mRNA Translation: AAC50640.1
U60521 mRNA Translation: AAC50776.1
AB019205 Genomic DNA Translation: BAA82697.1
AF093130 mRNA Translation: AAD12248.1
AB015653 mRNA Translation: BAA78780.1
AB020979 mRNA Translation: BAA87905.1
AF110376 mRNA Translation: AAD13615.1
AY732490 mRNA Translation: AAV33129.1
AY214168 Genomic DNA Translation: AAO21133.1
BT006911 mRNA Translation: AAP35557.1
AK303743 mRNA Translation: BAG64715.1
AL512883 Genomic DNA No translation available.
CH471167 Genomic DNA Translation: EAW51730.1
CH471167 Genomic DNA Translation: EAW51731.1
BC002452 mRNA Translation: AAH02452.1
BC006463 mRNA Translation: AAH06463.1
CCDSiCCDS158.1 [P55211-1]
CCDS159.2 [P55211-4]
CCDS59995.1 [P55211-2]
PIRiG02635
RefSeqiNP_001220.2, NM_001229.4 [P55211-1]
NP_001264983.1, NM_001278054.1 [P55211-2]
NP_127463.2, NM_032996.3 [P55211-4]
XP_005246071.1, XM_005246014.2 [P55211-4]
UniGeneiHs.329502

Genome annotation databases

EnsembliENST00000333868; ENSP00000330237; ENSG00000132906 [P55211-1]
ENST00000348549; ENSP00000255256; ENSG00000132906 [P55211-2]
ENST00000375890; ENSP00000365051; ENSG00000132906 [P55211-4]
GeneIDi842
KEGGihsa:842
UCSCiuc001awn.5 human [P55211-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

Caspase-9 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56390 mRNA Translation: AAC50640.1
U60521 mRNA Translation: AAC50776.1
AB019205 Genomic DNA Translation: BAA82697.1
AF093130 mRNA Translation: AAD12248.1
AB015653 mRNA Translation: BAA78780.1
AB020979 mRNA Translation: BAA87905.1
AF110376 mRNA Translation: AAD13615.1
AY732490 mRNA Translation: AAV33129.1
AY214168 Genomic DNA Translation: AAO21133.1
BT006911 mRNA Translation: AAP35557.1
AK303743 mRNA Translation: BAG64715.1
AL512883 Genomic DNA No translation available.
CH471167 Genomic DNA Translation: EAW51730.1
CH471167 Genomic DNA Translation: EAW51731.1
BC002452 mRNA Translation: AAH02452.1
BC006463 mRNA Translation: AAH06463.1
CCDSiCCDS158.1 [P55211-1]
CCDS159.2 [P55211-4]
CCDS59995.1 [P55211-2]
PIRiG02635
RefSeqiNP_001220.2, NM_001229.4 [P55211-1]
NP_001264983.1, NM_001278054.1 [P55211-2]
NP_127463.2, NM_032996.3 [P55211-4]
XP_005246071.1, XM_005246014.2 [P55211-4]
UniGeneiHs.329502

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JXQX-ray2.80A/B/C/D140-416[»]
1NW9X-ray2.40B140-416[»]
2AR9X-ray2.80A/B/C/D139-416[»]
3D9TX-ray1.50C/D316-321[»]
3V3KX-ray3.49A/C/E/G/I/K/M/O141-416[»]
3YGSX-ray2.50P1-95[»]
4RHWX-ray2.10E/F1-100[»]
5JUYelectron microscopy4.10O/P/Q/R1-95[»]
5WVCX-ray2.99B/D/F1-128[»]
5WVEelectron microscopy4.40S/T/U/V/Y1-100[»]
ProteinModelPortaliP55211
SMRiP55211
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107292, 35 interactors
CORUMiP55211
DIPiDIP-27625N
ELMiP55211
IntActiP55211, 18 interactors
MINTiP55211
STRINGi9606.ENSP00000330237

Chemistry databases

BindingDBiP55211
ChEMBLiCHEMBL2273
GuidetoPHARMACOLOGYi1625

Protein family/group databases

MEROPSiC14.010

PTM databases

iPTMnetiP55211
PhosphoSitePlusiP55211

Polymorphism and mutation databases

DMDMi28558771

Proteomic databases

EPDiP55211
MaxQBiP55211
PaxDbiP55211
PeptideAtlasiP55211
PRIDEiP55211
ProteomicsDBi56814
56815 [P55211-2]
56816 [P55211-3]

Protocols and materials databases

DNASUi842
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333868; ENSP00000330237; ENSG00000132906 [P55211-1]
ENST00000348549; ENSP00000255256; ENSG00000132906 [P55211-2]
ENST00000375890; ENSP00000365051; ENSG00000132906 [P55211-4]
GeneIDi842
KEGGihsa:842
UCSCiuc001awn.5 human [P55211-1]

Organism-specific databases

CTDi842
DisGeNETi842
EuPathDBiHostDB:ENSG00000132906.17
GeneCardsiCASP9
HGNCiHGNC:1511 CASP9
HPAiCAB004348
HPA001473
HPA046488
MIMi602234 gene
neXtProtiNX_P55211
OpenTargetsiENSG00000132906
PharmGKBiPA26094
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3573 Eukaryota
ENOG410ZQIE LUCA
GeneTreeiENSGT00760000118912
HOVERGENiHBG059022
InParanoidiP55211
KOiK04399
PhylomeDBiP55211
TreeFamiTF102023

Enzyme and pathway databases

BRENDAi3.4.22.62 2681
ReactomeiR-HSA-111458 Formation of apoptosome
R-HSA-111459 Activation of caspases through apoptosome-mediated cleavage
R-HSA-111463 SMAC binds to IAPs
R-HSA-111464 SMAC-mediated dissociation of IAP:caspase complexes
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-198323 AKT phosphorylates targets in the cytosol
R-HSA-418889 via Dependence Receptors in the absence of ligand
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
SABIO-RKiP55211
SIGNORiP55211

Miscellaneous databases

EvolutionaryTraceiP55211
GeneWikiiCaspase-9
GenomeRNAii842
PMAP-CutDBiP55211
PROiPR:P55211
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132906 Expressed in 232 organ(s), highest expression level in adrenal tissue
CleanExiHS_CASP9
ExpressionAtlasiP55211 baseline and differential
GenevisibleiP55211 HS

Family and domain databases

CDDicd00032 CASc, 1 hit
InterProiView protein in InterPro
IPR001315 CARD
IPR033171 Caspase-9
IPR029030 Caspase-like_dom_sf
IPR033139 Caspase_cys_AS
IPR016129 Caspase_his_AS
IPR011029 DEATH-like_dom_sf
IPR002398 Pept_C14
IPR002138 Pept_C14_p10
IPR001309 Pept_C14_p20
IPR015917 Pept_C14A
PANTHERiPTHR10454 PTHR10454, 2 hits
PTHR10454:SF157 PTHR10454:SF157, 2 hits
PfamiView protein in Pfam
PF00619 CARD, 1 hit
PRINTSiPR00376 IL1BCENZYME
SMARTiView protein in SMART
SM00114 CARD, 1 hit
SM00115 CASc, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
SSF52129 SSF52129, 1 hit
PROSITEiView protein in PROSITE
PS50209 CARD, 1 hit
PS01122 CASPASE_CYS, 1 hit
PS01121 CASPASE_HIS, 1 hit
PS50207 CASPASE_P10, 1 hit
PS50208 CASPASE_P20, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCASP9_HUMAN
AccessioniPrimary (citable) accession number: P55211
Secondary accession number(s): B4E1A3
, O95348, Q53Y70, Q5JRU9, Q5UGI1, Q92852, Q9BQ62, Q9UEQ3, Q9UIJ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 22, 2003
Last modified: November 7, 2018
This is version 209 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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