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Protein

Histone deacetylase 2

Gene

HDAC2

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

Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.2 Publications

Catalytic activityi

Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei142By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Hydrolase, Repressor
Biological processBiological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAi3.5.1.98 2681
ReactomeiR-HSA-193670 p75NTR negatively regulates cell cycle via SC1
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-3214815 HDACs deacetylate histones
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-6804758 Regulation of TP53 Activity through Acetylation
R-HSA-73762 RNA Polymerase I Transcription Initiation
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SABIO-RKiQ92769
SIGNORiQ92769

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 2 (EC:3.5.1.98)
Short name:
HD2
Gene namesi
Name:HDAC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000196591.11
HGNCiHGNC:4853 HDAC2
MIMi605164 gene
neXtProtiNX_Q92769

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

Organism-specific databases

DisGeNETi3066
OpenTargetsiENSG00000196591
PharmGKBiPA29227

Chemistry databases

ChEMBLiCHEMBL1937
DrugBankiDB01223 Aminophylline
DB05015 Belinostat
DB00227 Lovastatin
DB05651 MGCD-0103
DB01303 Oxtriphylline
DB06603 Panobinostat
DB06176 Romidepsin
DB05223 SB939
DB00277 Theophylline
DB00313 Valproic Acid
DB02546 Vorinostat
GuidetoPHARMACOLOGYi2616

Polymorphism and mutation databases

BioMutaiHDAC2
DMDMi68068066

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001146931 – 488Histone deacetylase 2Add BLAST488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei75N6-acetyllysine; alternateBy similarity1
Cross-linki75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei221N6-acetyllysineBy similarity1
Modified residuei262S-nitrosocysteineBy similarity1
Modified residuei274S-nitrosocysteineBy similarity1
Modified residuei394PhosphoserineCombined sources1
Modified residuei407PhosphoserineCombined sources1
Modified residuei422PhosphoserineCombined sources1
Modified residuei424PhosphoserineCombined sources1
Cross-linki439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki462Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki478Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiQ92769
MaxQBiQ92769
PaxDbiQ92769
PeptideAtlasiQ92769
PRIDEiQ92769
ProteomicsDBi75454

PTM databases

iPTMnetiQ92769
PhosphoSitePlusiQ92769

Expressioni

Tissue specificityi

Widely expressed; lower levels in brain and lung.

Gene expression databases

BgeeiENSG00000196591 Expressed in 232 organ(s), highest expression level in cerebral cortex
CleanExiHS_HDAC2
ExpressionAtlasiQ92769 baseline and differential
GenevisibleiQ92769 HS

Organism-specific databases

HPAiCAB005054
HPA011727

Interactioni

Subunit structurei

Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with SNW1, HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region). Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK and unphosphorylated DAXX. Part of a complex containing ATR and CHD4. Forms a heterologous complex at least with YY1. Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1, KDM4A and PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PIMREG. Interacts with BCL6 (non-acetylated form). Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. Interacts with CRY1, INSM1 and ZNF431. Interacts with NACC2. Interacts with MTA1, with a preference for sumoylated MTA1. Interacts with SIX3 (By similarity). Interacts with BEND3. Component of a histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2 (PubMed:21573134).By similarity29 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109316, 335 interactors
ComplexPortaliCPX-3321 SIN3A histone deacetylase complex
CPX-3322 SIN3B histone deacetylase complex
CPX-3323 SIN3A histone deacetylase complex, ES cell-specific variant
CPX-880 MBD2/NuRD nucleosome remodeling and deacetylase complex
CPX-922 MBD3/NuRD nucleosome remodeling and deacetylase complex
CORUMiQ92769
DIPiDIP-24220N
IntActiQ92769, 169 interactors
MINTiQ92769
STRINGi9606.ENSP00000430432

Chemistry databases

BindingDBiQ92769

Structurei

Secondary structure

1488
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ92769
SMRiQ92769
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92769

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 322Histone deacetylaseAdd BLAST314

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi300 – 303Poly-Gly4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1342 Eukaryota
COG0123 LUCA
GeneTreeiENSGT00910000144047
HOGENOMiHOG000225180
HOVERGENiHBG057112
InParanoidiQ92769
KOiK06067
OMAiCDIAINY
OrthoDBiEOG091G067J
PhylomeDBiQ92769
TreeFamiTF106171

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR000286 His_deacetylse
IPR003084 His_deacetylse_1
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR023696 Ureohydrolase_dom_sf
PANTHERiPTHR10625 PTHR10625, 1 hit
PfamiView protein in Pfam
PF00850 Hist_deacetyl, 1 hit
PIRSFiPIRSF037913 His_deacetylse_1, 1 hit
PRINTSiPR01270 HDASUPER
PR01271 HISDACETLASE
SUPFAMiSSF52768 SSF52768, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 9 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q92769-1) [UniParc]FASTAAdd to basket

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
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR
60 70 80 90 100
KMEIYRPHKA TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED
110 120 130 140 150
CPVFDGLFEF CQLSTGGSVA GAVKLNRQQT DMAVNWAGGL HHAKKSEASG
160 170 180 190 200
FCYVNDIVLA ILELLKYHQR VLYIDIDIHH GDGVEEAFYT TDRVMTVSFH
210 220 230 240 250
KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ IFKPIISKVM
260 270 280 290 300
EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG
310 320 330 340 350
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN
360 370 380 390 400
MTNQNTPEYM EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE
410 420 430 440 450
DPDKRISIRA SDKRIACDEE FSDSEDEGEG GRRNVADHKK GAKKARIEED
460 470 480
KKETEDKKTD VKEEDKSKDN SGEKTDTKGT KSEQLSNP
Length:488
Mass (Da):55,364
Last modified:June 21, 2005 - v2
Checksum:i775419CCCDAE07FA
GO
Isoform 2 (identifier: Q92769-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Note: No experimental confirmation available.
Show »
Length:458
Mass (Da):51,998
Checksum:i73BF368ACAA58819
GO

Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RFP9E5RFP9_HUMAN
Histone deacetylase 2
HDAC2
109Annotation score:
E5RH52E5RH52_HUMAN
Histone deacetylase 2
HDAC2
100Annotation score:
H3BM24H3BM24_HUMAN
Histone deacetylase 2
HDAC2
161Annotation score:
E5RG37E5RG37_HUMAN
Histone deacetylase 2
HDAC2
103Annotation score:
E5RGV4E5RGV4_HUMAN
Histone deacetylase 2
HDAC2
71Annotation score:
E5RFI6E5RFI6_HUMAN
Histone deacetylase 2
HDAC2
60Annotation score:
E5RHE7E5RHE7_HUMAN
Histone deacetylase 2
HDAC2
86Annotation score:
E5RJ04E5RJ04_HUMAN
Histone deacetylase 2
HDAC2
65Annotation score:
E5RK19E5RK19_HUMAN
Histone deacetylase 2
HDAC2
52Annotation score:

Sequence cautioni

The sequence AAH31055 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG59420 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti93 – 94QR → HI in AAC50814 (PubMed:8917507).Curated2
Sequence conflicti103V → A in AAC50814 (PubMed:8917507).Curated1
Sequence conflicti146S → Y in AAC50814 (PubMed:8917507).Curated1
Sequence conflicti248K → M in BAG59420 (PubMed:14702039).Curated1
Sequence conflicti281G → D in BAG59420 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025311230R → C1 PublicationCorresponds to variant dbSNP:rs1042903Ensembl.1
Natural variantiVAR_025312315Y → H1 PublicationCorresponds to variant dbSNP:rs17852888Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0561751 – 30Missing in isoform 2. 1 PublicationAdd BLAST30

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31814 mRNA Translation: AAC50814.1
AK092156 mRNA Translation: BAG52487.1
AK296856 mRNA Translation: BAG59420.1 Different initiation.
AL590398 Genomic DNA No translation available.
AL671967 Genomic DNA No translation available.
FO393415 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48252.1
CH471051 Genomic DNA Translation: EAW48253.1
CH471051 Genomic DNA Translation: EAW48254.1
CH471051 Genomic DNA Translation: EAW48255.1
BC031055 mRNA Translation: AAH31055.2 Different initiation.
CCDSiCCDS43493.2 [Q92769-1]
RefSeqiNP_001518.3, NM_001527.3 [Q92769-1]
XP_011534090.1, XM_011535788.1
XP_016866288.1, XM_017010799.1 [Q92769-3]
UniGeneiHs.3352

Genome annotation databases

EnsembliENST00000368632; ENSP00000357621; ENSG00000196591 [Q92769-3]
ENST00000519065; ENSP00000430432; ENSG00000196591 [Q92769-1]
ENST00000519108; ENSP00000430008; ENSG00000196591 [Q92769-3]
GeneIDi3066
KEGGihsa:3066
UCSCiuc003pwc.3 human [Q92769-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31814 mRNA Translation: AAC50814.1
AK092156 mRNA Translation: BAG52487.1
AK296856 mRNA Translation: BAG59420.1 Different initiation.
AL590398 Genomic DNA No translation available.
AL671967 Genomic DNA No translation available.
FO393415 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48252.1
CH471051 Genomic DNA Translation: EAW48253.1
CH471051 Genomic DNA Translation: EAW48254.1
CH471051 Genomic DNA Translation: EAW48255.1
BC031055 mRNA Translation: AAH31055.2 Different initiation.
CCDSiCCDS43493.2 [Q92769-1]
RefSeqiNP_001518.3, NM_001527.3 [Q92769-1]
XP_011534090.1, XM_011535788.1
XP_016866288.1, XM_017010799.1 [Q92769-3]
UniGeneiHs.3352

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MAXX-ray2.05A/B/C9-374[»]
4LXZX-ray1.85A/B/C8-376[»]
4LY1X-ray1.57A/B/C8-376[»]
5IWGX-ray1.66A/B/C8-375[»]
5IX0X-ray1.72A/B/C7-375[»]
6G3OX-ray2.27A/B/C7-376[»]
ProteinModelPortaliQ92769
SMRiQ92769
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109316, 335 interactors
ComplexPortaliCPX-3321 SIN3A histone deacetylase complex
CPX-3322 SIN3B histone deacetylase complex
CPX-3323 SIN3A histone deacetylase complex, ES cell-specific variant
CPX-880 MBD2/NuRD nucleosome remodeling and deacetylase complex
CPX-922 MBD3/NuRD nucleosome remodeling and deacetylase complex
CORUMiQ92769
DIPiDIP-24220N
IntActiQ92769, 169 interactors
MINTiQ92769
STRINGi9606.ENSP00000430432

Chemistry databases

BindingDBiQ92769
ChEMBLiCHEMBL1937
DrugBankiDB01223 Aminophylline
DB05015 Belinostat
DB00227 Lovastatin
DB05651 MGCD-0103
DB01303 Oxtriphylline
DB06603 Panobinostat
DB06176 Romidepsin
DB05223 SB939
DB00277 Theophylline
DB00313 Valproic Acid
DB02546 Vorinostat
GuidetoPHARMACOLOGYi2616

PTM databases

iPTMnetiQ92769
PhosphoSitePlusiQ92769

Polymorphism and mutation databases

BioMutaiHDAC2
DMDMi68068066

Proteomic databases

EPDiQ92769
MaxQBiQ92769
PaxDbiQ92769
PeptideAtlasiQ92769
PRIDEiQ92769
ProteomicsDBi75454

Protocols and materials databases

DNASUi3066
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368632; ENSP00000357621; ENSG00000196591 [Q92769-3]
ENST00000519065; ENSP00000430432; ENSG00000196591 [Q92769-1]
ENST00000519108; ENSP00000430008; ENSG00000196591 [Q92769-3]
GeneIDi3066
KEGGihsa:3066
UCSCiuc003pwc.3 human [Q92769-1]

Organism-specific databases

CTDi3066
DisGeNETi3066
EuPathDBiHostDB:ENSG00000196591.11
GeneCardsiHDAC2
HGNCiHGNC:4853 HDAC2
HPAiCAB005054
HPA011727
MIMi605164 gene
neXtProtiNX_Q92769
OpenTargetsiENSG00000196591
PharmGKBiPA29227
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1342 Eukaryota
COG0123 LUCA
GeneTreeiENSGT00910000144047
HOGENOMiHOG000225180
HOVERGENiHBG057112
InParanoidiQ92769
KOiK06067
OMAiCDIAINY
OrthoDBiEOG091G067J
PhylomeDBiQ92769
TreeFamiTF106171

Enzyme and pathway databases

BRENDAi3.5.1.98 2681
ReactomeiR-HSA-193670 p75NTR negatively regulates cell cycle via SC1
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-3214815 HDACs deacetylate histones
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-6804758 Regulation of TP53 Activity through Acetylation
R-HSA-73762 RNA Polymerase I Transcription Initiation
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SABIO-RKiQ92769
SIGNORiQ92769

Miscellaneous databases

ChiTaRSiHDAC2 human
EvolutionaryTraceiQ92769
GeneWikiiHistone_deacetylase_2
GenomeRNAii3066
PROiPR:Q92769
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196591 Expressed in 232 organ(s), highest expression level in cerebral cortex
CleanExiHS_HDAC2
ExpressionAtlasiQ92769 baseline and differential
GenevisibleiQ92769 HS

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR000286 His_deacetylse
IPR003084 His_deacetylse_1
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR023696 Ureohydrolase_dom_sf
PANTHERiPTHR10625 PTHR10625, 1 hit
PfamiView protein in Pfam
PF00850 Hist_deacetyl, 1 hit
PIRSFiPIRSF037913 His_deacetylse_1, 1 hit
PRINTSiPR01270 HDASUPER
PR01271 HISDACETLASE
SUPFAMiSSF52768 SSF52768, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHDAC2_HUMAN
AccessioniPrimary (citable) accession number: Q92769
Secondary accession number(s): B3KRS5
, B4DL58, E1P561, Q5SRI8, Q5SZ86, Q8NEH4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 21, 2005
Last modified: November 7, 2018
This is version 208 of the entry and version 2 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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Main funding by: National Institutes of Health

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