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Protein

Histone H2A type 1-B/E

Gene

HIST1H2AB

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

Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

GO - Molecular functioni

  • DNA binding Source: GO_Central
  • protein heterodimerization activity Source: InterPro

GO - Biological processi

  • chromatin organization Source: GO_Central
  • negative regulation of cell proliferation Source: UniProtKB

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-212300 PRC2 methylates histones and DNA
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-3214815 HDACs deacetylate histones
R-HSA-3214847 HATs acetylate histones
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-427359 SIRT1 negatively regulates rRNA expression
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5334118 DNA methylation
R-HSA-5578749 Transcriptional regulation by small RNAs
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689901 Metalloprotease DUBs
R-HSA-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-HSA-73728 RNA Polymerase I Promoter Opening
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 1-B/E
Alternative name(s):
Histone H2A.2
Histone H2A/a
Histone H2A/m
Gene namesi
Name:HIST1H2AB
Synonyms:H2AFM
AND
Name:HIST1H2AE
Synonyms:H2AFA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000277075.2
HostDB:ENSG00000278463.1
HGNCiHGNC:4734 HIST1H2AB
HGNC:4724 HIST1H2AE
MIMi602786 gene
602795 gene
neXtProtiNX_P04908

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

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2S → A: Blocks the inhibition of transcription by RPS6KA5/MSK1. 1 Publication1

Organism-specific databases

DisGeNETi3012
8335
OpenTargetsiENSG00000277075
ENSG00000278463
PharmGKBiPA29111

Polymorphism and mutation databases

BioMutaiHIST1H2AB
DMDMi124028530

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00000552372 – 130Histone H2A type 1-B/EAdd BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine3 Publications1
Modified residuei2Phosphoserine; by RPS6KA52 Publications1
Modified residuei4Citrulline; alternate1 Publication1
Modified residuei4Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei6N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei6N6-acetyllysine; alternateBy similarity1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-succinyllysine; alternate1 Publication1
Modified residuei14N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei37N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei37N6-crotonyllysine; alternate1 Publication1
Modified residuei75N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei76N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei96N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei96N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei96N6-succinyllysine; alternate1 Publication1
Modified residuei105N5-methylglutamine1 Publication1
Modified residuei119N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei119N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei119N6-crotonyllysine; alternate1 Publication1
Modified residuei120N6-crotonyllysine; alternate1 Publication1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate4 Publications
Modified residuei121Phosphothreonine; by DCAF12 Publications1
Modified residuei126N6-crotonyllysine1 Publication1

Post-translational modificationi

Deiminated on Arg-4 in granulocytes upon calcium entry.1 Publication
Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Monoubiquitination of Lys-120 (H2AK119Ub) by TRIM27 may promote transformation of cells in a number of breast cancers (PubMed:25470042). Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (PubMed:27083998). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.12 Publications
Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription.6 Publications
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (PubMed:24352239).1 Publication
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.By similarity
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP04908
PaxDbiP04908
PeptideAtlasiP04908
PRIDEiP04908
ProteomicsDBi51756
TopDownProteomicsiP04908

PTM databases

iPTMnetiP04908
PhosphoSitePlusiP04908
SwissPalmiP04908

Expressioni

Gene expression databases

BgeeiENSG00000277075 Expressed in 129 organ(s), highest expression level in stomach
CleanExiHS_HIST1H2AB
HS_HIST1H2AE
ExpressionAtlasiP04908 baseline and differential
GenevisibleiP04908 HS

Organism-specific databases

HPAiCAB012242
HPA041189

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST1H2BJP068999EBI-358971,EBI-6150252

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109266, 31 interactors
113931, 68 interactors
DIPiDIP-44197N
IntActiP04908, 48 interactors
MINTiP04908
STRINGi9606.ENSP00000303373

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP04908
SMRiP04908
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04908

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1756 Eukaryota
COG5262 LUCA
GeneTreeiENSGT00760000118967
HOGENOMiHOG000234652
HOVERGENiHBG009342
InParanoidiP04908
KOiK11251
OMAiGWITKFP
OrthoDBiEOG091G0XGD
PhylomeDBiP04908
TreeFamiTF300137

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit

Sequencei

Sequence statusi: Complete.

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

P04908-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR
110 120 130
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK
Length:130
Mass (Da):14,135
Last modified:January 23, 2007 - v2
Checksum:i9CFE6184B2CC89F5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38 – 39GN → AH in CAA24951 (PubMed:6647026).Curated2

Mass spectrometryi

Molecular mass is 14037.9 Da from positions 2 - 130. Determined by ESI. Monoisotopic with N-acetylserine.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00089 Genomic DNA Translation: CAA24951.1
M60752 Genomic DNA Translation: AAA63191.1
Z83741 Genomic DNA Translation: CAB06036.1
AY131983 Genomic DNA Translation: AAN59964.1
AY131986 Genomic DNA Translation: AAN59967.1
AL031777 Genomic DNA No translation available.
BC093836 mRNA Translation: AAH93836.1
BC093862 mRNA Translation: AAH93862.1
CCDSiCCDS4574.1
CCDS4595.1
PIRiB26318 HSHUA5
G40335
RefSeqiNP_003504.2, NM_003513.2
NP_066390.1, NM_021052.2
UniGeneiHs.121017
Hs.248174
Hs.709162

Genome annotation databases

EnsembliENST00000303910; ENSP00000303373; ENSG00000277075
ENST00000615868; ENSP00000483842; ENSG00000278463
GeneIDi3012
8335
KEGGihsa:3012
hsa:8335

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00089 Genomic DNA Translation: CAA24951.1
M60752 Genomic DNA Translation: AAA63191.1
Z83741 Genomic DNA Translation: CAB06036.1
AY131983 Genomic DNA Translation: AAN59964.1
AY131986 Genomic DNA Translation: AAN59967.1
AL031777 Genomic DNA No translation available.
BC093836 mRNA Translation: AAH93836.1
BC093862 mRNA Translation: AAH93862.1
CCDSiCCDS4574.1
CCDS4595.1
PIRiB26318 HSHUA5
G40335
RefSeqiNP_003504.2, NM_003513.2
NP_066390.1, NM_021052.2
UniGeneiHs.121017
Hs.248174
Hs.709162

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CV5X-ray2.50C/G1-130[»]
2RVQNMR-C1-130[»]
3A6NX-ray2.70C/G1-130[»]
3AFAX-ray2.50C/G1-130[»]
3AN2X-ray3.60C/G1-130[»]
3AV1X-ray2.50C/G1-130[»]
3AV2X-ray2.80C/G1-130[»]
3AYWX-ray2.90C/G1-130[»]
3AZEX-ray3.00C/G1-130[»]
3AZFX-ray2.70C/G1-130[»]
3AZGX-ray2.40C/G1-130[»]
3AZHX-ray3.49C/G1-130[»]
3AZIX-ray2.70C/G1-130[»]
3AZJX-ray2.89C/G1-130[»]
3AZKX-ray3.20C/G1-130[»]
3AZLX-ray2.70C/G1-130[»]
3AZMX-ray2.89C/G1-130[»]
3AZNX-ray3.00C/G1-130[»]
3W96X-ray3.00C/G11-130[»]
3W97X-ray3.20C/G1-130[»]
3W98X-ray3.42C/G1-130[»]
3W99X-ray3.00C/G1-130[»]
3WKJX-ray2.80C/G1-130[»]
3WTPX-ray2.67C/G1-130[»]
3X1SX-ray2.81C/G2-130[»]
3X1VX-ray2.92C/G2-130[»]
4YM5X-ray4.00C/G1-130[»]
4YM6X-ray3.51C/G1-130[»]
4Z5TX-ray2.80C/G1-130[»]
5AV5X-ray2.40C/G1-130[»]
5AV6X-ray2.20C/G1-130[»]
5AV8X-ray2.20C/G1-130[»]
5AV9X-ray2.20C/G1-130[»]
5AVBX-ray2.40C/G1-130[»]
5AVCX-ray2.40C/G1-130[»]
5AY8X-ray2.80C/G1-130[»]
5B0YX-ray2.56C/G1-130[»]
5B0ZX-ray1.99C/G1-130[»]
5B24X-ray3.60C/G1-130[»]
5B2IX-ray3.00C/G1-130[»]
5B2JX-ray2.60C/G1-130[»]
5B31X-ray2.20C1-130[»]
5B32X-ray2.35C1-130[»]
5B40X-ray3.33C/G1-130[»]
5CPIX-ray2.90C/G1-130[»]
5CPJX-ray3.15C/G1-130[»]
5CPKX-ray2.63C/G1-130[»]
5GSEX-ray3.14C/G/M1-130[»]
5GTCX-ray2.70C/G1-130[»]
5GXQX-ray2.85C/G1-130[»]
5JRGX-ray2.50C/G1-130[»]
5X7XX-ray2.18C/G1-130[»]
5XF3X-ray2.60C/G1-130[»]
5XF4X-ray2.87C/G1-130[»]
5XF5X-ray2.82C/G1-130[»]
5Y0CX-ray2.09C/G1-130[»]
5Y0DX-ray1.99C/G1-130[»]
6BUZelectron microscopy3.92C/G1-130[»]
6ETXelectron microscopy4.80K/O1-130[»]
ProteinModelPortaliP04908
SMRiP04908
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109266, 31 interactors
113931, 68 interactors
DIPiDIP-44197N
IntActiP04908, 48 interactors
MINTiP04908
STRINGi9606.ENSP00000303373

PTM databases

iPTMnetiP04908
PhosphoSitePlusiP04908
SwissPalmiP04908

Polymorphism and mutation databases

BioMutaiHIST1H2AB
DMDMi124028530

Proteomic databases

EPDiP04908
PaxDbiP04908
PeptideAtlasiP04908
PRIDEiP04908
ProteomicsDBi51756
TopDownProteomicsiP04908

Protocols and materials databases

DNASUi3012
8335
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303910; ENSP00000303373; ENSG00000277075
ENST00000615868; ENSP00000483842; ENSG00000278463
GeneIDi3012
8335
KEGGihsa:3012
hsa:8335

Organism-specific databases

CTDi3012
8335
DisGeNETi3012
8335
EuPathDBiHostDB:ENSG00000277075.2
HostDB:ENSG00000278463.1
GeneCardsiHIST1H2AB
HIST1H2AE
HGNCiHGNC:4734 HIST1H2AB
HGNC:4724 HIST1H2AE
HPAiCAB012242
HPA041189
MIMi602786 gene
602795 gene
neXtProtiNX_P04908
OpenTargetsiENSG00000277075
ENSG00000278463
PharmGKBiPA29111
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1756 Eukaryota
COG5262 LUCA
GeneTreeiENSGT00760000118967
HOGENOMiHOG000234652
HOVERGENiHBG009342
InParanoidiP04908
KOiK11251
OMAiGWITKFP
OrthoDBiEOG091G0XGD
PhylomeDBiP04908
TreeFamiTF300137

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-212300 PRC2 methylates histones and DNA
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-3214815 HDACs deacetylate histones
R-HSA-3214847 HATs acetylate histones
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-427359 SIRT1 negatively regulates rRNA expression
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5334118 DNA methylation
R-HSA-5578749 Transcriptional regulation by small RNAs
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689901 Metalloprotease DUBs
R-HSA-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-HSA-73728 RNA Polymerase I Promoter Opening
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation

Miscellaneous databases

EvolutionaryTraceiP04908
GeneWikiiHIST1H2AB
HIST1H2AE
PROiPR:P04908
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000277075 Expressed in 129 organ(s), highest expression level in stomach
CleanExiHS_HIST1H2AB
HS_HIST1H2AE
ExpressionAtlasiP04908 baseline and differential
GenevisibleiP04908 HS

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiH2A1B_HUMAN
AccessioniPrimary (citable) accession number: P04908
Secondary accession number(s): P28001, Q76P63
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 195 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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