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Protein

Histone H2A type 1-B/E

Gene

HIST1H2AB

more
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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: UniProtKB

GO - Biological processi

  • chromatin silencing Source: GO_Central
  • negative regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
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-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-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

HGNCiHGNC:4734. HIST1H2AB.
HGNC:4724. HIST1H2AE.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nuclear chromatin Source: GO_Central
  • nucleosome Source: UniProtKB-KW
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21S → A: Blocks the inhibition of transcription by RPS6KA5/MSK1. 1 Publication

Organism-specific databases

PharmGKBiPA29111.

Polymorphism and mutation databases

BioMutaiHIST1H2AB.
DMDMi124028530.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 130129Histone H2A type 1-B/EPRO_0000055237Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei2 – 21Phosphoserine; by RPS6KA52 Publications
Modified residuei4 – 41Citrulline; alternate1 Publication
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternateBy similarity
Modified residuei6 – 61N6-acetyllysineBy similarity
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei37 – 371N6-crotonyllysine1 Publication
Modified residuei105 – 1051N5-methylglutamine1 Publication
Modified residuei119 – 1191N6-crotonyllysine1 Publication
Modified residuei120 – 1201N6-crotonyllysine; alternate1 Publication
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate4 Publications
Modified residuei121 – 1211Phosphothreonine; by VPRBP2 Publications
Modified residuei126 – 1261N6-crotonyllysine1 Publication

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. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.11 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 VPRBP 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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP04908.
PaxDbiP04908.
PeptideAtlasiP04908.
PRIDEiP04908.
TopDownProteomicsiP04908.

PTM databases

iPTMnetiP04908.
PhosphoSiteiP04908.
SwissPalmiP04908.

Expressioni

Gene expression databases

BgeeiENSG00000137259.
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.

Protein-protein interaction databases

BioGridi109266. 19 interactions.
113931. 44 interactions.
DIPiDIP-44197N.
IntActiP04908. 28 interactions.
MINTiMINT-1139478.
STRINGi9606.ENSP00000303373.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 225Combined sources
Helixi28 – 3710Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 7327Combined sources
Beta strandi77 – 793Combined sources
Helixi81 – 899Combined sources
Helixi92 – 976Combined sources
Turni98 – 1003Combined sources
Beta strandi101 – 1033Combined sources
Helixi114 – 1163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5B40X-ray3.33C/G1-130[»]
5CPIX-ray2.90C/G1-130[»]
5CPJX-ray3.15C/G1-130[»]
5CPKX-ray2.63C/G1-130[»]
ProteinModelPortaliP04908.
SMRiP04908. Positions 12-119.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04908.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1756. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00760000118934.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP04908.
KOiK11251.
OMAiANEMFIN.
OrthoDBiEOG091G0XGD.
PhylomeDBiP04908.
TreeFamiTF300137.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 392GN → AH in CAA24951 (PubMed:6647026).Curated

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. Translation: CAB39192.1.
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.

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. Translation: CAB39192.1.
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
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[»]
5B40X-ray3.33C/G1-130[»]
5CPIX-ray2.90C/G1-130[»]
5CPJX-ray3.15C/G1-130[»]
5CPKX-ray2.63C/G1-130[»]
ProteinModelPortaliP04908.
SMRiP04908. Positions 12-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109266. 19 interactions.
113931. 44 interactions.
DIPiDIP-44197N.
IntActiP04908. 28 interactions.
MINTiMINT-1139478.
STRINGi9606.ENSP00000303373.

PTM databases

iPTMnetiP04908.
PhosphoSiteiP04908.
SwissPalmiP04908.

Polymorphism and mutation databases

BioMutaiHIST1H2AB.
DMDMi124028530.

Proteomic databases

EPDiP04908.
PaxDbiP04908.
PeptideAtlasiP04908.
PRIDEiP04908.
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.
GeneCardsiHIST1H2AB.
HIST1H2AE.
HGNCiHGNC:4734. HIST1H2AB.
HGNC:4724. HIST1H2AE.
HPAiCAB012242.
HPA041189.
MIMi602786. gene.
602795. gene.
neXtProtiNX_P04908.
PharmGKBiPA29111.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1756. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00760000118934.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP04908.
KOiK11251.
OMAiANEMFIN.
OrthoDBiEOG091G0XGD.
PhylomeDBiP04908.
TreeFamiTF300137.

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
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-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-912446. Meiotic recombination.
R-HSA-977225. Amyloid fiber formation.

Miscellaneous databases

EvolutionaryTraceiP04908.
GeneWikiiHIST1H2AB.
HIST1H2AE.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137259.
CleanExiHS_HIST1H2AB.
HS_HIST1H2AE.
ExpressionAtlasiP04908. baseline and differential.
GenevisibleiP04908. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH2A1B_HUMAN
AccessioniPrimary (citable) accession number: P04908
Secondary accession number(s): P28001, Q76P63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 174 of the entry and version 2 of the sequence. [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. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.