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Protein

Histone-binding protein RBBP4

Gene

RBBP4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.1 Publication

GO - Molecular functioni

  • histone binding Source: BHF-UCL
  • histone deacetylase activity Source: Reactome
  • histone deacetylase binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Cell cycle, DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000162521-MONOMER.
ReactomeiR-HSA-1538133. G0 and Early G1.
R-HSA-156711. Polo-like kinase mediated events.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
SignaLinkiQ09028.
SIGNORiQ09028.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-binding protein RBBP4
Alternative name(s):
Chromatin assembly factor 1 subunit C
Short name:
CAF-1 subunit C
Chromatin assembly factor I p48 subunit
Short name:
CAF-I 48 kDa subunit
Short name:
CAF-I p48
Nucleosome-remodeling factor subunit RBAP48
Retinoblastoma-binding protein 4
Short name:
RBBP-4
Retinoblastoma-binding protein p48
Gene namesi
Name:RBBP4
Synonyms:RBAP48
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9887. RBBP4.

Subcellular locationi

GO - Cellular componenti

  • CAF-1 complex Source: UniProtKB
  • ESC/E(Z) complex Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: HGNC
  • NuRD complex Source: UniProtKB
  • NURF complex Source: UniProtKB
  • protein complex Source: UniProtKB
  • Sin3 complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5928.
OpenTargetsiENSG00000162521.
PharmGKBiPA34251.

Chemistry databases

ChEMBLiCHEMBL3301388.

Polymorphism and mutation databases

BioMutaiRBBP4.
DMDMi1172846.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000511862 – 425Histone-binding protein RBBP4Add BLAST424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei4N6-acetyllysine; alternateCombined sources1
Cross-linki4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei110PhosphoserineCombined sources1
Modified residuei160N6-acetyllysine; alternateBy similarity1
Cross-linki160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei355PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ09028.
MaxQBiQ09028.
PaxDbiQ09028.
PeptideAtlasiQ09028.
PRIDEiQ09028.

PTM databases

iPTMnetiQ09028.
PhosphoSitePlusiQ09028.
SwissPalmiQ09028.

Expressioni

Gene expression databases

BgeeiENSG00000162521.
CleanExiHS_RBBP4.
ExpressionAtlasiQ09028. baseline and differential.
GenevisibleiQ09028. HS.

Organism-specific databases

HPAiCAB006264.
HPA060724.

Interactioni

Subunit structurei

Interacts with SUV39H1 and HDAC7 (By similarity). Binds directly to helix 1 of the histone fold of histone H4, a region that is not accessible when H4 is in chromatin. Subunit of the chromatin assembly factor 1 (CAF-1) complex, which is composed of RBBP4, CHAF1B and CHAF1A. Subunit of the core histone deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The core HDAC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylase complex (the NuRD complex). The NuRD complex may also interact with MBD3L1 and MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex, which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The PRC2/EED-EZH2 complex may also associate with HDAC1. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. Part of the nucleosome remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein-binding domain of the retinoblastoma protein (RB1). Interacts with SPEN/MINT. Interacts with BRCA1. Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with PHF6.By similarity25 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9BRL83EBI-620823,EBI-10297046
DHX30Q7L2E33EBI-620823,EBI-1211456
HAT1O149293EBI-620823,EBI-2339359
HDAC1Q135477EBI-620823,EBI-301834
MTA1Q133308EBI-620823,EBI-714236
NR2E3Q9Y5X42EBI-620823,EBI-7216962
RBBP7Q165763EBI-620823,EBI-352227
ZFPM1Q8IX074EBI-620823,EBI-3942619

GO - Molecular functioni

  • histone binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111863. 183 interactors.
DIPiDIP-33495N.
IntActiQ09028. 113 interactors.
MINTiMINT-90543.
STRINGi9606.ENSP00000362592.

Structurei

Secondary structure

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni12 – 14Combined sources3
Helixi16 – 31Combined sources16
Beta strandi32 – 39Combined sources8
Beta strandi47 – 54Combined sources8
Beta strandi60 – 69Combined sources10
Beta strandi73 – 75Combined sources3
Beta strandi77 – 87Combined sources11
Helixi95 – 98Combined sources4
Turni100 – 103Combined sources4
Beta strandi115 – 125Combined sources11
Beta strandi128 – 133Combined sources6
Beta strandi136 – 143Combined sources8
Beta strandi145 – 147Combined sources3
Beta strandi149 – 153Combined sources5
Helixi154 – 156Combined sources3
Beta strandi170 – 174Combined sources5
Beta strandi183 – 185Combined sources3
Beta strandi187 – 189Combined sources3
Beta strandi192 – 196Combined sources5
Beta strandi202 – 206Combined sources5
Helixi207 – 209Combined sources3
Helixi211 – 213Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi220 – 223Combined sources4
Beta strandi230 – 235Combined sources6
Beta strandi242 – 247Combined sources6
Beta strandi250 – 256Combined sources7
Beta strandi262 – 264Combined sources3
Beta strandi266 – 270Combined sources5
Beta strandi276 – 281Combined sources6
Beta strandi288 – 293Combined sources6
Beta strandi296 – 302Combined sources7
Beta strandi306 – 308Combined sources3
Beta strandi310 – 314Combined sources5
Beta strandi320 – 325Combined sources6
Beta strandi332 – 337Combined sources6
Beta strandi342 – 346Combined sources5
Helixi347 – 349Combined sources3
Helixi356 – 361Combined sources6
Beta strandi366 – 370Combined sources5
Beta strandi377 – 382Combined sources6
Beta strandi384 – 386Combined sources3
Beta strandi389 – 394Combined sources6
Beta strandi397 – 404Combined sources8
Helixi406 – 409Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XU7X-ray1.90A/B1-425[»]
3GFCX-ray2.30A1-425[»]
4PBYX-ray2.50A/B1-425[»]
4PBZX-ray2.15A1-425[»]
4PC0X-ray2.50A/B1-425[»]
4R7AX-ray1.85B1-425[»]
5FXYX-ray3.20A/C/E/G1-425[»]
ProteinModelPortaliQ09028.
SMRiQ09028.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09028.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati122 – 155WD 1Add BLAST34
Repeati175 – 206WD 2Add BLAST32
Repeati225 – 256WD 3Add BLAST32
Repeati271 – 302WD 4Add BLAST32
Repeati315 – 346WD 5Add BLAST32
Repeati372 – 403WD 6Add BLAST32

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0264. Eukaryota.
ENOG410XNU9. LUCA.
GeneTreeiENSGT00570000079069.
HOVERGENiHBG053236.
InParanoidiQ09028.
KOiK10752.
OMAiMLMVWDT.
OrthoDBiEOG091G0A20.
PhylomeDBiQ09028.
TreeFamiTF106485.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

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

Isoform 1 (identifier: Q09028-1) [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
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL
60 70 80 90 100
PDVTRPEGKD FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS
110 120 130 140 150
EKGEFGGFGS VSGKIEIEIK INHEGEVNRA RYMPQNPCII ATKTPSSDVL
160 170 180 190 200
VFDYTKHPSK PDPSGECNPD LRLRGHQKEG YGLSWNPNLS GHLLSASDDH
210 220 230 240 250
TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE SLFGSVADDQ
260 270 280 290 300
KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL
310 320 330 340 350
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI
360 370 380 390 400
GEEQSPEDAE DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ
410 420
VWQMAENIYN DEDPEGSVDP EGQGS
Length:425
Mass (Da):47,656
Last modified:January 23, 2007 - v3
Checksum:iB71E2D55A444C360
GO
Isoform 2 (identifier: Q09028-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: Missing.

Note: No experimental confirmation available.
Show »
Length:424
Mass (Da):47,585
Checksum:i52055B5C74BCF3D8
GO
Isoform 3 (identifier: Q09028-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     405-425: AENIYNDEDPEGSVDPEGQGS → ELVLDH

Note: No experimental confirmation available.
Show »
Length:410
Mass (Da):46,158
Checksum:i59B630D6055A70B2
GO
Isoform 4 (identifier: Q09028-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Note: No experimental confirmation available.
Show »
Length:390
Mass (Da):43,482
Checksum:iA61A43F6AC30C8CE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61F → G in AAH15123 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0400871 – 35Missing in isoform 4. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_0400887Missing in isoform 2. 1 Publication1
Alternative sequenceiVSP_040089405 – 425AENIY…EGQGS → ELVLDH in isoform 3. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74262 mRNA. Translation: CAA52321.1.
X71810 mRNA. Translation: CAA50685.1.
BT007309 mRNA. Translation: AAP35973.1.
AK299251 mRNA. Translation: BAG61282.1.
AK312571 mRNA. Translation: BAG35466.1.
AK222779 mRNA. Translation: BAD96499.1.
AC114489 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX07513.1.
CH471059 Genomic DNA. Translation: EAX07514.1.
BC003092 mRNA. Translation: AAH03092.1.
BC015123 mRNA. Translation: AAH15123.1.
BC053904 mRNA. Translation: AAH53904.1.
BC075836 mRNA. Translation: AAH75836.1.
CCDSiCCDS366.1. [Q09028-1]
CCDS44105.1. [Q09028-2]
CCDS44106.1. [Q09028-4]
PIRiS36112.
RefSeqiNP_001128727.1. NM_001135255.1. [Q09028-2]
NP_001128728.1. NM_001135256.1. [Q09028-4]
NP_005601.1. NM_005610.2. [Q09028-1]
UniGeneiHs.16003.

Genome annotation databases

EnsembliENST00000373485; ENSP00000362584; ENSG00000162521. [Q09028-3]
ENST00000373493; ENSP00000362592; ENSG00000162521. [Q09028-1]
ENST00000414241; ENSP00000398242; ENSG00000162521. [Q09028-2]
ENST00000458695; ENSP00000396057; ENSG00000162521. [Q09028-4]
GeneIDi5928.
KEGGihsa:5928.
UCSCiuc001bvr.3. human. [Q09028-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74262 mRNA. Translation: CAA52321.1.
X71810 mRNA. Translation: CAA50685.1.
BT007309 mRNA. Translation: AAP35973.1.
AK299251 mRNA. Translation: BAG61282.1.
AK312571 mRNA. Translation: BAG35466.1.
AK222779 mRNA. Translation: BAD96499.1.
AC114489 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX07513.1.
CH471059 Genomic DNA. Translation: EAX07514.1.
BC003092 mRNA. Translation: AAH03092.1.
BC015123 mRNA. Translation: AAH15123.1.
BC053904 mRNA. Translation: AAH53904.1.
BC075836 mRNA. Translation: AAH75836.1.
CCDSiCCDS366.1. [Q09028-1]
CCDS44105.1. [Q09028-2]
CCDS44106.1. [Q09028-4]
PIRiS36112.
RefSeqiNP_001128727.1. NM_001135255.1. [Q09028-2]
NP_001128728.1. NM_001135256.1. [Q09028-4]
NP_005601.1. NM_005610.2. [Q09028-1]
UniGeneiHs.16003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XU7X-ray1.90A/B1-425[»]
3GFCX-ray2.30A1-425[»]
4PBYX-ray2.50A/B1-425[»]
4PBZX-ray2.15A1-425[»]
4PC0X-ray2.50A/B1-425[»]
4R7AX-ray1.85B1-425[»]
5FXYX-ray3.20A/C/E/G1-425[»]
ProteinModelPortaliQ09028.
SMRiQ09028.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111863. 183 interactors.
DIPiDIP-33495N.
IntActiQ09028. 113 interactors.
MINTiMINT-90543.
STRINGi9606.ENSP00000362592.

Chemistry databases

ChEMBLiCHEMBL3301388.

PTM databases

iPTMnetiQ09028.
PhosphoSitePlusiQ09028.
SwissPalmiQ09028.

Polymorphism and mutation databases

BioMutaiRBBP4.
DMDMi1172846.

Proteomic databases

EPDiQ09028.
MaxQBiQ09028.
PaxDbiQ09028.
PeptideAtlasiQ09028.
PRIDEiQ09028.

Protocols and materials databases

DNASUi5928.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373485; ENSP00000362584; ENSG00000162521. [Q09028-3]
ENST00000373493; ENSP00000362592; ENSG00000162521. [Q09028-1]
ENST00000414241; ENSP00000398242; ENSG00000162521. [Q09028-2]
ENST00000458695; ENSP00000396057; ENSG00000162521. [Q09028-4]
GeneIDi5928.
KEGGihsa:5928.
UCSCiuc001bvr.3. human. [Q09028-1]

Organism-specific databases

CTDi5928.
DisGeNETi5928.
GeneCardsiRBBP4.
HGNCiHGNC:9887. RBBP4.
HPAiCAB006264.
HPA060724.
MIMi602923. gene.
neXtProtiNX_Q09028.
OpenTargetsiENSG00000162521.
PharmGKBiPA34251.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0264. Eukaryota.
ENOG410XNU9. LUCA.
GeneTreeiENSGT00570000079069.
HOVERGENiHBG053236.
InParanoidiQ09028.
KOiK10752.
OMAiMLMVWDT.
OrthoDBiEOG091G0A20.
PhylomeDBiQ09028.
TreeFamiTF106485.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000162521-MONOMER.
ReactomeiR-HSA-1538133. G0 and Early G1.
R-HSA-156711. Polo-like kinase mediated events.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
SignaLinkiQ09028.
SIGNORiQ09028.

Miscellaneous databases

ChiTaRSiRBBP4. human.
EvolutionaryTraceiQ09028.
GeneWikiiRBBP4.
GenomeRNAii5928.
PROiQ09028.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000162521.
CleanExiHS_RBBP4.
ExpressionAtlasiQ09028. baseline and differential.
GenevisibleiQ09028. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRBBP4_HUMAN
AccessioniPrimary (citable) accession number: Q09028
Secondary accession number(s): B2R6G9
, B4DRH0, D3DPQ3, P31149, Q53H02, Q96BV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 185 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.