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Protein

Chromatin assembly factor 1 subunit B

Gene

CHAF1B

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

Functioni

Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer.1 Publication

GO - Molecular functioni

  • chromatin binding Source: ProtInc
  • histone binding Source: UniProtKB
  • unfolded protein binding Source: ProtInc

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • chromatin assembly Source: UniProtKB
  • DNA repair Source: UniProtKB-KW
  • DNA replication Source: UniProtKB-KW
  • DNA replication-dependent nucleosome assembly Source: UniProtKB
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
  • protein complex assembly Source: ProtInc
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
  • xenophagy Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiQ13112.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin assembly factor 1 subunit B
Short name:
CAF-1 subunit B
Alternative name(s):
Chromatin assembly factor I p60 subunit
Short name:
CAF-I 60 kDa subunit
Short name:
CAF-I p60
M-phase phosphoprotein 7
Gene namesi
Name:CHAF1B
Synonyms:CAF1A, CAF1P60, MPHOSPH7, MPP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:1911. CHAF1B.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • Note: DNA replication foci. Cytoplasmic in M phase.

GO - Cellular componenti

  • CAF-1 complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26447.

Polymorphism and mutation databases

BioMutaiCHAF1B.
DMDMi3121829.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Chromatin assembly factor 1 subunit BPRO_0000050896Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei394 – 3941PhosphothreonineCombined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei419 – 4191PhosphothreonineCombined sources
Modified residuei429 – 4291PhosphoserineCombined sources
Modified residuei433 – 4331PhosphothreonineCombined sources
Modified residuei458 – 4581PhosphoserineCombined sources
Modified residuei494 – 4941N6-acetyllysineCombined sources
Modified residuei495 – 4951PhosphothreonineSequence analysis
Modified residuei509 – 5091PhosphothreonineSequence analysis
Modified residuei521 – 5211PhosphothreonineSequence analysis
Modified residuei531 – 5311PhosphothreonineSequence analysis
Modified residuei538 – 5381PhosphoserineCombined sources

Post-translational modificationi

Differentially phosphorylated during cell cycle. During mitosis the p60 subunit of inactive CAF-1 is hyperphosphorylated and displaced into the cytosol. Progressivly dephosphorylated from G1 to S and G2 phase. Phosphorylated p60 is recruited to chromatin undergoing DNA repair after UV irradiation in G1, S or G2 phases.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13112.
MaxQBiQ13112.
PaxDbiQ13112.
PeptideAtlasiQ13112.
PRIDEiQ13112.

PTM databases

iPTMnetiQ13112.
PhosphoSiteiQ13112.

Expressioni

Developmental stagei

Active complex is found in G1, S and G2 phases.

Gene expression databases

BgeeiQ13112.
CleanExiHS_CHAF1B.
HS_MPP7.
GenevisibleiQ13112. HS.

Organism-specific databases

HPAiCAB033604.
HPA021679.

Interactioni

Subunit structurei

Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts of RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase. In G2 and S phase also monomeric CHAF1B is detected.

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • unfolded protein binding Source: ProtInc

Protein-protein interaction databases

BioGridi113846. 37 interactions.
DIPiDIP-29243N.
IntActiQ13112. 21 interactions.
MINTiMINT-3027086.
STRINGi9606.ENSP00000315700.

Structurei

3D structure databases

ProteinModelPortaliQ13112.
SMRiQ13112. Positions 18-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati11 – 5444WD 1Add
BLAST
Repeati64 – 10340WD 2Add
BLAST
Repeati127 – 16640WD 3Add
BLAST
Repeati169 – 20840WD 4Add
BLAST
Repeati228 – 27952WD 5Add
BLAST
Repeati299 – 34042WD 6Add
BLAST
Repeati344 – 38542WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat HIR1 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1009. Eukaryota.
ENOG410XPU4. LUCA.
GeneTreeiENSGT00550000074968.
HOGENOMiHOG000183312.
HOVERGENiHBG050780.
InParanoidiQ13112.
KOiK10751.
OMAiQDGYCTL.
OrthoDBiEOG79SDWV.
PhylomeDBiQ13112.
TreeFamiTF313062.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR029129. CAF1_p60_C.
IPR001632. Gprotein_B.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF15512. CAF-1_p60_C. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVITCEIAW HNKEPVYSLD FQHGTAGRIH RLASAGVDTN VRIWKVEKGP
60 70 80 90 100
DGKAIVEFLS NLARHTKAVN VVRFSPTGEI LASGGDDAVI LLWKVNDNKE
110 120 130 140 150
PEQIAFQDED EAQLNKENWT VVKTLRGHLE DVYDICWATD GNLMASASVD
160 170 180 190 200
NTAIIWDVSK GQKISIFNEH KSYVQGVTWD PLGQYVATLS CDRVLRVYSI
210 220 230 240 250
QKKRVAFNVS KMLSGIGAEG EARSYRMFHD DSMKSFFRRL SFTPDGSLLL
260 270 280 290 300
TPAGCVESGE NVMNTTYVFS RKNLKRPIAH LPCPGKATLA VRCCPVYFEL
310 320 330 340 350
RPVVETGVEL MSLPYRLVFA VASEDSVLLY DTQQSFPFGY VSNIHYHTLS
360 370 380 390 400
DISWSSDGAF LAISSTDGYC SFVTFEKDEL GIPLKEKPVL NMRTPDTAKK
410 420 430 440 450
TKSQTHRGSS PGPRPVEGTP ASRTQDPSSP GTTPPQARQA PAPTVIRDPP
460 470 480 490 500
SITPAVKSPL PGPSEEKTLQ PSSQNTKAHP SRRVTLNTLQ AWSKTTPRRI
510 520 530 540 550
NLTPLKTDTP PSSVPTSVIS TPSTEEIQSE TPGDAQGSPP ELKRPRLDEN

KGGTESLDP
Length:559
Mass (Da):61,493
Last modified:November 1, 1996 - v1
Checksum:iAD1846CC81B8DC9F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti494 – 4941K → N in CAA66915 (PubMed:8885239).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti506 – 5061K → Q.
Corresponds to variant rs74900401 [ dbSNP | Ensembl ].
VAR_053387

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20980 mRNA. Translation: AAA76737.1.
AP000694 Genomic DNA. Translation: BAA89426.1.
AP001725 Genomic DNA. Translation: BAA95549.1.
BC021218 mRNA. Translation: AAH21218.1.
X98262 mRNA. Translation: CAA66915.1.
CCDSiCCDS13644.1.
PIRiB56731.
RefSeqiNP_005432.1. NM_005441.2.
XP_011528055.1. XM_011529753.1.
XP_011528056.1. XM_011529754.1.
UniGeneiHs.75238.

Genome annotation databases

EnsembliENST00000314103; ENSP00000315700; ENSG00000159259.
GeneIDi8208.
KEGGihsa:8208.
UCSCiuc002yvj.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20980 mRNA. Translation: AAA76737.1.
AP000694 Genomic DNA. Translation: BAA89426.1.
AP001725 Genomic DNA. Translation: BAA95549.1.
BC021218 mRNA. Translation: AAH21218.1.
X98262 mRNA. Translation: CAA66915.1.
CCDSiCCDS13644.1.
PIRiB56731.
RefSeqiNP_005432.1. NM_005441.2.
XP_011528055.1. XM_011529753.1.
XP_011528056.1. XM_011529754.1.
UniGeneiHs.75238.

3D structure databases

ProteinModelPortaliQ13112.
SMRiQ13112. Positions 18-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113846. 37 interactions.
DIPiDIP-29243N.
IntActiQ13112. 21 interactions.
MINTiMINT-3027086.
STRINGi9606.ENSP00000315700.

PTM databases

iPTMnetiQ13112.
PhosphoSiteiQ13112.

Polymorphism and mutation databases

BioMutaiCHAF1B.
DMDMi3121829.

Proteomic databases

EPDiQ13112.
MaxQBiQ13112.
PaxDbiQ13112.
PeptideAtlasiQ13112.
PRIDEiQ13112.

Protocols and materials databases

DNASUi8208.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314103; ENSP00000315700; ENSG00000159259.
GeneIDi8208.
KEGGihsa:8208.
UCSCiuc002yvj.4. human.

Organism-specific databases

CTDi8208.
GeneCardsiCHAF1B.
HGNCiHGNC:1911. CHAF1B.
HPAiCAB033604.
HPA021679.
MIMi601245. gene.
neXtProtiNX_Q13112.
PharmGKBiPA26447.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1009. Eukaryota.
ENOG410XPU4. LUCA.
GeneTreeiENSGT00550000074968.
HOGENOMiHOG000183312.
HOVERGENiHBG050780.
InParanoidiQ13112.
KOiK10751.
OMAiQDGYCTL.
OrthoDBiEOG79SDWV.
PhylomeDBiQ13112.
TreeFamiTF313062.

Enzyme and pathway databases

SignaLinkiQ13112.

Miscellaneous databases

GeneWikiiCHAF1B.
GenomeRNAii8208.
PROiQ13112.
SOURCEiSearch...

Gene expression databases

BgeeiQ13112.
CleanExiHS_CHAF1B.
HS_MPP7.
GenevisibleiQ13112. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR029129. CAF1_p60_C.
IPR001632. Gprotein_B.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF15512. CAF-1_p60_C. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication."
    Kaufman P.D., Kobayashi R., Kessler N., Stillman B.
    Cell 81:1105-1114(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 100-123.
  2. "Genomic sequencing of 1.2-Mb region on human chromosome 21q22.2."
    Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Nakatoh E., Shintani A., Asakawa S., Shimizu N.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  5. "Identification of novel M phase phosphoproteins by expression cloning."
    Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.
    Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 474-559, PHOSPHORYLATION.
    Tissue: Lymphoblast.
  6. "Recruitment of phosphorylated chromatin assembly factor 1 to chromatin after UV irradiation of human cells."
    Martini E., Roche D.M., Marheineke K., Verreault A., Almouzni G.
    J. Cell Biol. 143:563-575(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle."
    Marheineke K., Krude T.
    J. Biol. Chem. 273:15279-15286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
  8. "CAF-1 and the inheritance of chromatin states: at the crossroads of DNA replication and repair."
    Ridgway P., Almouzni G.
    J. Cell Sci. 113:2647-2658(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-419; SER-429; THR-433 AND SER-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394; THR-419; SER-429; THR-433 AND SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiCAF1B_HUMAN
AccessioniPrimary (citable) accession number: Q13112
Secondary accession number(s): Q99548
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 173 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  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. 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.