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Protein

Remodeling and spacing factor 1

Gene

RSF1

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

Functioni

Required for assembly of regular nucleosome arrays by the RSF chromatin-remodeling complex (PubMed:12972596). Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF-alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain (PubMed:11944984, PubMed:11788598).3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri891 – 941PHD-typePROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • CENP-A containing nucleosome assembly Source: Reactome
  • chromatin modification Source: UniProtKB-KW
  • chromatin remodeling Source: UniProtKB
  • DNA-templated transcription, initiation Source: UniProtKB
  • negative regulation of DNA binding Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • nucleosome assembly Source: UniProtKB
  • nucleosome positioning Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of viral transcription Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Names & Taxonomyi

Protein namesi
Recommended name:
Remodeling and spacing factor 1
Short name:
Rsf-1
Alternative name(s):
HBV pX-associated protein 8
Hepatitis B virus X-associated protein
p325 subunit of RSF chromatin-remodeling complex
Gene namesi
Name:RSF1
Synonyms:HBXAP, XAP8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:18118. RSF1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • RSF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi51773.
OpenTargetsiENSG00000048649.
PharmGKBiPA29210.

Polymorphism and mutation databases

BioMutaiRSF1.
DMDMi251757329.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000593261 – 1441Remodeling and spacing factor 1Add BLAST1441

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei227PhosphoserineCombined sources1
Cross-linki243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki284Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki309Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki323Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki337Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki390Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei392PhosphoserineCombined sources1
Modified residuei397PhosphoserineCombined sources1
Cross-linki415Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei429PhosphoserineCombined sources1
Cross-linki456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei473PhosphoserineCombined sources1
Modified residuei524PhosphoserineCombined sources1
Modified residuei570PhosphoserineCombined sources1
Modified residuei604PhosphoserineCombined sources1
Modified residuei622PhosphoserineCombined sources1
Modified residuei628PhosphothreonineCombined sources1
Modified residuei629PhosphoserineCombined sources1
Cross-linki663Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki677Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei748PhosphoserineCombined sources1
Cross-linki758Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki768Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei882PhosphoserineCombined sources1
Modified residuei1050N6-acetyllysineCombined sources1
Modified residuei1096PhosphoserineCombined sources1
Modified residuei1098PhosphoserineCombined sources1
Modified residuei1105PhosphoserineCombined sources1
Modified residuei1221PhosphoserineCombined sources1
Modified residuei1223PhosphoserineCombined sources1
Modified residuei1226PhosphoserineCombined sources1
Modified residuei1258PhosphoserineCombined sources1
Modified residuei1277PhosphoserineCombined sources1
Modified residuei1278PhosphothreonineCombined sources1
Modified residuei1305PhosphothreonineCombined sources1
Modified residuei1325PhosphoserineCombined sources1
Modified residuei1336PhosphoserineCombined sources1
Modified residuei1339N6-acetyllysineCombined sources1
Modified residuei1345PhosphoserineCombined sources1
Modified residuei1359PhosphoserineCombined sources1
Modified residuei1375PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96T23.
MaxQBiQ96T23.
PaxDbiQ96T23.
PeptideAtlasiQ96T23.
PRIDEiQ96T23.

PTM databases

iPTMnetiQ96T23.
PhosphoSitePlusiQ96T23.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiENSG00000048649.
CleanExiHS_RSF1.
ExpressionAtlasiQ96T23. baseline and differential.
GenevisibleiQ96T23. HS.

Organism-specific databases

HPAiCAB022626.
HPA046129.
HPA057547.
HPA064567.

Interactioni

Subunit structurei

Interacts with SMARCA5/SNF2H to form the RSF complex (PubMed:12972596). Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (PubMed:27499292). Also binds the HBV pX/HBx protein, which is required to activate transcription of the viral genome (PubMed:11944984, PubMed:11788598).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMARCA5O602645EBI-926768,EBI-352588

GO - Molecular functioni

  • histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119724. 22 interactors.
IntActiQ96T23. 19 interactors.
MINTiMINT-3058575.
STRINGi9606.ENSP00000311513.

Structurei

3D structure databases

ProteinModelPortaliQ96T23.
SMRiQ96T23.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 84DDTAdd BLAST68

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili942 – 1012Sequence analysisAdd BLAST71

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi226 – 372Glu-richAdd BLAST147
Compositional biasi875 – 884Poly-Glu10
Compositional biasi1080 – 1083Poly-Ala4
Compositional biasi1146 – 1243Arg-richAdd BLAST98
Compositional biasi1286 – 1292Poly-Glu7
Compositional biasi1419 – 1424Poly-Glu6

Sequence similaritiesi

Contains 1 DDT domain.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri891 – 941PHD-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IFYI. Eukaryota.
ENOG410YTDT. LUCA.
GeneTreeiENSGT00530000064411.
HOGENOMiHOG000154205.
HOVERGENiHBG105728.
InParanoidiQ96T23.
KOiK11657.
OMAiQINYKED.
OrthoDBiEOG091G02DZ.
PhylomeDBiQ96T23.
TreeFamiTF106405.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028938. Rsf-1.
IPR028942. WHIM1_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10615:SF113. PTHR10615:SF113. 4 hits.
PfamiPF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q96T23-1) [UniParc]FASTAAdd to basket
Also known as: Alpha, XAP8alpha

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
MATAAAAAAV MAPPGCPGSC PNFAVVCSFL ERYGPLLDLP ELPFPELERV
60 70 80 90 100
LQAPPPDVGN GEVPKELVEL HLKLMRKIGK SVTADRWEKY LIKICQEFNS
110 120 130 140 150
TWAWEMEKKG YLEMSVECKL ALLKYLCECQ FDDNLKFKNI INEEDADTMR
160 170 180 190 200
LQPIGRDKDG LMYWYQLDQD HNVRMYIEEQ DDQDGSSWKC IVRNRNELAE
210 220 230 240 250
TLALLKAQID PVLLKNSSQQ DNSSRESPSL EDEETKKEEE TPKQEEQKES
260 270 280 290 300
EKMKSEEQPM DLENRSTANV LEETTVKKEK EDEKELVKLP VIVKLEKPLP
310 320 330 340 350
ENEEKKIIKE ESDSFKENVK PIKVEVKECR ADPKDTKSSM EKPVAQEPER
360 370 380 390 400
IEFGGNIKSS HEITEKSTEE TEKLKNDQQA KIPLKKREIK LSDDFDSPVK
410 420 430 440 450
GPLCKSVTPT KEFLKDEIKQ EEETCKRIST ITALGHEGKQ LVNGEVSDER
460 470 480 490 500
VAPNFKTEPI ETKFYETKEE SYSPSKDRNI ITEGNGTESL NSVITSMKTG
510 520 530 540 550
ELEKETAPLR KDADSSISVL EIHSQKAQIE EPDPPEMETS LDSSEMAKDL
560 570 580 590 600
SSKTALSSTE SCTMKGEEKS PKTKKDKRPP ILECLEKLEK SKKTFLDKDA
610 620 630 640 650
QRLSPIPEEV PKSTLESEKP GSPEAAETSP PSNIIDHCEK LASEKEVVEC
660 670 680 690 700
QSTSTVGGQS VKKVDLETLK EDSEFTKVEM DNLDNAQTSG IEEPSETKGS
710 720 730 740 750
MQKSKFKYKL VPEEETTASE NTEITSERQK EGIKLTIRIS SRKKKPDSPP
760 770 780 790 800
KVLEPENKQE KTEKEEEKTN VGRTLRRSPR ISRPTAKVAE IRDQKADKKR
810 820 830 840 850
GEGEDEVEEE STALQKTDKK EILKKSEKDT NSKVSKVKPK GKVRWTGSRT
860 870 880 890 900
RGRWKYSSND ESEGSGSEKS SAASEEEEEK ESEEAILADD DEPCKKCGLP
910 920 930 940 950
NHPELILLCD SCDSGYHTAC LRPPLMIIPD GEWFCPPCQH KLLCEKLEEQ
960 970 980 990 1000
LQDLDVALKK KERAERRKER LVYVGISIEN IIPPQEPDFS EDQEEKKKDS
1010 1020 1030 1040 1050
KKSKANLLER RSTRTRKCIS YRFDEFDEAI DEAIEDDIKE ADGGGVGRGK
1060 1070 1080 1090 1100
DISTITGHRG KDISTILDEE RKENKRPQRA AAARRKKRRR LNDLDSDSNL
1110 1120 1130 1140 1150
DEEESEDEFK ISDGSQDEFV VSDENPDESE EDPPSNDDSD TDFCSRRLRR
1160 1170 1180 1190 1200
HPSRPMRQSR RLRRKTPKKK YSDDDEEEES EENSRDSESD FSDDFSDDFV
1210 1220 1230 1240 1250
ETRRRRSRRN QKRQINYKED SESDGSQKSL RRGKEIRRVH KRRLSSSESE
1260 1270 1280 1290 1300
ESYLSKNSED DELAKESKRS VRKRGRSTDE YSEADEEEEE EEGKPSRKRL
1310 1320 1330 1340 1350
HRIETDEEES CDNAHGDANQ PARDSQPRVL PSEQESTKKP YRIESDEEED
1360 1370 1380 1390 1400
FENVGKVGSP LDYSLVDLPS TNGQSPGKAI ENLIGKPTEK SQTPKDNSTA
1410 1420 1430 1440
SASLASNGTS GGQEAGAPEE EEDELLRVTD LVDYVCNSEQ L
Length:1,441
Mass (Da):163,821
Last modified:July 7, 2009 - v2
Checksum:i0FCB9499B5097A2F
GO
Isoform 2 (identifier: Q96T23-2) [UniParc]FASTAAdd to basket
Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     93-123: Missing.

Show »
Length:1,410
Mass (Da):160,129
Checksum:i0C5AF21D8B1642C4
GO
Isoform 3 (identifier: Q96T23-3) [UniParc]FASTAAdd to basket
Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.

Show »
Length:1,189
Mass (Da):134,946
Checksum:iF5652F52FD1CFEF0
GO

Sequence cautioni

The sequence AAG43114 differs from that shown. Reason: Frameshift at position 549.Curated
The sequence AAH46124 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAK57515 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA91591 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti132D → G in AAG43114 (Ref. 4) Curated1
Sequence conflicti270V → G in AAG43114 (Ref. 4) Curated1
Sequence conflicti276V → G in AAG43114 (Ref. 4) Curated1
Sequence conflicti287V → A in AAG43114 (Ref. 4) Curated1
Sequence conflicti291V → G in AAG43114 (Ref. 4) Curated1
Sequence conflicti305K → N in AAG43114 (Ref. 4) Curated1
Sequence conflicti314 – 315SF → PS in AAG43114 (Ref. 4) Curated2
Sequence conflicti353F → L in AAG43114 (Ref. 4) Curated1
Sequence conflicti381K → E in AAG43114 (Ref. 4) Curated1
Sequence conflicti1063I → V in BAA91591 (PubMed:14702039).Curated1
Sequence conflicti1137D → E in AAK57515 (PubMed:11944984).Curated1
Sequence conflicti1137D → E in AAF61709 (PubMed:11788598).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_061741304E → D.Corresponds to variant rs58758035dbSNPEnsembl.1
Natural variantiVAR_020885475S → P.Corresponds to variant rs7950873dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0124991 – 252Missing in isoform 3. 2 PublicationsAdd BLAST252
Alternative sequenceiVSP_01250093 – 123Missing in isoform 2. 1 PublicationAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF380176 mRNA. Translation: AAK57515.1. Different initiation.
AF227948 mRNA. Translation: AAF61709.2.
AP000580 Genomic DNA. No translation available.
AP000609 Genomic DNA. No translation available.
AP002343 Genomic DNA. No translation available.
AF059317 mRNA. Translation: AAG43114.1. Sequence problems.
BC046124 mRNA. Translation: AAH46124.2. Sequence problems.
AK001268 mRNA. Translation: BAA91591.1. Different initiation.
CCDSiCCDS8253.1. [Q96T23-1]
RefSeqiNP_057662.3. NM_016578.3. [Q96T23-1]
UniGeneiHs.420229.
Hs.593415.

Genome annotation databases

EnsembliENST00000308488; ENSP00000311513; ENSG00000048649. [Q96T23-1]
ENST00000480887; ENSP00000434509; ENSG00000048649. [Q96T23-3]
GeneIDi51773.
KEGGihsa:51773.
UCSCiuc001oym.4. human. [Q96T23-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF380176 mRNA. Translation: AAK57515.1. Different initiation.
AF227948 mRNA. Translation: AAF61709.2.
AP000580 Genomic DNA. No translation available.
AP000609 Genomic DNA. No translation available.
AP002343 Genomic DNA. No translation available.
AF059317 mRNA. Translation: AAG43114.1. Sequence problems.
BC046124 mRNA. Translation: AAH46124.2. Sequence problems.
AK001268 mRNA. Translation: BAA91591.1. Different initiation.
CCDSiCCDS8253.1. [Q96T23-1]
RefSeqiNP_057662.3. NM_016578.3. [Q96T23-1]
UniGeneiHs.420229.
Hs.593415.

3D structure databases

ProteinModelPortaliQ96T23.
SMRiQ96T23.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119724. 22 interactors.
IntActiQ96T23. 19 interactors.
MINTiMINT-3058575.
STRINGi9606.ENSP00000311513.

PTM databases

iPTMnetiQ96T23.
PhosphoSitePlusiQ96T23.

Polymorphism and mutation databases

BioMutaiRSF1.
DMDMi251757329.

Proteomic databases

EPDiQ96T23.
MaxQBiQ96T23.
PaxDbiQ96T23.
PeptideAtlasiQ96T23.
PRIDEiQ96T23.

Protocols and materials databases

DNASUi51773.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308488; ENSP00000311513; ENSG00000048649. [Q96T23-1]
ENST00000480887; ENSP00000434509; ENSG00000048649. [Q96T23-3]
GeneIDi51773.
KEGGihsa:51773.
UCSCiuc001oym.4. human. [Q96T23-1]

Organism-specific databases

CTDi51773.
DisGeNETi51773.
GeneCardsiRSF1.
H-InvDBHIX0022742.
HGNCiHGNC:18118. RSF1.
HPAiCAB022626.
HPA046129.
HPA057547.
HPA064567.
MIMi608522. gene.
neXtProtiNX_Q96T23.
OpenTargetsiENSG00000048649.
PharmGKBiPA29210.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFYI. Eukaryota.
ENOG410YTDT. LUCA.
GeneTreeiENSGT00530000064411.
HOGENOMiHOG000154205.
HOVERGENiHBG105728.
InParanoidiQ96T23.
KOiK11657.
OMAiQINYKED.
OrthoDBiEOG091G02DZ.
PhylomeDBiQ96T23.
TreeFamiTF106405.

Enzyme and pathway databases

ReactomeiR-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Miscellaneous databases

ChiTaRSiRSF1. human.
GeneWikiiRSF1.
GenomeRNAii51773.
PROiQ96T23.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000048649.
CleanExiHS_RSF1.
ExpressionAtlasiQ96T23. baseline and differential.
GenevisibleiQ96T23. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028938. Rsf-1.
IPR028942. WHIM1_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10615:SF113. PTHR10615:SF113. 4 hits.
PfamiPF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRSF1_HUMAN
AccessioniPrimary (citable) accession number: Q96T23
Secondary accession number(s): Q86X86
, Q9H3L8, Q9NVZ8, Q9NYU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: July 7, 2009
Last modified: November 2, 2016
This is version 143 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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.