Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone deacetylase 5

Gene

HDAC5

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

Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.1 Publication

Catalytic activityi

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi696ZincBy similarity1
Metal bindingi698ZincBy similarity1
Metal bindingi704ZincBy similarity1
Metal bindingi781ZincBy similarity1
Active sitei833By similarity1

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • core promoter binding Source: UniProtKB
  • histone deacetylase activity Source: BHF-UCL
  • histone deacetylase binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  • protein deacetylase activity Source: UniProtKB
  • protein kinase C binding Source: UniProtKB
  • repressing transcription factor binding Source: BHF-UCL
  • RNA polymerase III transcription factor binding Source: UniProtKB
  • transcription factor binding Source: BHF-UCL

GO - Biological processi

  • B cell activation Source: UniProtKB
  • B cell differentiation Source: UniProtKB
  • cellular response to insulin stimulus Source: BHF-UCL
  • cellular response to lipopolysaccharide Source: Ensembl
  • chromatin organization Source: UniProtKB
  • chromatin remodeling Source: ProtInc
  • chromatin silencing Source: ProtInc
  • histone deacetylation Source: BHF-UCL
  • inflammatory response Source: UniProtKB
  • negative regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • negative regulation of myotube differentiation Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • neuron differentiation Source: Ensembl
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein deacetylation Source: UniProtKB
  • regulation of gene expression, epigenetic Source: UniProtKB
  • regulation of myotube differentiation Source: UniProtKB
  • regulation of protein binding Source: BHF-UCL
  • response to activity Source: Ensembl
  • response to cocaine Source: Ensembl
  • response to drug Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS03168-MONOMER.
ReactomeiR-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SIGNORiQ9UQL6.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 5 (EC:3.5.1.98)
Short name:
HD5
Alternative name(s):
Antigen NY-CO-9
Gene namesi
Name:HDAC5
Synonyms:KIAA0600
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:14068. HDAC5.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-259 and Ser-498 by AMPK, CaMK1 and SIK1.

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • Golgi apparatus Source: HPA
  • histone deacetylase complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi259S → A: Reduces AMPK- and caMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-498. Does not affect phosphorylation by PKN1 and PKN2. 3 Publications1
Mutagenesisi279S → A: No effect. 1 Publication1
Mutagenesisi291S → A: Does not affect phosphorylation by PKC. 1 Publication1
Mutagenesisi292T → A: Abolishes phosphorylation by PKC. 1 Publication1
Mutagenesisi498S → A: Reduces AMPK- and CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259. 2 Publications1
Mutagenesisi661S → A: No effect. 1 Publication1
Mutagenesisi713S → A: No effect. 1 Publication1
Mutagenesisi1086V → A: Reduces CaMK-dependent nuclear export. 1 Publication1
Mutagenesisi1092L → A: Reduces CaMK-dependent nuclear export. 1 Publication1

Organism-specific databases

DisGeNETi10014.
OpenTargetsiENSG00000108840.
PharmGKBiPA29230.

Chemistry databases

ChEMBLiCHEMBL2563.
DrugBankiDB06603. Panobinostat.
GuidetoPHARMACOLOGYi2660.

Polymorphism and mutation databases

BioMutaiHDAC5.
DMDMi296434519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001147011 – 1122Histone deacetylase 5Add BLAST1122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei259Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD13 Publications1
Modified residuei292Phosphothreonine; by PKC1 Publication1
Modified residuei498Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD13 Publications1
Modified residuei533N6-acetyllysineCombined sources1
Modified residuei611PhosphoserineCombined sources1
Modified residuei661PhosphoserineCombined sources1
Modified residuei1108PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and Ser-498. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription (By similarity).By similarity
Ubiquitinated. Polyubiquitination however does not lead to its degradation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9UQL6.
PeptideAtlasiQ9UQL6.
PRIDEiQ9UQL6.

PTM databases

iPTMnetiQ9UQL6.
PhosphoSitePlusiQ9UQL6.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000108840.
CleanExiHS_HDAC5.
ExpressionAtlasiQ9UQL6. baseline and differential.
GenevisibleiQ9UQL6. HS.

Organism-specific databases

HPAiCAB019400.
HPA030991.

Interactioni

Subunit structurei

Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts with EP300 in the presence of TFAP2C. Interacts with ANKRA2. Interacts with CUL7 (as part of the 3M complex); negatively regulated by ANKRA2.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRMS1Q9HCU92EBI-715576,EBI-714781
ICP0P083933EBI-715576,EBI-6148881From a different organism.
RUNX3Q137615EBI-715576,EBI-925990
SFNP319473EBI-715576,EBI-476295
YWHAZP631042EBI-715576,EBI-347088

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • protein kinase C binding Source: UniProtKB
  • repressing transcription factor binding Source: BHF-UCL
  • RNA polymerase III transcription factor binding Source: UniProtKB
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi115331. 346 interactors.
DIPiDIP-38260N.
IntActiQ9UQL6. 30 interactors.
MINTiMINT-1407477.
STRINGi9606.ENSP00000225983.

Chemistry databases

BindingDBiQ9UQL6.

Structurei

3D structure databases

ProteinModelPortaliQ9UQL6.
SMRiQ9UQL6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni684 – 1028Histone deacetylaseAdd BLAST345

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1081 – 1122Nuclear export signalAdd BLAST42

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi47 – 52Poly-Gly6
Compositional biasi85 – 92Poly-Gln8
Compositional biasi596 – 599Poly-Glu4
Compositional biasi1099 – 1104Poly-Ala6

Domaini

The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1343. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062809.
HOGENOMiHOG000232065.
HOVERGENiHBG057100.
InParanoidiQ9UQL6.
KOiK11406.
OMAiAANMRTV.
OrthoDBiEOG091G0EQO.
PhylomeDBiQ9UQL6.
TreeFamiTF106174.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
IPR030703. Histone_deacetylase_5.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 2 hits.
PTHR10625:SF57. PTHR10625:SF57. 2 hits.
PfamiPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSiPR01270. HDASUPER.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9UQL6-1) [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
MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG
60 70 80 90 100
GGSPSPVELR GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK
110 120 130 140 150
QHDHLTRQHE VQLQKHLKQQ QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ
160 170 180 190 200
RQEELEKQRL EQQLLILRNK EKSKESAIAS TEVKLRLQEF LLSKSKEPTP
210 220 230 240 250
GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL PLPGPYDSRD
260 270 280 290 300
DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI
310 320 330 340 350
TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR
360 370 380 390 400
ALPLDSSPNQ FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE
410 420 430 440 450
RQALQSLRQG GTLTGKFMST SSIPGCLLGV ALEGDGSPHG HASLLQHVLL
460 470 480 490 500
LEQARQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH RPLSRTQSSP
510 520 530 540 550
LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE LPRQPTTHPE
560 570 580 590 600
ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED
610 620 630 640 650
CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT
660 670 680 690 700
VPHQALGRTQ SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN
710 720 730 740 750
THVHPEHAGR IQSIWSRLQE TGLLSKCERI RGRKATLDEI QTVHSEYHTL
760 770 780 790 800
LYGTSPLNRQ KLDSKKLLGP ISQKMYAVLP CGGIGVDSDT VWNEMHSSSA
810 820 830 840 850
VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM GFCFFNSVAI
860 870 880 890 900
TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF
910 920 930 940 950
FPGSGAPEEV GGGPGVGYNV NVAWTGGVDP PIGDVEYLTA FRTVVMPIAH
960 970 980 990 1000
EFSPDVVLVS AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL
1010 1020 1030 1040 1050
ALEGGHDLTA ICDASEACVS ALLSVELQPL DEAVLQQKPN INAVATLEKV
1060 1070 1080 1090 1100
IEIQSKHWSC VQKFAAGLGR SLREAQAGET EEAETVSAMA LLSVGAEQAQ
1110 1120
AAAAREHSPR PAEEPMEQEP AL
Length:1,122
Mass (Da):121,978
Last modified:May 18, 2010 - v2
Checksum:iCF4BE774E3588FEC
GO
Isoform 2 (identifier: Q9UQL6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     684-768: Missing.

Note: No experimental confirmation available.
Show »
Length:1,037
Mass (Da):112,191
Checksum:iD4F09B907D2C1457
GO
Isoform 3 (identifier: Q9UQL6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: S → SA

Show »
Length:1,123
Mass (Da):122,049
Checksum:i909ED5CCFEE3FB4F
GO

Sequence cautioni

The sequence AAC18040 differs from that shown. Reason: Frameshift at position 1085.Curated
The sequence BAA25526 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37V → L in BX458255 (Ref. 6) Curated1
Sequence conflicti139Q → R in BX458255 (Ref. 6) Curated1
Sequence conflicti147R → G in BX458255 (Ref. 6) Curated1
Sequence conflicti593D → E in AAD29047 (PubMed:10220385).Curated1
Sequence conflicti593D → E in AAH51824 (PubMed:15489334).Curated1
Sequence conflicti593D → E in AAC18040 (PubMed:9610721).Curated1
Sequence conflicti671S → N in AAC18040 (PubMed:9610721).Curated1
Sequence conflicti684G → S in AAC18040 (PubMed:9610721).Curated1
Sequence conflicti1026E → K in AAC18040 (PubMed:9610721).Curated1
Sequence conflicti1074E → G in AAC18040 (PubMed:9610721).Curated1
Sequence conflicti1093S → L in AAC18040 (PubMed:9610721).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055903137R → Q.Corresponds to variant rs438096dbSNPEnsembl.1
Natural variantiVAR_055904565G → A.Corresponds to variant rs33916560dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0391807S → SA in isoform 3. 1 Publication1
Alternative sequenceiVSP_002081684 – 768Missing in isoform 2. 1 PublicationAdd BLAST85

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132608 mRNA. Translation: AAD29047.1.
AB011172 mRNA. Translation: BAA25526.2. Different initiation.
AC023855 Genomic DNA. No translation available.
BC013140 mRNA. Translation: AAH13140.1. Different termination.
BC051824 mRNA. Translation: AAH51824.1.
BX458255 mRNA. No translation available.
AF039691 mRNA. Translation: AAC18040.1. Frameshift.
BK000028 Genomic DNA. Translation: DAA00017.1.
CCDSiCCDS32663.1. [Q9UQL6-3]
CCDS45696.1. [Q9UQL6-1]
RefSeqiNP_001015053.1. NM_001015053.1. [Q9UQL6-3]
NP_005465.2. NM_005474.4. [Q9UQL6-1]
XP_005256963.1. XM_005256906.4. [Q9UQL6-1]
UniGeneiHs.438782.

Genome annotation databases

EnsembliENST00000225983; ENSP00000225983; ENSG00000108840. [Q9UQL6-3]
ENST00000336057; ENSP00000337290; ENSG00000108840. [Q9UQL6-2]
ENST00000586802; ENSP00000468004; ENSG00000108840. [Q9UQL6-1]
GeneIDi10014.
KEGGihsa:10014.
UCSCiuc002ifd.2. human. [Q9UQL6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132608 mRNA. Translation: AAD29047.1.
AB011172 mRNA. Translation: BAA25526.2. Different initiation.
AC023855 Genomic DNA. No translation available.
BC013140 mRNA. Translation: AAH13140.1. Different termination.
BC051824 mRNA. Translation: AAH51824.1.
BX458255 mRNA. No translation available.
AF039691 mRNA. Translation: AAC18040.1. Frameshift.
BK000028 Genomic DNA. Translation: DAA00017.1.
CCDSiCCDS32663.1. [Q9UQL6-3]
CCDS45696.1. [Q9UQL6-1]
RefSeqiNP_001015053.1. NM_001015053.1. [Q9UQL6-3]
NP_005465.2. NM_005474.4. [Q9UQL6-1]
XP_005256963.1. XM_005256906.4. [Q9UQL6-1]
UniGeneiHs.438782.

3D structure databases

ProteinModelPortaliQ9UQL6.
SMRiQ9UQL6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115331. 346 interactors.
DIPiDIP-38260N.
IntActiQ9UQL6. 30 interactors.
MINTiMINT-1407477.
STRINGi9606.ENSP00000225983.

Chemistry databases

BindingDBiQ9UQL6.
ChEMBLiCHEMBL2563.
DrugBankiDB06603. Panobinostat.
GuidetoPHARMACOLOGYi2660.

PTM databases

iPTMnetiQ9UQL6.
PhosphoSitePlusiQ9UQL6.

Polymorphism and mutation databases

BioMutaiHDAC5.
DMDMi296434519.

Proteomic databases

PaxDbiQ9UQL6.
PeptideAtlasiQ9UQL6.
PRIDEiQ9UQL6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225983; ENSP00000225983; ENSG00000108840. [Q9UQL6-3]
ENST00000336057; ENSP00000337290; ENSG00000108840. [Q9UQL6-2]
ENST00000586802; ENSP00000468004; ENSG00000108840. [Q9UQL6-1]
GeneIDi10014.
KEGGihsa:10014.
UCSCiuc002ifd.2. human. [Q9UQL6-1]

Organism-specific databases

CTDi10014.
DisGeNETi10014.
GeneCardsiHDAC5.
H-InvDBHIX0013862.
HGNCiHGNC:14068. HDAC5.
HPAiCAB019400.
HPA030991.
MIMi605315. gene.
neXtProtiNX_Q9UQL6.
OpenTargetsiENSG00000108840.
PharmGKBiPA29230.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1343. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062809.
HOGENOMiHOG000232065.
HOVERGENiHBG057100.
InParanoidiQ9UQL6.
KOiK11406.
OMAiAANMRTV.
OrthoDBiEOG091G0EQO.
PhylomeDBiQ9UQL6.
TreeFamiTF106174.

Enzyme and pathway databases

BioCyciZFISH:HS03168-MONOMER.
ReactomeiR-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SIGNORiQ9UQL6.

Miscellaneous databases

ChiTaRSiHDAC5. human.
GeneWikiiHistone_deacetylase_5.
GenomeRNAii10014.
PROiQ9UQL6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108840.
CleanExiHS_HDAC5.
ExpressionAtlasiQ9UQL6. baseline and differential.
GenevisibleiQ9UQL6. HS.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
IPR030703. Histone_deacetylase_5.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 2 hits.
PTHR10625:SF57. PTHR10625:SF57. 2 hits.
PfamiPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSiPR01270. HDASUPER.
ProtoNetiSearch...

Entry informationi

Entry nameiHDAC5_HUMAN
AccessioniPrimary (citable) accession number: Q9UQL6
Secondary accession number(s): C9JFV9
, O60340, O60528, Q96DY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 177 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 17
    Human chromosome 17: 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.