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Protein

DNA-binding protein SATB1

Gene

SATB1

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

Functioni

Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma (By similarity). Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes (e.g. PML at the MHC-I locus) and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis.By similarity18 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei390Matrix attachment region (MAR) DNA1
Binding sitei425Matrix attachment region (MAR) DNA1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi361 – 448CUT 1PROSITE-ProRule annotationAdd BLAST88
DNA bindingi484 – 571CUT 2PROSITE-ProRule annotationAdd BLAST88
DNA bindingi645 – 704HomeoboxPROSITE-ProRule annotationAdd BLAST60

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • double-stranded DNA binding Source: ProtInc
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: NTNU_SB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:G66-33818-MONOMER.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
SIGNORiQ01826.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein SATB1
Alternative name(s):
Special AT-rich sequence-binding protein 1
Gene namesi
Name:SATB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10541. SATB1.

Subcellular locationi

  • Nucleus matrix
  • NucleusPML body

  • Note: Organized into a cage-like network anchoring loops of heterochromatin and tethering specialized DNA sequences. When sumoylated, localized in promyelocytic leukemia nuclear bodies (PML NBs).

GO - Cellular componenti

  • nuclear heterochromatin Source: Ensembl
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29K → A: Loss of nuclear localization, cytoplasmic. 1 Publication1
Mutagenesisi32R → A: Loss of nuclear localization, cytoplasmic. 1 Publication1
Mutagenesisi34E → A: Normal nuclear localization. 1 Publication1
Mutagenesisi36N → A: Normal nuclear localization. 1 Publication1
Mutagenesisi136K → A, Q or R: No acetylation. 2 Publications1
Mutagenesisi185S → A: No phosphorylation. 1 Publication1
Mutagenesisi254D → A: CASP6-resistant. 1 Publication1
Mutagenesisi373S → A: Slightly reduced MAR-DNA-binding. 1 Publication1
Mutagenesisi380R → N: Reduced MAR-DNA-binding. 1 Publication1
Mutagenesisi384K → N: Impaired MAR-DNA-binding. 1 Publication1
Mutagenesisi395R → N: Reduced MAR-DNA-binding. 1 Publication1
Mutagenesisi402Q → A: Impaired MAR-DNA-binding. 1 Publication1
Mutagenesisi403G → A: Impaired MAR-DNA-binding. 1 Publication1
Mutagenesisi406S → A: Impaired MAR-DNA-binding. 1 Publication1
Mutagenesisi410R → N: Impaired MAR-DNA-binding. 1 Publication1
Mutagenesisi411K → R: Normal sumoylation. 1 Publication1
Mutagenesisi416K → N: Impaired MAR-DNA-binding. 1 Publication1
Mutagenesisi427R → N: Reduced MAR-DNA-binding. 1 Publication1
Mutagenesisi442R → N: Reduced MAR-DNA-binding. 1 Publication1
Mutagenesisi451S → A: Slightly reduced MAR-DNA-binding. 1 Publication1
Mutagenesisi475K → N: Reduced MAR-DNA-binding. 1 Publication1
Mutagenesisi486K → R: Normal sumoylation. 1 Publication1
Mutagenesisi646R → A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-648. 1 Publication1
Mutagenesisi648R → A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-646. 1 Publication1
Mutagenesisi693 – 695FQN → AAA: Reduced interaction with matrix attachment region (MAR) DNA. 1 Publication3
Mutagenesisi720K → R: Normal sumoylation. 1 Publication1
Mutagenesisi744K → R: Loss of sumoylation. 1 Publication1

Organism-specific databases

DisGeNETi6304.
OpenTargetsiENSG00000182568.
PharmGKBiPA34951.

Polymorphism and mutation databases

BioMutaiSATB1.
DMDMi417747.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002023981 – 763DNA-binding protein SATB1Add BLAST763

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei136N6-acetyllysine1 Publication1
Modified residuei185Phosphoserine1 Publication1
Modified residuei637PhosphoserineBy similarity1
Cross-linki744Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Sumoylated. Sumoylation promotes cleavage by caspases.2 Publications
Phosphorylated by PKC. Acetylated by PCAF. Phosphorylated form interacts with HDAC1, but unphosphorylated form interacts with PCAF. DNA binding properties are activated by phosphorylation and inactivated by acetylation. In opposition, gene expression is down-regulated by phosphorylation but up-regulated by acetylation.1 Publication
Cleaved at Asp-254 by caspase-3 and caspase-6 during T-cell apoptosis in thymus and during B-cell stimulation. The cleaved forms cannot dimerize and lose transcription regulation function because of impaired DNA and chromatin association.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei254 – 255Cleavage; by caspases2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ01826.
MaxQBiQ01826.
PeptideAtlasiQ01826.
PRIDEiQ01826.

PTM databases

iPTMnetiQ01826.
PhosphoSitePlusiQ01826.

Miscellaneous databases

PMAP-CutDBQ01826.

Expressioni

Tissue specificityi

Expressed predominantly in thymus.1 Publication

Gene expression databases

BgeeiENSG00000182568.
CleanExiHS_SATB1.
ExpressionAtlasiQ01826. baseline and differential.
GenevisibleiQ01826. HS.

Organism-specific databases

HPAiCAB023814.
HPA051769.

Interactioni

Subunit structurei

Interacts with CUX1 (via DNA-binding domains); the interaction inhibits the attachment of both proteins to DNA (By similarity). Homodimer. Part of the nuclear protein complex gamma-globin promoter and enhancer binding factor (gamma-PE) composed at least of SATB1 and HOXB2. Interaction with CtBP1 when not acetylated stabalizes attachment to DNA and promotes transcription repression. Interacts with PCAF. Interacts with sumoylated PML, HDAC1 and HIV-1 Tat via the PDZ-like dimerization domain. Interacts also with DYNLT3 and POLR2J2. Binds to EP300.By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
G2XKQ03EBI-743747,EBI-10175576
CASP6P552122EBI-743747,EBI-718729
SUMO1P631652EBI-743747,EBI-80140

Protein-protein interaction databases

BioGridi112211. 49 interactors.
DIPiDIP-48757N.
IntActiQ01826. 30 interactors.
MINTiMINT-1478608.

Structurei

Secondary structure

1763
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi72 – 83Combined sources12
Beta strandi92 – 102Combined sources11
Helixi107 – 109Combined sources3
Helixi110 – 117Combined sources8
Helixi122 – 127Combined sources6
Beta strandi129 – 134Combined sources6
Helixi142 – 144Combined sources3
Helixi153 – 157Combined sources5
Turni158 – 163Combined sources6
Beta strandi164 – 169Combined sources6
Helixi181 – 183Combined sources3
Helixi186 – 196Combined sources11
Turni197 – 199Combined sources3
Helixi202 – 208Combined sources7
Beta strandi209 – 211Combined sources3
Helixi213 – 221Combined sources9
Helixi230 – 245Combined sources16
Helixi375 – 386Combined sources12
Helixi390 – 398Combined sources9
Helixi402 – 411Combined sources10
Helixi415 – 417Combined sources3
Helixi420 – 433Combined sources14
Helixi437 – 452Combined sources16
Helixi653 – 665Combined sources13
Helixi672 – 681Combined sources10
Helixi687 – 702Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YSENMR-A353-490[»]
2L1PNMR-A179-250[»]
2MW8NMR-A641-707[»]
2O49X-ray2.00A368-452[»]
2O4AX-ray1.75A368-452[»]
3NZLX-ray1.20A179-250[»]
3TUOX-ray1.70A/B/C/D71-171[»]
ProteinModelPortaliQ01826.
SMRiQ01826.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01826.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni90 – 204PDZ-like dimerization domainAdd BLAST115
Regioni224 – 278Nuclear matrix targeting sequence (NMTS)Add BLAST55
Regioni400 – 410Matrix attachment region (MAR) DNA-bindingAdd BLAST11

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi20 – 40Nuclear localization signal1 PublicationAdd BLAST21
Motifi139 – 143Protein interaction5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi591 – 607Poly-GlnAdd BLAST17
Compositional biasi609 – 614Poly-Pro6

Sequence similaritiesi

Belongs to the CUT homeobox family.Curated
Contains 2 CUT DNA-binding domains.PROSITE-ProRule annotation
Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Homeobox, Repeat

Phylogenomic databases

GeneTreeiENSGT00390000008096.
HOGENOMiHOG000004805.
HOVERGENiHBG054240.
InParanoidiQ01826.
OMAiSMNINAS.
OrthoDBiEOG091G02HV.
PhylomeDBiQ01826.
TreeFamiTF332714.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.260.40. 2 hits.
InterProiIPR003350. CUT_dom.
IPR032355. CUTL.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
IPR032392. ULD.
[Graphical view]
PfamiPF02376. CUT. 2 hits.
PF16557. CUTL. 1 hit.
PF00046. Homeobox. 1 hit.
PF16534. ULD. 1 hit.
[Graphical view]
SMARTiSM01109. CUT. 2 hits.
SM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 2 hits.
PROSITEiPS51042. CUT. 2 hits.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q01826-1) [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
MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGA
60 70 80 90 100
KMQGVPLKHS GHLMKTNLRK GTMLPVFCVV EHYENAIEYD CKEEHAEFVL
110 120 130 140 150
VRKDMLFNQL IEMALLSLGY SHSSAAQAKG LIQVGKWNPV PLSYVTDAPD
160 170 180 190 200
ATVADMLQDV YHVVTLKIQL HSCPKLEDLP PEQWSHTTVR NALKDLLKDM
210 220 230 240 250
NQSSLAKECP LSQSMISSIV NSTYYANVSA AKCQEFGRWY KHFKKTKDMM
260 270 280 290 300
VEMDSLSELS QQGANHVNFG QQPVPGNTAE QPPSPAQLSH GSQPSVRTPL
310 320 330 340 350
PNLHPGLVST PISPQLVNQQ LVMAQLLNQQ YAVNRLLAQQ SLNQQYLNHP
360 370 380 390 400
PPVSRSMNKP LEQQVSTNTE VSSEIYQWVR DELKRAGISQ AVFARVAFNR
410 420 430 440 450
TQGLLSEILR KEEDPKTASQ SLLVNLRAMQ NFLQLPEAER DRIYQDERER
460 470 480 490 500
SLNAASAMGP APLISTPPSR PPQVKTATIA TERNGKPENN TMNINASIYD
510 520 530 540 550
EIQQEMKRAK VSQALFAKVA ATKSQGWLCE LLRWKEDPSP ENRTLWENLS
560 570 580 590 600
MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQQQQQQQQ
610 620 630 640 650
QQQQQQQAPP PPQPQQQPQT GPRLPPRQPT VASPAESDEE NRQKTRPRTK
660 670 680 690 700
ISVEALGILQ SFIQDVGLYP DEEAIQTLSA QLDLPKYTII KFFQNQRYYL
710 720 730 740 750
KHHGKLKDNS GLEVDVAEYK EEELLKDLEE SVQDKNTNTL FSVKLEEELS
760
VEGNTDINTD LKD
Length:763
Mass (Da):85,957
Last modified:October 1, 1993 - v1
Checksum:iD4FE09B09FB7683B
GO
Isoform 2 (identifier: Q01826-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     592-592: I → IQSPSPTTLGKGESRGVFLPGLPTPAPWLGAAP

Show »
Length:795
Mass (Da):89,127
Checksum:i4883C06CCD96D9FF
GO

Sequence cautioni

The sequence BAD92998 differs from that shown. Reason: Erroneous initiation.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_038296592I → IQSPSPTTLGKGESRGVFLP GLPTPAPWLGAAP in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97287 mRNA. Translation: AAA60304.1.
AK127242 mRNA. Translation: BAG54463.1.
AB209761 mRNA. Translation: BAD92998.1. Different initiation.
AC139618 Genomic DNA. No translation available.
AC144521 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64291.1.
BC001744 mRNA. Translation: AAH01744.1.
CCDSiCCDS2631.1. [Q01826-1]
CCDS56242.1. [Q01826-2]
PIRiA43314.
RefSeqiNP_001124482.1. NM_001131010.3. [Q01826-1]
NP_001182399.1. NM_001195470.2. [Q01826-2]
NP_001309800.1. NM_001322871.1. [Q01826-2]
NP_001309801.1. NM_001322872.1. [Q01826-1]
NP_001309802.1. NM_001322873.1. [Q01826-1]
NP_001309803.1. NM_001322874.1. [Q01826-1]
NP_001309804.1. NM_001322875.1. [Q01826-1]
NP_002962.1. NM_002971.5. [Q01826-1]
XP_011532290.1. XM_011533988.2. [Q01826-2]
XP_011532291.1. XM_011533989.2. [Q01826-2]
UniGeneiHs.517717.
Hs.593276.

Genome annotation databases

EnsembliENST00000338745; ENSP00000341024; ENSG00000182568. [Q01826-1]
ENST00000417717; ENSP00000399518; ENSG00000182568. [Q01826-2]
ENST00000454909; ENSP00000399708; ENSG00000182568. [Q01826-1]
GeneIDi6304.
KEGGihsa:6304.
UCSCiuc003cbh.4. human. [Q01826-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97287 mRNA. Translation: AAA60304.1.
AK127242 mRNA. Translation: BAG54463.1.
AB209761 mRNA. Translation: BAD92998.1. Different initiation.
AC139618 Genomic DNA. No translation available.
AC144521 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64291.1.
BC001744 mRNA. Translation: AAH01744.1.
CCDSiCCDS2631.1. [Q01826-1]
CCDS56242.1. [Q01826-2]
PIRiA43314.
RefSeqiNP_001124482.1. NM_001131010.3. [Q01826-1]
NP_001182399.1. NM_001195470.2. [Q01826-2]
NP_001309800.1. NM_001322871.1. [Q01826-2]
NP_001309801.1. NM_001322872.1. [Q01826-1]
NP_001309802.1. NM_001322873.1. [Q01826-1]
NP_001309803.1. NM_001322874.1. [Q01826-1]
NP_001309804.1. NM_001322875.1. [Q01826-1]
NP_002962.1. NM_002971.5. [Q01826-1]
XP_011532290.1. XM_011533988.2. [Q01826-2]
XP_011532291.1. XM_011533989.2. [Q01826-2]
UniGeneiHs.517717.
Hs.593276.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YSENMR-A353-490[»]
2L1PNMR-A179-250[»]
2MW8NMR-A641-707[»]
2O49X-ray2.00A368-452[»]
2O4AX-ray1.75A368-452[»]
3NZLX-ray1.20A179-250[»]
3TUOX-ray1.70A/B/C/D71-171[»]
ProteinModelPortaliQ01826.
SMRiQ01826.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112211. 49 interactors.
DIPiDIP-48757N.
IntActiQ01826. 30 interactors.
MINTiMINT-1478608.

PTM databases

iPTMnetiQ01826.
PhosphoSitePlusiQ01826.

Polymorphism and mutation databases

BioMutaiSATB1.
DMDMi417747.

Proteomic databases

EPDiQ01826.
MaxQBiQ01826.
PeptideAtlasiQ01826.
PRIDEiQ01826.

Protocols and materials databases

DNASUi6304.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338745; ENSP00000341024; ENSG00000182568. [Q01826-1]
ENST00000417717; ENSP00000399518; ENSG00000182568. [Q01826-2]
ENST00000454909; ENSP00000399708; ENSG00000182568. [Q01826-1]
GeneIDi6304.
KEGGihsa:6304.
UCSCiuc003cbh.4. human. [Q01826-1]

Organism-specific databases

CTDi6304.
DisGeNETi6304.
GeneCardsiSATB1.
HGNCiHGNC:10541. SATB1.
HPAiCAB023814.
HPA051769.
MIMi602075. gene.
neXtProtiNX_Q01826.
OpenTargetsiENSG00000182568.
PharmGKBiPA34951.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000008096.
HOGENOMiHOG000004805.
HOVERGENiHBG054240.
InParanoidiQ01826.
OMAiSMNINAS.
OrthoDBiEOG091G02HV.
PhylomeDBiQ01826.
TreeFamiTF332714.

Enzyme and pathway databases

BioCyciZFISH:G66-33818-MONOMER.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
SIGNORiQ01826.

Miscellaneous databases

ChiTaRSiSATB1. human.
EvolutionaryTraceiQ01826.
GeneWikiiSATB1.
GenomeRNAii6304.
PMAP-CutDBQ01826.
PROiQ01826.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000182568.
CleanExiHS_SATB1.
ExpressionAtlasiQ01826. baseline and differential.
GenevisibleiQ01826. HS.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.260.40. 2 hits.
InterProiIPR003350. CUT_dom.
IPR032355. CUTL.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
IPR032392. ULD.
[Graphical view]
PfamiPF02376. CUT. 2 hits.
PF16557. CUTL. 1 hit.
PF00046. Homeobox. 1 hit.
PF16534. ULD. 1 hit.
[Graphical view]
SMARTiSM01109. CUT. 2 hits.
SM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 2 hits.
PROSITEiPS51042. CUT. 2 hits.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSATB1_HUMAN
AccessioniPrimary (citable) accession number: Q01826
Secondary accession number(s): B3KXF1, C9JTR6, Q59EQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 30, 2016
This is version 166 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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.