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P48552 (NRIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor-interacting protein 1
Alternative name(s):
Nuclear factor RIP140
Receptor-interacting protein 140
Gene names
Name:NRIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1158 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors. Ref.1 Ref.5 Ref.6 Ref.8 Ref.10 Ref.12

Subunit structure

Interacts with RARA and RXRB homodimers and RARA/RXRB heterodimers in the presence of ligand. Interacts with HDAC1 and HDAC3 via its N-terminal domain. Interacts with NR2C1 (sumoylated form and via the ligand-binding domain); the interaction results in promoting the repressor activity of NR2C1 By similarity. Interacts with CTBP1, CTBP2, ESR1, HDAC1, HDAC2, HDAC5, HDAC6, NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with both NR3C1 and YWHAH. Interacts with ZNF366. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Nucleus. Note: Localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1. Ref.1 Ref.7 Ref.9 Ref.12

Domain

Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have different affinities for nuclear receptors. The C-terminal LTKTNPILYYMLQK motif is required for ligand-dependent interaction with RAAR and RXRB homodimers and heterodimers, for the corepressor activity, and for the formation of an HDAC3 complex with RARA/RXRB By similarity. Contains at least four autonomous repression domains (RD1-4). RD1 functions via a histone deacetylase (HDAC)-independent mechanism, whereas RD2, RD3 and RD4 can function by HDAC-dependent or independent mechanisms, depending on cell type. RD2 is dependent on CTBP binding. Ref.11

Post-translational modification

Acetylation regulates its nuclear translocation and corepressive activity By similarity. Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH. Ref.6

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

lipid storage

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.5. Source: UniProtKB

ovarian follicle rupture

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.5Ref.1. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

histone deacetylase complex

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.7Ref.9Ref.1. Source: UniProtKB

   Molecular_functionandrogen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

estrogen receptor binding

Inferred from physical interaction Ref.1. Source: UniProtKB

glucocorticoid receptor binding

Inferred from physical interaction Ref.5Ref.7Ref.9. Source: UniProtKB

nuclear hormone receptor binding

Inferred from physical interaction Ref.8. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.5Ref.8Ref.1. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11581158Nuclear receptor-interacting protein 1
PRO_0000057951

Regions

Region1 – 415415Interaction with ZNF366
Region78 – 333256Repression domain 1
Region410 – 700291Repression domain 2
Region431 – 47242Required for targeting to small nuclear foci
Region735 – 885151Repression domain 3
Region753 – 1158406Interaction with ZNF366
Region1118 – 115841Repression domain 4
Motif21 – 255LXXLL motif 1
Motif133 – 1375LXXLL motif 2
Motif185 – 1895LXXLL motif 3
Motif266 – 2705LXXLL motif 4
Motif380 – 3845LXXLL motif 5
Motif440 – 4467CTBP-binding; principal site
Motif500 – 5045LXXLL motif 6
Motif565 – 5695CTBP-binding
Motif599 – 6035CTBP-binding Potential
Motif713 – 7175LXXLL motif 7
Motif819 – 8235LXXLL motif 8
Motif936 – 9405LXXLL motif 9
Motif946 – 9505CTBP-binding
Motif1061 – 107414Ligand-dependent nuclear receptor binding By similarity

Amino acid modifications

Modified residue1041Phosphoserine By similarity
Modified residue1111N6-acetyllysine By similarity
Modified residue1581N6-acetyllysine By similarity
Modified residue2071Phosphothreonine By similarity
Modified residue2861N6-acetyllysine By similarity
Modified residue3101N6-acetyllysine By similarity
Modified residue3561Phosphoserine By similarity
Modified residue3781Phosphoserine By similarity
Modified residue4461N6-acetyllysine Ref.6
Modified residue4811N6-acetyllysine By similarity
Modified residue4871Phosphoserine By similarity
Modified residue5181Phosphoserine By similarity
Modified residue5281N6-acetyllysine By similarity
Modified residue5421Phosphoserine By similarity
Modified residue6061N6-acetyllysine By similarity
Modified residue6711Phosphoserine By similarity
Modified residue9311N6-acetyllysine By similarity
Modified residue10011Phosphoserine By similarity

Natural variations

Natural variant371V → I.
Corresponds to variant rs9941840 [ dbSNP | Ensembl ].
VAR_051241
Natural variant2211H → R. Ref.16
Corresponds to variant rs139263261 [ dbSNP | Ensembl ].
VAR_023706
Natural variant3151Y → F.
Corresponds to variant rs2228507 [ dbSNP | Ensembl ].
VAR_034142
Natural variant4411I → V. Ref.16
Corresponds to variant rs150468995 [ dbSNP | Ensembl ].
VAR_023707
Natural variant4481R → G Common polymorphism. Ref.1 Ref.16
Corresponds to variant rs2229742 [ dbSNP | Ensembl ].
VAR_023708
Natural variant5671N → S.
Corresponds to variant rs9975169 [ dbSNP | Ensembl ].
VAR_051242
Natural variant8031S → L. Ref.16
Corresponds to variant rs61750208 [ dbSNP | Ensembl ].
VAR_023709
Natural variant10791V → F. Ref.16
VAR_023710

Experimental info

Mutagenesis440 – 4434PIDL → AAAA: Abolishes interaction with CTBP1. Ref.6
Mutagenesis440 – 4423PID → AIA: Abolishes interaction with CTBP1 and attenuates nuclear hormone receptor-dependent transcription repression.
Mutagenesis442 – 4432DL → AA: Reduces, but does not completely abolish, interaction with CTBP. Reduces transcriptional repression. Ref.12
Mutagenesis442 – 4432DL → AS: Disrupts interaction with CTBP1, and CTBP2 to a lesser extent. Disrupts transcriptional repression; when associated with 567-AS-568. Ref.12
Mutagenesis4461K → Q: Disrupts interaction with CTBP1. Decreases lysine acetylation. Disrupts nuclear hormone receptor-dependent transcription repression. Ref.6
Mutagenesis4461K → R: Does not disrupt nuclear hormone receptor-dependent transcription repression. Ref.6
Mutagenesis567 – 5682NL → AA: Disrupts transcriptional repression. Ref.11 Ref.12
Mutagenesis567 – 5682NL → AS: Disrupts interaction with CTBP1 and CTBP2. Disrupts transcriptional repression; when associated with 442-AS-443. Ref.11 Ref.12
Mutagenesis599 – 6035SMDLT → PIAAS: Does not further disrupt transcriptional repression; when associated with 442-AA-443 and 567-AA-568.
Mutagenesis948 – 9492DL → AA: Abolishes CTBP binding but retains transcriptional repressor activity. Ref.11
Sequence conflict1241P → R in CAA59108. Ref.1
Sequence conflict721 – 7266NKGKSE → TKGRVK in CAA59108. Ref.1
Sequence conflict9541S → I in AAH40361. Ref.3
Sequence conflict10801T → A in CAA59108. Ref.1

Secondary structure

... 1158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48552 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 81FC424968E9A5F6

FASTA1,158126,942
        10         20         30         40         50         60 
MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAVDKK SAGHNEEDQN FNISGSAFPT 

        70         80         90        100        110        120 
CQSNGPVLNT HTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIMNLNV KKEALLAGMV 

       130        140        150        160        170        180 
DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHDSLK VEKDLRCYGV 

       190        200        210        220        230        240 
ASSHLKTLLK KSKVKDQKPD TNLPDVTKNL IRDRFAESPH HVGQSGTKVM SEPLSCAARL 

       250        260        270        280        290        300 
QAVASMVEKR ASPATSPKPS VACSQLALLL SSEAHLQQYS REHALKTQNA NQAASERLAA 

       310        320        330        340        350        360 
MARLQENGQK DVGSYQLPKG MSSHLNGQAR TSSSKLMASK SSATVFQNPM GIIPSSPKNA 

       370        380        390        400        410        420 
GYKNSLERNN IKQAANNSLL LHLLKSQTIP KPMNGHSHSE RGSIFEESST PTTIDEYSDN 

       430        440        450        460        470        480 
NPSFTDDSSG DESSYSNCVP IDLSCKHRTE KSESDQPVSL DNFTQSLLNT WDPKVPDVDI 

       490        500        510        520        530        540 
KEDQDTSKNS KLNSHQKVTL LQLLLGHKNE ENVEKNTSPQ GVHNDVSKFN TQNYARTSVI 

       550        560        570        580        590        600 
ESPSTNRTTP VSTPPLLTSS KAGSPINLSQ HSLVIKWNSP PYVCSTQSEK LTNTASNHSM 

       610        620        630        640        650        660 
DLTKSKDPPG EKPAQNEGAQ NSATFSASKL LQNLAQCGMQ SSMSVEEQRP SKQLLTGNTD 

       670        680        690        700        710        720 
KPIGMIDRLN SPLLSNKTNA VEENKAFSSQ PTGPEPGLSG SEIENLLERR TVLQLLLGNP 

       730        740        750        760        770        780 
NKGKSEKKEK TPLRDESTQE HSERALSEQI LMVKIKSEPC DDLQIPNTNV HLSHDAKSAP 

       790        800        810        820        830        840 
FLGMAPAVQR SAPALPVSED FKSEPVSPQD FSFSKNGLLS RLLRQNQDSY LADDSDRSHR 

       850        860        870        880        890        900 
NNEMALLESK NLCMVPKKRK LYTEPLENPF KKMKNNIVDA ANNHSAPEVL YGSLLNQEEL 

       910        920        930        940        950        960 
KFSRNDLEFK YPAGHGSASE SEHRSWARES KSFNVLKQLL LSENCVRDLS PHRSNSVADS 

       970        980        990       1000       1010       1020 
KKKGHKNNVT NSKPEFSISS LNGLMYSSTQ PSSCMDNRTF SYPGVVKTPV SPTFPEHLGC 

      1030       1040       1050       1060       1070       1080 
AGSRPESGLL NGCSMPSEKG PIKWVITDAE KNEYEKDSPR LTKTNPILYY MLQKGGNSVT 

      1090       1100       1110       1120       1130       1140 
SRETQDKDIW REASSAESVS QVTAKEELLP TAETKASFFN LRSPYNSHMG NNASRPHSAN 

      1150 
GEVYGLLGSV LTIKKESE 

« Hide

References

« Hide 'large scale' references
[1]"Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor."
Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S., Kushner P.J., Parker M.G.
EMBO J. 14:3741-3751(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR LOCATION, VARIANT GLY-448.
Tissue: Mammary gland.
[2]"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. expand/collapse author list , 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].
[3]"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: Skin.
[4]"Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4."
Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., Jetten A.M.
J. Biol. Chem. 273:10948-10957(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C2.
[5]"Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids."
Subramaniam N., Treuter E., Okret S.
J. Biol. Chem. 274:18121-18127(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NR3C1.
[6]"Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP."
Vo N., Fjeld C., Goodman R.H.
Mol. Cell. Biol. 21:6181-6188(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTBP1, MUTAGENESIS OF 440-PRO--LEU-443 AND LYS-446, ACETYLATION AT LYS-446.
[7]"Regulation of glucocorticoid receptor activity by 14-3-3-dependent intracellular relocalization of the corepressor RIP140."
Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.
Mol. Endocrinol. 15:501-511(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR3C1 AND YWHAH, IDENTIFICATION IN A COMPLEX WITH NR3C1 AND YWHAH, SUBCELLULAR LOCATION.
[8]"A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action."
Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.
Mol. Endocrinol. 15:1586-1598(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NR3C2.
[9]"Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140."
Tazawa H., Osman W., Shoji Y., Treuter E., Gustafsson J.-A., Zilliacus J.
Mol. Cell. Biol. 23:4187-4198(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
[10]"Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-induced activator protein-1 activity by reversing glucocorticoid receptor-interacting protein 1 effect."
Teyssier C., Belguise K., Galtier F., Cavailles V., Chalbos D.
Mol. Endocrinol. 17:287-299(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ESR1; FOS AND JUN.
[11]"Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140."
Christian M., Tullet J.M.A., Parker M.G.
J. Biol. Chem. 279:15645-15651(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF 442-ASP--LEU-443; 567-ASN--LEU-568 AND 948-ASP--LEU-949, IDENTIFICATION OF REPRESSION DOMAINS.
[12]"Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition."
Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V.
Nucleic Acids Res. 32:1957-1966(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTBP1; CTBP2; HDAC1; HDAC2; HDAC5 AND HDAC6, MUTAGENESIS OF 442-ASP--LEU-443 AND 567-ASN--LEU-568, SUBCELLULAR LOCATION.
[13]"Modulation of testicular receptor 4 activity by mitogen-activated protein kinase-mediated phosphorylation."
Huq M.D., Gupta P., Tsai N.P., Wei L.N.
Mol. Cell. Proteomics 5:2072-2082(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C2.
[14]"ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylases."
Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.
Nucleic Acids Res. 34:6126-6136(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF366.
[15]"X-ray crystal structures of the estrogen-related receptor-gamma ligand binding domain in three functional states reveal the molecular basis of small molecule regulation."
Wang L., Zuercher W.J., Consler T.G., Lambert M.H., Miller A.B., Orband-Miller L.A., McKee D.D., Willson T.M., Nolte R.T.
J. Biol. Chem. 281:37773-37781(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 366-390 IN COMPLEX WITH ESRRG.
[16]"Preliminary molecular genetic analysis of the receptor interacting protein 140 (RIP140) in women affected by endometriosis."
Caballero V., Ruiz R., Sainz J.A., Cruz M., Lopez-Nevot M.A., Galan J.J., Real L.M., de Castro F., Lopez-Villaverde V., Ruiz A.
J. Exp. Clin. Assist. Reprod. 2:11-11(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-221; VAL-441; GLY-448; LEU-803 AND PHE-1079.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84373 mRNA. Translation: CAA59108.1.
AF248484 Genomic DNA. Translation: AAF62185.1.
AF127577 Genomic DNA. Translation: AAF35255.1.
AL163207 Genomic DNA. Translation: CAB90396.1.
BC040361 mRNA. Translation: AAH40361.1.
PIRS57348.
RefSeqNP_003480.2. NM_003489.3.
XP_005261120.1. XM_005261063.1.
XP_005261122.1. XM_005261065.1.
XP_005261123.1. XM_005261066.1.
UniGeneHs.155017.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GPOX-ray1.95C366-390[»]
2GPPX-ray2.60C/D366-390[»]
ProteinModelPortalP48552.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113843. 54 interactions.
DIPDIP-5964N.
IntActP48552. 21 interactions.
MINTMINT-192711.
STRING9606.ENSP00000327213.

PTM databases

PhosphoSiteP48552.

Polymorphism databases

DMDM9988061.

Proteomic databases

PaxDbP48552.
PRIDEP48552.

Protocols and materials databases

DNASU8204.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318948; ENSP00000327213; ENSG00000180530.
ENST00000400199; ENSP00000383060; ENSG00000180530.
ENST00000400202; ENSP00000383063; ENSG00000180530.
GeneID8204.
KEGGhsa:8204.
UCSCuc002yjx.2. human.

Organism-specific databases

CTD8204.
GeneCardsGC21M016333.
H-InvDBHIX0027827.
HGNCHGNC:8001. NRIP1.
HPAHPA046571.
MIM602490. gene.
neXtProtNX_P48552.
PharmGKBPA31780.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47583.
HOGENOMHOG000236277.
HOVERGENHBG052667.
InParanoidP48552.
KOK17965.
OMAEPLSCAA.
OrthoDBEOG7H1JJQ.
PhylomeDBP48552.
TreeFamTF332210.

Enzyme and pathway databases

SignaLinkP48552.

Gene expression databases

ArrayExpressP48552.
BgeeP48552.
CleanExHS_NRIP1.
GenevestigatorP48552.

Family and domain databases

InterProIPR026649. NRIP1.
[Graphical view]
PANTHERPTHR15088. PTHR15088. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP48552.
GeneWikiNRIP1.
GenomeRNAi8204.
NextBio30914.
PROP48552.
SOURCESearch...

Entry information

Entry nameNRIP1_HUMAN
AccessionPrimary (citable) accession number: P48552
Secondary accession number(s): Q8IWE8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

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