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O60244 (MED14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of RNA polymerase II transcription subunit 14
Alternative name(s):
Activator-recruited cofactor 150 kDa component
Short name=ARC150
Cofactor required for Sp1 transcriptional activation subunit 2
Short name=CRSP complex subunit 2
Mediator complex subunit 14
RGR1 homolog
Short name=hRGR1
Thyroid hormone receptor-associated protein complex 170 kDa component
Short name=Trap170
Transcriptional coactivator CRSP150
Vitamin D3 receptor-interacting protein complex 150 kDa component
Short name=DRIP150
Gene names
Name:MED14
Synonyms:ARC150, CRSP2, CXorf4, DRIP150, EXLM1, RGR1, TRAP170
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Ref.13 Ref.14 Ref.16

Subunit structure

Interacts with GATA1 By similarity. Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with AR, ESR1, SREBF1 and STAT2. Ref.3 Ref.4 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Nucleus Probable.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the Mediator complex subunit 14 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

intracellular steroid hormone receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12037571. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10198638. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentmediator complex

Inferred from direct assay PubMed 10198638. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionRNA polymerase II transcription cofactor activity

Inferred from direct assay PubMed 10198638. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Non-traceable author statement Ref.3. Source: UniProtKB

receptor activity

Inferred from direct assay Ref.9. Source: UniProtKB

thyroid hormone receptor binding

Inferred from direct assay PubMed 10198638. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 12037571. Source: MGI

transcription cofactor activity

Inferred from direct assay Ref.9. Source: UniProtKB

vitamin D receptor binding

Non-traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14541454Mediator of RNA polymerase II transcription subunit 14
PRO_0000079357

Regions

Region188 – 566379Interaction with STAT2
Region500 – 824325Interaction with SREBF1
Motif69 – 735LXXLL motif 1
Motif1182 – 11865LXXLL motif 2
Compositional bias1002 – 1165164Pro-rich

Amino acid modifications

Modified residue6171Phosphoserine Ref.17 Ref.19
Modified residue9861Phosphoserine Ref.19
Modified residue11121Phosphoserine Ref.20 Ref.21
Modified residue11191Phosphoserine Ref.21
Modified residue11281Phosphoserine Ref.18 Ref.20 Ref.21
Modified residue11361Phosphoserine Ref.18 Ref.20 Ref.21
Modified residue11441Phosphoserine Ref.18

Natural variations

Natural variant13251F → L in a breast cancer sample; somatic mutation. Ref.23
VAR_036608

Experimental info

Sequence conflict309 – 3102HS → LT in AAD24360. Ref.4
Sequence conflict12651V → L in BAA28626. Ref.1
Sequence conflict12651V → L in AAD12725. Ref.2
Sequence conflict12651V → L in AAG22547. Ref.3
Sequence conflict14511G → V in BAA28626. Ref.1
Sequence conflict14511G → V in AAD12725. Ref.2
Sequence conflict14511G → V in AAG22547. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O60244 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 144308E3F08D3D9B

FASTA1,454160,607
        10         20         30         40         50         60 
MAPVQLENHQ LVPPGGGGGG SGGPPSAPAP PPPGAAVAAA AAAAASPGYR LSTLIEFLLH 

        70         80         90        100        110        120 
RAYSELMVLT DLLPRKSDVE RKIEIVQFAS RTRQLFVRLL ALVKWANNAG KVEKCAMISS 

       130        140        150        160        170        180 
FLDQQAILFV DTADRLASLA RDALVHARLP SFAIPYAIDV LTTGSYPRLP TCIRDKIIPP 

       190        200        210        220        230        240 
DPITKIEKQA TLHQLNQILR HRLVTTDLPP QLANLTVANG RVKFRVEGEF EATLTVMGDD 

       250        260        270        280        290        300 
PDVPWRLLKL EILVEDKETG DGRALVHSMQ ISFIHQLVQS RLFADEKPLQ DMYNCLHSFC 

       310        320        330        340        350        360 
LSLQLEVLHS QTLMLIRERW GDLVQVERYH AGKCLSLSVW NQQVLGRKTG TASVHKVTIK 

       370        380        390        400        410        420 
IDENDVSKPL QIFHDPPLPA SDSKLVERAM KIDHLSIEKL LIDSVHARAH QKLQELKAIL 

       430        440        450        460        470        480 
RGFNANENSS IETALPALVV PILEPCGNSE CLHIFVDLHS GMFQLMLYGL DQATLDDMEK 

       490        500        510        520        530        540 
SVNDDMKRII PWIQQLKFWL GQQRCKQSIK HLPTISSETL QLSNYSTHPI GNLSKNKLFI 

       550        560        570        580        590        600 
KLTRLPQYYI VVEMLEVPNK PTQLSYKYYF MSVNAADRED SPAMALLLQQ FKENIQDLVF 

       610        620        630        640        650        660 
RTKTGKQTRT NAKRKLSDDP CPVESKKTKR AGEMCAFNKV LAHFVAMCDT NMPFVGLRLE 

       670        680        690        700        710        720 
LSNLEIPHQG VQVEGDGFSH AIRLLKIPPC KGITEETQKA LDRSLLDCTF RLQGRNNRTW 

       730        740        750        760        770        780 
VAELVFANCP LNGTSTREQG PSRHVYLTYE NLLSEPVGGR KVVEMFLNDW NSIARLYECV 

       790        800        810        820        830        840 
LEFARSLPDI PAHLNIFSEV RVYNYRKLIL CYGTTKGSSI SIQWNSIHQK FHISLGTVGP 

       850        860        870        880        890        900 
NSGCSNCHNT ILHQLQEMFN KTPNVVQLLQ VLFDTQAPLN AINKLPTVPM LGLTQRTNTA 

       910        920        930        940        950        960 
YQCFSILPQS STHIRLAFRN MYCIDIYCRS RGVVAIRDGA YSLFDNSKLV EGFYPAPGLK 

       970        980        990       1000       1010       1020 
TFLNMFVDSN QDARRRSVNE DDNPPSPIGG DMMDSLISQL QPPPQQQPFP KQPGTSGAYP 

      1030       1040       1050       1060       1070       1080 
LTSPPTSYHS TVNQSPSMMH TQSPGNLHAA SSPSGALRAP SPASFVPTPP PSSHGISIGP 

      1090       1100       1110       1120       1130       1140 
GASFASPHGT LDPSSPYTMV SPSGRAGNWP GSPQVSGPSP AARMPGMSPA NPSLHSPVPD 

      1150       1160       1170       1180       1190       1200 
ASHSPRAGTS SQTMPTNMPP PRKLPQRSWA ASIPTILTHS ALNILLLPSP TPGLVPGLAG 

      1210       1220       1230       1240       1250       1260 
SYLCSPLERF LGSVIMRRHL QRIIQQETLQ LINSNEPGVI MFKTDALKCR VALSPKTNQT 

      1270       1280       1290       1300       1310       1320 
LQLKVTPENA GQWKPDELQV LEKFFETRVA GPPFKANTLI AFTKLLGAPT HILRDCVHIM 

      1330       1340       1350       1360       1370       1380 
KLELFPDQAT QLKWNVQFCL TIPPSAPPIA PPGTPAVVLK SKMLFFLQLT QKTSVPPQEP 

      1390       1400       1410       1420       1430       1440 
VSIIVPIIYD MASGTTQQAD IPRQQNSSVA APMMVSNILK RFAEMNPPRQ GECTIFAAVR 

      1450 
DLMANLTLPP GGRP 

« Hide

References

« Hide 'large scale' references
[1]"Detection and isolation of a novel human gene located on Xp11.2-p11.4 that escapes X-inactivation using a two-dimensional DNA mapping method."
Yoshikawa H., Fujiyama A., Nakai K., Inazawa J., Matsubara K.
Genomics 49:237-246(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1."
Ryu S., Zhou S., Ladurner A.G., Tjian R.
Nature 397:446-450(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex."
Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M., Erdjument-Bromage H., Tempst P., Freedman L.P.
Nature 398:824-828(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 250-263 AND 1106-1146, IDENTIFICATION IN ARC COMPLEX.
Tissue: Cervix carcinoma.
[4]"A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation."
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G.
Mol. Cell 3:97-108(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SMCC COMPLEX.
[5]Erratum
Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G.
Mol. Cell 3:541-541(1999)
[6]"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: Placenta.
[7]"NAT, a human complex containing Srb polypeptides that functions as a negative regulator of activated transcription."
Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.
Mol. Cell 2:213-222(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A FORM OF THE MEDIATOR COMPLEX.
[8]"Composite co-activator ARC mediates chromatin-directed transcriptional activation."
Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.
Nature 398:828-832(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 4-13 AND 1256-1264, IDENTIFICATION IN ARC COMPLEX.
[9]"A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression."
Wang Q., Sharma D., Ren Y., Fondell J.D.
J. Biol. Chem. 277:42852-42858(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AR.
[10]"The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro."
Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
[11]"Role of metazoan mediator proteins in interferon-responsive transcription."
Lau J.F., Nusinzon I., Burakov D., Freedman L.P., Horvath C.M.
Mol. Cell. Biol. 23:620-628(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STAT2.
[12]"A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology."
Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B., Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W., Conaway R.C.
Mol. Cell 14:685-691(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX.
[13]"Selective coactivator interactions in gene activation by SREBP-1a and -1c."
Toth J.I., Datta S., Athanikar J.N., Freedman L.P., Osborne T.F.
Mol. Cell. Biol. 24:8288-8300(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SREBF1.
[14]"DRIP150 coactivation of estrogen receptor alpha in ZR-75 breast cancer cells is independent of LXXLL motifs."
Lee J.E., Kim K., Sacchettini J.C., Smith C.V., Safe S.
J. Biol. Chem. 280:8819-8830(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ESR1.
[15]"MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription."
Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T., Roeder R.G.
Mol. Cell 19:89-100(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MED1 AND MED10, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[16]"Human Mediator enhances basal transcription by facilitating recruitment of transcription factor IIB during preinitiation complex assembly."
Baek H.J., Kang Y.K., Roeder R.G.
J. Biol. Chem. 281:15172-15181(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MED1 AND MED10.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1128; SER-1136 AND SER-1144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617 AND SER-986, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-1112; SER-1128 AND SER-1136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"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-1112; SER-1119; SER-1128 AND SER-1136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-1325.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB006651 mRNA. Translation: BAA28626.1.
AB006652 Genomic DNA. Translation: BAA28627.1.
AF104256 mRNA. Translation: AAD12725.1.
AF304448 mRNA. Translation: AAG22547.1.
AF135802 mRNA. Translation: AAD24360.1.
BC098377 mRNA. Translation: AAH98377.1.
BC132672 mRNA. Translation: AAI32673.1.
BC132674 mRNA. Translation: AAI32675.1.
RefSeqNP_004220.2. NM_004229.3.
UniGeneHs.407604.

3D structure databases

ProteinModelPortalO60244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114699. 56 interactions.
DIPDIP-31460N.
IntActO60244. 18 interactions.
MINTMINT-2796527.
STRING9606.ENSP00000323720.

PTM databases

PhosphoSiteO60244.

Proteomic databases

PaxDbO60244.
PRIDEO60244.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324817; ENSP00000323720; ENSG00000180182.
GeneID9282.
KEGGhsa:9282.
UCSCuc004dex.4. human.

Organism-specific databases

CTD9282.
GeneCardsGC0XM040507.
HGNCHGNC:2370. MED14.
MIM300182. gene.
neXtProtNX_O60244.
PharmGKBPA26890.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281210.
HOGENOMHOG000045361.
HOVERGENHBG104308.
InParanoidO60244.
KOK15156.
OMASTHPIGN.
OrthoDBEOG7SR4KK.
PhylomeDBO60244.
TreeFamTF314388.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_71. Gene Expression.
SignaLinkO60244.

Gene expression databases

ArrayExpressO60244.
BgeeO60244.
CleanExHS_MED14.
GenevestigatorO60244.

Family and domain databases

InterProIPR013947. Mediator_Med14.
[Graphical view]
PfamPF08638. Med14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMED14. human.
GeneWikiMED14.
GenomeRNAi9282.
NextBio34783.
PROO60244.
SOURCESearch...

Entry information

Entry nameMED14_HUMAN
AccessionPrimary (citable) accession number: O60244
Secondary accession number(s): Q4KMR7, Q9UNB3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: April 17, 2007
Last modified: April 16, 2014
This is version 128 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

SIMILARITY comments

Index of protein domains and families

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 X

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