Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UHV7 (MED13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of RNA polymerase II transcription subunit 13
Alternative name(s):
Activator-recruited cofactor 250 kDa component
Short name=ARC250
Mediator complex subunit 13
Thyroid hormone receptor-associated protein 1
Thyroid hormone receptor-associated protein complex 240 kDa component
Short name=Trap240
Vitamin D3 receptor-interacting protein complex component DRIP250
Short name=DRIP250
Gene names
Name:MED13
Synonyms:ARC250, KIAA0593, THRAP1, TRAP240
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2174 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.11

Subunit structure

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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous. Ref.1

Sequence similarities

Belongs to the Mediator complex subunit 13 family.

Sequence caution

The sequence AAD22032.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

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

Inferred from direct assay PubMed 12218053. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

intracellular steroid hormone receptor signaling pathway

Inferred from direct assay PubMed 11867769. 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 Ref.1. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 12218053. Source: UniProtKB

   Cellular_componentmediator complex

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

ligand-dependent nuclear receptor transcription coactivator activity

Non-traceable author statement Ref.7. Source: UniProtKB

receptor activity

Inferred from direct assay PubMed 12218053. Source: UniProtKB

thyroid hormone receptor binding

Inferred from direct assay Ref.1. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 12037571. Source: MGI

transcription cofactor activity

Inferred from direct assay PubMed 12218053. Source: UniProtKB

vitamin D receptor binding

Non-traceable author statement Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21742174Mediator of RNA polymerase II transcription subunit 13
PRO_0000065584

Regions

Motif1188 – 11925LXXLL motif 1
Motif1279 – 12835LXXLL motif 2
Compositional bias1508 – 157366Ser-rich

Amino acid modifications

Modified residue5001Phosphoserine Ref.12
Modified residue5041Phosphoserine Ref.13
Modified residue5371Phosphoserine Ref.13
Modified residue10291Phosphoserine Ref.12

Natural variations

Natural variant13701A → P.
Corresponds to variant rs34805963 [ dbSNP | Ensembl ].
VAR_057792
Natural variant13851A → P.
Corresponds to variant rs35996128 [ dbSNP | Ensembl ].
VAR_057793

Experimental info

Sequence conflict1061V → M in AAD22032. Ref.1
Sequence conflict3921R → K in AAD22032. Ref.1
Sequence conflict4671K → E in AAD22032. Ref.1
Sequence conflict7121K → A AA sequence Ref.1
Sequence conflict8001K → R in AAD22032. Ref.1
Sequence conflict9301P → L in AAD22032. Ref.1
Sequence conflict9841F → C in AAD22032. Ref.1
Sequence conflict10901F → S in AAD22032. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UHV7 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 0FA54C84FE2C91E2

FASTA2,174239,297
        10         20         30         40         50         60 
MSASFVPNGA SLEDCHCNLF CLADLTGIKW KKYVWQGPTS APILFPVTEE DPILSSFSRC 

        70         80         90        100        110        120 
LKADVLGVWR RDQRPGRREL WIFWWGEDPS FADLIHHDLS EEEDGVWENG LSYECRTLLF 

       130        140        150        160        170        180 
KAVHNLLERC LMNRNFVRIG KWFVKPYEKD EKPINKSEHL SCSFTFFLHG DSNVCTSVEI 

       190        200        210        220        230        240 
NQHQPVYLLS EEHITLAQQS NSPFQVILCP FGLNGTLTGQ AFKMSDSATK KLIGEWKQFY 

       250        260        270        280        290        300 
PISCCLKEMS EEKQEDMDWE DDSLAAVEVL VAGVRMIYPA CFVLVPQSDI PTPSPVGSTH 

       310        320        330        340        350        360 
CSSSCLGVHQ VPASTRDPAM SSVTLTPPTS PEEVQTVDPQ SVQKWVKFSS VSDGFNSDST 

       370        380        390        400        410        420 
SHHGGKIPRK LANHVVDRVW QECNMNRAQN KRKYSASSGG LCEEATAAKV ASWDFVEATQ 

       430        440        450        460        470        480 
RTNCSCLRHK NLKSRNAGQQ GQAPSLGQQQ QILPKHKTNE KQEKSEKPQK RPLTPFHHRV 

       490        500        510        520        530        540 
SVSDDVGMDA DSASQRLVIS APDSQVRFSN IRTNDVAKTP QMHGTEMANS PQPPPLSPHP 

       550        560        570        580        590        600 
CDVVDEGVTK TPSTPQSQHF YQMPTPDPLV PSKPMEDRID SLSQSFPPQY QEAVEPTVYV 

       610        620        630        640        650        660 
GTAVNLEEDE ANIAWKYYKF PKKKDVEFLP PQLPSDKFKD DPVGPFGQES VTSVTELMVQ 

       670        680        690        700        710        720 
CKKPLKVSDE LVQQYQIKNQ CLSAIASDAE QEPKIDPYAF VEGDEEFLFP DKKDRQNSER 

       730        740        750        760        770        780 
EAGKKHKVED GTSSVTVLSH EEDAMSLFSP SIKQDAPRPT SHARPPSTSL IYDSDLAVSY 

       790        800        810        820        830        840 
TDLDNLFNSD EDELTPGSKK SANGSDDKAS CKESKTGNLD PLSCISTADL HKMYPTPPSL 

       850        860        870        880        890        900 
EQHIMGFSPM NMNNKEYGSM DTTPGGTVLE GNSSSIGAQF KIEVDEGFCS PKPSEIKDFS 

       910        920        930        940        950        960 
YVYKPENCQI LVGCSMFAPL KTLPSQYLPP IKLPEECIYR QSWTVGKLEL LSSGPSMPFI 

       970        980        990       1000       1010       1020 
KEGDGSNMDQ EYGTAYTPQT HTSFGMPPSS APPSNSGAGI LPSPSTPRFP TPRTPRTPRT 

      1030       1040       1050       1060       1070       1080 
PRGAGGPASA QGSVKYENSD LYSPASTPST CRPLNSVEPA TVPSIPEAHS LYVNLILSES 

      1090       1100       1110       1120       1130       1140 
VMNLFKDCNF DSCCICVCNM NIKGADVGVY IPDPTQEAQY RCTCGFSAVM NRKFGNNSGL 

      1150       1160       1170       1180       1190       1200 
FLEDELDIIG RNTDCGKEAE KRFEALRATS AEHVNGGLKE SEKLSDDLIL LLQDQCTNLF 

      1210       1220       1230       1240       1250       1260 
SPFGAADQDP FPKSGVISNW VRVEERDCCN DCYLALEHGR QFMDNMSGGK VDEALVKSSC 

      1270       1280       1290       1300       1310       1320 
LHPWSKRNDV SMQCSQDILR MLLSLQPVLQ DAIQKKRTVR PWGVQGPLTW QQFHKMAGRG 

      1330       1340       1350       1360       1370       1380 
SYGTDESPEP LPIPTFLLGY DYDYLVLSPF ALPYWERLML EPYGSQRDIA YVVLCPENEA 

      1390       1400       1410       1420       1430       1440 
LLNGAKSFFR DLTAIYESCR LGQHRPVSRL LTDGIMRVGS TASKKLSEKL VAEWFSQAAD 

      1450       1460       1470       1480       1490       1500 
GNNEAFSKLK LYAQVCRYDL GPYLASLPLD SSLLSQPNLV APTSQSLITP PQMTNTGNAN 

      1510       1520       1530       1540       1550       1560 
TPSATLASAA SSTMTVTSGV AISTSVATAN STLTTASTSS SSSSNLNSGV SSNKLPSFPP 

      1570       1580       1590       1600       1610       1620 
FGSMNSNAAG SMSTQANTVQ SGQLGGQQTS ALQTAGISGE SSSLPTQPHP DVSESTMDRD 

      1630       1640       1650       1660       1670       1680 
KVGIPTDGDS HAVTYPPAIV VYIIDPFTYE NTDESTNSSS VWTLGLLRCF LEMVQTLPPH 

      1690       1700       1710       1720       1730       1740 
IKSTVSVQII PCQYLLQPVK HEDREIYPQH LKSLAFSAFT QCRRPLPTST NVKTLTGFGP 

      1750       1760       1770       1780       1790       1800 
GLAMETALRS PDRPECIRLY APPFILAPVK DKQTELGETF GEAGQKYNVL FVGYCLSHDQ 

      1810       1820       1830       1840       1850       1860 
RWILASCTDL YGELLETCII NIDVPNRARR KKSSARKFGL QKLWEWCLGL VQMSSLPWRV 

      1870       1880       1890       1900       1910       1920 
VIGRLGRIGH GELKDWSCLL SRRNLQSLSK RLKDMCRMCG ISAADSPSIL SACLVAMEPQ 

      1930       1940       1950       1960       1970       1980 
GSFVIMPDSV STGSVFGRST TLNMQTSQLN TPQDTSCTHI LVFPTSASVQ VASATYTTEN 

      1990       2000       2010       2020       2030       2040 
LDLAFNPNND GADGMGIFDL LDTGDDLDPD IINILPASPT GSPVHSPGSH YPHGGDAGKG 

      2050       2060       2070       2080       2090       2100 
QSTDRLLSTE PHEEVPNILQ QPLALGYFVS TAKAGPLPDW FWSACPQAQY QCPLFLKASL 

      2110       2120       2130       2140       2150       2160 
HLHVPSVQSD ELLHSKHSHP LDSNQTSDVL RFVLEQYNAL SWLTCDPATQ DRRSCLPIHF 

      2170 
VVLNQLYNFI MNML 

« Hide

References

« Hide 'large scale' references
[1]"Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators."
Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.-Y., Zhang X., Qin J., Roeder R.G.
Mol. Cell 3:361-370(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 696-713, TISSUE SPECIFICITY, IDENTIFICATION IN TRAP COMPLEX.
Tissue: Cervix carcinoma.
[2]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Brain.
[5]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-2174.
Tissue: Brain.
[6]Ohara O., Nagase T., Ishikawa K.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[7]"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: PROTEIN SEQUENCE OF 1401-1408 AND 1358-1367, IDENTIFICATION IN ARC COMPLEX.
Tissue: Cervix carcinoma.
[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: IDENTIFICATION IN ARC COMPLEX, PROTEIN SEQUENCE OF 1429-1438; 1772-1783 AND 2073-2084.
[9]"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, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[10]"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; MED18; MED21; MED28; MED29 AND MED30, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[11]"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.
[12]"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-500 AND SER-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-504 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF117754 mRNA. Translation: AAD22032.1. Frameshift.
AC008158 Genomic DNA. No translation available.
AC018628 Genomic DNA. No translation available.
AC060798 Genomic DNA. No translation available.
CH471179 Genomic DNA. Translation: EAW51438.1.
BC140891 mRNA. Translation: AAI40892.1.
AB011165 mRNA. Translation: BAA25519.2.
CCDSCCDS42366.1.
PIRT01238.
RefSeqNP_005112.2. NM_005121.2.
UniGeneHs.282678.

3D structure databases

ProteinModelPortalQ9UHV7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115294. 33 interactions.
DIPDIP-31468N.
IntActQ9UHV7. 14 interactions.
MINTMINT-4329245.
STRING9606.ENSP00000380888.

PTM databases

PhosphoSiteQ9UHV7.

Polymorphism databases

DMDM317373421.

Proteomic databases

MaxQBQ9UHV7.
PaxDbQ9UHV7.
PRIDEQ9UHV7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397786; ENSP00000380888; ENSG00000108510.
GeneID9969.
KEGGhsa:9969.
UCSCuc002izo.3. human.

Organism-specific databases

CTD9969.
GeneCardsGC17M060019.
H-InvDBHIX0014059.
HGNCHGNC:22474. MED13.
MIM603808. gene.
neXtProtNX_Q9UHV7.
PharmGKBPA162395168.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304462.
HOGENOMHOG000012893.
HOVERGENHBG058069.
KOK15164.
OMAFHHRVSV.
OrthoDBEOG73FQKS.
PhylomeDBQ9UHV7.
TreeFamTF316867.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9UHV7.
BgeeQ9UHV7.
CleanExHS_MED13.
GenevestigatorQ9UHV7.

Family and domain databases

InterProIPR009401. Mediator_Med13.
IPR021643. Mediator_Med13_N_met/fun.
[Graphical view]
PfamPF06333. Med13_C. 1 hit.
PF11597. Med13_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMED13. human.
GeneWikiMED13.
GenomeRNAi9969.
NextBio37622.
PROQ9UHV7.
SOURCESearch...

Entry information

Entry nameMED13_HUMAN
AccessionPrimary (citable) accession number: Q9UHV7
Secondary accession number(s): B2RU05, O60334
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 124 of the entry and version 3 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 17

Human chromosome 17: entries, gene names and cross-references to MIM