SubmitCancel

Skip Header

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

O60244

- MED14_HUMAN

UniProt

O60244 - MED14_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Mediator of RNA polymerase II transcription subunit 14

Gene
MED14, ARC150, CRSP2, CXorf4, DRIP150, EXLM1, RGR1, TRAP170
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  2. receptor activity Source: UniProtKB
  3. RNA polymerase II transcription cofactor activity Source: UniProtKB
  4. thyroid hormone receptor binding Source: UniProtKB
  5. transcription coactivator activity Source: MGI
  6. transcription cofactor activity Source: UniProtKB
  7. vitamin D receptor binding Source: UniProtKB

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. gene expression Source: Reactome
  3. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  6. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  7. stem cell maintenance Source: Ensembl
  8. transcription initiation from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_12627. Generic Transcription Pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiO60244.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MED14
Synonyms:ARC150, CRSP2, CXorf4, DRIP150, EXLM1, RGR1, TRAP170
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:2370. MED14.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. mediator complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26890.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14541454Mediator of RNA polymerase II transcription subunit 14PRO_0000079357Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei617 – 6171Phosphoserine2 Publications
Modified residuei986 – 9861Phosphoserine1 Publication
Modified residuei1112 – 11121Phosphoserine2 Publications
Modified residuei1119 – 11191Phosphoserine1 Publication
Modified residuei1128 – 11281Phosphoserine3 Publications
Modified residuei1136 – 11361Phosphoserine3 Publications
Modified residuei1144 – 11441Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60244.
PaxDbiO60244.
PRIDEiO60244.

PTM databases

PhosphoSiteiO60244.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiO60244.
BgeeiO60244.
CleanExiHS_MED14.
GenevestigatoriO60244.

Interactioni

Subunit structurei

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 STAT2.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005191EBI-394489,EBI-375543
FYNP062411EBI-394489,EBI-515315
GRB2P629931EBI-394489,EBI-401755
NCK1P163331EBI-394489,EBI-389883

Protein-protein interaction databases

BioGridi114699. 56 interactions.
DIPiDIP-31460N.
IntActiO60244. 19 interactions.
MINTiMINT-2796527.
STRINGi9606.ENSP00000323720.

Structurei

3D structure databases

ProteinModelPortaliO60244.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 566379Interaction with STAT2Add
BLAST
Regioni500 – 824325Interaction with SREBF1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi69 – 735LXXLL motif 1
Motifi1182 – 11865LXXLL motif 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1002 – 1165164Pro-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG281210.
HOGENOMiHOG000045361.
HOVERGENiHBG104308.
InParanoidiO60244.
KOiK15156.
OMAiKPLQISH.
OrthoDBiEOG7SR4KK.
PhylomeDBiO60244.
TreeFamiTF314388.

Family and domain databases

InterProiIPR013947. Mediator_Med14.
[Graphical view]
PfamiPF08638. Med14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60244-1 [UniParc]FASTAAdd to Basket

« Hide

MAPVQLENHQ LVPPGGGGGG SGGPPSAPAP PPPGAAVAAA AAAAASPGYR     50
LSTLIEFLLH RAYSELMVLT DLLPRKSDVE RKIEIVQFAS RTRQLFVRLL 100
ALVKWANNAG KVEKCAMISS FLDQQAILFV DTADRLASLA RDALVHARLP 150
SFAIPYAIDV LTTGSYPRLP TCIRDKIIPP DPITKIEKQA TLHQLNQILR 200
HRLVTTDLPP QLANLTVANG RVKFRVEGEF EATLTVMGDD PDVPWRLLKL 250
EILVEDKETG DGRALVHSMQ ISFIHQLVQS RLFADEKPLQ DMYNCLHSFC 300
LSLQLEVLHS QTLMLIRERW GDLVQVERYH AGKCLSLSVW NQQVLGRKTG 350
TASVHKVTIK IDENDVSKPL QIFHDPPLPA SDSKLVERAM KIDHLSIEKL 400
LIDSVHARAH QKLQELKAIL RGFNANENSS IETALPALVV PILEPCGNSE 450
CLHIFVDLHS GMFQLMLYGL DQATLDDMEK SVNDDMKRII PWIQQLKFWL 500
GQQRCKQSIK HLPTISSETL QLSNYSTHPI GNLSKNKLFI KLTRLPQYYI 550
VVEMLEVPNK PTQLSYKYYF MSVNAADRED SPAMALLLQQ FKENIQDLVF 600
RTKTGKQTRT NAKRKLSDDP CPVESKKTKR AGEMCAFNKV LAHFVAMCDT 650
NMPFVGLRLE LSNLEIPHQG VQVEGDGFSH AIRLLKIPPC KGITEETQKA 700
LDRSLLDCTF RLQGRNNRTW VAELVFANCP LNGTSTREQG PSRHVYLTYE 750
NLLSEPVGGR KVVEMFLNDW NSIARLYECV LEFARSLPDI PAHLNIFSEV 800
RVYNYRKLIL CYGTTKGSSI SIQWNSIHQK FHISLGTVGP NSGCSNCHNT 850
ILHQLQEMFN KTPNVVQLLQ VLFDTQAPLN AINKLPTVPM LGLTQRTNTA 900
YQCFSILPQS STHIRLAFRN MYCIDIYCRS RGVVAIRDGA YSLFDNSKLV 950
EGFYPAPGLK TFLNMFVDSN QDARRRSVNE DDNPPSPIGG DMMDSLISQL 1000
QPPPQQQPFP KQPGTSGAYP LTSPPTSYHS TVNQSPSMMH TQSPGNLHAA 1050
SSPSGALRAP SPASFVPTPP PSSHGISIGP GASFASPHGT LDPSSPYTMV 1100
SPSGRAGNWP GSPQVSGPSP AARMPGMSPA NPSLHSPVPD ASHSPRAGTS 1150
SQTMPTNMPP PRKLPQRSWA ASIPTILTHS ALNILLLPSP TPGLVPGLAG 1200
SYLCSPLERF LGSVIMRRHL QRIIQQETLQ LINSNEPGVI MFKTDALKCR 1250
VALSPKTNQT LQLKVTPENA GQWKPDELQV LEKFFETRVA GPPFKANTLI 1300
AFTKLLGAPT HILRDCVHIM KLELFPDQAT QLKWNVQFCL TIPPSAPPIA 1350
PPGTPAVVLK SKMLFFLQLT QKTSVPPQEP VSIIVPIIYD MASGTTQQAD 1400
IPRQQNSSVA APMMVSNILK RFAEMNPPRQ GECTIFAAVR DLMANLTLPP 1450
GGRP 1454
Length:1,454
Mass (Da):160,607
Last modified:April 17, 2007 - v2
Checksum:i144308E3F08D3D9B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1325 – 13251F → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036608

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3102HS → LT in AAD24360. 1 Publication
Sequence conflicti1265 – 12651V → L in BAA28626. 1 Publication
Sequence conflicti1265 – 12651V → L in AAD12725. 1 Publication
Sequence conflicti1265 – 12651V → L in AAG22547. 1 Publication
Sequence conflicti1451 – 14511G → V in BAA28626. 1 Publication
Sequence conflicti1451 – 14511G → V in AAD12725. 1 Publication
Sequence conflicti1451 – 14511G → V in AAG22547. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14254.1.
RefSeqiNP_004220.2. NM_004229.3.
UniGeneiHs.407604.

Genome annotation databases

EnsembliENST00000324817; ENSP00000323720; ENSG00000180182.
GeneIDi9282.
KEGGihsa:9282.
UCSCiuc004dex.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14254.1.
RefSeqi NP_004220.2. NM_004229.3.
UniGenei Hs.407604.

3D structure databases

ProteinModelPortali O60244.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114699. 56 interactions.
DIPi DIP-31460N.
IntActi O60244. 19 interactions.
MINTi MINT-2796527.
STRINGi 9606.ENSP00000323720.

PTM databases

PhosphoSitei O60244.

Proteomic databases

MaxQBi O60244.
PaxDbi O60244.
PRIDEi O60244.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324817 ; ENSP00000323720 ; ENSG00000180182 .
GeneIDi 9282.
KEGGi hsa:9282.
UCSCi uc004dex.4. human.

Organism-specific databases

CTDi 9282.
GeneCardsi GC0XM040507.
HGNCi HGNC:2370. MED14.
MIMi 300182. gene.
neXtProti NX_O60244.
PharmGKBi PA26890.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG281210.
HOGENOMi HOG000045361.
HOVERGENi HBG104308.
InParanoidi O60244.
KOi K15156.
OMAi KPLQISH.
OrthoDBi EOG7SR4KK.
PhylomeDBi O60244.
TreeFami TF314388.

Enzyme and pathway databases

Reactomei REACT_116145. PPARA activates gene expression.
REACT_12627. Generic Transcription Pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki O60244.

Miscellaneous databases

ChiTaRSi MED14. human.
GeneWikii MED14.
GenomeRNAii 9282.
NextBioi 34783.
PROi O60244.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60244.
Bgeei O60244.
CleanExi HS_MED14.
Genevestigatori O60244.

Family and domain databases

InterProi IPR013947. Mediator_Med14.
[Graphical view ]
Pfami PF08638. Med14. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "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.
  6. "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.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1128; SER-1136 AND SER-1144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617 AND SER-986, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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.
  20. "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.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-1325.

Entry informationi

Entry nameiMED14_HUMAN
AccessioniPrimary (citable) accession number: O60244
Secondary accession number(s): Q4KMR7, Q9UNB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: April 17, 2007
Last modified: September 3, 2014
This is version 131 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

External Data

Dasty 3

Similar proteinsi