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Q6PD62

- CTR9_HUMAN

UniProt

Q6PD62 - CTR9_HUMAN

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Protein

RNA polymerase-associated protein CTR9 homolog

Gene
CTR9, KIAA0155, SH2BP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 By similarity.7 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. cellular response to lipopolysaccharide Source: UniProtKB
  2. endodermal cell fate commitment Source: UniProtKB
  3. histone H2B ubiquitination Source: UniProtKB
  4. histone H3-K4 trimethylation Source: UniProtKB
  5. histone monoubiquitination Source: UniProtKB
  6. interleukin-6-mediated signaling pathway Source: UniProtKB
  7. JAK-STAT cascade Source: UniProtKB
  8. negative regulation of myeloid cell differentiation Source: UniProtKB
  9. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. positive regulation of histone H3-K4 methylation Source: UniProtKB
  11. positive regulation of histone H3-K79 methylation Source: UniProtKB
  12. positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  13. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  14. stem cell maintenance Source: UniProtKB
  15. transcription, DNA-templated Source: UniProtKB-KW
  16. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase-associated protein CTR9 homolog
Alternative name(s):
SH2 domain-binding protein 1
Gene namesi
Name:CTR9
Synonyms:KIAA0155, SH2BP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:16850. CTR9.

Subcellular locationi

Nucleus speckle By similarity
Note: Found in speckles By similarity.

GO - Cellular componenti

  1. Cdc73/Paf1 complex Source: UniProtKB
  2. nuclear speck Source: UniProtKB-SubCell
  3. transcriptionally active chromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134896774.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11731173RNA polymerase-associated protein CTR9 homologPRO_0000231588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei925 – 9251Phosphothreonine7 Publications
Modified residuei932 – 9321Phosphoserine1 Publication
Modified residuei941 – 9411Phosphoserine4 Publications
Modified residuei943 – 9431Phosphoserine4 Publications
Modified residuei970 – 9701Phosphoserine4 Publications
Modified residuei1020 – 10201Phosphoserine2 Publications
Modified residuei1021 – 10211Phosphoserine2 Publications
Modified residuei1097 – 10971Phosphoserine1 Publication
Modified residuei1102 – 11021Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6PD62.
PaxDbiQ6PD62.
PRIDEiQ6PD62.

PTM databases

PhosphoSiteiQ6PD62.

Miscellaneous databases

PMAP-CutDBQ6PD62.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ArrayExpressiQ6PD62.
BgeeiQ6PD62.
CleanExiHS_CTR9.
GenevestigatoriQ6PD62.

Interactioni

Subunit structurei

Component of the mammalian PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with KMT2A/MLL1. Interacts with STAT3 By similarity.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC73Q6P1J915EBI-1019583,EBI-930143
KMT2AQ031645EBI-1019583,EBI-591370
PAF1Q8N7H522EBI-1019583,EBI-2607770
WDR61Q9GZS39EBI-1019583,EBI-358545

Protein-protein interaction databases

BioGridi115004. 27 interactions.
DIPiDIP-31693N.
IntActiQ6PD62. 29 interactions.
MINTiMINT-1182366.
STRINGi9606.ENSP00000355013.

Structurei

3D structure databases

ProteinModelPortaliQ6PD62.
SMRiQ6PD62. Positions 265-749.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati41 – 7535TPR 1Add
BLAST
Repeati129 – 16234TPR 2Add
BLAST
Repeati163 – 19634TPR 3Add
BLAST
Repeati198 – 23134TPR 4Add
BLAST
Repeati235 – 26834TPR 5Add
BLAST
Repeati306 – 33934TPR 6Add
BLAST
Repeati341 – 37434TPR 7Add
BLAST
Repeati412 – 44433TPR 8Add
BLAST
Repeati451 – 48434TPR 9Add
BLAST
Repeati497 – 53034TPR 10Add
BLAST
Repeati531 – 56434TPR 11Add
BLAST
Repeati566 – 59833TPR 12Add
BLAST
Repeati613 – 64634TPR 13Add
BLAST
Repeati647 – 68034TPR 14Add
BLAST
Repeati681 – 71434TPR 15Add
BLAST
Repeati717 – 75034TPR 16Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi844 – 1011168Lys-richAdd
BLAST
Compositional biasi904 – 9085Poly-Gly
Compositional biasi933 – 9364Poly-Lys
Compositional biasi956 – 9594Poly-Lys
Compositional biasi1015 – 1172158Ser-richAdd
BLAST

Sequence similaritiesi

Contains 16 TPR repeats.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
HOGENOMiHOG000246926.
HOVERGENiHBG081372.
InParanoidiQ6PD62.
KOiK15176.
OMAiTQNDTYS.
OrthoDBiEOG79KPDH.
PhylomeDBiQ6PD62.
TreeFamiTF314342.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 7 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 9 hits.
[Graphical view]
PROSITEiPS50005. TPR. 10 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PD62-1 [UniParc]FASTAAdd to Basket

« Hide

MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE     50
YYKQGKTEEF VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE 100
KNKDNKKDLI TQATLLYTMA DKIIMYDQNH LLGRACFCLL EGDKMDQADA 150
QFHFVLNQSP NNIPALLGKA CISFNKKDYR GALAYYKKAL RTNPGCPAEV 200
RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV LELNNKEADS 250
IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE 300
VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM 350
YIYRGDKENA SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH 400
LKKVTEQYPD DVEAWIELAQ ILEQTDIQGA LSAYGTATRI LQEKVQADVP 450
PEILNNVGAL HFRLGNLGEA KKYFLASLDR AKAEAEHDEH YYNAISVTTS 500
YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM ARDKGNFYEA 550
SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPSTQSD 600
TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA 650
NGIGAVLAHK GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA 700
VQMYENCLRK FYKHQNTEVV LYLARALFKC GKLQECKQTL LKARHVAPSD 750
TVLMFNVALV LQRLATSVLK DEKSNLKEVL NAVKELELAH RYFSYLSKVG 800
DKMRFDLALA ATEARQCSDL LSQAQYHVAR ARKQDEEERE LRAKQEQEKE 850
LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE 900
KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP ISKKKKRRKG SGSEQEGEDE 950
EGGERKKKKR RRHPKGEEGS DDDETENGPK PKKRRPPKAE KKKAPKPERL 1000
PPSMKGKIKS KAIISSSDDS SDEDKLKIAD EGHPRNSNSN SDSDEDEQRK 1050
KCASSESDSD ENQNKSGSEA GSPRRPRRQR SDQDSDSDQP SRKRRPSGSE 1100
QSDNESVQSG RSHSGVSEND SRPASPSAES DHESERGSDN EGSGQGSGNE 1150
SEPEGSNNEA SDRGSEHGSD DSD 1173
Length:1,173
Mass (Da):133,502
Last modified:July 5, 2004 - v1
Checksum:i4B5AC22A5C5573C6
GO

Sequence cautioni

The sequence BAA09925.2 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63875 mRNA. Translation: BAA09925.2. Different initiation.
CH471064 Genomic DNA. Translation: EAW68557.1.
CH471064 Genomic DNA. Translation: EAW68558.1.
BC058914 mRNA. Translation: AAH58914.1.
CCDSiCCDS7805.1.
RefSeqiNP_055448.1. NM_014633.3.
UniGeneiHs.725151.

Genome annotation databases

EnsembliENST00000361367; ENSP00000355013; ENSG00000198730.
GeneIDi9646.
KEGGihsa:9646.
UCSCiuc001mja.3. human.

Polymorphism databases

DMDMi74758318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63875 mRNA. Translation: BAA09925.2 . Different initiation.
CH471064 Genomic DNA. Translation: EAW68557.1 .
CH471064 Genomic DNA. Translation: EAW68558.1 .
BC058914 mRNA. Translation: AAH58914.1 .
CCDSi CCDS7805.1.
RefSeqi NP_055448.1. NM_014633.3.
UniGenei Hs.725151.

3D structure databases

ProteinModelPortali Q6PD62.
SMRi Q6PD62. Positions 265-749.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115004. 27 interactions.
DIPi DIP-31693N.
IntActi Q6PD62. 29 interactions.
MINTi MINT-1182366.
STRINGi 9606.ENSP00000355013.

PTM databases

PhosphoSitei Q6PD62.

Polymorphism databases

DMDMi 74758318.

Proteomic databases

MaxQBi Q6PD62.
PaxDbi Q6PD62.
PRIDEi Q6PD62.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361367 ; ENSP00000355013 ; ENSG00000198730 .
GeneIDi 9646.
KEGGi hsa:9646.
UCSCi uc001mja.3. human.

Organism-specific databases

CTDi 9646.
GeneCardsi GC11P010772.
HGNCi HGNC:16850. CTR9.
MIMi 609366. gene.
neXtProti NX_Q6PD62.
PharmGKBi PA134896774.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0457.
HOGENOMi HOG000246926.
HOVERGENi HBG081372.
InParanoidi Q6PD62.
KOi K15176.
OMAi TQNDTYS.
OrthoDBi EOG79KPDH.
PhylomeDBi Q6PD62.
TreeFami TF314342.

Miscellaneous databases

ChiTaRSi CTR9. human.
GeneWikii CTR9.
GenomeRNAii 9646.
NextBioi 36207.
PMAP-CutDB Q6PD62.
PROi Q6PD62.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6PD62.
Bgeei Q6PD62.
CleanExi HS_CTR9.
Genevestigatori Q6PD62.

Family and domain databases

Gene3Di 1.25.40.10. 5 hits.
InterProi IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF00515. TPR_1. 7 hits.
PF07719. TPR_2. 1 hit.
[Graphical view ]
SMARTi SM00028. TPR. 9 hits.
[Graphical view ]
PROSITEi PS50005. TPR. 10 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
    Tissue: Bone marrow.
  2. Ohara O., Nagase T., Kikuno R., Nomura N.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. 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: Uterus.
  5. "The human PAF complex coordinates transcription with events downstream of RNA synthesis."
    Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K., Tempst P., Reinberg D.
    Genes Dev. 19:1668-1673(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE PAF1 COMPLEX.
  6. "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
    Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
    Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943 AND SER-970, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; SER-943; SER-1020 AND SER-1021, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  10. "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 THR-925, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-970, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: FUNCTION.
  14. "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles in RNA polymerase II elongation."
    Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M., Hisatake K., Handa H.
    Genes Dev. 23:2765-2777(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-932, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis."
    Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L.
    Cancer Cell 17:609-621(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH KMT2A.
  17. "The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS."
    Kim J., Guermah M., Roeder R.G.
    Cell 140:491-503(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX.
  18. "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 THR-925; SER-941; SER-943 AND SER-970, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Transcriptional activators enhance polyadenylation of mRNA precursors."
    Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M., Manley J.L.
    Mol. Cell 41:409-418(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FUNCTION OF THE PAF1 COMPLEX.
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943; SER-970; SER-1020; SER-1021; SER-1097 AND SER-1102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCTR9_HUMAN
AccessioniPrimary (citable) accession number: Q6PD62
Secondary accession number(s): D3DQV8, Q15015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 104 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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