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O94776

- MTA2_HUMAN

UniProt

O94776 - MTA2_HUMAN

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Protein

Metastasis-associated protein MTA2

Gene

MTA2

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

Functioni

May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri367 – 39428GATA-type; atypicalAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. histone deacetylase activity Source: Ensembl
  3. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  4. RNA polymerase II transcription factor binding Source: BHF-UCL
  5. sequence-specific DNA binding Source: InterPro
  6. sequence-specific DNA binding transcription factor activity Source: InterPro
  7. transcription factor binding transcription factor activity Source: Ensembl
  8. transcription regulatory region DNA binding Source: Ensembl
  9. zinc ion binding Source: InterPro

GO - Biological processi

  1. ATP-dependent chromatin remodeling Source: UniProt
  2. chromatin assembly or disassembly Source: ProtInc
  3. DNA methylation Source: Ensembl
  4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_953. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Metastasis-associated protein MTA2
Alternative name(s):
Metastasis-associated 1-like 1
Short name:
MTA1-L1 protein
p53 target protein in deacetylase complex
Gene namesi
Name:MTA2
Synonyms:MTA1L1, PID
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:7411. MTA2.

Subcellular locationi

Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. histone deacetylase complex Source: ProtInc
  2. membrane Source: UniProtKB
  3. nuclear chromatin Source: UniProt
  4. nucleus Source: HPA
  5. NuRD complex Source: UniProtKB
  6. protein complex Source: UniProt
  7. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31219.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668Metastasis-associated protein MTA2PRO_0000083496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei152 – 1521N6-acetyllysine1 Publication
Modified residuei433 – 4331Phosphoserine1 Publication
Modified residuei435 – 4351Phosphoserine3 Publications
Modified residuei460 – 4601N6-acetyllysineBy similarity
Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)Curated
Modified residuei522 – 5221N6-acetyllysineBy similarity
Modified residuei531 – 5311N6-acetyllysineBy similarity
Modified residuei534 – 5341Phosphothreonine1 Publication
Modified residuei548 – 5481Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO94776.
PaxDbiO94776.
PeptideAtlasiO94776.
PRIDEiO94776.

PTM databases

PhosphoSiteiO94776.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiO94776.
CleanExiHS_MTA2.
ExpressionAtlasiO94776. baseline and differential.
GenevestigatoriO94776.

Organism-specific databases

HPAiCAB005315.
CAB017522.
HPA006214.

Interactioni

Subunit structurei

Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC7, p53/TP53, MINT and MBD3 By similarity. Interacts with FAM64A. Interacts with NACC2.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033723EBI-1783035,EBI-78473
PARK7Q994973EBI-1783035,EBI-1164361

Protein-protein interaction databases

BioGridi114652. 101 interactions.
DIPiDIP-46519N.
IntActiO94776. 29 interactions.
STRINGi9606.ENSP00000278823.

Structurei

3D structure databases

ProteinModelPortaliO94776.
SMRiO94776. Positions 145-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 144144BAHPROSITE-ProRule annotationAdd
BLAST
Domaini145 – 256112ELM2PROSITE-ProRule annotationAdd
BLAST
Domaini263 – 31553SANTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BAH domain.PROSITE-ProRule annotation
Contains 1 ELM2 domain.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.Curated
Contains 1 SANT domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri367 – 39428GATA-type; atypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG252834.
GeneTreeiENSGT00580000081398.
HOGENOMiHOG000045387.
HOVERGENiHBG002598.
InParanoidiO94776.
KOiK11660.
OMAiNAVKAEC.
OrthoDBiEOG780RM1.
PhylomeDBiO94776.
TreeFamiTF106444.

Family and domain databases

InterProiIPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]
PfamiPF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O94776-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD
60 70 80 90 100
ISSSLNSLAD SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT
110 120 130 140 150
HIRGKCSVTL LNETDILSQY LEKEDCFFYS LVFDPVQKTL LADQGEIRVG
160 170 180 190 200
CKYQAEIPDR LVEGESDNRN QQKMEMKVWD PDNPLTDRQI DQFLVVARAV
210 220 230 240 250
GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR NGYDLAKAMS
260 270 280 290 300
TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL
310 320 330 340 350
ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV
360 370 380 390 400
GSKPGMNGAG FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK
410 420 430 440 450
YGGLKTPTQL EGATRGTTEP HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN
460 470 480 490 500
RQTFLLQTTK LTRLARRMCR DLLQPRRAAR RPYAPINANA IKAECSIRLP
510 520 530 540 550
KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT PINRNQLSQN
560 570 580 590 600
RGLGGIMVKR AYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD
610 620 630 640 650
APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLIAVRPPVP
660
LPAPSHPAST NEPIVLED
Length:668
Mass (Da):75,023
Last modified:May 1, 1999 - v1
Checksum:i65087AF798BA64EC
GO
Isoform 2 (identifier: O94776-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-173: Missing.

Note: No experimental confirmation available.

Show »
Length:495
Mass (Da):55,037
Checksum:iF6072C422C0F80C6
GO

Sequence cautioni

The sequence AAH23656.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751V → M in BAA36707. (PubMed:9929979)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 173173Missing in isoform 2. 2 PublicationsVSP_055083Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB012922 Genomic DNA. Translation: BAA36562.1.
AB016591 mRNA. Translation: BAA36707.1.
AF295807 mRNA. Translation: AAG02241.1.
AK301569 mRNA. Translation: BAG63063.1.
CR749481 mRNA. Translation: CAH18309.1.
AP001458 Genomic DNA. No translation available.
BC023656 mRNA. Translation: AAH23656.1. Sequence problems.
BC053650 mRNA. Translation: AAH53650.1.
CCDSiCCDS8022.1. [O94776-1]
RefSeqiNP_004730.2. NM_004739.3. [O94776-1]
UniGeneiHs.173043.

Genome annotation databases

EnsembliENST00000278823; ENSP00000278823; ENSG00000149480. [O94776-1]
ENST00000524902; ENSP00000431346; ENSG00000149480. [O94776-2]
ENST00000527204; ENSP00000431797; ENSG00000149480. [O94776-2]
GeneIDi9219.
KEGGihsa:9219.
UCSCiuc001ntq.2. human. [O94776-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB012922 Genomic DNA. Translation: BAA36562.1 .
AB016591 mRNA. Translation: BAA36707.1 .
AF295807 mRNA. Translation: AAG02241.1 .
AK301569 mRNA. Translation: BAG63063.1 .
CR749481 mRNA. Translation: CAH18309.1 .
AP001458 Genomic DNA. No translation available.
BC023656 mRNA. Translation: AAH23656.1 . Sequence problems.
BC053650 mRNA. Translation: AAH53650.1 .
CCDSi CCDS8022.1. [O94776-1 ]
RefSeqi NP_004730.2. NM_004739.3. [O94776-1 ]
UniGenei Hs.173043.

3D structure databases

ProteinModelPortali O94776.
SMRi O94776. Positions 145-321.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114652. 101 interactions.
DIPi DIP-46519N.
IntActi O94776. 29 interactions.
STRINGi 9606.ENSP00000278823.

PTM databases

PhosphoSitei O94776.

Proteomic databases

MaxQBi O94776.
PaxDbi O94776.
PeptideAtlasi O94776.
PRIDEi O94776.

Protocols and materials databases

DNASUi 9219.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278823 ; ENSP00000278823 ; ENSG00000149480 . [O94776-1 ]
ENST00000524902 ; ENSP00000431346 ; ENSG00000149480 . [O94776-2 ]
ENST00000527204 ; ENSP00000431797 ; ENSG00000149480 . [O94776-2 ]
GeneIDi 9219.
KEGGi hsa:9219.
UCSCi uc001ntq.2. human. [O94776-1 ]

Organism-specific databases

CTDi 9219.
GeneCardsi GC11M062360.
HGNCi HGNC:7411. MTA2.
HPAi CAB005315.
CAB017522.
HPA006214.
MIMi 603947. gene.
neXtProti NX_O94776.
PharmGKBi PA31219.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG252834.
GeneTreei ENSGT00580000081398.
HOGENOMi HOG000045387.
HOVERGENi HBG002598.
InParanoidi O94776.
KOi K11660.
OMAi NAVKAEC.
OrthoDBi EOG780RM1.
PhylomeDBi O94776.
TreeFami TF106444.

Enzyme and pathway databases

Reactomei REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSi MTA2. human.
GeneWikii MTA2.
GenomeRNAii 9219.
NextBioi 34563.
PROi O94776.
SOURCEi Search...

Gene expression databases

Bgeei O94776.
CleanExi HS_MTA2.
ExpressionAtlasi O94776. baseline and differential.
Genevestigatori O94776.

Family and domain databases

InterProi IPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view ]
Pfami PF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view ]
SMARTi SM00439. BAH. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
PROSITEi PS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, mapping and characterization of a novel human gene, MTA1-L1. showing homology to a metastasis-associated gene, MTA1."
    Futamura M., Nishimori H., Shiratsuchi T., Saji S., Nakamura Y., Tokino T.
    J. Hum. Genet. 44:52-56(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Deacetylation of p53 modulates its effect on cell growth and apoptosis."
    Luo J., Su F., Chen D., Shiloh A., Gu W.
    Nature 408:377-381(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Mammary gland.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Retina.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Brain and Uterus.
  7. "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
    Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
    Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MINT.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "RCS1, a substrate of APC/C, controls the metaphase to anaphase transition."
    Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III, Fang G.
    Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM64A.
  13. "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-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-435 AND THR-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
    Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
    J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  18. "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 SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "RBB, a novel transcription repressor, represses the transcription of HDM2 oncogene."
    Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L., Yao Z., Shang Y.
    Oncogene 32:3711-3721(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NACC2.

Entry informationi

Entry nameiMTA2_HUMAN
AccessioniPrimary (citable) accession number: O94776
Secondary accession number(s): Q68DB1, Q9UQB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 132 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