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

Q03112 (EVI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MDS1 and EVI1 complex locus protein EVI1
Alternative name(s):
Ecotropic virus integration site 1 protein homolog
Short name=EVI-1
Gene names
Name:MECOM
Synonyms:EVI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1051 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a transcriptional regulator binding to DNA sequences in the promoter region of target genes and regulating positively or negatively their expression. Oncogene which plays a role in development, cell proliferation and differentiation. May also play a role in apoptosis through regulation of the JNK and TGF-beta signaling. Involved in hematopoiesis. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16

Subunit structure

Homooligomer. Interacts with SUV39H1 (via SET domain); enhances MECOM transcriptional repression activity By similarity. Interacts with CTBP1. Interacts with SMAD3 (via MH2 domain); the interaction is direct. Interacts with SMAD4; through interaction with SMAD3. Interacts with CREBBP, KAT2B and histone deacetylases. Interacts with MAPK8 and MAPK9; inhibits JNK signaling. Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Nucleus. Nucleus speckle Ref.9 Ref.11 Ref.12.

Domain

Both zinc finger regions are required for the transcriptional activation of PBX1.

Post-translational modification

Phosphorylated By similarity.

May be acetylated by CREBBP and KAT2B. Ref.11

Involvement in disease

A chromosomal aberration involving EVI1 is a cause of chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22) with RUNX1/AML1.

Sequence similarities

Contains 10 C2H2-type zinc fingers.

Sequence caution

The sequence AAB29907.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAB37456.1 differs from that shown. Reason: Probable cloning artifact.

The sequence AAI30521.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAH14103.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
   Biological processApoptosis
Differentiation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

embryonic forelimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

hematopoietic stem cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of JNK cascade

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of programmed cell death

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.10Ref.11. Source: UniProtKB

neutrophil homeostasis

Inferred from electronic annotation. Source: Ensembl

pericardium development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.11Ref.16. Source: UniProtKB

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

renal system development

Inferred from electronic annotation. Source: Ensembl

response to bacterium

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear speck

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.10Ref.11Ref.12. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.12. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ctbp2P565463EBI-1384862,EBI-1384883From a different organism.
SIRT1Q96EB62EBI-1384862,EBI-1802965
UXTQ9UBK95EBI-1384862,EBI-357355

Alternative products

This entry describes 6 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q03112-1)

Also known as: Long; Evi-1a;

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.
Isoform 2 (identifier: Q03112-3)

Also known as: Evi-1c; Mds1/Evi1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRSKGRARKL...APGEELLLFM
Note: Produced by alternative promoter usage. Contains an additional SET domain at positions 79-194. Unable to form homooligomers, to interact with CTBP1 and SMAD3 and to repress TGF-beta signaling.
Isoform 3 (identifier: Q13465-1)

Also known as: Mds1;

The sequence of this isoform can be found in the external entry Q13465.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by alternative promoter usage.
Isoform 4 (identifier: Q03112-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MILDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFM
     138-138: K → KQ
Isoform 5 (identifier: Q03112-5)

The sequence of this isoform differs from the canonical sequence as follows:
     672-680: Missing.
Isoform 6 (identifier: Q03112-6)

The sequence of this isoform differs from the canonical sequence as follows:
     138-138: K → KQ
     672-680: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10511051MDS1 and EVI1 complex locus protein EVI1
PRO_0000047273

Regions

Zinc finger21 – 4424C2H2-type 1
Zinc finger75 – 9723C2H2-type 2
Zinc finger103 – 12523C2H2-type 3
Zinc finger131 – 15424C2H2-type 4
Zinc finger160 – 18223C2H2-type 5
Zinc finger188 – 21023C2H2-type 6
Zinc finger217 – 23923C2H2-type 7
Zinc finger733 – 75523C2H2-type 8
Zinc finger761 – 78424C2H2-type 9
Zinc finger790 – 81223C2H2-type 10
Region1 – 252252Interaction with MAPK9, SMAD3 and probably SUV39H1
Motif421 – 43414Nuclear localization signal Potential
Motif553 – 5575CTBP-binding motif 1 By similarity
Motif584 – 5885CTBP-binding motif 2 By similarity
Compositional bias886 – 93752Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue8601Phosphoserine Ref.17

Natural variations

Alternative sequence11M → MRSKGRARKLATNNECVYGN YPEIPLEEMPDADGVASTPS LNIQEPCSPATSSEAFTPKE GSPYKAPIYIPDDIPIPAEF ELRESNMPGAGLGIWTKRKI EVGEKFGPYVGEQRSNLKDP SYGWEILDEFYNVKFCIDAS QPDVGSWLKYIRFAGCYDQH NLVACQINDQIFYRVVADIA PGEELLLFM in isoform 2.
VSP_038733
Alternative sequence11M → MILDEFYNVKFCIDASQPDV GSWLKYIRFAGCYDQHNLVA CQINDQIFYRVVADIAPGEE LLLFM in isoform 4.
VSP_038734
Alternative sequence1381K → KQ in isoform 4 and isoform 6.
VSP_038735
Alternative sequence672 – 6809Missing in isoform 5 and isoform 6.
VSP_038736
Natural variant1071Q → R.
Corresponds to variant rs34896995 [ dbSNP | Ensembl ].
VAR_061928

Experimental info

Mutagenesis555 – 5562DL → AS: Partial loss of interaction with CTBP1. Loss of interaction with CTBP1; when associated with 586-A-S-587. Ref.11
Mutagenesis586 – 5872DL → AS: Partial loss of interaction with CTBP1. Loss of interaction with CTBP1; when associated with 555-A-S-556. Ref.11
Sequence conflict201Q → R in CAE45952. Ref.4
Sequence conflict1751L → P in CAE45952. Ref.4
Sequence conflict3011F → S in BAF85554. Ref.3
Sequence conflict3031F → V in CAA38735. Ref.1
Sequence conflict4431S → P in CAI46086. Ref.4
Sequence conflict5431K → R in CAE45952. Ref.4
Sequence conflict7301K → R in BAF85554. Ref.3
Sequence conflict7411I → V in CAI46086. Ref.4
Sequence conflict7961D → Y in CAA38735. Ref.1
Sequence conflict8751D → E in CAA38735. Ref.1
Sequence conflict8811T → P in CAA38735. Ref.1
Sequence conflict9061N → Y in CAA38735. Ref.1
Sequence conflict9921V → A in BAF85554. Ref.3
Sequence conflict10131L → P in CAE45952. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) (Evi-1a) [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: BD132C53EA08D263

FASTA1,051118,276
        10         20         30         40         50         60 
MKSEDYPHET MAPDIHEERQ YRCEDCDQLF ESKAELADHQ KFPCSTPHSA FSMVEEDFQQ 

        70         80         90        100        110        120 
KLESENDLQE IHTIQECKEC DQVFPDLQSL EKHMLSHTEE REYKCDQCPK AFNWKSNLIR 

       130        140        150        160        170        180 
HQMSHDSGKH YECENCAKVF TDPSNLQRHI RSQHVGARAH ACPECGKTFA TSSGLKQHKH 

       190        200        210        220        230        240 
IHSSVKPFIC EVCHKSYTQF SNLCRHKRMH ADCRTQIKCK DCGQMFSTTS SLNKHRRFCE 

       250        260        270        280        290        300 
GKNHFAAGGF FGQGISLPGT PAMDKTSMVN MSHANPGLAD YFGANRHPAG LTFPTAPGFS 

       310        320        330        340        350        360 
FSFPGLFPSG LYHRPPLIPA SSPVKGLSST EQTNKSQSPL MTHPQILPAT QDILKALSKH 

       370        380        390        400        410        420 
PSVGDNKPVE LQPERSSEER PFEKISDQSE SSDLDDVSTP SGSDLETTSG SDLESDIESD 

       430        440        450        460        470        480 
KEKFKENGKM FKDKVSPLQN LASINNKKEY SNHSIFSPSL EEQTAVSGAV NDSIKAIASI 

       490        500        510        520        530        540 
AEKYFGSTGL VGLQDKKVGA LPYPSMFPLP FFPAFSQSMY PFPDRDLRSL PLKMEPQSPG 

       550        560        570        580        590        600 
EVKKLQKGSS ESPFDLTTKR KDEKPLTPVP SKPPVTPATS QDQPLDLSMG SRSRASGTKL 

       610        620        630        640        650        660 
TEPRKNHVFG GKKGSNVESR PASDGSLQHA RPTPFFMDPI YRVEKRKLTD PLEALKEKYL 

       670        680        690        700        710        720 
RPSPGFLFHP QFQLPDQRTW MSAIENMAEK LESFSALKPE ASELLQSVPS MFNFRAPPNA 

       730        740        750        760        770        780 
LPENLLRKGK ERYTCRYCGK IFPRSANLTR HLRTHTGEQP YRCKYCDRSF SISSNLQRHV 

       790        800        810        820        830        840 
RNIHNKEKPF KCHLCDRCFG QQTNLDRHLK KHENGNMSGT ATSSPHSELE STGAILDDKE 

       850        860        870        880        890        900 
DAYFTEIRNF IGNSNHGSQS PRNVEERMNG SHFKDEKALV TSQNSDLLDD EEVEDEVLLD 

       910        920        930        940        950        960 
EEDEDNDITG KTGKEPVTSN LHEGNPEDDY EETSALEMSC KTSPVRYKEE EYKSGLSALD 

       970        980        990       1000       1010       1020 
HIRHFTDSLK MRKMEDNQYS EAELSSFSTS HVPEELKQPL HRKSKSQAYA MMLSLSDKES 

      1030       1040       1050 
LHSTSHSSSN VWHSMARAAA ESSAIQSISH V 

« Hide

Isoform 2 (Evi-1c) (Mds1/Evi1) [UniParc].

Checksum: E8A5EAD310102D53
Show »

FASTA1,239139,308
Isoform 3 (Mds1) [UniParc].

See Q13465.

Isoform 4 [UniParc].

Checksum: 772D3F793270B394
Show »

FASTA1,116125,807
Isoform 5 [UniParc].

Checksum: 97476C1D04DB2007
Show »

FASTA1,042117,104
Isoform 6 [UniParc].

Checksum: B6A0605E499FF208
Show »

FASTA1,043117,232

References

« Hide 'large scale' references
[1]"Unique expression of the human Evi-1 gene in an endometrial carcinoma cell line: sequence of cDNAs and structure of alternatively spliced transcripts."
Morishita K., Parganas E., Douglass E.C., Ihle J.N.
Oncogene 5:963-971(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
[2]"Generation of the AML1-EVI-1 fusion gene in the t(3;21)(q26;q22) causes blastic crisis in chronic myelocytic leukemia."
Mitani K., Ogawa S., Tanaka T., Miyoshi H., Kurokawa M., Mano H., Yazaki Y., Ohki M., Hirai H.
EMBO J. 13:504-510(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), CHROMOSOMAL TRANSLOCATION WITH RUNX1 IN CHRONIC MYELOCYTIC LEUKEMIA.
[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. expand/collapse author list , 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 [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-759 (ISOFORM 2).
Tissue: Trachea.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Adipose tissue and Fetal kidney.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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] (ISOFORMS 4 AND 6), NUCLEOTIDE SEQUENCE [MRNA] OF 516-1051 (ISOFORM 5).
Tissue: Lung.
[8]"Structurally altered Evi-1 protein generated in the 3q21q26 syndrome."
Ogawa S., Kurokawa M., Tanaka T., Mitani K., Inazawa J., Hangaishi A., Tanaka K., Matsuo Y., Minowada J., Tsubota T., Yazaki Y., Hirai H.
Oncogene 13:183-191(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 970-1007 (ISOFORM 1).
[9]"The oncoprotein Evi-1 represses TGF-beta signalling by inhibiting Smad3."
Kurokawa M., Mitani K., Irie K., Matsuyama T., Takahashi T., Chiba S., Yazaki Y., Matsumoto K., Hirai H.
Nature 394:92-96(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TGF-BETA SIGNALING, INTERACTION WITH SMAD3 AND SMAD4, SUBCELLULAR LOCATION.
[10]"The evi-1 oncoprotein inhibits c-Jun N-terminal kinase and prevents stress-induced cell death."
Kurokawa M., Mitani K., Yamagata T., Takahashi T., Izutsu K., Ogawa S., Moriguchi T., Nishida E., Yazaki Y., Hirai H.
EMBO J. 19:2958-2968(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK8 AND MAPK9.
[11]"Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles."
Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.
J. Biol. Chem. 276:44936-44943(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION, INTERACTION WITH CREBBP; CTBP1; KAT2B AND HISTONE DEACETYLASES, SUBCELLULAR LOCATION, MUTAGENESIS OF 555-ASP-LEU-556 AND 586-ASP-LEU-587.
[12]"Oligomerization of Evi-1 regulated by the PR domain contributes to recruitment of corepressor CtBP."
Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S., Kurokawa M., Hirai H.
Oncogene 24:6165-6173(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), HOMOOLIGOMERIZATION, INTERACTION WITH CTBP1 AND SMAD3, SUBCELLULAR LOCATION.
[13]"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.
[14]"Evi1 is a survival factor which conveys resistance to both TGFbeta- and taxol-mediated cell death via PI3K/AKT."
Liu Y., Chen L., Ko T.C., Fields A.P., Thompson E.A.
Oncogene 25:3565-3575(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS.
[15]"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.
[16]"Pbx1 is a downstream target of Evi-1 in hematopoietic stem/progenitors and leukemic cells."
Shimabe M., Goyama S., Watanabe-Okochi N., Yoshimi A., Ichikawa M., Imai Y., Kurokawa M.
Oncogene 28:4364-4374(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"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-860, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54989 mRNA. Translation: CAA38735.1.
S69002 mRNA. Translation: AAB29907.1. Different initiation.
AK292865 mRNA. Translation: BAF85554.1.
AK304098 mRNA. Translation: BAH14103.1. Sequence problems.
BX640908 mRNA. Translation: CAE45952.1.
BX647613 mRNA. Translation: CAI46086.1.
AC007849 Genomic DNA. No translation available.
AC024099 Genomic DNA. No translation available.
AC069220 Genomic DNA. No translation available.
AC074033 Genomic DNA. No translation available.
AC078985 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78553.1.
CH471052 Genomic DNA. Translation: EAW78556.1.
CH471052 Genomic DNA. Translation: EAW78557.1.
BC031019 mRNA. Translation: AAH31019.1.
BC130520 mRNA. Translation: AAI30521.1. Different initiation.
BC143951 mRNA. Translation: AAI43952.1.
BC143952 mRNA. Translation: AAI43953.1.
S82592 mRNA. Translation: AAB37456.1. Sequence problems.
CCDSCCDS3205.1. [Q03112-1]
CCDS54669.1. [Q03112-5]
CCDS54670.1. [Q03112-4]
PIRA60191.
S41705.
RefSeqNP_001098547.3. NM_001105077.3. [Q03112-4]
NP_001098548.2. NM_001105078.3. [Q03112-1]
NP_001157471.1. NM_001163999.1. [Q03112-6]
NP_001157472.1. NM_001164000.1. [Q03112-5]
NP_001192123.1. NM_001205194.1. [Q03112-1]
NP_004982.2. NM_004991.3. [Q03112-3]
NP_005232.2. NM_005241.3. [Q03112-1]
XP_005247276.1. XM_005247219.1.
XP_005247277.1. XM_005247220.1.
XP_005247278.1. XM_005247221.1.
XP_005247280.1. XM_005247223.1. [Q03112-1]
XP_006713599.1. XM_006713536.1. [Q03112-4]
UniGeneHs.744090.

3D structure databases

ProteinModelPortalQ03112.
SMRQ03112. Positions 19-237, 733-813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108423. 18 interactions.
DIPDIP-38639N.
IntActQ03112. 3 interactions.
STRING9606.ENSP00000264674.

PTM databases

PhosphoSiteQ03112.

Polymorphism databases

DMDM145559472.

Proteomic databases

MaxQBQ03112.
PaxDbQ03112.
PRIDEQ03112.

Protocols and materials databases

DNASU2122.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264674; ENSP00000264674; ENSG00000085276. [Q03112-4]
ENST00000392736; ENSP00000376493; ENSG00000085276. [Q03112-1]
ENST00000433243; ENSP00000394302; ENSG00000085276.
ENST00000464456; ENSP00000419770; ENSG00000085276. [Q03112-5]
ENST00000468789; ENSP00000419995; ENSG00000085276. [Q03112-1]
ENST00000472280; ENSP00000420048; ENSG00000085276.
GeneID2122.
KEGGhsa:2122.
UCSCuc003ffi.3. human. [Q03112-1]
uc003ffj.3. human. [Q03112-4]
uc003ffk.2. human. [Q03112-5]
uc011bpi.1. human. [Q03112-6]
uc011bpj.1. human. [Q03112-3]

Organism-specific databases

CTD2122.
GeneCardsGC03M168802.
H-InvDBHIX0003836.
HGNCHGNC:3498. MECOM.
HPAHPA046537.
MIM165215. gene.
neXtProtNX_Q03112.
Orphanet52688. Myelodysplastic syndromes.
PharmGKBPA27912.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOVERGENHBG005619.
InParanoidQ03112.
KOK04462.
OrthoDBEOG72G16H.
PhylomeDBQ03112.
TreeFamTF315309.

Enzyme and pathway databases

SignaLinkQ03112.

Gene expression databases

ArrayExpressQ03112.
BgeeQ03112.
CleanExHS_EVI1.
GenevestigatorQ03112.

Family and domain databases

Gene3D3.30.160.60. 8 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 10 hits.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 10 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 8 hits.
PS50157. ZINC_FINGER_C2H2_2. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMECOM. human.
GeneWikiMECOM.
GenomeRNAi2122.
NextBio8579.
SOURCESearch...

Entry information

Entry nameEVI1_HUMAN
AccessionPrimary (citable) accession number: Q03112
Secondary accession number(s): A1L4F3 expand/collapse secondary AC list , A8KA00, B7Z8W7, B7ZLQ3, B7ZLQ4, C9JAK0, D3DNP7, Q16122, Q5HYI1, Q6MZS6, Q8NEI5, Q99917
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 141 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 3

Human chromosome 3: entries, gene names and cross-references to MIM