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Protein

MDS1 and EVI1 complex locus protein EVI1

Gene

MECOM

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

Functioni

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.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri21 – 4424C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri75 – 9723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri103 – 12523C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri131 – 15424C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri160 – 18223C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri188 – 21023C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri217 – 23923C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri733 – 75523C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri761 – 78424C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri790 – 81223C2H2-type 10PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. protein homodimerization activity Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. embryonic forelimb morphogenesis Source: Ensembl
  4. embryonic hindlimb morphogenesis Source: Ensembl
  5. forebrain development Source: Ensembl
  6. hematopoietic stem cell proliferation Source: UniProtKB
  7. inflammatory response Source: Ensembl
  8. in utero embryonic development Source: Ensembl
  9. negative regulation of JNK cascade Source: UniProtKB
  10. negative regulation of programmed cell death Source: UniProtKB
  11. negative regulation of transcription, DNA-templated Source: UniProtKB
  12. neutrophil homeostasis Source: Ensembl
  13. pericardium development Source: Ensembl
  14. positive regulation of transcription, DNA-templated Source: UniProtKB
  15. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  16. post-embryonic development Source: Ensembl
  17. regulation of cell cycle Source: UniProtKB
  18. regulation of cell proliferation Source: Ensembl
  19. renal system development Source: Ensembl
  20. response to bacterium Source: Ensembl
  21. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ03112.

Names & Taxonomyi

Protein namesi
Recommended name:
MDS1 and EVI1 complex locus protein EVI1
Alternative name(s):
Ecotropic virus integration site 1 protein homolog
Short name:
EVI-1
Gene namesi
Name:MECOM
Synonyms:EVI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3498. MECOM.

Subcellular locationi

GO - Cellular componenti

  1. aggresome Source: HPA
  2. cytoplasm Source: HPA
  3. Golgi apparatus Source: HPA
  4. intracellular membrane-bounded organelle Source: HPA
  5. nuclear speck Source: UniProtKB
  6. nucleoplasm Source: HPA
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi555 – 5562DL → AS: Partial loss of interaction with CTBP1. Loss of interaction with CTBP1; when associated with 586-A-S-587. 1 Publication
Mutagenesisi586 – 5872DL → AS: Partial loss of interaction with CTBP1. Loss of interaction with CTBP1; when associated with 555-A-S-556. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti402020. 'Acute myeloid leukemia with inv3(p21;q26.2) or t(3;3)(p21;q26.2)'.
52688. Myelodysplastic syndrome.
PharmGKBiPA27912.

Polymorphism and mutation databases

BioMutaiARHGAP32.
DMDMi145559472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10511051MDS1 and EVI1 complex locus protein EVI1PRO_0000047273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei860 – 8601Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated.By similarity
May be acetylated by CREBBP and KAT2B.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ03112.
PaxDbiQ03112.
PRIDEiQ03112.

PTM databases

PhosphoSiteiQ03112.

Expressioni

Gene expression databases

BgeeiQ03112.
CleanExiHS_EVI1.
ExpressionAtlasiQ03112. baseline and differential.
GenevestigatoriQ03112.

Organism-specific databases

HPAiHPA046537.
HPA052977.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ctbp2P565463EBI-1384862,EBI-1384883From a different organism.
SIRT1Q96EB62EBI-1384862,EBI-1802965
UXTQ9UBK95EBI-1384862,EBI-357355

Protein-protein interaction databases

BioGridi108423. 21 interactions.
DIPiDIP-38639N.
IntActiQ03112. 3 interactions.
STRINGi9606.ENSP00000264674.

Structurei

3D structure databases

ProteinModelPortaliQ03112.
SMRiQ03112. Positions 19-237, 733-813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 252252Interaction with MAPK9, SMAD3 and probably SUV39H1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi421 – 43414Nuclear localization signalSequence AnalysisAdd
BLAST
Motifi553 – 5575CTBP-binding motif 1By similarity
Motifi584 – 5885CTBP-binding motif 2By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi886 – 93752Asp/Glu-rich (acidic)Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 10 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri21 – 4424C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri75 – 9723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri103 – 12523C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri131 – 15424C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri160 – 18223C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri188 – 21023C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri217 – 23923C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri733 – 75523C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri761 – 78424C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri790 – 81223C2H2-type 10PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00530000063676.
HOVERGENiHBG005619.
InParanoidiQ03112.
KOiK04462.
OrthoDBiEOG72G16H.
PhylomeDBiQ03112.
TreeFamiTF315309.

Family and domain databases

Gene3Di3.30.160.60. 8 hits.
InterProiIPR030413. Evi1/Prdm16.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR24393. PTHR24393. 1 hit.
PfamiPF00096. zf-C2H2. 10 hits.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 10 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 8 hits.
PS50157. ZINC_FINGER_C2H2_2. 10 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q03112-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKSEDYPHET MAPDIHEERQ YRCEDCDQLF ESKAELADHQ KFPCSTPHSA
60 70 80 90 100
FSMVEEDFQQ KLESENDLQE IHTIQECKEC DQVFPDLQSL EKHMLSHTEE
110 120 130 140 150
REYKCDQCPK AFNWKSNLIR HQMSHDSGKH YECENCAKVF TDPSNLQRHI
160 170 180 190 200
RSQHVGARAH ACPECGKTFA TSSGLKQHKH IHSSVKPFIC EVCHKSYTQF
210 220 230 240 250
SNLCRHKRMH ADCRTQIKCK DCGQMFSTTS SLNKHRRFCE GKNHFAAGGF
260 270 280 290 300
FGQGISLPGT PAMDKTSMVN MSHANPGLAD YFGANRHPAG LTFPTAPGFS
310 320 330 340 350
FSFPGLFPSG LYHRPPLIPA SSPVKGLSST EQTNKSQSPL MTHPQILPAT
360 370 380 390 400
QDILKALSKH PSVGDNKPVE LQPERSSEER PFEKISDQSE SSDLDDVSTP
410 420 430 440 450
SGSDLETTSG SDLESDIESD KEKFKENGKM FKDKVSPLQN LASINNKKEY
460 470 480 490 500
SNHSIFSPSL EEQTAVSGAV NDSIKAIASI AEKYFGSTGL VGLQDKKVGA
510 520 530 540 550
LPYPSMFPLP FFPAFSQSMY PFPDRDLRSL PLKMEPQSPG EVKKLQKGSS
560 570 580 590 600
ESPFDLTTKR KDEKPLTPVP SKPPVTPATS QDQPLDLSMG SRSRASGTKL
610 620 630 640 650
TEPRKNHVFG GKKGSNVESR PASDGSLQHA RPTPFFMDPI YRVEKRKLTD
660 670 680 690 700
PLEALKEKYL RPSPGFLFHP QFQLPDQRTW MSAIENMAEK LESFSALKPE
710 720 730 740 750
ASELLQSVPS MFNFRAPPNA LPENLLRKGK ERYTCRYCGK IFPRSANLTR
760 770 780 790 800
HLRTHTGEQP YRCKYCDRSF SISSNLQRHV RNIHNKEKPF KCHLCDRCFG
810 820 830 840 850
QQTNLDRHLK KHENGNMSGT ATSSPHSELE STGAILDDKE DAYFTEIRNF
860 870 880 890 900
IGNSNHGSQS PRNVEERMNG SHFKDEKALV TSQNSDLLDD EEVEDEVLLD
910 920 930 940 950
EEDEDNDITG KTGKEPVTSN LHEGNPEDDY EETSALEMSC KTSPVRYKEE
960 970 980 990 1000
EYKSGLSALD HIRHFTDSLK MRKMEDNQYS EAELSSFSTS HVPEELKQPL
1010 1020 1030 1040 1050
HRKSKSQAYA MMLSLSDKES LHSTSHSSSN VWHSMARAAA ESSAIQSISH

V
Length:1,051
Mass (Da):118,276
Last modified:April 17, 2007 - v2
Checksum:iBD132C53EA08D263
GO
Isoform 2 (identifier: Q03112-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:1,239
Mass (Da):139,308
Checksum:iE8A5EAD310102D53
GO
Isoform 3 (identifier: Q13465-1) [UniParc]FASTAAdd to basket

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.

Length:169
Mass (Da):18,696
GO
Isoform 4 (identifier: Q03112-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MILDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFM
     138-138: K → KQ

Show »
Length:1,116
Mass (Da):125,807
Checksum:i772D3F793270B394
GO
Isoform 5 (identifier: Q03112-5) [UniParc]FASTAAdd to basket

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

Show »
Length:1,042
Mass (Da):117,104
Checksum:i97476C1D04DB2007
GO
Isoform 6 (identifier: Q03112-6) [UniParc]FASTAAdd to basket

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

Show »
Length:1,043
Mass (Da):117,232
Checksum:iB6A0605E499FF208
GO

Sequence cautioni

The sequence AAB29907.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAB37456.1 differs from that shown.Probable cloning artifact.Curated
The sequence AAI30521.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAH14103.1 differs from that shown.Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201Q → R in CAE45952 (PubMed:17974005).Curated
Sequence conflicti175 – 1751L → P in CAE45952 (PubMed:17974005).Curated
Sequence conflicti301 – 3011F → S in BAF85554 (PubMed:14702039).Curated
Sequence conflicti303 – 3031F → V in CAA38735 (PubMed:2115646).Curated
Sequence conflicti443 – 4431S → P in CAI46086 (PubMed:17974005).Curated
Sequence conflicti543 – 5431K → R in CAE45952 (PubMed:17974005).Curated
Sequence conflicti730 – 7301K → R in BAF85554 (PubMed:14702039).Curated
Sequence conflicti741 – 7411I → V in CAI46086 (PubMed:17974005).Curated
Sequence conflicti796 – 7961D → Y in CAA38735 (PubMed:2115646).Curated
Sequence conflicti875 – 8751D → E in CAA38735 (PubMed:2115646).Curated
Sequence conflicti881 – 8811T → P in CAA38735 (PubMed:2115646).Curated
Sequence conflicti906 – 9061N → Y in CAA38735 (PubMed:2115646).Curated
Sequence conflicti992 – 9921V → A in BAF85554 (PubMed:14702039).Curated
Sequence conflicti1013 – 10131L → P in CAE45952 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071Q → R.
Corresponds to variant rs34896995 [ dbSNP | Ensembl ].
VAR_061928

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRSKGRARKLATNNECVYGN YPEIPLEEMPDADGVASTPS LNIQEPCSPATSSEAFTPKE GSPYKAPIYIPDDIPIPAEF ELRESNMPGAGLGIWTKRKI EVGEKFGPYVGEQRSNLKDP SYGWEILDEFYNVKFCIDAS QPDVGSWLKYIRFAGCYDQH NLVACQINDQIFYRVVADIA PGEELLLFM in isoform 2. 1 PublicationVSP_038733
Alternative sequencei1 – 11M → MILDEFYNVKFCIDASQPDV GSWLKYIRFAGCYDQHNLVA CQINDQIFYRVVADIAPGEE LLLFM in isoform 4. 1 PublicationVSP_038734
Alternative sequencei138 – 1381K → KQ in isoform 4 and isoform 6. 1 PublicationVSP_038735
Alternative sequencei672 – 6809Missing in isoform 5 and isoform 6. 3 PublicationsVSP_038736

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3205.1. [Q03112-1]
CCDS54669.1. [Q03112-5]
CCDS54670.1. [Q03112-4]
PIRiA60191.
S41705.
RefSeqiNP_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_005247219.2.
XP_005247277.1. XM_005247220.2.
XP_005247278.1. XM_005247221.2.
XP_005247280.1. XM_005247223.2. [Q03112-1]
UniGeneiHs.744090.

Genome annotation databases

EnsembliENST00000264674; ENSP00000264674; ENSG00000085276. [Q03112-4]
ENST00000464456; ENSP00000419770; ENSG00000085276. [Q03112-5]
ENST00000468789; ENSP00000419995; ENSG00000085276. [Q03112-1]
GeneIDi2122.
KEGGihsa:2122.
UCSCiuc003ffi.3. human. [Q03112-1]
uc003ffj.3. human. [Q03112-4]
uc003ffk.2. human. [Q03112-5]
uc011bpi.1. human. [Q03112-6]
uc011bpj.1. human. [Q03112-3]

Polymorphism and mutation databases

BioMutaiARHGAP32.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3205.1. [Q03112-1]
CCDS54669.1. [Q03112-5]
CCDS54670.1. [Q03112-4]
PIRiA60191.
S41705.
RefSeqiNP_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_005247219.2.
XP_005247277.1. XM_005247220.2.
XP_005247278.1. XM_005247221.2.
XP_005247280.1. XM_005247223.2. [Q03112-1]
UniGeneiHs.744090.

3D structure databases

ProteinModelPortaliQ03112.
SMRiQ03112. Positions 19-237, 733-813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108423. 21 interactions.
DIPiDIP-38639N.
IntActiQ03112. 3 interactions.
STRINGi9606.ENSP00000264674.

PTM databases

PhosphoSiteiQ03112.

Polymorphism and mutation databases

BioMutaiARHGAP32.
DMDMi145559472.

Proteomic databases

MaxQBiQ03112.
PaxDbiQ03112.
PRIDEiQ03112.

Protocols and materials databases

DNASUi2122.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264674; ENSP00000264674; ENSG00000085276. [Q03112-4]
ENST00000464456; ENSP00000419770; ENSG00000085276. [Q03112-5]
ENST00000468789; ENSP00000419995; ENSG00000085276. [Q03112-1]
GeneIDi2122.
KEGGihsa:2122.
UCSCiuc003ffi.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

CTDi2122.
GeneCardsiGC03M168802.
H-InvDBHIX0003836.
HGNCiHGNC:3498. MECOM.
HPAiHPA046537.
HPA052977.
MIMi165215. gene.
neXtProtiNX_Q03112.
Orphaneti402020. 'Acute myeloid leukemia with inv3(p21;q26.2) or t(3;3)(p21;q26.2)'.
52688. Myelodysplastic syndrome.
PharmGKBiPA27912.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00530000063676.
HOVERGENiHBG005619.
InParanoidiQ03112.
KOiK04462.
OrthoDBiEOG72G16H.
PhylomeDBiQ03112.
TreeFamiTF315309.

Enzyme and pathway databases

SignaLinkiQ03112.

Miscellaneous databases

ChiTaRSiMECOM. human.
GeneWikiiMECOM.
GenomeRNAii2122.
NextBioi8579.
SOURCEiSearch...

Gene expression databases

BgeeiQ03112.
CleanExiHS_EVI1.
ExpressionAtlasiQ03112. baseline and differential.
GenevestigatoriQ03112.

Family and domain databases

Gene3Di3.30.160.60. 8 hits.
InterProiIPR030413. Evi1/Prdm16.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR24393. PTHR24393. 1 hit.
PfamiPF00096. zf-C2H2. 10 hits.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 10 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 8 hits.
PS50157. ZINC_FINGER_C2H2_2. 10 hits.
[Graphical view]
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Publicationsi

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  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.
    , 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. 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.
    , 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. 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.

Entry informationi

Entry nameiEVI1_HUMAN
AccessioniPrimary (citable) accession number: Q03112
Secondary accession number(s): A1L4F3
, A8KA00, B7Z8W7, B7ZLQ3, B7ZLQ4, C9JAK0, D3DNP7, Q16122, Q5HYI1, Q6MZS6, Q8NEI5, Q99917
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 17, 2007
Last modified: April 29, 2015
This is version 147 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.