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Protein

GEM-interacting protein

Gene

GMIP

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

Functioni

Stimulates, in vitro and in vivo, the GTPase activity of RhoA.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri493 – 53745Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • GTPase activator activity Source: HGNC
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • intracellular signal transduction Source: HGNC
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • negative regulation of GTPase activity Source: BHF-UCL
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
  • positive regulation of GTPase activity Source: GOC
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • xenophagy Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
GEM-interacting protein
Short name:
GMIP
Gene namesi
Name:GMIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:24852. GMIP.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • intracellular Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134963566.

Polymorphism and mutation databases

DMDMi212286192.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 970970GEM-interacting proteinPRO_0000056725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei234 – 2341PhosphoserineCombined sources
Modified residuei243 – 2431PhosphoserineCombined sources
Modified residuei437 – 4371PhosphoserineBy similarity
Modified residuei441 – 4411PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P107.
MaxQBiQ9P107.
PaxDbiQ9P107.
PRIDEiQ9P107.

PTM databases

iPTMnetiQ9P107.
PhosphoSiteiQ9P107.

Expressioni

Gene expression databases

BgeeiQ9P107.
CleanExiHS_GMIP.
ExpressionAtlasiQ9P107. baseline and differential.
GenevisibleiQ9P107. HS.

Organism-specific databases

HPAiHPA042484.
HPA045481.

Interactioni

Subunit structurei

Interacts with GEM through its N-terminal.1 Publication

Protein-protein interaction databases

BioGridi119442. 3 interactions.
IntActiQ9P107. 1 interaction.
STRINGi9606.ENSP00000203556.

Structurei

Secondary structure

1
970
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi81 – 899Combined sources
Helixi93 – 14048Combined sources
Helixi149 – 17628Combined sources
Helixi178 – 22952Combined sources
Helixi248 – 32275Combined sources
Helixi324 – 33512Combined sources
Turni336 – 3383Combined sources
Helixi343 – 3519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QWEX-ray2.40A80-357[»]
ProteinModelPortaliQ9P107.
SMRiQ9P107. Positions 80-352, 483-757.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P107.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 344264F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini554 – 757204Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi252 – 2576Poly-Arg
Compositional biasi354 – 41966Pro-richAdd
BLAST
Compositional biasi763 – 82866Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri493 – 53745Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IPS0. Eukaryota.
ENOG410XPZ9. LUCA.
GeneTreeiENSGT00840000129703.
HOGENOMiHOG000112746.
HOVERGENiHBG052839.
InParanoidiQ9P107.
OMAiFEPGQRY.
OrthoDBiEOG7QNVK4.
PhylomeDBiQ9P107.
TreeFamiTF351450.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR031160. F_BAR.
IPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P107-1) [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
MDAAEPGLPP GPEGRKRYSD IFRSLDNLEI SLGNVTLEML AGDPLLSEDP
60 70 80 90 100
EPDKTPTATV TNEASCWSGP SPEGPVPLTG EELDLRLIRT KGGVDAALEY
110 120 130 140 150
AKTWSRYAKE LLAWTEKRAS YELEFAKSTM KIAEAGKVSI QQQSHMPLQY
160 170 180 190 200
IYTLFLEHDL SLGTLAMETV AQQKRDYYQP LAAKRTEIEK WRKEFKEQWM
210 220 230 240 250
KEQKRMNEAV QALRRAQLQY VQRSEDLRAR SQGSPEDSAP QASPGPSKQQ
260 270 280 290 300
ERRRRSREEA QAKAQEAEAL YQACVREANA RQQDLEIAKQ RIVSHVRKLV
310 320 330 340 350
FQGDEVLRRV TLSLFGLRGA QAERGPRAFA ALAECCAPFE PGQRYQEFVR
360 370 380 390 400
ALRPEAPPPP PPAFSFQEFL PSLNSSPLDI RKKLSGPLPP RLDENSAEPG
410 420 430 440 450
PWEDPGTGWR WQGTPGPTPG SDVDSVGGGS ESRSLDSPTS SPGAGTRQLV
460 470 480 490 500
KASSTGTESS DDFEERDPDL GDGLENGLGS PFGKWTLSSA AQTHQLRRLR
510 520 530 540 550
GPAKCRECEA FMVSGTECEE CFLTCHKRCL ETLLILCGHR RLPARTPLFG
560 570 580 590 600
VDFLQLPRDF PEEVPFVVTK CTAEIEHRAL DVQGIYRVSG SRVRVERLCQ
610 620 630 640 650
AFENGRALVE LSGNSPHDVS SVLKRFLQEL TEPVIPFHLY DAFISLAKTL
660 670 680 690 700
HADPGDDPGT PSPSPEVIRS LKTLLVQLPD SNYNTLRHLV AHLFRVAARF
710 720 730 740 750
MENKMSANNL GIVFGPTLLR PPDGPRAASA IPVTCLLDSG HQAQLVEFLI
760 770 780 790 800
VHYEQIFGMD ELPQATEPPP QDSSPAPGPL TTSSQPPPPH LDPDSQPPVL
810 820 830 840 850
ASDPGPDPQH HSTLEQHPTA TPTEIPTPQS DQREDVAEDT KDGGGEVSSQ
860 870 880 890 900
GPEDSLLGTQ SRGHFSRQPV KYPRGGVRPV THQLSSLALV ASKLCEETPI
910 920 930 940 950
TSVPRGSLRG RGPSPAAASP EGSPLRRTPL PKHFEITQET ARLLSKLDSE
960 970
AVPRATCCPD VQPEEAEDHL
Length:970
Mass (Da):106,683
Last modified:July 22, 2008 - v2
Checksum:i8163EF62F85EB2EE
GO
Isoform 2 (identifier: Q9P107-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     442-467: Missing.

Note: No experimental confirmation available.
Show »
Length:944
Mass (Da):103,960
Checksum:iF74C3C7AD265BEBE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti666 – 6661E → D in AAF61330 (PubMed:12093360).Curated
Sequence conflicti773 – 7731S → F in AAF61330 (PubMed:12093360).Curated
Sequence conflicti870 – 8701V → C in AAF61330 (PubMed:12093360).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti641 – 6411D → N.
Corresponds to variant rs12003 [ dbSNP | Ensembl ].
VAR_044518

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei442 – 46726Missing in isoform 2. 1 PublicationVSP_056142Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132541 mRNA. Translation: AAF61330.1.
AC011458 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84839.1.
BC126436 mRNA. Translation: AAI26437.1.
BC144142 mRNA. Translation: AAI44143.1.
CCDSiCCDS12408.1. [Q9P107-1]
CCDS74318.1. [Q9P107-2]
PIRiD59435.
RefSeqiNP_001275927.1. NM_001288998.1.
NP_001275928.1. NM_001288999.1. [Q9P107-2]
NP_057657.2. NM_016573.3. [Q9P107-1]
UniGeneiHs.49427.

Genome annotation databases

EnsembliENST00000203556; ENSP00000203556; ENSG00000089639. [Q9P107-1]
ENST00000587238; ENSP00000467054; ENSG00000089639. [Q9P107-2]
GeneIDi51291.
KEGGihsa:51291.
UCSCiuc002nnd.5. human. [Q9P107-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132541 mRNA. Translation: AAF61330.1.
AC011458 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84839.1.
BC126436 mRNA. Translation: AAI26437.1.
BC144142 mRNA. Translation: AAI44143.1.
CCDSiCCDS12408.1. [Q9P107-1]
CCDS74318.1. [Q9P107-2]
PIRiD59435.
RefSeqiNP_001275927.1. NM_001288998.1.
NP_001275928.1. NM_001288999.1. [Q9P107-2]
NP_057657.2. NM_016573.3. [Q9P107-1]
UniGeneiHs.49427.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QWEX-ray2.40A80-357[»]
ProteinModelPortaliQ9P107.
SMRiQ9P107. Positions 80-352, 483-757.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119442. 3 interactions.
IntActiQ9P107. 1 interaction.
STRINGi9606.ENSP00000203556.

PTM databases

iPTMnetiQ9P107.
PhosphoSiteiQ9P107.

Polymorphism and mutation databases

DMDMi212286192.

Proteomic databases

EPDiQ9P107.
MaxQBiQ9P107.
PaxDbiQ9P107.
PRIDEiQ9P107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000203556; ENSP00000203556; ENSG00000089639. [Q9P107-1]
ENST00000587238; ENSP00000467054; ENSG00000089639. [Q9P107-2]
GeneIDi51291.
KEGGihsa:51291.
UCSCiuc002nnd.5. human. [Q9P107-1]

Organism-specific databases

CTDi51291.
GeneCardsiGMIP.
H-InvDBHIX0039963.
HGNCiHGNC:24852. GMIP.
HPAiHPA042484.
HPA045481.
MIMi609694. gene.
neXtProtiNX_Q9P107.
PharmGKBiPA134963566.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPS0. Eukaryota.
ENOG410XPZ9. LUCA.
GeneTreeiENSGT00840000129703.
HOGENOMiHOG000112746.
HOVERGENiHBG052839.
InParanoidiQ9P107.
OMAiFEPGQRY.
OrthoDBiEOG7QNVK4.
PhylomeDBiQ9P107.
TreeFamiTF351450.

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiGMIP. human.
EvolutionaryTraceiQ9P107.
GenomeRNAii51291.
PROiQ9P107.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P107.
CleanExiHS_GMIP.
ExpressionAtlasiQ9P107. baseline and differential.
GenevisibleiQ9P107. HS.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR031160. F_BAR.
IPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases."
    Aresta S., de Tand-Heim M.-F., Beranger F., de Gunzburg J.
    Biochem. J. 367:57-65(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GEM.
    Tissue: Leukemia.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Crystal structure of the N-terminal domain of the GEM interacting protein."
    Structural genomics consortium (SGC)
    Submitted (MAR-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 80-357.

Entry informationi

Entry nameiGMIP_HUMAN
AccessioniPrimary (citable) accession number: Q9P107
Secondary accession number(s): A0AVN9, B7ZLZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 22, 2008
Last modified: June 8, 2016
This is version 120 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.