Q9P107 (GMIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GEM-interacting protein
Short name=GMIP

Gene names

Name:

GMIP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	970 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Stimulates, in vitro and in vivo, the GTPase activity of RhoA. Ref.1
Subunit structure	Interacts with GEM through its N-terminal. Ref.1
Sequence similarities	Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 Rho-GAP domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of Rho GTPase activity Inferred from direct assay Ref.1. Source: BHF-UCL small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	Rho GTPase activator activity Inferred from direct assay Ref.1. Source: HGNC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 970

970

GEM-interacting protein

PRO_0000056725

Regions

Domain

554 – 757

204

Rho-GAP

Zinc finger

493 – 537

45

Phorbol-ester/DAG-type

Compositional bias

252 – 257

6

Poly-Arg

Compositional bias

354 – 419

66

Pro-rich

Compositional bias

763 – 828

66

Pro-rich

Amino acid modifications

Modified residue

71

1

Phosphoserine By similarity

Modified residue

234

1

Phosphoserine Ref.6 Ref.7 Ref.8

Modified residue

243

1

Phosphoserine Ref.6

Modified residue

437

1

Phosphoserine By similarity

Natural variations

Natural variant

641

1

D → N.
Corresponds to variant rs12003 [ dbSNP | Ensembl ].

VAR_044518

Experimental info

Sequence conflict

666

1

E → D in AAF61330. Ref.1

Sequence conflict

773

1

S → F in AAF61330. Ref.1

Sequence conflict

870

1

V → C in AAF61330. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

970

Helix Strand Turn

Details...

Helix

81 – 89

9

Helix

93 – 140

48

Helix

149 – 176

28

Helix

178 – 229

52

Helix

248 – 322

75

Helix

324 – 335

12

Turn

336 – 338

3

Helix

343 – 351

9

Sequences

	Sequence		Length	Mass (Da)
	Q9P107 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: 8163EF62F85EB2EE	FASTA	970	106,683
	10 20 30 40 50 60 MDAAEPGLPP GPEGRKRYSD IFRSLDNLEI SLGNVTLEML AGDPLLSEDP EPDKTPTATV 70 80 90 100 110 120 TNEASCWSGP SPEGPVPLTG EELDLRLIRT KGGVDAALEY AKTWSRYAKE LLAWTEKRAS 130 140 150 160 170 180 YELEFAKSTM KIAEAGKVSI QQQSHMPLQY IYTLFLEHDL SLGTLAMETV AQQKRDYYQP 190 200 210 220 230 240 LAAKRTEIEK WRKEFKEQWM KEQKRMNEAV QALRRAQLQY VQRSEDLRAR SQGSPEDSAP 250 260 270 280 290 300 QASPGPSKQQ ERRRRSREEA QAKAQEAEAL YQACVREANA RQQDLEIAKQ RIVSHVRKLV 310 320 330 340 350 360 FQGDEVLRRV TLSLFGLRGA QAERGPRAFA ALAECCAPFE PGQRYQEFVR ALRPEAPPPP 370 380 390 400 410 420 PPAFSFQEFL PSLNSSPLDI RKKLSGPLPP RLDENSAEPG PWEDPGTGWR WQGTPGPTPG 430 440 450 460 470 480 SDVDSVGGGS ESRSLDSPTS SPGAGTRQLV KASSTGTESS DDFEERDPDL GDGLENGLGS 490 500 510 520 530 540 PFGKWTLSSA AQTHQLRRLR GPAKCRECEA FMVSGTECEE CFLTCHKRCL ETLLILCGHR 550 560 570 580 590 600 RLPARTPLFG VDFLQLPRDF PEEVPFVVTK CTAEIEHRAL DVQGIYRVSG SRVRVERLCQ 610 620 630 640 650 660 AFENGRALVE LSGNSPHDVS SVLKRFLQEL TEPVIPFHLY DAFISLAKTL HADPGDDPGT 670 680 690 700 710 720 PSPSPEVIRS LKTLLVQLPD SNYNTLRHLV AHLFRVAARF MENKMSANNL GIVFGPTLLR 730 740 750 760 770 780 PPDGPRAASA IPVTCLLDSG HQAQLVEFLI VHYEQIFGMD ELPQATEPPP QDSSPAPGPL 790 800 810 820 830 840 TTSSQPPPPH LDPDSQPPVL ASDPGPDPQH HSTLEQHPTA TPTEIPTPQS DQREDVAEDT 850 860 870 880 890 900 KDGGGEVSSQ GPEDSLLGTQ SRGHFSRQPV KYPRGGVRPV THQLSSLALV ASKLCEETPI 910 920 930 940 950 960 TSVPRGSLRG RGPSPAAASP EGSPLRRTPL PKHFEITQET ARLLSKLDSE AVPRATCCPD 970 VQPEEAEDHL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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], FUNCTION, INTERACTION WITH GEM. Tissue: Leukemia.
[2]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"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.
[5]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[6]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-243, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, MASS SPECTROMETRY.
[8]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF132541 mRNA. Translation: AAF61330.1.
CH471106 Genomic DNA. Translation: EAW84839.1.
BC126436 mRNA. Translation: AAI26437.1.

IPI

IPI00292376.

PIR

D59435.

RefSeq

NP_057657.2. NM_016573.2.

UniGene

Hs.49427.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QWE	X-ray	2.40	A	80-357	[»]

ProteinModelPortal

Q9P107.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000203556.

PTM databases

PhosphoSite

Q9P107.

Polymorphism databases

DMDM

212286192.

Proteomic databases

PaxDb

Q9P107.

PRIDE

Q9P107.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000203556; ENSP00000203556; ENSG00000089639.

GeneID

51291.

KEGG

hsa:51291.

UCSC

uc002nnd.3. human.

Organism-specific databases

CTD

51291.

GeneCards

GC19M019740.

H-InvDB

HIX0039963.

HGNC

HGNC:24852. GMIP.

HPA

HPA042484.
HPA045481.

MIM

609694. gene.

neXtProt

NX_Q9P107.

PharmGKB

PA134963566.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG240124.

HOGENOM

HOG000112746.

HOVERGEN

HBG052839.

InParanoid

Q9P107.

OMA

NYNTLRH.

PhylomeDB

Q9P107.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q9P107.

Bgee

Q9P107.

CleanEx

HS_GMIP.

Genevestigator

Q9P107.

GermOnline

ENSG00000089639. Homo sapiens.

Family and domain databases

Gene3D

1.10.555.10. 1 hit.

InterPro

IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]

Pfam

PF00620. RhoGAP. 1 hit.
[Graphical view]

SMART

SM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]

SUPFAM

SSF48350. Rho_GAP. 1 hit.

PROSITE

PS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GMIP. human.

EvolutionaryTrace

Q9P107.

GenomeRNAi

51291.

NextBio

54551.

SOURCE

Search...

Entry information

Entry name

GMIP_HUMAN

Accession

Primary (citable) accession number: Q9P107
Secondary accession number(s): A0AVN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	July 22, 2008
Last modified:	May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.