GIMA2_HUMAN
ID GIMA2_HUMAN Reviewed; 337 AA.
AC Q9UG22; Q96L25;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=GTPase IMAP family member 2;
DE AltName: Full=Immunity-associated protein 2;
DE Short=hIMAP2;
GN Name=GIMAP2; Synonyms=IMAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH GIMAP7, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23454188; DOI=10.1016/j.str.2013.01.014;
RA Schwefel D., Arasu B.S., Marino S.F., Lamprecht B., Kochert K.,
RA Rosenbaum E., Eichhorst J., Wiesner B., Behlke J., Rocks O., Mathas S.,
RA Daumke O.;
RT "Structural insights into the mechanism of GTPase activation in the GIMAP
RT family.";
RL Structure 21:550-559(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-260 IN COMPLEXES WITH GDP AND
RP GTP, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-54 AND ARG-117.
RX PubMed=21059949; DOI=10.1073/pnas.1010322107;
RA Schwefel D., Frohlich C., Eichhorst J., Wiesner B., Behlke J., Aravind L.,
RA Daumke O.;
RT "Structural basis of oligomerization in septin-like GTPase of immunity-
RT associated protein 2 (GIMAP2).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20299-20304(2010).
CC -!- FUNCTION: The heterodimer formed by GIMAP2 and GIMAP7 has GTPase
CC activity. In contrast, GIMAP2 has no GTPase activity by itself.
CC {ECO:0000269|PubMed:23454188}.
CC -!- SUBUNIT: Monomer in the presence of bound GDP and in the absence of
CC bound nucleotide. Homodimer in the presence of bound GTP. Can form
CC linear oligomers. Heterodimer with GIMAP7.
CC {ECO:0000269|PubMed:21059949}.
CC -!- INTERACTION:
CC Q9UG22; Q9UG22: GIMAP2; NbExp=4; IntAct=EBI-15891037, EBI-15891037;
CC Q9UG22; Q8NHV1: GIMAP7; NbExp=2; IntAct=EBI-15891037, EBI-16039011;
CC Q9UG22; P42858: HTT; NbExp=6; IntAct=EBI-15891037, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:23454188}.
CC -!- TISSUE SPECIFICITY: Detected in T-cells. {ECO:0000269|PubMed:23454188}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC IAN subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL110151; CAB53662.2; -; mRNA.
DR EMBL; BC013934; AAH13934.1; -; mRNA.
DR EMBL; BC032345; AAH32345.1; -; mRNA.
DR CCDS; CCDS5905.1; -.
DR PIR; T14742; T14742.
DR RefSeq; NP_056475.1; NM_015660.2.
DR PDB; 2XTM; X-ray; 1.70 A; A/B=1-234.
DR PDB; 2XTN; X-ray; 1.90 A; A=1-234.
DR PDB; 2XTO; X-ray; 2.80 A; A/B=21-260.
DR PDB; 2XTP; X-ray; 1.50 A; A=1-260.
DR PDB; 3P1J; X-ray; 2.58 A; A/B/C/D=19-226.
DR PDBsum; 2XTM; -.
DR PDBsum; 2XTN; -.
DR PDBsum; 2XTO; -.
DR PDBsum; 2XTP; -.
DR PDBsum; 3P1J; -.
DR AlphaFoldDB; Q9UG22; -.
DR SMR; Q9UG22; -.
DR BioGRID; 117588; 9.
DR DIP; DIP-59483N; -.
DR IntAct; Q9UG22; 7.
DR STRING; 9606.ENSP00000223293; -.
DR iPTMnet; Q9UG22; -.
DR PhosphoSitePlus; Q9UG22; -.
DR SwissPalm; Q9UG22; -.
DR BioMuta; GIMAP2; -.
DR DMDM; 38372396; -.
DR jPOST; Q9UG22; -.
DR MassIVE; Q9UG22; -.
DR MaxQB; Q9UG22; -.
DR PaxDb; Q9UG22; -.
DR PeptideAtlas; Q9UG22; -.
DR PRIDE; Q9UG22; -.
DR ProteomicsDB; 84198; -.
DR Antibodypedia; 2832; 154 antibodies from 27 providers.
DR DNASU; 26157; -.
DR Ensembl; ENST00000223293.10; ENSP00000223293.5; ENSG00000106560.11.
DR GeneID; 26157; -.
DR KEGG; hsa:26157; -.
DR MANE-Select; ENST00000223293.10; ENSP00000223293.5; NM_015660.3; NP_056475.1.
DR UCSC; uc003who.4; human.
DR CTD; 26157; -.
DR GeneCards; GIMAP2; -.
DR HGNC; HGNC:21789; GIMAP2.
DR HPA; ENSG00000106560; Tissue enhanced (lymphoid).
DR MIM; 608085; gene.
DR neXtProt; NX_Q9UG22; -.
DR OpenTargets; ENSG00000106560; -.
DR PharmGKB; PA134984698; -.
DR VEuPathDB; HostDB:ENSG00000106560; -.
DR eggNOG; ENOG502RB0C; Eukaryota.
DR GeneTree; ENSGT00940000163457; -.
DR HOGENOM; CLU_010468_1_1_1; -.
DR InParanoid; Q9UG22; -.
DR OMA; WGEREMV; -.
DR OrthoDB; 1092873at2759; -.
DR PhylomeDB; Q9UG22; -.
DR TreeFam; TF330845; -.
DR PathwayCommons; Q9UG22; -.
DR SignaLink; Q9UG22; -.
DR BioGRID-ORCS; 26157; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; GIMAP2; human.
DR EvolutionaryTrace; Q9UG22; -.
DR GenomeRNAi; 26157; -.
DR Pharos; Q9UG22; Tbio.
DR PRO; PR:Q9UG22; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UG22; protein.
DR Bgee; ENSG00000106560; Expressed in leukocyte and 142 other tissues.
DR ExpressionAtlas; Q9UG22; baseline and differential.
DR Genevisible; Q9UG22; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Lipid droplet; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..337
FT /note="GTPase IMAP family member 2"
FT /id="PRO_0000190986"
FT DOMAIN 20..223
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 29..36
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 56..60
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 77..80
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 146..149
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 183..185
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT BINDING 31..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21059949,
FT ECO:0007744|PDB:2XTM, ECO:0007744|PDB:2XTN,
FT ECO:0007744|PDB:2XTO"
FT BINDING 50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21059949,
FT ECO:0007744|PDB:2XTN, ECO:0007744|PDB:2XTO"
FT BINDING 57..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21059949,
FT ECO:0007744|PDB:2XTN"
FT BINDING 147..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21059949,
FT ECO:0007744|PDB:2XTM, ECO:0007744|PDB:2XTN,
FT ECO:0007744|PDB:2XTO"
FT BINDING 184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21059949,
FT ECO:0007744|PDB:2XTM, ECO:0007744|PDB:2XTN,
FT ECO:0007744|PDB:2XTO"
FT BINDING 318..320
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT VARIANT 74
FT /note="V -> F (in dbSNP:rs11558054)"
FT /id="VAR_049531"
FT VARIANT 152
FT /note="N -> S (in dbSNP:rs17173567)"
FT /id="VAR_049532"
FT VARIANT 161
FT /note="H -> R (in dbSNP:rs2075078)"
FT /id="VAR_017305"
FT MUTAGEN 54
FT /note="S->A: Abolishes GTP-induced dimerization."
FT /evidence="ECO:0000269|PubMed:21059949"
FT MUTAGEN 117
FT /note="R->D: Abolishes GTP-induced dimerization."
FT /evidence="ECO:0000269|PubMed:21059949"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:2XTP"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2XTP"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:2XTP"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:2XTP"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:2XTP"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2XTP"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 188..208
FT /evidence="ECO:0007829|PDB:2XTP"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:2XTP"
FT HELIX 237..253
FT /evidence="ECO:0007829|PDB:2XTP"
SQ SEQUENCE 337 AA; 38017 MW; 0CCAB6768527C87B CRC64;
MDQNEHSHWG PHAKGQCASR SELRIILVGK TGTGKSAAGN SILRKQAFES KLGSQTLTKT
CSKSQGSWGN REIVIIDTPD MFSWKDHCEA LYKEVQRCYL LSAPGPHVLL LVTQLGRYTS
QDQQAAQRVK EIFGEDAMGH TIVLFTHKED LNGGSLMDYM HDSDNKALSK LVAACGGRIC
AFNNRAEGSN QDDQVKELMD CIEDLLMEKN GDHYTNGLYS LIQRSKCGPV GSDERVKEFK
QSLIKYMETQ RSYTALAEAN CLKGALIKTQ LCVLFCIQLF LRLIILWLCI LHSMCNLFCC
LLFSMCNLFC SLLFIIPKKL MIFLRTVIRL ERKTPRL
