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Protein

GTPase IMAP family member 2

Gene

GIMAP2

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

Functioni

The heterodimer formed by GIMAP2 and GIMAP7 has GTPase activity. In contrast, GIMAP2 has no GTPase activity by itself.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50GTP1
Binding sitei184GTP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 37GTP9
Nucleotide bindingi57 – 58GTP2
Nucleotide bindingi147 – 149GTP3

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000106560-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GTPase IMAP family member 2
Alternative name(s):
Immunity-associated protein 2
Short name:
hIMAP2
Gene namesi
Name:GIMAP2
Synonyms:IMAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:21789. GIMAP2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei271 – 291HelicalSequence analysisAdd BLAST21
Transmembranei297 – 317HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • lipid particle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lipid droplet, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi54S → A: Abolishes GTP-induced dimerization. 1 Publication1
Mutagenesisi117R → D: Abolishes GTP-induced dimerization. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000106560.
PharmGKBiPA134984698.

Polymorphism and mutation databases

BioMutaiGIMAP2.
DMDMi38372396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001909861 – 337GTPase IMAP family member 2Add BLAST337

Proteomic databases

MaxQBiQ9UG22.
PaxDbiQ9UG22.
PeptideAtlasiQ9UG22.
PRIDEiQ9UG22.

PTM databases

iPTMnetiQ9UG22.
PhosphoSitePlusiQ9UG22.
SwissPalmiQ9UG22.

Expressioni

Tissue specificityi

Detected in T-cells.1 Publication

Gene expression databases

BgeeiENSG00000106560.
CleanExiHS_GIMAP2.
ExpressionAtlasiQ9UG22. baseline and differential.
GenevisibleiQ9UG22. HS.

Organism-specific databases

HPAiHPA013589.

Interactioni

Subunit structurei

Monomer in the presence of bound GDP and in the absence of bound nucleotide. Homodimer in the presence of bound GTP. Can form linear oligomers. Heterodimer with GIMAP7.1 Publication

Protein-protein interaction databases

BioGridi117588. 4 interactors.
DIPiDIP-59483N.
STRINGi9606.ENSP00000223293.

Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 29Combined sources7
Helixi35 – 43Combined sources9
Beta strandi62 – 68Combined sources7
Beta strandi71 – 77Combined sources7
Helixi80 – 83Combined sources4
Helixi89 – 102Combined sources14
Beta strandi107 – 114Combined sources8
Helixi120 – 133Combined sources14
Helixi135 – 140Combined sources6
Beta strandi141 – 146Combined sources6
Helixi148 – 151Combined sources4
Helixi156 – 162Combined sources7
Helixi166 – 174Combined sources9
Turni175 – 177Combined sources3
Beta strandi179 – 181Combined sources3
Helixi188 – 208Combined sources21
Turni209 – 211Combined sources3
Helixi217 – 221Combined sources5
Helixi237 – 253Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XTMX-ray1.70A/B1-234[»]
2XTNX-ray1.90A1-234[»]
2XTOX-ray2.80A/B21-260[»]
2XTPX-ray1.50A1-260[»]
3P1JX-ray2.58A/B/C/D19-226[»]
ProteinModelPortaliQ9UG22.
SMRiQ9UG22.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UG22.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 223AIG1-type GAdd BLAST204

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J90P. Eukaryota.
ENOG410Y0H9. LUCA.
GeneTreeiENSGT00760000118989.
HOGENOMiHOG000115747.
HOVERGENiHBG004016.
InParanoidiQ9UG22.
OMAiDTPDMFS.
OrthoDBiEOG091G0I0X.
PhylomeDBiQ9UG22.
TreeFamiTF330845.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006703. G_AIG1.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF04548. AIG1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51720. G_AIG1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UG22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQNEHSHWG PHAKGQCASR SELRIILVGK TGTGKSAAGN SILRKQAFES
60 70 80 90 100
KLGSQTLTKT CSKSQGSWGN REIVIIDTPD MFSWKDHCEA LYKEVQRCYL
110 120 130 140 150
LSAPGPHVLL LVTQLGRYTS QDQQAAQRVK EIFGEDAMGH TIVLFTHKED
160 170 180 190 200
LNGGSLMDYM HDSDNKALSK LVAACGGRIC AFNNRAEGSN QDDQVKELMD
210 220 230 240 250
CIEDLLMEKN GDHYTNGLYS LIQRSKCGPV GSDERVKEFK QSLIKYMETQ
260 270 280 290 300
RSYTALAEAN CLKGALIKTQ LCVLFCIQLF LRLIILWLCI LHSMCNLFCC
310 320 330
LLFSMCNLFC SLLFIIPKKL MIFLRTVIRL ERKTPRL
Length:337
Mass (Da):38,017
Last modified:November 14, 2003 - v2
Checksum:i0CCAB6768527C87B
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04953174V → F.Corresponds to variant rs11558054dbSNPEnsembl.1
Natural variantiVAR_049532152N → S.Corresponds to variant rs17173567dbSNPEnsembl.1
Natural variantiVAR_017305161H → R.Corresponds to variant rs2075078dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL110151 mRNA. Translation: CAB53662.2.
BC013934 mRNA. Translation: AAH13934.1.
BC032345 mRNA. Translation: AAH32345.1.
CCDSiCCDS5905.1.
PIRiT14742.
RefSeqiNP_056475.1. NM_015660.2.
UniGeneiHs.647071.

Genome annotation databases

EnsembliENST00000223293; ENSP00000223293; ENSG00000106560.
GeneIDi26157.
KEGGihsa:26157.
UCSCiuc003who.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL110151 mRNA. Translation: CAB53662.2.
BC013934 mRNA. Translation: AAH13934.1.
BC032345 mRNA. Translation: AAH32345.1.
CCDSiCCDS5905.1.
PIRiT14742.
RefSeqiNP_056475.1. NM_015660.2.
UniGeneiHs.647071.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XTMX-ray1.70A/B1-234[»]
2XTNX-ray1.90A1-234[»]
2XTOX-ray2.80A/B21-260[»]
2XTPX-ray1.50A1-260[»]
3P1JX-ray2.58A/B/C/D19-226[»]
ProteinModelPortaliQ9UG22.
SMRiQ9UG22.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117588. 4 interactors.
DIPiDIP-59483N.
STRINGi9606.ENSP00000223293.

PTM databases

iPTMnetiQ9UG22.
PhosphoSitePlusiQ9UG22.
SwissPalmiQ9UG22.

Polymorphism and mutation databases

BioMutaiGIMAP2.
DMDMi38372396.

Proteomic databases

MaxQBiQ9UG22.
PaxDbiQ9UG22.
PeptideAtlasiQ9UG22.
PRIDEiQ9UG22.

Protocols and materials databases

DNASUi26157.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223293; ENSP00000223293; ENSG00000106560.
GeneIDi26157.
KEGGihsa:26157.
UCSCiuc003who.4. human.

Organism-specific databases

CTDi26157.
GeneCardsiGIMAP2.
HGNCiHGNC:21789. GIMAP2.
HPAiHPA013589.
MIMi608085. gene.
neXtProtiNX_Q9UG22.
OpenTargetsiENSG00000106560.
PharmGKBiPA134984698.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J90P. Eukaryota.
ENOG410Y0H9. LUCA.
GeneTreeiENSGT00760000118989.
HOGENOMiHOG000115747.
HOVERGENiHBG004016.
InParanoidiQ9UG22.
OMAiDTPDMFS.
OrthoDBiEOG091G0I0X.
PhylomeDBiQ9UG22.
TreeFamiTF330845.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000106560-MONOMER.

Miscellaneous databases

ChiTaRSiGIMAP2. human.
EvolutionaryTraceiQ9UG22.
GenomeRNAii26157.
PROiQ9UG22.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106560.
CleanExiHS_GIMAP2.
ExpressionAtlasiQ9UG22. baseline and differential.
GenevisibleiQ9UG22. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006703. G_AIG1.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF04548. AIG1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51720. G_AIG1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGIMA2_HUMAN
AccessioniPrimary (citable) accession number: Q9UG22
Secondary accession number(s): Q96L25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: November 2, 2016
This is version 112 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 7
    Human chromosome 7: 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.