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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501GTP
Binding sitei184 – 1841GTP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 379GTP
Nucleotide bindingi57 – 582GTP
Nucleotide bindingi147 – 1493GTP

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

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)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei271 – 29121HelicalSequence analysisAdd
BLAST
Transmembranei297 – 31721HelicalSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541S → A: Abolishes GTP-induced dimerization. 1 Publication
Mutagenesisi117 – 1171R → D: Abolishes GTP-induced dimerization. 1 Publication

Organism-specific databases

PharmGKBiPA134984698.

Polymorphism and mutation databases

BioMutaiGIMAP2.
DMDMi38372396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337GTPase IMAP family member 2PRO_0000190986Add
BLAST

Proteomic databases

MaxQBiQ9UG22.
PaxDbiQ9UG22.
PeptideAtlasiQ9UG22.
PRIDEiQ9UG22.

PTM databases

iPTMnetiQ9UG22.
PhosphoSiteiQ9UG22.
SwissPalmiQ9UG22.

Expressioni

Tissue specificityi

Detected in T-cells.1 Publication

Gene expression databases

BgeeiQ9UG22.
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 interactions.
DIPiDIP-59483N.
STRINGi9606.ENSP00000223293.

Structurei

Secondary structure

1
337
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 297Combined sources
Helixi35 – 439Combined sources
Beta strandi62 – 687Combined sources
Beta strandi71 – 777Combined sources
Helixi80 – 834Combined sources
Helixi89 – 10214Combined sources
Beta strandi107 – 1148Combined sources
Helixi120 – 13314Combined sources
Helixi135 – 1406Combined sources
Beta strandi141 – 1466Combined sources
Helixi148 – 1514Combined sources
Helixi156 – 1627Combined sources
Helixi166 – 1749Combined sources
Turni175 – 1773Combined sources
Beta strandi179 – 1813Combined sources
Helixi188 – 20821Combined sources
Turni209 – 2113Combined sources
Helixi217 – 2215Combined sources
Helixi237 – 25317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 21-255.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UG22.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 223204AIG1-type GAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J90P. Eukaryota.
ENOG410Y0H9. LUCA.
GeneTreeiENSGT00760000118989.
HOGENOMiHOG000115747.
HOVERGENiHBG004016.
InParanoidiQ9UG22.
OMAiDTPDMFS.
OrthoDBiEOG7XM2Z9.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741V → F.
Corresponds to variant rs11558054 [ dbSNP | Ensembl ].
VAR_049531
Natural varianti152 – 1521N → S.
Corresponds to variant rs17173567 [ dbSNP | Ensembl ].
VAR_049532
Natural varianti161 – 1611H → R.
Corresponds to variant rs2075078 [ dbSNP | Ensembl ].
VAR_017305

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
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. Positions 21-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9UG22.
PhosphoSiteiQ9UG22.
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.
PharmGKBiPA134984698.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J90P. Eukaryota.
ENOG410Y0H9. LUCA.
GeneTreeiENSGT00760000118989.
HOGENOMiHOG000115747.
HOVERGENiHBG004016.
InParanoidiQ9UG22.
OMAiDTPDMFS.
OrthoDBiEOG7XM2Z9.
PhylomeDBiQ9UG22.
TreeFamiTF330845.

Miscellaneous databases

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

Gene expression databases

BgeeiQ9UG22.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  2. "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: Lung and Prostate.
  3. Cited for: INTERACTION WITH GIMAP7, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2)."
    Schwefel D., Frohlich C., Eichhorst J., Wiesner B., Behlke J., Aravind L., Daumke O.
    Proc. Natl. Acad. Sci. U.S.A. 107:20299-20304(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-260 IN COMPLEXES WITH GDP AND GTP, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-54 AND ARG-117.

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: July 6, 2016
This is version 109 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.