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Q9UN86 (G3BP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras GTPase-activating protein-binding protein 2

Short name=G3BP-2
Alternative name(s):
GAP SH3 domain-binding protein 2
Gene names
Name:G3BP2
Synonyms:KIAA0660
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable scaffold protein that may be involved in mRNA transport Potential.

Subunit structure

Binds to the N-terminal domain of I-kappa-B-alpha. Ref.9

Subcellular location

Cytoplasm.

Post-translational modification

Arg-457 and Arg-468 are dimethylated, probably to asymmetric dimethylarginine. Ref.10

Sequence similarities

Contains 1 NTF2 domain.

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence BAA31635.2 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9UN86-1)

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.
Isoform B (identifier: Q9UN86-2)

The sequence of this isoform differs from the canonical sequence as follows:
     243-275: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 482481Ras GTPase-activating protein-binding protein 2
PRO_0000194800

Regions

Domain11 – 133123NTF2
Domain331 – 40979RRM
Compositional bias134 – 22390Glu-rich
Compositional bias419 – 47961Gly-rich

Sites

Site21Not acetylated

Amino acid modifications

Modified residue1411Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15
Modified residue1491Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15
Modified residue2251Phosphoserine Ref.14
Modified residue2261Phosphothreonine Ref.14
Modified residue2271Phosphothreonine Ref.11 Ref.13 Ref.14 Ref.15
Modified residue2351Phosphoserine Ref.13
Modified residue4571Omega-N-methylated arginine Ref.10
Modified residue4681Omega-N-methylated arginine Ref.10

Natural variations

Alternative sequence243 – 27533Missing in isoform B.
VSP_003605
Natural variant4341P → L in a breast cancer sample; somatic mutation. Ref.17
VAR_036128

Experimental info

Sequence conflict2671P → S in AAD51932. Ref.1
Sequence conflict3591E → V in AAC15705. Ref.3
Sequence conflict4601M → I in AAC15705. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 74B8EA43C0560229

FASTA48254,121
        10         20         30         40         50         60 
MVMEKPSPLL VGREFVRQYY TLLNKAPEYL HRFYGRNSSY VHGGVDASGK PQEAVYGQND 

        70         80         90        100        110        120 
IHHKVLSLNF SECHTKIRHV DAHATLSDGV VVQVMGLLSN SGQPERKFMQ TFVLAPEGSV 

       130        140        150        160        170        180 
PNKFYVHNDM FRYEDEVFGD SEPELDEESE DEVEEEQEER QPSPEPVQEN ANSGYYEAHP 

       190        200        210        220        230        240 
VTNGIEEPLE ESSHEPEPEP ESETKTEELK PQVEEKNLEE LEEKSTTPPP AEPVSLPQEP 

       250        260        270        280        290        300 
PKAFSWASVT SKNLPPSGTV SSSGIPPHVK APVSQPRVEA KPEVQSQPPR VREQRPRERP 

       310        320        330        340        350        360 
GFPPRGPRPG RGDMEQNDSD NRRIIRYPDS HQLFVGNLPH DIDENELKEF FMSFGNVVEL 

       370        380        390        400        410        420 
RINTKGVGGK LPNFGFVVFD DSEPVQRILI AKPIMFRGEV RLNVEEKKTR AARERETRGG 

       430        440        450        460        470        480 
GDDRRDIRRN DRGPGGPRGI VGGGMMRDRD GRGPPPRGGM AQKLGSGRGT GQMEGRFTGQ 


RR 

« Hide

Isoform B [UniParc].

Checksum: 1B0F021C138992E0
Show »

FASTA44950,817

References

« Hide 'large scale' references
[1]"Characterisation and chromosomal location of G3BP-1 and G3BP-2a/b, members of a novel SH3 domain-binding and RNA-binding protein family implicated in signal transduction."
Kennedy D., Mattick J.S.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
Tissue: Brain.
[2]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Brain.
[3]Guitard E.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Tissue: Brain.
[4]Kennedy D., Ru K., Mattick J.S.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Tissue: Brain.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Placenta.
[6]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. expand/collapse author list , 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].
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: B-cell.
[8]Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Vousden K.H., Lukashchuk N., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 18-32; 124-132; 206-224; 243-252; 278-290; 371-397 AND 439-447, CLEAVAGE OF INITIATOR METHIONINE, LACK OF N-TERMINAL ACETYLATION, MASS SPECTROMETRY.
Tissue: Colon carcinoma, Lung carcinoma and Ovarian carcinoma.
[9]"IkappaBalpha and IkappaBalpha /NF-kappa B complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2."
Prigent M., Barlat I., Langen H., Dargemont C.
J. Biol. Chem. 275:36441-36449(2000) [PubMed: 10969074] [Abstract]
Cited for: INTERACTION WITH IKAPPABALPHA.
[10]"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
Ong S.E., Mittler G., Mann M.
Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract]
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-457 AND ARG-468, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-149 AND THR-227, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-149; SER-235 AND THR-227, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; THR-226 AND THR-227, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[15]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-149 AND THR-227, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[16]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-434.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF145284 mRNA. Translation: AAD51932.1.
AB014560 mRNA. Translation: BAA31635.2. Different initiation.
AF051311 mRNA. Translation: AAC15705.1.
AF053535 mRNA. Translation: AAC95292.1.
AK291786 mRNA. Translation: BAF84475.1.
CH471057 Genomic DNA. Translation: EAX05742.1.
BC011731 mRNA. Translation: AAH11731.1.
IPIIPI00009057.
IPI00179890.
RefSeqNP_036429.2. NM_012297.4.
NP_987100.1. NM_203504.2.
NP_987101.1. NM_203505.2.
UniGeneHs.303676.

3D structure databases

ProteinModelPortalQ9UN86.
SMRQ9UN86. Positions 1-139, 328-407.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UN86. 25 interactions.
MINTMINT-3082700.
STRINGQ9UN86.

PTM databases

PhosphoSiteQ9UN86.

Polymorphism databases

DMDM116242482.

Proteomic databases

PRIDEQ9UN86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359707; ENSP00000352738; ENSG00000138757.
ENST00000395719; ENSP00000379069; ENSG00000138757.
GeneID9908.
KEGGhsa:9908.
UCSCuc003hir.1. human.
uc003hit.1. human.

Organism-specific databases

CTD9908.
GeneCardsGC04M076567.
H-InvDBHIX0004298.
HGNCHGNC:30291. G3BP2.
HPAHPA018304.
HPA018425.
neXtProtNX_Q9UN86.
PharmGKBPA162389134.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13856.
GeneTreeENSGT00390000011365.
HOGENOMHBG445300.
HOVERGENHBG007211.
InParanoidQ9UN86.
OMAAGQMEGR.
OrthoDBEOG4XWFZ0.
PhylomeDBQ9UN86.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9UN86.
BgeeQ9UN86.
CleanExHS_G3BP2.
GenevestigatorQ9UN86.
GermOnlineENSG00000138757. Homo sapiens.

Family and domain databases

InterProIPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
PfamPF02136. NTF2. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio37365.

Entry information

Entry nameG3BP2_HUMAN
AccessionPrimary (citable) accession number: Q9UN86
Secondary accession number(s): A8K6X1 expand/collapse secondary AC list , O60606, O75149, Q9UPA1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families