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Reviewed, UniProtKB/Swiss-Prot Q6P4F7 (RHGBA_HUMAN)

Last modified November 24, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Rho GTPase-activating protein 11A
Alternative name(s):
    Rho-type GTPase-activating protein 11A
Gene names
Name: ARHGAP11A
Synonyms: KIAA0013
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1023 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Sequence similarities

Contains 1 Rho-GAP domain.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   Molecular functionGTPase activation
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processsignal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular functionGTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10231023Rho GTPase-activating protein 11A
PRO_0000267213

Regions

Domain49 – 239191Rho-GAP

Amino acid modifications

Modified residue2851Phosphoserine Ref.5 Ref.6
Modified residue3061Phosphothreonine Ref.4
Modified residue3161Phosphoserine Ref.6
Modified residue3181Phosphoserine Ref.6
Modified residue3231Phosphothreonine Ref.6
Modified residue3391Phosphoserine Ref.6
Modified residue3401Phosphoserine Ref.6
Modified residue4151Phosphoserine Ref.6
Modified residue4221Phosphoserine Ref.6
Modified residue4841Phosphoserine Ref.6 Ref.4
Modified residue5081Phosphothreonine Ref.6 Ref.4
Modified residue5591Phosphoserine
Modified residue5691Phosphoserine
Modified residue5821Phosphoserine Ref.6
Modified residue5851Phosphoserine Ref.6
Modified residue6751Phosphoserine Ref.5 Ref.6 Ref.4 Ref.3
Modified residue8471Phosphoserine
Modified residue8681Phosphoserine Ref.4

Natural variations

Natural variant6051E → K in a breast cancer sample; somatic mutation. Ref.9
VAR_035546

Experimental info

Sequence conflict496 – 5016SEKISK → TFTYYC in AAH63444. Ref.2

Secondary structure

................................ 1023
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6P4F7-1 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 053C89371B5F614F

FASTA1,023113,866
        10         20         30         40         50         60 
MWDQRLVRLA LLQHLRAFYG IKVKGVRGQC DRRRHETAAT EIGGKIFGVP FNALPHSAVP 

        70         80         90        100        110        120 
EYGHIPSFLV DACTSLEDHI HTEGLFRKSG SVIRLKALKN KVDHGEGCLS SAPPCDIAGL 

       130        140        150        160        170        180 
LKQFFRELPE PILPADLHEA LLKAQQLGTE EKNKATLLLS CLLADHTVHV LRYFFNFLRN 

       190        200        210        220        230        240 
VSLRSSENKM DSSNLAVIFA PNLLQTSEGH EKMSSNTEKK LRLQAAVVQT LIDYASDIGR 

       250        260        270        280        290        300 
VPDFILEKIP AMLGIDGLCA TPSLEGFEEG EYETPGEYKR KRRQSVGDFV SGALNKFKPN 

       310        320        330        340        350        360 
RTPSITPQEE RIAQLSESPV ILTPNAKRTL PVDSSHGFSS KKRKSIKHNF NFELLPSNLF 

       370        380        390        400        410        420 
NSSSTPVSVH IDTSSEGSSQ SSLSPVLIGG NHLITAGVPR RSKRIAGKKV CRVESGKAGC 

       430        440        450        460        470        480 
FSPKISHKEK VRRSLRLKFN LGKNGREVNG CSGVNRYESV GWRLANQQSL KNRIESVKTG 

       490        500        510        520        530        540 
LLFSPDVDEK LPKKGSEKIS KSEETLLTPE RLVGTNYRMS WTGPNNSSFQ EVDANEASSM 

       550        560        570        580        590        600 
VENLEVENSL EPDIMVEKSP ATSCELTPSN LNNKHNSNIT SSPLSGDENN MTKETLVKVQ 

       610        620        630        640        650        660 
KAFSESGSNL HALMNQRQSS VTNVGKVKLT EPSYLEDSPE ENLFETNDLT IVESKEKYEH 

       670        680        690        700        710        720 
HTGKGEKCFS ERDFSPLQTQ TFNRETTIKC YSTQMKMEHE KDIHSNMPKD YLSKQEFSSD 

       730        740        750        760        770        780 
EEIKKQQSPK DKLNNKLKEN ENMMEGNLPK CAAHSKDEAR SSFSQQSTCV VTNLSKPRPM 

       790        800        810        820        830        840 
RIAKQQSLET CEKTVSESSQ MTEHRKVSDH IQWFNKLSLN EPNRIKVKSP LKFQRTPVRQ 

       850        860        870        880        890        900 
SVRRINSLLE YSRQPTGHKL ASLGDTASPL VKSVSCDGAL SSCIESASKD SSVSCIKSGP 

       910        920        930        940        950        960 
KEQKSMSCEE SNIGAISKSS MELPSKSFLK MRKHPDSVNA SLRSTTVYKQ KILSDGQVKV 

       970        980        990       1000       1010       1020 
PLDDLTNHDI VKPVVNNNMG ISSGINNRVL RRPSERGRAW YKGSPKHPIG KTQLLPTSKP 


VDL 

« Hide

References

[1]"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
DNA Res. 1:27-35(1994) [PubMed: 7584026] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and Uterus.
[3]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, MASS SPECTROMETRY.
Tissue: Epithelium.
[4]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-306; SER-484; THR-508; SER-675 AND SER-868, MASS SPECTROMETRY.
[5]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-675, MASS SPECTROMETRY.
[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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; SER-316; SER-318; THR-323; SER-339; SER-340; SER-415; SER-422; SER-484; THR-508; SER-582; SER-585 AND SER-675, MASS SPECTROMETRY.
[7]"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-318; THR-323; SER-559 AND SER-569, 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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; SER-318; THR-323; SER-675 AND SER-847, MASS SPECTROMETRY.
Tissue: T-cell.
[9]"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] LYS-605.

Cross-references

Sequence databases

D87717 mRNA. Translation: BAA13442.2. Different initiation.
BC039563 mRNA. Translation: AAH39563.1.
BC063444 mRNA. Translation: AAH63444.1.
IPIIPI00477330.
PIRA59431.
RefSeqNP_055598.1.
NP_955389.1.
UniGeneHs.591130

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3EAPX-ray2.30A/B/C/D1-253[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6P4F7.

PTM databases

PhosphoSiteQ6P4F7.

Proteomic databases

PRIDEQ6P4F7.

Genome annotation databases

EnsemblENST00000361627; ENSP00000355090; ENSG00000198826; Homo sapiens. [Genome view]
GeneID9824.
KEGGhsa:9824.
UCSCuc001zgy.1. human.

Organism-specific databases

CTD9824.
GeneCardsGC15P030694.
HGNCHGNC:15783. ARHGAP11A.
MIM610589. gene.
PharmGKBPA134982615.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ6P4F7.
OMAGSTRVCK
OrthoDBEOG980MGF

Enzyme and pathway databases

ReactomeREACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpressQ6P4F7.
BgeeQ6P4F7.
CleanExHS_ARHGAP11A.
GenevestigatorQ6P4F7.
GermOnlineENSG00000198826. Homo sapiens.

Family and domain databases

InterProIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP.
[Graphical view]
PfamPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00324. RhoGAP. 1 hit.
[Graphical view]
PROSITEPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio37002.
SOURCESearch...

Entry information

Entry nameRHGBA_HUMAN
AccessionPrimary (citable) accession number: Q6P4F7
Secondary accession number(s): Q6PI96, Q9Y3S6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: November 24, 2009
This is version 47 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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 15

Human chromosome 15: 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents