Q6P4F7 (RHGBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho GTPase-activating protein 11A

Alternative name(s):
Rho-type GTPase-activating protein 11A

Gene names

Name:	ARHGAP11A
Synonyms:	KIAA0013

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1023 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities	Contains 1 Rho-GAP domain.
Sequence caution	The sequence BAA13442.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1023

1023

Rho GTPase-activating protein 11A

PRO_0000267213

Regions

Domain

49 – 239

191

Rho-GAP

Amino acid modifications

Modified residue

285

1

Phosphoserine Ref.5 Ref.6 Ref.8

Modified residue

306

1

Phosphothreonine Ref.4

Modified residue

316

1

Phosphoserine Ref.6

Modified residue

318

1

Phosphoserine Ref.6 Ref.7 Ref.8

Modified residue

323

1

Phosphothreonine Ref.6 Ref.7 Ref.8

Modified residue

339

1

Phosphoserine Ref.6

Modified residue

340

1

Phosphoserine Ref.6

Modified residue

415

1

Phosphoserine Ref.6

Modified residue

422

1

Phosphoserine Ref.6

Modified residue

484

1

Phosphoserine Ref.4 Ref.6

Modified residue

508

1

Phosphothreonine Ref.4 Ref.6

Modified residue

559

1

Phosphoserine Ref.7

Modified residue

569

1

Phosphoserine Ref.7

Modified residue

582

1

Phosphoserine Ref.6

Modified residue

585

1

Phosphoserine Ref.6

Modified residue

675

1

Phosphoserine Ref.3 Ref.4 Ref.5 Ref.6 Ref.8

Modified residue

847

1

Phosphoserine Ref.8

Modified residue

868

1

Phosphoserine Ref.4

Natural variations

Natural variant

605

1

E → K in a breast cancer sample; somatic mutation. Ref.9

VAR_035546

Experimental info

Sequence conflict

496 – 501

6

SEKISK → TFTYYC in AAH63444. Ref.2

Secondary structure

1

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1023

Helix Strand Turn

Details...

Helix

4 – 18

15

Helix

51 – 53

3

Helix

67 – 76

10

Helix

77 – 79

3

Helix

92 – 103

12

Helix

114 – 117

4

Helix

121 – 127

7

Beta strand

128 – 130

3

Helix

135 – 137

3

Helix

138 – 144

7

Helix

150 – 160

11

Helix

165 – 183

19

Helix

185 – 188

4

Helix

192 – 204

13

Helix

215 – 233

19

Helix

235 – 237

3

Helix

243 – 246

4

Sequences

	Sequence		Length	Mass (Da)
	Q6P4F7 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 053C89371B5F614F	FASTA	1,023	113,866
	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

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: Cervix adenocarcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Embryonic kidney.
[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: Leukemic 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. , 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D87717 mRNA. Translation: BAA13442.2. Different initiation.
BC039563 mRNA. Translation: AAH39563.1.
BC063444 mRNA. Translation: AAH63444.1.

IPI

IPI00477330.

PIR

A59431.

RefSeq

NP_055598.1. NM_014783.3.
NP_955389.1. NM_199357.1.

UniGene

Hs.591130.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EAP	X-ray	2.30	A/B/C/D	1-253	[»]

ProteinModelPortal

Q6P4F7.

SMR

Q6P4F7. Positions 3-248.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-3974818.

STRING

Q6P4F7.

PTM databases

PhosphoSite

Q6P4F7.

Polymorphism databases

DMDM

119361641.

Proteomic databases

PRIDE

Q6P4F7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361627; ENSP00000355090; ENSG00000198826.

GeneID

9824.

KEGG

hsa:9824.

UCSC

uc001zgy.1. human.

Organism-specific databases

CTD

9824.

GeneCards

GC15P032907.

H-InvDB

HIX0012073.

HGNC

HGNC:15783. ARHGAP11A.

HPA

HPA040419.
HPA040830.

MIM

610589. gene.

neXtProt

NX_Q6P4F7.

PharmGKB

PA134982615.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18745.

GeneTree

ENSGT00600000084127.

HOGENOM

HBG713092.

HOVERGEN

HBG062938.

InParanoid

Q6P4F7.

OMA

STRVCKQ.

OrthoDB

EOG4RV2R3.

PhylomeDB

Q6P4F7.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q6P4F7.

Bgee

Q6P4F7.

CleanEx

HS_ARHGAP11A.

Genevestigator

Q6P4F7.

GermOnline

ENSG00000198826. Homo sapiens.

Family and domain databases

InterPro

IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]

Gene3D

G3DSA:1.10.555.10. RhoGAP. 1 hit.

Pfam

PF00620. RhoGAP. 1 hit.
[Graphical view]

SMART

SM00324. RhoGAP. 1 hit.
[Graphical view]

SUPFAM

SSF48350. Rho_GAP. 1 hit.

PROSITE

PS50238. RHOGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

37002.

SOURCE

Search...

Entry information

Entry name

RHGBA_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.