Reviewed, UniProtKB/Swiss-Prot Q9H0H5 (RGAP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Rac GTPase-activating protein 1
Alternative name(s):
    Male germ cell RacGap
      Short name=MgcRacGAP

Gene names

Name:	RACGAP1
Synonyms:	KIAA1478, MGCRACGAP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	632 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential for the early stages of embryogenesis and may play a role in the microtubule-dependent steps in cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Required for initiation of cleavage furrow ingression by regulating ECT2 and for assembly of the contractile ring. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. Ref.1 Ref.7 Ref.8 Ref.9 Ref.12 Ref.14 UniProtKB Q9WVM1
Subunit structure	Associates with alpha-, beta- and gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP domain and basic region with PRC1. The interaction with PRC1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Associates with ECT2 at anaphase and during cytokinesis. Interacts with SLC26A8 via its N-terminus. Ref.8 Ref.9 Ref.14 Ref.10 Ref.11 Ref.13
Subcellular location	Nucleus. Cytoplasm. Spindle. Acrosome. Note: During interphase, localized to the nucleus and cytoplasm along with microtubules, in anaphase, is redistributed to the central spindle and, in telophase and cytokinesis, to the midbody. Colocalizes with RHOA at the contractile ring during cytokinesis. Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the acrosome. Ref.8 Ref.14 Ref.10
Tissue specificity	Highly expressed in testis, thymus and placenta. Expressed at lower levels in spleen and peripheral blood lymphocytes. In testis, expression is restricted to germ cells with the highest levels of expression found in spermatocytes. Expression is regulated in a cell cycle-dependent manner and peaks during G2/M phase. Ref.1 Ref.7 Ref.9 Ref.10
Induction	Expression is down-regulated during macrophage differention of HL-60 cells. Ref.1
Domain	The coiled coil region is indispensible for localization to the midbody during cytokinesis. Ref.8
Post-translational modification	Phosphorylated at multiple sites in the midbody during cytokinesis. Phosphorylation by AURKB on SER-387 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA. Ref.11 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Sequence similarities	Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 Rho-GAP domain.
Sequence caution	The sequence AAH24144.1 differs from that shown. Reason: Frameshift at positions 171, 205 and 437.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Ion transport Spermatogenesis Transport
Cellular component	Cytoplasm Microtubule Nucleus
Domain	Coiled coil Phorbol-ester binding Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Developmental protein GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cytokinesis, contractile ring formation Ref.14 Inferred from mutant phenotype. Source: UniProtKB cytokinesis, initiation of separation Ref.14 Inferred from mutant phenotype. Source: UniProtKB embryonic development Inferred from sequence or structural similarity. Source: UniProtKB intracellular signaling cascade Inferred from electronic annotation. Source: InterPro neuroblast proliferation Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Ref.10 Inferred from expression pattern. Source: UniProtKB sulfate transport Ref.9 Inferred from direct assay. Source: UniProtKB
Cellular component	acrosomal vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Ref.8 Inferred from direct assay. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTPase activator activity Ref.1 Inferred from direct assay. Source: UniProtKB alpha-tubulin binding Ref.8 Inferred from direct assay. Source: UniProtKB beta-tubulin binding Ref.8 Inferred from direct assay. Source: UniProtKB diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW gamma-tubulin binding Ref.8 Inferred from direct assay. Source: UniProtKB protein C-terminus binding Ref.9 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SLC26A8	Q96RN1	1	EBI-717233,EBI-1792052
YWHAB	P31946	1	EBI-717233,EBI-359815
YWHAG	P61981	1	EBI-717233,EBI-359832

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 632

632

Rac GTPase-activating protein 1

PRO_0000228808

Regions

Domain

349 – 539

191

Rho-GAP

Zinc finger

286 – 335

50

Phorbol-ester/DAG-type

Region

106 – 285

180

Interaction with SLC26A8

Coiled coil

53 – 110

58

Potential

Amino acid modifications

Modified residue

161

1

Phosphothreonine Ref.15 Ref.17

Modified residue

164

1

Phosphoserine Ref.15 Ref.17

Modified residue

170

1

Phosphoserine Ref.17

Modified residue

185

1

Phosphoserine Ref.19

Modified residue

187

1

Phosphoserine Ref.19

Modified residue

203

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.21

Modified residue

206

1

Phosphoserine Ref.15 Ref.21

Modified residue

214

1

Phosphoserine Ref.17

Modified residue

257

1

Phosphoserine Ref.21

Modified residue

342

1

Phosphothreonine Ref.17 Ref.21

Modified residue

387

1

Phosphoserine Ref.11

Modified residue

573

1

Phosphoserine Ref.21

Modified residue

580

1

Phosphothreonine Ref.17 Ref.20 Ref.21

Modified residue

588

1

Phosphothreonine Ref.17 Ref.21

Modified residue

590

1

Phosphoserine Ref.17

Modified residue

591

1

Phosphoserine Ref.21

Modified residue

600

1

Phosphoserine Ref.21

Modified residue

601

1

Phosphothreonine Ref.21

Modified residue

606

1

Phosphothreonine Ref.18 Ref.21

Modified residue

628

1

Phosphoserine Ref.17 Ref.18 Ref.21

Experimental info

Mutagenesis

385

1

R → A: Abolishes GAP activity towards RAC1 and CDC42 and induces multiple blebs during cytokinesis. Ref.1 Ref.12

Sequence conflict

155

1

D → H in BAA91347. Ref.3

Sequence conflict

518

1

L → S in BAA90247. Ref.1

Secondary structure

1

.

.

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632

Helix Strand Turn

Details...

Helix

351 – 354

4

Beta strand

357 – 360

4

Helix

364 – 376

13

Turn

377 – 379

3

Turn

381 – 385

5

Helix

390 – 401

12

Helix

409 – 411

3

Helix

415 – 427

13

Beta strand

429 – 431

3

Turn

436 – 438

3

Helix

439 – 447

9

Helix

451 – 463

13

Helix

467 – 485

19

Helix

493 – 504

12

Beta strand

508 – 511

4

Helix

514 – 533

20

Helix

536 – 540

5

Helix

541 – 543

3

Sequences

	Sequence		Length	Mass (Da)
	Q9H0H5-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 032B7DF9CEA8F39D	FASTA	632	71,027
	10 20 30 40 50 60 MDTMMLNVRN LFEQLVRRVE ILSEGNEVQF IQLAKDFEDF RKKWQRTDHE LGKYKDLLMK 70 80 90 100 110 120 AETERSALDV KLKHARNQVD VEIKRRQRAE ADCEKLERQI QLIREMLMCD TSGSIQLSEE 130 140 150 160 170 180 QKSALAFLNR GQPSSSNAGN KRLSTIDESG SILSDISFDK TDESLDWDSS LVKTFKLKKR 190 200 210 220 230 240 EKRRSTSRQF VDGPPGPVKK TRSIGSAVDQ GNESIVAKTT VTVPNDGGPI EAVSTIETVP 250 260 270 280 290 300 YWTRSRRKTG TLQPWNSDST LNSRQLEPRT ETDSVGTPQS NGGMRLHDFV SKTVIKPESC 310 320 330 340 350 360 VPCGKRIKFG KLSLKCRDCR VVSHPECRDR CPLPCIPTLI GTPVKIGEGM LADFVSQTSP 370 380 390 400 410 420 MIPSIVVHCV NEIEQRGLTE TGLYRISGCD RTVKELKEKF LRVKTVPLLS KVDDIHAICS 430 440 450 460 470 480 LLKDFLRNLK EPLLTFRLNR AFMEAAEITD EDNSIAAMYQ AVGELPQANR DTLAFLMIHL 490 500 510 520 530 540 QRVAQSPHTK MDVANLAKVF GPTIVAHAVP NPDPVTMLQD IKRQPKVVER LLSLPLEYWS 550 560 570 580 590 600 QFMMVEQENI DPLHVIENSN AFSTPQTPDI KVSLLGPVTT PEHQLLKTPS SSSLSQRVRS 610 620 630 TLTKNTPRFG SKSKSATNLG RQGNFFASPM LK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MgcRacGAP is involved in the control of growth and differentiation of hematopoietic cells." Kawashima T., Hirose K., Satoh T., Kaneko A., Ikeda Y., Kaziro Y., Nosaka T., Kitamura T. Blood 96:2116-2124(2000) [PubMed: 10979956] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-385, INDUCTION.
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	"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. , 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]. Tissue: Hepatoma.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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: Placenta and Testis.
[6]	"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:143-150(2000) [PubMed: 10819331] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-632. Tissue: Brain.
[7]	"MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male germ cells." Toure A., Dorseuil O., Morin L., Timmons P., Jegou B., Reibel L., Gacon G. J. Biol. Chem. 273:6019-6023(1998) [PubMed: 9497316] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-632, FUNCTION, TISSUE SPECIFICITY. Tissue: Placenta.
[8]	"MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody." Hirose K., Kawashima T., Iwamoto I., Nosaka T., Kitamura T. J. Biol. Chem. 276:5821-5828(2001) [PubMed: 11085985] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN.
[9]	"Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to rhogtpase signaling." Toure A., Morin L., Pineau C., Becq F., Dorseuil O., Gacon G. J. Biol. Chem. 276:20309-20315(2001) [PubMed: 11278976] [Abstract] Cited for: FUNCTION, INTERACTION WITH SLC26A8, TISSUE SPECIFICITY.
[10]	"Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells." Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D., Chardin P., Gacon G. Biochem. J. 372:105-112(2003) [PubMed: 12590651] [Abstract] Cited for: INTERACTION WITH RND2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]	"Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis." Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A., Bao Y.C., Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T., Semba K., Inoue T., Satoh T., Inagaki M., Kitamura T. Dev. Cell 4:549-560(2003) [PubMed: 12689593] [Abstract] Cited for: INTERACTION WITH AURKB, PHOSPHORYLATION AT SER-387.
[12]	"MgcRacGAP regulates cortical activity through RhoA during cytokinesis." Lee J.S., Kamijo K., Ohara N., Kitamura T., Miki T. Exp. Cell Res. 293:275-282(2004) [PubMed: 14729465] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-385.
[13]	"Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase." Ban R., Irino Y., Fukami K., Tanaka H. J. Biol. Chem. 279:16394-16402(2004) [PubMed: 14744859] [Abstract] Cited for: INTERACTION WITH PRC1.
[14]	"MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis." Zhao W.-M., Fang G. Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005) [PubMed: 16129829] [Abstract] Cited for: FUNCTION, INTERACTION WITH ECT2, SUBCELLULAR LOCATION.
[15]	"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 THR-161; SER-164; SER-203 AND SER-206, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"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 THR-161; SER-164; SER-170; SER-203; SER-214; THR-342; THR-580; THR-588; SER-590 AND SER-628, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606 AND SER-628, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, MASS SPECTROMETRY.
[20]	"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 THR-580, MASS SPECTROMETRY.
[21]	"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-203; SER-206; SER-257; THR-342; SER-573; THR-580; THR-588; SER-591; SER-600; THR-601; THR-606 AND SER-628, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB030251 mRNA. Translation: BAA90247.1.
AL136794 mRNA. Translation: CAB66728.1.
AK000733 mRNA. Translation: BAA91347.1.
CR533565 mRNA. Translation: CAG38596.1.
BC024144 mRNA. Translation: AAH24144.1. Frameshift.
BC032754 mRNA. Translation: AAH32754.1.
AB040911 mRNA. Translation: BAA96002.1.

IPI

IPI00152946.

PIR

D59430.

RefSeq

NP_001119575.1.
NP_001119576.1.
NP_037409.2.

UniGene

Hs.505469

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OVJ	X-ray	1.49	A	348-546	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H0H5. 7 interactions.

PTM databases

PhosphoSite

Q9H0H5.

Proteomic databases

PeptideAtlas

Q9H0H5.

PRIDE

Q9H0H5.

Genome annotation databases

Ensembl

ENSG00000161800. Homo sapiens. [Contig view]

GeneID

29127.

KEGG

hsa:29127.

UCSC

uc001rvs.2. human.

Organism-specific databases

GeneCards

GC12M048669.

H-InvDB

HIX0036723.

HGNC

HGNC:9804. RACGAP1.

MIM

604980. gene.

PharmGKB

PA34165.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9H0H5.

HOVERGEN

Q9H0H5.

OMA

Q9H0H5. CDRTVKE.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.

Reactome

REACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpress

Q9H0H5.

Bgee

Q9H0H5.

CleanEx

HS_RACGAP1.

GermOnline

ENSG00000161800. Homo sapiens.

Family and domain databases

InterPro

IPR002219. DAG_PE_bd.
IPR000198. RhoGAP.
[Graphical view]

Gene3D

G3DSA:1.10.555.10. RhoGAP. 1 hit.

Pfam

PF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]

SMART

SM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]

PROSITE

PS50238. RHOGAP. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

52240.

PMAP-CutDB

Q9H0H5.

SOURCE

Search...

Entry information

Entry name

RGAP1_HUMAN

Accession

Primary (citable) accession number: Q9H0H5
Secondary accession number(s): Q6PJ26 , Q9NWN2, Q9P250, Q9P2W2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	March 1, 2001
Last modified:	July 7, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)