Q9H0H5 (RGAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rac GTPase-activating protein 1

Alternative name(s):
Male germ cell RacGap
Short name=MgcRacGAP
Protein CYK4 homolog
Short name=CYK4
Short name=HsCYK-4

Gene names

Name:	RACGAP1
Synonyms:	KIAA1478, MGCRACGAP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	632 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle 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. Essential for the early stages of embryogenesis. 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.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.23 Ref.24
Subunit structure	Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. 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. Interacts with SLC26A8 via its N-terminus. Interacts with RAB11FIP3. Interacts with ECT2; the interaction is direct, occurs at anaphase and during cytokinesis in a microtubule-dependent manner and is enhanced by phosphorylation by PLK1. Interacts with KIF23; the interaction is direct. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21 Ref.24
Subcellular location	Nucleus. Cytoplasm. Cytoplasm › cytoskeleton › spindle. Cytoplasmic vesicle › secretory vesicle › acrosome. Cleavage furrow. Midbody. Note: Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the acrosome By similarity. 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 myosin contractile ring during cytokinesis. Colocalizes with ECT2 to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalizes with Cdc42 to spindle microtubules from prometaphase to telophase. Ref.8 Ref.11 Ref.15 Ref.16 Ref.17 Ref.19 Ref.23 Ref.24
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.11
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. Phosphorylation on multiple serine residues by PLK1 enhances its association with ECT2 and is critical for cleavage furrow formation. Ref.12 Ref.23 Ref.24
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 Cytoplasmic vesicle Cytoskeleton Microtubule Nucleus
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Developmental protein GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cytokinesis, actomyosin contractile ring assembly Inferred from mutant phenotype Ref.17. Source: UniProtKB cytokinesis, initiation of separation Inferred from mutant phenotype Ref.17. Source: UniProtKB embryo development Inferred from sequence or structural similarity. Source: UniProtKB microtubule-based movement Traceable author statement. Source: Reactome neuroblast proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell cycle cytokinesis Inferred from direct assay Ref.16. Source: UniProtKB regulation of attachment of spindle microtubules to kinetochore Inferred from mutant phenotype Ref.15. Source: UniProtKB regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome spermatogenesis Inferred from expression pattern Ref.11. Source: UniProtKB spindle midzone assembly involved in mitosis Inferred from direct assay Ref.16. Source: UniProtKB sulfate transport Inferred from direct assay Ref.9. Source: UniProtKB
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell centralspindlin complex Inferred from direct assay Ref.10Ref.19. Source: UniProtKB cleavage furrow Inferred from direct assay Ref.16. Source: UniProtKB cytosol Traceable author statement. Source: Reactome microtubule Inferred from electronic annotation. Source: UniProtKB-KW midbody Inferred from direct assay Ref.10Ref.16Ref.21. Source: UniProtKB nucleus Inferred from direct assay Ref.8Ref.10Ref.16. Source: UniProtKB spindle midzone Inferred from direct assay Ref.23. Source: UniProtKB
Molecular_function	GTPase activator activity Inferred from direct assay Ref.1. Source: UniProtKB alpha-tubulin binding Inferred from direct assay Ref.8. Source: UniProtKB beta-tubulin binding Inferred from direct assay Ref.8. Source: UniProtKB gamma-tubulin binding Inferred from direct assay Ref.8. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SLC26A8	Q96RN1	2	EBI-717233,EBI-1792052

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

149

1

Phosphoserine; by PLK1 Ref.24

Modified residue

154

1

Phosphoserine Ref.25 Ref.26 Ref.28

Modified residue

157

1

Phosphoserine; by PLK1 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28

Modified residue

161

1

Phosphothreonine Ref.18

Modified residue

164

1

Phosphoserine; by PLK1 Ref.18 Ref.23 Ref.24

Modified residue

170

1

Phosphoserine; by PLK1 Ref.23 Ref.24

Modified residue

203

1

Phosphoserine Ref.18 Ref.20 Ref.22 Ref.25 Ref.26

Modified residue

206

1

Phosphoserine Ref.22 Ref.25

Modified residue

214

1

Phosphoserine Ref.23

Modified residue

257

1

Phosphoserine Ref.22

Modified residue

260

1

Phosphothreonine Ref.23

Modified residue

342

1

Phosphothreonine Ref.22 Ref.26

Modified residue

387

1

Phosphoserine; by AURKB Ref.12

Modified residue

410

1

Phosphoserine; by AURKB Ref.12

Modified residue

567

1

Phosphothreonine Ref.26

Modified residue

580

1

Phosphothreonine Ref.22

Modified residue

588

1

Phosphothreonine Ref.20 Ref.22 Ref.26

Modified residue

600

1

Phosphoserine Ref.22

Modified residue

601

1

Phosphothreonine Ref.22

Modified residue

606

1

Phosphothreonine Ref.22

Experimental info

Mutagenesis

149

1

S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170. Ref.24

Mutagenesis

157

1

S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-164 and A-170. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-164; A-170 and A-214. Ref.23 Ref.24

Mutagenesis

164

1

S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-170. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-170 and A-214. Ref.23 Ref.24

Mutagenesis

170

1

S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-164. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-214. Ref.23 Ref.24

Mutagenesis

214

1

S → A: Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170. Ref.23

Mutagenesis

385

1

R → A: Abolishes GAP activity towards RAC1. Abolishes GAP activity towards CDC42 in prometaphase. Induces multiple blebs during cytokinesis. Ref.1 Ref.13 Ref.15

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...

Beta strand

289 – 293

5

Turn

301 – 303

3

Beta strand

312 – 320

9

Helix

325 – 330

6

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SLC26A8, TISSUE SPECIFICITY.
[10]	"Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity." Mishima M., Kaitna S., Glotzer M. Dev. Cell 2:41-54(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, ASSOCIATION TO MICROTUBULES, INTERACTION WITH KIF23.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RND2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AURKB, PHOSPHORYLATION AT SER-387 AND SER-410.
[13]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-385.
[14]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRC1.
[15]	"Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis." Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T., Hiraoka Y., Haraguchi T., Narumiya S. J. Cell Biol. 168:221-232(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-385.
[16]	"An ECT2-centralspindlin complex regulates the localization and function of RhoA." Yuce O., Piekny A., Glotzer M. J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ECT2 AND KIF23, SUBCELLULAR LOCATION.
[17]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ECT2, SUBCELLULAR LOCATION.
[18]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; SER-164 AND SER-203, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Dissecting the role of Rho-mediated signaling in contractile ring formation." Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T. Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH ECT2 AND KIF23, SUBCELLULAR LOCATION.
[20]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-588, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis." Simon G.C., Schonteich E., Wu C.C., Piekny A., Ekiert D., Yu X., Gould G.W., Glotzer M., Prekeris R. EMBO J. 27:1791-1803(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB11FIP3.
[22]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-206; SER-257; THR-342; THR-580; THR-588; SER-600; THR-601 AND THR-606, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells." Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M., Lowery D.M., Clauser K.R., Zhang C., Shokat K.M., Carr S.A., Yaffe M.B., Jallepalli P.V. PLoS Biol. 7:E1000111-E1000111(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-157; SER-164; SER-170; SER-214 AND THR-260, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-157; SER-164; SER-170 AND SER-214.
[24]	"Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation." Wolfe B.A., Takaki T., Petronczki M., Glotzer M. PLoS Biol. 7:E1000110-E1000110(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ECT2, PHOSPHORYLATION AT SER-149; SER-157; SER-164 AND SER-170, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-149; SER-157; SER-164 AND SER-170.
[25]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-157; SER-203 AND SER-206, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-157; SER-203; THR-342; THR-567 AND THR-588, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-157, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_001126103.1.
NP_001119576.1. NM_001126104.1.
NP_037409.2. NM_013277.3.

UniGene

Hs.505469.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OVJ	X-ray	1.49	A	348-546	[»]
4B6D	X-ray	2.20	A/B/C/D/E/F	284-339	[»]

ProteinModelPortal

Q9H0H5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33087N.

IntAct

Q9H0H5. 12 interactions.

MINT

MINT-256435.

STRING

9606.ENSP00000309871.

PTM databases

PhosphoSite

Q9H0H5.

Polymorphism databases

DMDM

74762727.

Proteomic databases

PaxDb

Q9H0H5.

PeptideAtlas

Q9H0H5.

PRIDE

Q9H0H5.

Protocols and materials databases

DNASU

29127.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000312377; ENSP00000309871; ENSG00000161800.
ENST00000427314; ENSP00000404190; ENSG00000161800.
ENST00000434422; ENSP00000413241; ENSG00000161800.
ENST00000454520; ENSP00000404808; ENSG00000161800.
ENST00000547905; ENSP00000449370; ENSG00000161800.
ENST00000551016; ENSP00000449374; ENSG00000161800.

GeneID

29127.

KEGG

hsa:29127.

UCSC

uc001rvs.2. human.

Organism-specific databases

CTD

29127.

GeneCards

GC12M050370.

H-InvDB

HIX0036723.

HGNC

HGNC:9804. RACGAP1.

HPA

CAB025859.
HPA043912.

MIM

604980. gene.

neXtProt

NX_Q9H0H5.

PharmGKB

PA34165.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG305341.

HOGENOM

HOG000230702.

HOVERGEN

HBG062009.

InParanoid

Q9H0H5.

KO

K16733.

OMA

CIPTLIG.

OrthoDB

EOG4CRKZM.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9H0H5.

Bgee

Q9H0H5.

CleanEx

HS_RACGAP1.

Genevestigator

Q9H0H5.

GermOnline

ENSG00000161800. Homo sapiens.

Family and domain databases

Gene3D

1.10.555.10. 1 hit.

InterPro

IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]

Pfam

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

SMART

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

SUPFAM

SSF48350. Rho_GAP. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

Q9H0H5.

GenomeRNAi

29127.

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:	May 1, 2013
This is version 115 of the entry and version 1 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.