Q68EM7 (RHG17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho GTPase-activating protein 17

Alternative name(s):
Rho-type GTPase-activating protein 17
RhoGAP interacting with CIP4 homologs protein 1
Short name=RICH-1

Gene names

Name:	ARHGAP17
Synonyms:	RICH1
ORF Names:	MSTP066, MSTP110

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	881 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca2+-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activitor in vitro for RAC1. Ref.1 Ref.7
Subunit structure	Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and SH3KBP1/CIN85. Ref.1 Ref.6 Ref.7
Subcellular location	Membrane; Peripheral membrane protein. Cytoplasm. Cell junction › tight junction. Note: Associates with membranes and concentrates at sites of cell-cell contact. Ref.1 Ref.7
Tissue specificity	Ubiquitously expressed. Expressed at higher level in heart and placenta. Ref.1
Domain	The BAR domain mediates the interaction with the coiled coil domain of AMOT, leading to its recruitment to tight junctions. Ref.7
Sequence similarities	Contains 1 BAR domain. Contains 1 Rho-GAP domain.
Sequence caution	The sequence AAH01241.1 differs from that shown. Reason: Erroneous initiation. The sequence AAQ13586.1 differs from that shown. Reason: Erroneous initiation. The sequence AAQ13632.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Membrane Tight junction
Coding sequence diversity	Alternative splicing
Domain	SH3-binding
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC 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 membrane Inferred from electronic annotation. Source: UniProtKB-SubCell tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AMOT	Q4VCS5	2	EBI-1642807,EBI-2511319
AMOT	Q4VCS5-2	4	EBI-1642807,EBI-3891843

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q68EM7-1)

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 2 (identifier: Q68EM7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     497-574: Missing.

Isoform 3 (identifier: Q68EM7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-273: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q68EM7-4)

Also known as: RICH1B;

The sequence of this isoform differs from the canonical sequence as follows:
     215-226: LLEAQADYHRKA → ISGRKNQPLGLP
     227-881: Missing.

Isoform 5 (identifier: Q68EM7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     839-881: DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → GFQNRIAASFLKCTQTQPAKTCLAASCWI

Note: No experimental confirmation available.

Isoform 6 (identifier: Q68EM7-6)

The sequence of this isoform differs from the canonical sequence as follows:
     840-881: SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → V

Isoform 7 (identifier: Q68EM7-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-467: Missing.
     468-496: TGNDSDSGTLERKRPASMAVMEGDLVKKE → MCGFNTCGPMGFCLSSLLAWCVDCFFSLC

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 881	881	Rho GTPase-activating protein 17		PRO_0000280462
Regions
	Domain	14 – 246	233	BAR
	Domain	252 – 442	191	Rho-GAP
	Motif	753 – 766	14	SH3-binding Potential
	Compositional bias	521 – 816	296	Pro-rich
Amino acid modifications
	Modified residue	161	1	Phosphoserine By similarity
	Modified residue	575	1	Phosphoserine Ref.8 Ref.12
	Modified residue	679	1	Phosphothreonine Ref.9
Natural variations
	Alternative sequence	1 – 467	467	Missing in isoform 7.		VSP_023682
	Alternative sequence	1 – 273	273	Missing in isoform 3.		VSP_023683
	Alternative sequence	215 – 226	12	LLEAQ…YHRKA → ISGRKNQPLGLP in isoform 4.		VSP_023684
	Alternative sequence	227 – 881	655	Missing in isoform 4.		VSP_023685
	Alternative sequence	468 – 496	29	TGNDS…LVKKE → MCGFNTCGPMGFCLSSLLAW CVDCFFSLC in isoform 7.		VSP_023686
	Alternative sequence	497 – 574	78	Missing in isoform 2.		VSP_023687
	Alternative sequence	839 – 881	43	DSNSR…ESTAL → GFQNRIAASFLKCTQTQPAK TCLAASCWI in isoform 5.		VSP_023688
	Alternative sequence	840 – 881	42	SNSRV…ESTAL → V in isoform 6.		VSP_023689
Experimental info
	Mutagenesis	288	1	R → A: Loss of function; leading to defects in tight junction maintenance. Ref.1
	Sequence conflict	139	1	K → E in BAB55203. Ref.2
	Sequence conflict	167	1	Q → R in CAC37948. Ref.1
	Sequence conflict	186	1	K → R in CAC37948. Ref.1
	Sequence conflict	255	1	E → A in BAB14506. Ref.2
	Sequence conflict	404	1	G → A in BAB55203. Ref.2
	Sequence conflict	575	1	S → C in BAC86144. Ref.2
	Sequence conflict	855	1	M → V in BAB55203. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 92029DBFFEAD1001	FASTA	881	95,437
	10 20 30 40 50 60 MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT 70 80 90 100 110 120 DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV 130 140 150 160 170 180 DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM 190 200 210 220 230 240 DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH 250 260 270 280 290 300 QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK 310 320 330 340 350 360 AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV QDQDKKLQDL 370 380 390 400 410 420 WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA RNEGTLAEMA 430 440 450 460 470 480 AATSVHVVAV IEPIIQHADW FFPEEVEFNV SEAFVPLTTP SSNHSFHTGN DSDSGTLERK 490 500 510 520 530 540 RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP 550 560 570 580 590 600 EPPPQSSRAE SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG 610 620 630 640 650 660 QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH PGGQSSSGTS 670 680 690 700 710 720 QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR YSSSLSPIQA PNHPPPQPPT 730 740 750 760 770 780 QATPLMHTKP NSQGPPNPMA LPSEHGLEQP SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA 790 800 810 820 830 840 GGNPETAQPH AGTLPRPRPV PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTDS 850 860 870 880 NSRVSEPHRS IFPEMHSDSA SKDVPGRILL DIDNDTESTA L
	Isoform 2 [UniParc]. Checksum: 9F42C390ACBAFADA	FASTA	803	87,609
	10 20 30 40 50 60 MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT 70 80 90 100 110 120 DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV 130 140 150 160 170 180 DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM 190 200 210 220 230 240 DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH 250 260 270 280 290 300 QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK 310 320 330 340 350 360 AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV QDQDKKLQDL 370 380 390 400 410 420 WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA RNEGTLAEMA 430 440 450 460 470 480 AATSVHVVAV IEPIIQHADW FFPEEVEFNV SEAFVPLTTP SSNHSFHTGN DSDSGTLERK 490 500 510 520 530 540 RPASMAVMEG DLVKKESPPK PKDPVSAAVP APGRNNSQIA SGQNQPQAAA GSHQLSMGQP 550 560 570 580 590 600 HNAAGPSPHT LRRAVKKPAP APPKPGNPPP GHPGGQSSSG TSQHPPSLSP KPPTRSPSPP 610 620 630 640 650 660 TQHTGQPPGQ PSAPSQLSAP RRYSSSLSPI QAPNHPPPQP PTQATPLMHT KPNSQGPPNP 670 680 690 700 710 720 MALPSEHGLE QPSHTPPQTP TPPSTPPLGK QNPSLPAPQT LAGGNPETAQ PHAGTLPRPR 730 740 750 760 770 780 PVPKPRNRPS VPPPPQPPGV HSAGDSSLTN TAPTASKIVT DSNSRVSEPH RSIFPEMHSD 790 800 SASKDVPGRI LLDIDNDTES TAL
	Isoform 3 [UniParc]. Checksum: 8060364C667A5535	FASTA	608	64,267
	10 20 30 40 50 60 MLLLETGMKE EGLFRIGAGA SKLKKLKAAL DCSTSHLDEF YSDPHAVAGA LKSYLRELPE 70 80 90 100 110 120 PLMTFNLYEE WTQVASVQDQ DKKLQDLWRT CQKLPPQNFV NFRYLIKFLA KLAQTSDVNK 130 140 150 160 170 180 MTPSNIAIVL GPNLLWARNE GTLAEMAAAT SVHVVAVIEP IIQHADWFFP EEVEFNVSEA 190 200 210 220 230 240 FVPLTTPSSN HSFHTGNDSD SGTLERKRPA SMAVMEGDLV KKESFGVKLM DFQAHRRGGT 250 260 270 280 290 300 LNRKHISPAF QPPLPPTDGS TVVPAGPEPP PQSSRAESSS GGGTVPSSAG ILEQGPSPGD 310 320 330 340 350 360 GSPPKPKDPV SAAVPAPGRN NSQIASGQNQ PQAAAGSHQL SMGQPHNAAG PSPHTLRRAV 370 380 390 400 410 420 KKPAPAPPKP GNPPPGHPGG QSSSGTSQHP PSLSPKPPTR SPSPPTQHTG QPPGQPSAPS 430 440 450 460 470 480 QLSAPRRYSS SLSPIQAPNH PPPQPPTQAT PLMHTKPNSQ GPPNPMALPS EHGLEQPSHT 490 500 510 520 530 540 PPQTPTPPST PPLGKQNPSL PAPQTLAGGN PETAQPHAGT LPRPRPVPKP RNRPSVPPPP 550 560 570 580 590 600 QPPGVHSAGD SSLTNTAPTA SKIVTDSNSR VSEPHRSIFP EMHSDSASKD VPGRILLDID NDTESTAL
	Isoform 4 (RICH1B) [UniParc]. Checksum: C849839D16E68AE1	FASTA	226	25,760
	10 20 30 40 50 60 MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT 70 80 90 100 110 120 DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV 130 140 150 160 170 180 DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM 190 200 210 220 DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTISGRKN QPLGLP
	Isoform 5 [UniParc]. Checksum: B2797018F447B1FF	FASTA	867	93,855
	10 20 30 40 50 60 MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT 70 80 90 100 110 120 DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV 130 140 150 160 170 180 DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM 190 200 210 220 230 240 DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH 250 260 270 280 290 300 QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK 310 320 330 340 350 360 AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV QDQDKKLQDL 370 380 390 400 410 420 WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA RNEGTLAEMA 430 440 450 460 470 480 AATSVHVVAV IEPIIQHADW FFPEEVEFNV SEAFVPLTTP SSNHSFHTGN DSDSGTLERK 490 500 510 520 530 540 RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP 550 560 570 580 590 600 EPPPQSSRAE SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG 610 620 630 640 650 660 QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH PGGQSSSGTS 670 680 690 700 710 720 QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR YSSSLSPIQA PNHPPPQPPT 730 740 750 760 770 780 QATPLMHTKP NSQGPPNPMA LPSEHGLEQP SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA 790 800 810 820 830 840 GGNPETAQPH AGTLPRPRPV PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTGF 850 860 QNRIAASFLK CTQTQPAKTC LAASCWI
	Isoform 6 [UniParc]. Checksum: 333F5437A7222C79	FASTA	840	90,929
	10 20 30 40 50 60 MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT 70 80 90 100 110 120 DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV 130 140 150 160 170 180 DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM 190 200 210 220 230 240 DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH 250 260 270 280 290 300 QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK 310 320 330 340 350 360 AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV QDQDKKLQDL 370 380 390 400 410 420 WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA RNEGTLAEMA 430 440 450 460 470 480 AATSVHVVAV IEPIIQHADW FFPEEVEFNV SEAFVPLTTP SSNHSFHTGN DSDSGTLERK 490 500 510 520 530 540 RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP 550 560 570 580 590 600 EPPPQSSRAE SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG 610 620 630 640 650 660 QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH PGGQSSSGTS 670 680 690 700 710 720 QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR YSSSLSPIQA PNHPPPQPPT 730 740 750 760 770 780 QATPLMHTKP NSQGPPNPMA LPSEHGLEQP SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA 790 800 810 820 830 840 GGNPETAQPH AGTLPRPRPV PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTDV
	Isoform 7 [UniParc]. Checksum: B20A13496205E5A8	FASTA	414	42,512
	10 20 30 40 50 60 MCGFNTCGPM GFCLSSLLAW CVDCFFSLCS FGVKLMDFQA HRRGGTLNRK HISPAFQPPL 70 80 90 100 110 120 PPTDGSTVVP AGPEPPPQSS RAESSSGGGT VPSSAGILEQ GPSPGDGSPP KPKDPVSAAV 130 140 150 160 170 180 PAPGRNNSQI ASGQNQPQAA AGSHQLSMGQ PHNAAGPSPH TLRRAVKKPA PAPPKPGNPP 190 200 210 220 230 240 PGHPGGQSSS GTSQHPPSLS PKPPTRSPSP PTQHTGQPPG QPSAPSQLSA PRRYSSSLSP 250 260 270 280 290 300 IQAPNHPPPQ PPTQATPLMH TKPNSQGPPN PMALPSEHGL EQPSHTPPQT PTPPSTPPLG 310 320 330 340 350 360 KQNPSLPAPQ TLAGGNPETA QPHAGTLPRP RPVPKPRNRP SVPPPPQPPG VHSAGDSSLT 370 380 390 400 410 NTAPTASKIV TDSNSRVSEP HRSIFPEMHS DSASKDVPGR ILLDIDNDTE STAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1." Richnau N., Aspenstroem P. J. Biol. Chem. 276:35060-35070(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FNBP1 AND TRIP10, MUTAGENESIS OF ARG-288.
[2]	"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] (ISOFORMS 1; 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 634-881 (ISOFORM 5). Tissue: Placenta and Teratocarcinoma.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). Tissue: Brain.
[4]	"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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-881 (ISOFORM 6). Tissue: Cervix and Eye.
[5]	Liu Y.Q., Zhao B., Xu Y.Y., Wang X.Y., Liu B., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-881. Tissue: Aorta.
[6]	"Identification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP." Reczek D., Bretscher A. J. Cell Biol. 153:191-206(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SLC9A3R1.
[7]	"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells." Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T. Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAR, INTERACTION WITH AMOT; MPP5; INADL; PARD3; CAPZA; CAPZB; CD2AP AND SH3KBP1.
[8]	"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-575, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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 THR-679, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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-575, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ306731 mRNA. Translation: CAC37948.1. AJ306732 mRNA. Translation: CAC37949.1. AK001170 mRNA. No translation available. AK023281 mRNA. Translation: BAB14506.1. AK027567 mRNA. Translation: BAB55203.1. AK125358 mRNA. Translation: BAC86144.1. AK291691 mRNA. Translation: BAF84380.1. AL833975 mRNA. Translation: CAD38819.1. BC001241 mRNA. Translation: AAH01241.1. Different initiation. BC080195 mRNA. Translation: AAH80195.1. AF163257 mRNA. Translation: AAQ13586.1. Different initiation. AF173885 mRNA. Translation: AAQ13632.1. Different initiation.
IPI	IPI00064767. IPI00168527. IPI00386947. IPI00829657. IPI00829687. IPI00830020. IPI00830043.
PIR	F59433.
RefSeq	NP_001006635.1. NM_001006634.1. NP_060524.4. NM_018054.4.
UniGene	Hs.373793.
3D structure databases
HSSP	HSSP built from PDB template 1RGP based on UniProtKB Q07960.
ProteinModelPortal	Q68EM7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q68EM7. 7 interactions.
MINT	MINT-195688.
PTM databases
PhosphoSite	Q68EM7.
Polymorphism databases
DMDM	74736331.
Proteomic databases
PaxDb	Q68EM7.
PRIDE	Q68EM7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000289968; ENSP00000289968; ENSG00000140750. ENST00000303665; ENSP00000303130; ENSG00000140750. ENST00000441763; ENSP00000406950; ENSG00000140750.
GeneID	55114.
KEGG	hsa:55114.
UCSC	uc002dmy.3. human. uc002dna.3. human. uc002dnc.3. human. uc002dng.1. human.
Organism-specific databases
CTD	55114.
GeneCards	GC16M024931.
HGNC	HGNC:18239. ARHGAP17.
HPA	HPA041703.
MIM	608293. gene.
neXtProt	NX_Q68EM7.
PharmGKB	PA134908575.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG329716.
HOVERGEN	HBG000015.
InParanoid	Q68EM7.
OMA	TTPNSNH.
OrthoDB	EOG4GB75X.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q68EM7.
Bgee	Q68EM7.
Genevestigator	Q68EM7.
Family and domain databases
Gene3D	1.10.555.10. 1 hit. 1.20.1270.60. 1 hit.
InterPro	IPR027267. AH/BAR-dom. IPR004148. BAR_dom. IPR008936. Rho_GTPase_activation_prot. IPR000198. RhoGAP_dom. [Graphical view]
Pfam	PF03114. BAR. 1 hit. PF00620. RhoGAP. 1 hit. [Graphical view]
SMART	SM00721. BAR. 1 hit. SM00324. RhoGAP. 1 hit. [Graphical view]
SUPFAM	SSF48350. Rho_GAP. 1 hit.
PROSITE	PS51021. BAR. 1 hit. PS50238. RHOGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ARHGAP17. human.
GenomeRNAi	55114.
NextBio	58744.
SOURCE	Search...

Entry information

Entry name

RHG17_HUMAN

Accession

Primary (citable) accession number: Q68EM7
Secondary accession number(s): A8K6M6 , Q6ZUS4, Q7Z2F2, Q8NDG2, Q96KS2, Q96KS3, Q96SS8, Q9BVF6, Q9H8U5, Q9NW54

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 86 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.