Q9Y3P9 (RBGP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rab GTPase-activating protein 1

Alternative name(s):
GAP and centrosome-associated protein
Rab6 GTPase-activating protein GAPCenA

Gene names

Name:	RABGAP1
ORF Names:	HSPC094

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	1069 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May act as a GTPase-activating protein of RAB6A. May play a role in microtubule nucleation by centrosome. May participate in a RAB6A-mediated pathway involved in the metaphase-anaphase transition. Ref.1 Ref.9
Subunit structure	Interacts with RAB6A and tubulin gamma. Ref.1
Subcellular location	Cytoplasm › cytosol. Cytoplasm › cytoskeleton › centrosome. Note: Predominantly cytosolic but also associated with the centrosome. Ref.1
Sequence similarities	Contains 1 PID domain. Contains 1 Rab-GAP TBC domain.
Sequence caution	The sequence AAF28917.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAH20609.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH54492.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AK022408 differs from that shown. Reason: Intron retention. The sequence CAB40267.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Traceable author statement Ref.1. Source: ProtInc positive regulation of Rab GTPase activity Inferred from electronic annotation. Source: GOC
Cellular_component	centrosome Traceable author statement Ref.1. Source: ProtInc cytosol Traceable author statement Ref.1. Source: ProtInc microtubule associated complex Traceable author statement Ref.1. Source: ProtInc
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro GTPase activator activity Traceable author statement Ref.1. Source: ProtInc Rab GTPase activator activity Inferred from electronic annotation. Source: InterPro tubulin binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAPL1	Q9H0R8	2	EBI-1057545,EBI-746969

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: Q9Y3P9-1)

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 Ref.4 (identifier: Q9Y3P9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.
     637-667: AYSVYDEEIGYCQGQSFLAAVLLLHMPEEQA → VFHVKKKKDSILSGGSTLKLHKKQLQSVICI
     668-1069: Missing.

Note: No experimental confirmation available.

Isoform 3 Ref.2 (identifier: Q9Y3P9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     480-1069: Missing.

Note: No experimental confirmation available.

Isoform 4 Ref.4 (identifier: Q9Y3P9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     258-265: RILYSFAT → PQEKTLCK
     266-1069: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1069	1069	Rab GTPase-activating protein 1		PRO_0000298779
Regions
	Domain	142 – 298	157	PID
	Domain	566 – 752	187	Rab-GAP TBC
	Coiled coil	798 – 1047	250	Potential
Amino acid modifications
	Modified residue	996	1	Phosphothreonine Ref.10
Natural variations
	Alternative sequence	1 – 68	68	Missing in isoform 2. Ref.4		VSP_052510
	Alternative sequence	258 – 265	8	RILYSFAT → PQEKTLCK in isoform 4. Ref.4		VSP_052511
	Alternative sequence	266 – 1069	804	Missing in isoform 4. Ref.4		VSP_052512
	Alternative sequence	480 – 1069	590	Missing in isoform 3. Ref.2		VSP_052515
	Alternative sequence	637 – 667	31	AYSVY…PEEQA → VFHVKKKKDSILSGGSTLKL HKKQLQSVICI in isoform 2. Ref.4		VSP_052513
	Alternative sequence	668 – 1069	402	Missing in isoform 2. Ref.4		VSP_052514

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 21, 2007. Version 3. Checksum: F3B09BD3CF993F3A	FASTA	1,069	121,737
	10 20 30 40 50 60 MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK IVGNGSEQQL 70 80 90 100 110 120 QKELADVLMD PPMDDQPGEK ELVKRSQLDG EGDGPLSNQL SASSTINPVP LVGLQKPEMS 130 140 150 160 170 180 LPVKPGQGDS EASSPFTPVA DEDSVVFSKL TYLGCASVNA PRSEVEALRM MSILRSQCQI 190 200 210 220 230 240 SLDVTLSVPN VSEGIVRLLD PQTNTEIANY PIYKILFCVR GHDGTPESDC FAFTESHYNA 250 260 270 280 290 300 ELFRIHVFRC EIQEAVSRIL YSFATAFRRS AKQTPLSATA APQTPDSDIF TFSVSLEIKE 310 320 330 340 350 360 DDGKGYFSAV PKDKDRQCFK LRQGIDKKIV IYVQQTTNKE LAIERCFGLL LSPGKDVRNS 370 380 390 400 410 420 DMHLLDLESM GKSSDGKSYV ITGSWNPKSP HFQVVNEETP KDKVLFMTTA VDLVITEVQE 430 440 450 460 470 480 PVRFLLETKV RVCSPNERLF WPFSKRSTTE NFFLKLKQIK QRERKNNTDT LYEVVCLESE 490 500 510 520 530 540 SERERRKTTA SPSVRLPQSG SQSSVIPSPP EDDEEEDNDE PLLSGSGDVS KECAEKILET 550 560 570 580 590 600 WGELLSKWHL NLNVRPKQLS SLVRNGVPEA LRGEVWQLLA GCHNNDHLVE KYRILITKES 610 620 630 640 650 660 PQDSAITRDI NRTFPAHDYF KDTGGDGQDS LYKICKAYSV YDEEIGYCQG QSFLAAVLLL 670 680 690 700 710 720 HMPEEQAFSV LVKIMFDYGL RELFKQNFED LHCKFYQLER LMQEYIPDLY NHFLDISLEA 730 740 750 760 770 780 HMYASQWFLT LFTAKFPLYM VFHIIDLLLC EGISVIFNVA LGLLKTSKDD LLLTDFEGAL 790 800 810 820 830 840 KFFRVQLPKR YRSEENAKKL MELACNMKIS QKKLKKYEKE YHTMREQQAQ QEDPIERFER 850 860 870 880 890 900 ENRRLQEANM RLEQENDDLA HELVTSKIAL RKDLDNAEEK ADALNKELLM TKQKLIDAEE 910 920 930 940 950 960 EKRRLEEESA QLKEMCRREL DKAESEIKKN SSIIGDYKQI CSQLSERLEK QQTANKVEIE 970 980 990 1000 1010 1020 KIRQKVDDCE RCREFFNKEG RVKGISSTKE VLDEDTDEEK ETLKNQLREM ELELAQTKLQ 1030 1040 1050 1060 LVEAECKIQD LEHHLGLALN EVQAAKKTWF NRTLSSIKTA TGVQGKETC
	Isoform 2 [UniParc]. Checksum: 549686265A37B8BB	FASTA	599	67,098
	10 20 30 40 50 60 MDPPMDDQPG EKELVKRSQL DGEGDGPLSN QLSASSTINP VPLVGLQKPE MSLPVKPGQG 70 80 90 100 110 120 DSEASSPFTP VADEDSVVFS KLTYLGCASV NAPRSEVEAL RMMSILRSQC QISLDVTLSV 130 140 150 160 170 180 PNVSEGIVRL LDPQTNTEIA NYPIYKILFC VRGHDGTPES DCFAFTESHY NAELFRIHVF 190 200 210 220 230 240 RCEIQEAVSR ILYSFATAFR RSAKQTPLSA TAAPQTPDSD IFTFSVSLEI KEDDGKGYFS 250 260 270 280 290 300 AVPKDKDRQC FKLRQGIDKK IVIYVQQTTN KELAIERCFG LLLSPGKDVR NSDMHLLDLE 310 320 330 340 350 360 SMGKSSDGKS YVITGSWNPK SPHFQVVNEE TPKDKVLFMT TAVDLVITEV QEPVRFLLET 370 380 390 400 410 420 KVRVCSPNER LFWPFSKRST TENFFLKLKQ IKQRERKNNT DTLYEVVCLE SESERERRKT 430 440 450 460 470 480 TASPSVRLPQ SGSQSSVIPS PPEDDEEEDN DEPLLSGSGD VSKECAEKIL ETWGELLSKW 490 500 510 520 530 540 HLNLNVRPKQ LSSLVRNGVP EALRGEVWQL LAGCHNNDHL VEKYRILITK ESPQDSAITR 550 560 570 580 590 DINRTFPAHD YFKDTGGDGQ DSLYKICKVF HVKKKKDSIL SGGSTLKLHK KQLQSVICI
	Isoform 3 [UniParc]. Checksum: 56599C32796E7909	FASTA	479	53,195
	10 20 30 40 50 60 MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK IVGNGSEQQL 70 80 90 100 110 120 QKELADVLMD PPMDDQPGEK ELVKRSQLDG EGDGPLSNQL SASSTINPVP LVGLQKPEMS 130 140 150 160 170 180 LPVKPGQGDS EASSPFTPVA DEDSVVFSKL TYLGCASVNA PRSEVEALRM MSILRSQCQI 190 200 210 220 230 240 SLDVTLSVPN VSEGIVRLLD PQTNTEIANY PIYKILFCVR GHDGTPESDC FAFTESHYNA 250 260 270 280 290 300 ELFRIHVFRC EIQEAVSRIL YSFATAFRRS AKQTPLSATA APQTPDSDIF TFSVSLEIKE 310 320 330 340 350 360 DDGKGYFSAV PKDKDRQCFK LRQGIDKKIV IYVQQTTNKE LAIERCFGLL LSPGKDVRNS 370 380 390 400 410 420 DMHLLDLESM GKSSDGKSYV ITGSWNPKSP HFQVVNEETP KDKVLFMTTA VDLVITEVQE 430 440 450 460 470 PVRFLLETKV RVCSPNERLF WPFSKRSTTE NFFLKLKQIK QRERKNNTDT LYEVVCLES
	Isoform 4 [UniParc]. Checksum: 7BA5E80C1D8A71FF	FASTA	265	28,712
	10 20 30 40 50 60 MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK IVGNGSEQQL 70 80 90 100 110 120 QKELADVLMD PPMDDQPGEK ELVKRSQLDG EGDGPLSNQL SASSTINPVP LVGLQKPEMS 130 140 150 160 170 180 LPVKPGQGDS EASSPFTPVA DEDSVVFSKL TYLGCASVNA PRSEVEALRM MSILRSQCQI 190 200 210 220 230 240 SLDVTLSVPN VSEGIVRLLD PQTNTEIANY PIYKILFCVR GHDGTPESDC FAFTESHYNA 250 260 ELFRIHVFRC EIQEAVSPQE KTLCK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome." Cuif M.-H., Possmayer F., Zander H., Bordes N., Jollivet F., Couedel-Courteille A., Janoueix-Lerosey I., Langsley G., Bornens M., Goud B. EMBO J. 18:1772-1782(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RAB6A AND TUBULIN GAMMA, SUBCELLULAR LOCATION. Tissue: Placenta.
[2]	"Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that possesses Rab3A-GAP activity." Ishibashi K., Kanno E., Itoh T., Fukuda M. Genes Cells 14:41-52(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Human partial CDS from CD34+ stem cells." Zhang Q.H., Ye M., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L., Fan H.Y., Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Umbilical cord blood.
[4]	"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 2 AND 4). Tissue: Mammary gland and Testis.
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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). Tissue: Placenta and Uterus.
[8]	"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] OF 824-1069 (ISOFORM 1). Tissue: Uterus.
[9]	"A role for the Rab6A' GTPase in the inactivation of the Mad2-spindle checkpoint." Miserey-Lenkei S., Couedel-Courteille A., Del Nery E., Bardin S., Piel M., Racine V., Sibarita J.-B., Perez F., Bornens M., Goud B. EMBO J. 25:278-289(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"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 THR-996, MASS SPECTROMETRY. 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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ011679 mRNA. Translation: CAB40267.2. Different initiation. AB449897 mRNA. Translation: BAH16640.1. AF161357 mRNA. Translation: AAF28917.1. Frameshift. AK022408 mRNA. No translation available. AK131449 mRNA. Translation: BAD18594.1. AL365338, AC007066 Genomic DNA. Translation: CAH70298.2. CH471090 Genomic DNA. Translation: EAW87555.1. BC020609 mRNA. Translation: AAH20609.1. Sequence problems. BC054492 mRNA. Translation: AAH54492.1. Different initiation. AL050195 mRNA. Translation: CAB43313.1.
IPI	IPI00016702. IPI00386898. IPI00855799. IPI00856033.
PIR	T13163.
RefSeq	NP_036329.3. NM_012197.3.
UniGene	Hs.271341.
3D structure databases
ProteinModelPortal	Q9Y3P9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y3P9. 12 interactions.
MINT	MINT-258769.
STRING	9606.ENSP00000362751.
PTM databases
PhosphoSite	Q9Y3P9.
Polymorphism databases
DMDM	156633605.
Proteomic databases
PaxDb	Q9Y3P9.
PRIDE	Q9Y3P9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000317419; ENSP00000324973; ENSG00000011454. ENST00000373647; ENSP00000362751; ENSG00000011454. ENST00000456584; ENSP00000414386; ENSG00000011454.
GeneID	23637.
KEGG	hsa:23637.
UCSC	uc004bnm.1. human. uc011lzh.2. human.
Organism-specific databases
CTD	23637.
GeneCards	GC09P125703.
H-InvDB	HIX0008361.
HGNC	HGNC:17155. RABGAP1.
neXtProt	NX_Q9Y3P9.
PharmGKB	PA134977298.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5210.
HOGENOM	HOG000007923.
HOVERGEN	HBG063892.
InParanoid	Q9Y3P9.
OMA	MIPSPPE.
OrthoDB	EOG4QC14X.
Gene expression databases
ArrayExpress	Q9Y3P9.
Bgee	Q9Y3P9.
CleanEx	HS_RABGAP1.
Genevestigator	Q9Y3P9.
Family and domain databases
Gene3D	1.10.10.60. 1 hit. 2.30.29.30. 1 hit.
InterPro	IPR009057. Homeodomain-like. IPR022164. Kinesin-like. IPR011993. PH_like_dom. IPR006020. PTyr_interaction_dom. IPR000195. Rab-GTPase-TBC_dom. [Graphical view]
Pfam	PF12473. DUF3694. 1 hit. PF00640. PID. 1 hit. PF00566. RabGAP-TBC. 1 hit. [Graphical view]
SMART	SM00462. PTB. 1 hit. SM00164. TBC. 1 hit. [Graphical view]
SUPFAM	SSF47923. RabGAP_TBC. 2 hits.
PROSITE	PS01179. PID. 1 hit. PS50086. TBC_RABGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RABGAP1. human.
GenomeRNAi	23637.
NextBio	46429.

Entry information

Entry name

RBGP1_HUMAN

Accession

Primary (citable) accession number: Q9Y3P9
Secondary accession number(s): B9A6L2 , Q05CW2, Q6ZMY1, Q9HA28, Q9P0E2, Q9UG67

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	August 21, 2007
Last modified:	May 1, 2013
This is version 105 of the entry and version 3 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.