Reviewed, UniProtKB/Swiss-Prot Q9UPQ3 (AGAP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
      Short name=AGAP-1
Alternative name(s):
    Centaurin-gamma-2
    GTP-binding and GTPase-activating protein 1
      Short name=GGAP1

Gene names

Name:	AGAP1
Synonyms:	CENTG2, KIAA1099

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

General annotation (Comments)

Function	GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system. Ref.1
Enzyme regulation	GAP activity stimulated by phosphatidylinositol 3,4,5-trisphosphate (PIP3) and, to a lesser extent, by phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidic acid potentiates PIP2 stimulation.
Subunit structure	Homodimer. Interacts with several subunits of the AP-3 protein complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3 and GUCY1B3. Ref.8 Ref.9
Subcellular location	Cytoplasm. Note: Associates with the endocytic compartment. Ref.1 Ref.7
Tissue specificity	Widely expressed. Ref.1 Ref.9 Ref.7 Ref.10
Domain	The PH domain mediates AP-3 binding.
Post-translational modification	Phosphorylated on tyrosines. Ref.9 Ref.11 Ref.12
Sequence similarities	Belongs to the centaurin gamma-like family. Contains 2 ANK repeats. Contains 1 Arf-GAP domain. Contains 1 PH domain.
Sequence caution	The sequence AAH60814.1 differs from that shown. Reason: Miscellaneous discrepancy. A 4-nucleotides insertion of unknown origin disrupts the reading frame.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	ANK repeat Repeat Zinc-finger
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of ARF GTPase activity Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ARF GTPase activator activity Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UPQ3-1)

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: Q9UPQ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     442-494: Missing.

Isoform 3 (identifier: Q9UPQ3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     352-405: MLLKRSGKSL...IDLLRTTVKV → LPFFVLALTA...SAQLSGAMMN
     406-857: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 857	857	Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1		PRO_0000074218
Regions
	Domain	346 – 588	243	PH
	Domain	609 – 729	121	Arf-GAP
	Repeat	768 – 797	30	ANK 1
	Repeat	801 – 830	30	ANK 2
	Nucleotide binding	78 – 85	8	GTP Potential
	Nucleotide binding	122 – 126	5	GTP Potential
	Nucleotide binding	178 – 181	4	GTP Potential
	Zinc finger	624 – 647	24	C4-type
	Region	66 – 276	211	Small GTPase-like
Amino acid modifications
	Modified residue	315	1	Phosphoserine Ref.12
	Modified residue	836	1	Phosphothreonine Ref.11
Natural variations
	Alternative sequence	352 – 405	54	MLLKR…TTVKV → LPFFVLALTASTYLRPAGAR ARQSSPWPGPRGGQTSPHCA EGPQSAQLSGAMMN in isoform 3.		VSP_011181
	Alternative sequence	406 – 857	452	Missing in isoform 3.		VSP_011182
	Alternative sequence	442 – 494	53	Missing in isoform 2.		VSP_011183
	Natural variant	82	1	S → G in an autistic patient. Ref.13		VAR_026446
	Natural variant	148	1	D → G: dbSNP rs17855721. Ref.5		VAR_026447
	Natural variant	522	1	P → L: dbSNP rs17840725.		VAR_048331
	Natural variant	671	1	V → I: dbSNP rs2034648. Ref.1 Ref.13 Ref.2 Ref.3 Ref.6		VAR_026448
	Natural variant	798	1	R → G in an autistic patient. Ref.13		VAR_026449
	Natural variant	829	1	E → K: dbSNP rs15718.		VAR_019550
	Natural variant	854	1	P → T in a family with an autistic patient. Ref.13		VAR_026450
Experimental info
	Mutagenesis	647	1	C → S: Loss of GAP activity. Ref.7
	Mutagenesis	652	1	R → K: Loss of GAP activity. No effect on AP-3-binding. Ref.7
	Sequence conflict	288	1	T → I Ref.1
	Sequence conflict	288	1	T → I Ref.2
	Sequence conflict	288	1	T → I Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 13, 2007. Version 4. Checksum: BBFDB8DA0ECD55E8	FASTA	857	94,470
	10 20 30 40 50 60 MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV IAIEDAFVNS 70 80 90 100 110 120 QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL 130 140 150 160 170 180 LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD 190 200 210 220 230 240 AISSANPRVI DDARARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI 250 260 270 280 290 300 GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT 310 320 330 340 350 360 ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS 370 380 390 400 410 420 LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSACAPI 430 440 450 460 470 480 SSPKTNGLSK DMSSLHISPN SGNVTSASGS QMASGISLVS FNSRPDGMHQ RSYSVSSADQ 490 500 510 520 530 540 WSEATVIANS AISSDTGLGD SVCSSPSISS TTSPKLDPPP SPHANRKKHR RKKSTSNFKA 550 560 570 580 590 600 DGLSGTAEEQ EENFEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK 610 620 630 640 650 660 SRLTSQSEAM ALQSIRNMRG NSHCVDCETQ NPNWASLNLG ALMCIECSGI HRNLGTHLSR 670 680 690 700 710 720 VRSLDLDDWP VELIKVMSSI GNELANSVWE ESSQGRTKPS VDSTREEKER WIRAKYEQKL 730 740 750 760 770 780 FLAPLPCTEL SLGQHLLRAT ADEDLRTAIL LLAHGSRDEV NETCGEGDGR TALHLACRKG 790 800 810 820 830 840 NVVLAQLLIW YGVDVTARDA HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS 850 RRNNNRNNSS GRVPTII
	Isoform 2. Checksum: 6014F37974C24A52	FASTA	804	89,066
	10 20 30 40 50 60 MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV IAIEDAFVNS 70 80 90 100 110 120 QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL 130 140 150 160 170 180 LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD 190 200 210 220 230 240 AISSANPRVI DDARARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI 250 260 270 280 290 300 GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT 310 320 330 340 350 360 ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS 370 380 390 400 410 420 LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSACAPI 430 440 450 460 470 480 SSPKTNGLSK DMSSLHISPN SDTGLGDSVC SSPSISSTTS PKLDPPPSPH ANRKKHRRKK 490 500 510 520 530 540 STSNFKADGL SGTAEEQEEN FEFIIVSLTG QTWHFEATTY EERDAWVQAI ESQILASLQS 550 560 570 580 590 600 CESSKNKSRL TSQSEAMALQ SIRNMRGNSH CVDCETQNPN WASLNLGALM CIECSGIHRN 610 620 630 640 650 660 LGTHLSRVRS LDLDDWPVEL IKVMSSIGNE LANSVWEESS QGRTKPSVDS TREEKERWIR 670 680 690 700 710 720 AKYEQKLFLA PLPCTELSLG QHLLRATADE DLRTAILLLA HGSRDEVNET CGEGDGRTAL 730 740 750 760 770 780 HLACRKGNVV LAQLLIWYGV DVTARDAHGN TALAYARQAS SQECIDVLLQ YGCPDERFVL 790 800 MATPNLSRRN NNRNNSSGRV PTII
	Isoform 3. Checksum: 0B179759420981A9	FASTA	405	44,512
	10 20 30 40 50 60 MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV IAIEDAFVNS 70 80 90 100 110 120 QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL 130 140 150 160 170 180 LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD 190 200 210 220 230 240 AISSANPRVI DDARARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI 250 260 270 280 290 300 GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT 310 320 330 340 350 360 ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GLPFFVLALT 370 380 390 400 ASTYLRPAGA RARQSSPWPG PRGGQTSPHC AEGPQSAQLS GAMMN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"GGAPs, a new family of bifunctional GTP-binding and GTPase-activating proteins." Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M. Mol. Cell. Biol. 23:2476-2488(2003) [PubMed: 12640130] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-671, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION. Tissue: Heart.
[2]	"Kiaa1099 as a member (centaurin gamma2) of the centaurin ArfGAP protein family." Hong W. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-671.
[3]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed: 10470851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-671. Tissue: Brain.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 3), VARIANT GLY-148. Tissue: Placenta.
[6]	"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] OF 429-857 (ISOFORM 1), VARIANT ILE-671. Tissue: Teratocarcinoma.
[7]	"AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton." Nie Z., Stanley K.T., Stauffer S., Jacques K.M., Hirsch D.S., Takei J., Randazzo P.A. J. Biol. Chem. 277:48965-48975(2002) [PubMed: 12388557] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-647 AND ARG-652.
[8]	"Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1." Nie Z., Boehm M., Boja E.S., Vass W.C., Bonifacino J.S., Fales H.M., Randazzo P.A. Dev. Cell 5:513-521(2003) [PubMed: 12967569] [Abstract] Cited for: INTERACTION WITH THE AP-3 COMPLEX.
[9]	"AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase." Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S. J. Biol. Chem. 279:49346-49354(2004) [PubMed: 15381706] [Abstract] Cited for: SUBUNIT, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH GUCY1A3 AND GUCY1B3.
[10]	"The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3." Nie Z., Fei J., Premont R.T., Randazzo P.A. J. Cell Sci. 118:3555-3566(2005) [PubMed: 16079295] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"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 THR-836, MASS SPECTROMETRY.
[12]	"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-315, MASS SPECTROMETRY.
[13]	"Evaluation of the chromosome 2q37.3 gene CENTG2 as an autism susceptibility gene." Wassink T.H., Piven J., Vieland V.J., Jenkins L., Frantz R., Bartlett C.W., Goedken R., Childress D., Spence M.A., Smith M., Sheffield V.C. Am. J. Med. Genet. B Neuropsychiatr. Genet. 136:36-44(2005) [PubMed: 15892143] [Abstract] Cited for: VARIANTS GLY-82; ILE-671; GLY-798 AND THR-854.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY033765 mRNA. Translation: AAK56506.1. AF413078 mRNA. Translation: AAL04172.1. AB029022 mRNA. Translation: BAA83051.2. Different initiation. AC012305 Genomic DNA. No translation available. AC019047 Genomic DNA. No translation available. AC064874 Genomic DNA. No translation available. AC073989 Genomic DNA. No translation available. AC079400 Genomic DNA. No translation available. BC060814 mRNA. Translation: AAH60814.1. Sequence problems. BC140856 mRNA. Translation: AAI40857.1. AK001722 mRNA. Translation: BAA91862.1. Different initiation.
IPI	IPI00456242. IPI00456244. IPI00456246.
RefSeq	NP_001032208.1. NP_055729.2.
UniGene	Hs.435039
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UPQ3.
PTM databases
PhosphoSite	Q9UPQ3.
Genome annotation databases
Ensembl	ENST00000304032; ENSP00000307634; ENSG00000157985; Homo sapiens. [Genome view]
GeneID	116987.
KEGG	hsa:116987.
UCSC	uc002vvs.1. human. uc002vvt.1. human.
Organism-specific databases
CTD	116987.
GeneCards	GC02P236068.
H-InvDB	HIX0007225. HIX0008821. HIX0020594.
HGNC	HGNC:16922. AGAP1.
MIM	608651. gene.
PharmGKB	PA26412.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9UPQ3.
HOVERGEN	Q9UPQ3.
OrthoDB	EOG94F8VM
Gene expression databases
ArrayExpress	Q9UPQ3.
Bgee	Q9UPQ3.
CleanEx	HS_AGAP1.
Genevestigator	Q9UPQ3.
GermOnline	ENSG00000157985. Homo sapiens.
Family and domain databases
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR001164. ArfGAP. IPR013684. MIRO-like. IPR001849. Pleckstrin_homology. IPR005225. Small_GTP_bd. IPR020851. Small_GTPase. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit.
Pfam	PF00023. Ank. 2 hits. PF01412. ArfGap. 1 hit. PF08477. Miro. 1 hit. PF00169. PH. 1 hit. [Graphical view]
PRINTS	PR00405. REVINTRACTNG.
SMART	SM00248. ANK. 2 hits. SM00105. ArfGap. 1 hit. SM00233. PH. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. PS50115. ARFGAP. 1 hit. PS50003. PH_DOMAIN. 1 hit. PS51419. RAB. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	80074.
SOURCE	Search...

Entry information

Entry name

AGAP1_HUMAN

Accession

Primary (citable) accession number: Q9UPQ3
Secondary accession number(s): B2RTX7 , Q541S5, Q6P9D7, Q9NV93

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	November 13, 2007
Last modified:	November 24, 2009
This is version 99 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.