Q15057 (ACAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2

Alternative name(s):
Centaurin-beta-2
Short name=Cnt-b2

Gene names

Name:	ACAP2
Synonyms:	CENTB2, KIAA0041

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

General annotation (Comments)

Function	GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6). Ref.1
Enzyme regulation	GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid. Ref.1
Tissue specificity	Widely expressed. Highest level in lung. Ref.1
Sequence similarities	Contains 3 ANK repeats. Contains 1 Arf-GAP domain. Contains 1 BAR domain. Contains 1 PH domain.
Sequence caution	The sequence BAA05064.2 differs from that shown. Reason: Erroneous initiation. The sequence CAB41450.1 differs from that shown. Reason: Frameshift at positions 98, 106 and 111.

Ontologies

Keywords
Domain	ANK repeat Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
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 ARF GTPase activity Inferred from electronic annotation. Source: InterPro
Molecular_function	ARF GTPase activator activity Inferred from electronic annotation. Source: InterPro phospholipid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 778	778	Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2		PRO_0000074210
Regions
	Domain	1 – 226	226	BAR
	Domain	266 – 361	96	PH
	Domain	399 – 520	122	Arf-GAP
	Repeat	640 – 669	30	ANK 1
	Repeat	673 – 702	30	ANK 2
	Repeat	706 – 735	30	ANK 3
	Zinc finger	414 – 437	24	C4-type
Amino acid modifications
	Modified residue	384	1	Phosphoserine Ref.8
	Modified residue	521	1	Phosphoserine Ref.10
	Modified residue	742	1	Phosphotyrosine Ref.7
Experimental info
	Mutagenesis	442	1	R → Q: Loss of GAP activity. Ref.1
	Sequence conflict	5	1	V → G in CAB41450. Ref.1
	Sequence conflict	42	1	C → G in CAB41450. Ref.1
	Sequence conflict	229	1	V → G in CAB41450. Ref.1
	Sequence conflict	252	1	S → R in CAB41450. Ref.1
	Sequence conflict	258	1	E → K in CAB41450. Ref.1
	Sequence conflict	296	1	L → V in CAB41450. Ref.1
	Sequence conflict	564	1	G → E in AAH60767. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q15057 [UniParc]. Last modified December 15, 2003. Version 3. Checksum: 64B620957FEE6195	FASTA	778	88,029
	10 20 30 40 50 60 MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM 70 80 90 100 110 120 NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF 130 140 150 160 170 180 KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL 190 200 210 220 230 240 QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ 250 260 270 280 290 300 KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK 310 320 330 340 350 360 KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI 370 380 390 400 410 420 ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NASCCDCGLA 430 440 450 460 470 480 DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE 490 500 510 520 530 540 ANVEKMGIKK PQPGQRQEKE AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS 550 560 570 580 590 600 ISKFGPGDQV RASAQSSVRS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSMFLD 610 620 630 640 650 660 SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL GGSLVTCEFL 670 680 690 700 710 720 LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ HATDEEGKDP LSIAVEAANA 730 740 750 760 770 DIVTLLRLAR MNEEMRESEG LYGQPGDETY QDIFRDFSQM ASNNPEKLNR FQQDSQKF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ACAPs are arf6 GTPase-activating proteins that function in the cell periphery." Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., Hsu V.W., Donaldson J.G., Randazzo P.A. J. Cell Biol. 151:627-638(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-442. Tissue: Leukocyte.
[2]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[3]	Ohara O., Nagase T., Kikuno R., Nomura N. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[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]. Tissue: Tongue.
[5]	Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Brain and Placenta.
[7]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-742, MASS SPECTROMETRY.
[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-384, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, 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].
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ238248 mRNA. Translation: CAB41450.1. Frameshift. D26069 mRNA. Translation: BAA05064.2. Different initiation. AK290369 mRNA. Translation: BAF83058.1. CH471052 Genomic DNA. Translation: EAW78027.1. BC031005 mRNA. Translation: AAH31005.1. BC060767 mRNA. Translation: AAH60767.1.
IPI	IPI00014264.
RefSeq	NP_036419.3. NM_012287.5.
UniGene	Hs.593373.
3D structure databases
ProteinModelPortal	Q15057.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15057. 1 interaction.
STRING	9606.ENSP00000324287.
PTM databases
PhosphoSite	Q15057.
Polymorphism databases
DMDM	39932727.
Proteomic databases
PaxDb	Q15057.
PeptideAtlas	Q15057.
PRIDE	Q15057.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326793; ENSP00000324287; ENSG00000114331.
GeneID	23527.
KEGG	hsa:23527.
UCSC	uc003fun.4. human.
Organism-specific databases
CTD	23527.
GeneCards	GC03M194995.
HGNC	HGNC:16469. ACAP2.
HPA	HPA034807. HPA034808.
MIM	607766. gene.
neXtProt	NX_Q15057.
PharmGKB	PA26407.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5347.
HOGENOM	HOG000220815.
HOVERGEN	HBG050889.
InParanoid	Q15057.
KO	K12489.
OMA	SGIQQCS.
OrthoDB	EOG48SGSK.
PhylomeDB	Q15057.
Enzyme and pathway databases
Pathway_Interaction_DB	arf6cyclingpathway. Arf6 signaling events.
Gene expression databases
ArrayExpress	Q15057.
Bgee	Q15057.
CleanEx	HS_ACAP2.
Genevestigator	Q15057.
GermOnline	ENSG00000114331. Homo sapiens.
Family and domain databases
Gene3D	1.20.1270.60. 1 hit. 1.25.40.20. 1 hit. 2.30.29.30. 1 hit.
InterPro	IPR027267. AH/BAR-dom. IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR001164. ArfGAP. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. [Graphical view]
Pfam	PF00023. Ank. 2 hits. PF01412. ArfGap. 1 hit. PF00169. PH. 1 hit. [Graphical view]
PRINTS	PR00405. REVINTRACTNG.
SMART	SM00248. ANK. 3 hits. SM00105. ArfGap. 1 hit. SM00233. PH. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 2 hits. PS50115. ARFGAP. 1 hit. PS51021. BAR. False negative. PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ACAP2. human.
GenomeRNAi	23527.
NextBio	45992.
SOURCE	Search...

Entry information

Entry name

ACAP2_HUMAN

Accession

Primary (citable) accession number: Q15057
Secondary accession number(s): A8K2V4, Q8N5Z8, Q9UQR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	December 15, 2003
Last modified:	May 1, 2013
This is version 132 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.