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Protein

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

Gene

ACAP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6).1 Publication

Enzyme regulationi

GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri414 – 43724C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ARF GTPase activator activity Source: InterPro
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to nerve growth factor stimulus Source: UniProtKB
  2. protein localization to endosome Source: UniProtKB
  3. regulation of ARF GTPase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:ACAP2
Synonyms:CENTB2, KIAA0041
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:16469. ACAP2.

Subcellular locationi

Endosome membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. endosome membrane Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi442 – 4421R → Q: Loss of GAP activity. 1 Publication

Organism-specific databases

PharmGKBiPA26407.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 778778Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2PRO_0000074210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei384 – 3841Phosphoserine1 Publication
Modified residuei521 – 5211Phosphoserine1 Publication
Modified residuei742 – 7421Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15057.
PaxDbiQ15057.
PeptideAtlasiQ15057.
PRIDEiQ15057.

PTM databases

PhosphoSiteiQ15057.

Expressioni

Tissue specificityi

Widely expressed. Highest level in lung.1 Publication

Gene expression databases

BgeeiQ15057.
CleanExiHS_ACAP2.
ExpressionAtlasiQ15057. baseline and differential.
GenevestigatoriQ15057.

Organism-specific databases

HPAiHPA034807.
HPA034808.

Interactioni

Subunit structurei

Interacts with RAB35 (GTP-bound form); the interaction is direct and probably recruits ACAP2 to membranes. Interacts with MICALL1; the interaction is indirect through RAB35 (By similarity).By similarity

Protein-protein interaction databases

BioGridi117073. 4 interactions.
IntActiQ15057. 2 interactions.
STRINGi9606.ENSP00000324287.

Structurei

3D structure databases

ProteinModelPortaliQ15057.
SMRiQ15057. Positions 7-360, 378-758.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 226226BARAdd
BLAST
Domaini266 – 36196PHPROSITE-ProRule annotationAdd
BLAST
Domaini399 – 520122Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Repeati640 – 66930ANK 1Add
BLAST
Repeati673 – 70230ANK 2Add
BLAST
Repeati706 – 73530ANK 3Add
BLAST

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation
Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
Contains 1 BAR domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri414 – 43724C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000220815.
HOVERGENiHBG050889.
InParanoidiQ15057.
KOiK12489.
OMAiQHATDED.
OrthoDBiEOG7PVWNT.
PhylomeDBiQ15057.
TreeFamiTF318315.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15057-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK
60 70 80 90 100
AFCVANKQFM NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ
110 120 130 140 150
TQRSIKAQLQ NFVKEDLRKF KDAKKQFEKV SEEKENALVK NAQVQRNKQH
160 170 180 190 200
EVEEATNILT ATRKCFRHIA LDYVLQINVL QSKRRSEILK SMLSFMYAHL
210 220 230 240 250
AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ KHSTIQQKDF
260 270 280 290 300
SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
310 320 330 340 350
KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ
360 370 380 390 400
AWIKAVQTSI ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES
410 420 430 440 450
ALQRVQCIPG NASCCDCGLA DPRWASINLG ITLCIECSGI HRSLGVHFSK
460 470 480 490 500
VRSLTLDTWE PELLKLMCEL GNDVINRVYE ANVEKMGIKK PQPGQRQEKE
510 520 530 540 550
AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS ISKFGPGDQV
560 570 580 590 600
RASAQSSVRS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSMFLD
610 620 630 640 650
SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL
660 670 680 690 700
GGSLVTCEFL LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ
710 720 730 740 750
HATDEEGKDP LSIAVEAANA DIVTLLRLAR MNEEMRESEG LYGQPGDETY
760 770
QDIFRDFSQM ASNNPEKLNR FQQDSQKF
Length:778
Mass (Da):88,029
Last modified:December 15, 2003 - v3
Checksum:i64B620957FEE6195
GO

Sequence cautioni

The sequence BAA05064.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB41450.1 differs from that shown. Reason: Frameshift at positions 98, 106 and 111. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51V → G in CAB41450. (PubMed:11062263)Curated
Sequence conflicti42 – 421C → G in CAB41450. (PubMed:11062263)Curated
Sequence conflicti229 – 2291V → G in CAB41450. (PubMed:11062263)Curated
Sequence conflicti252 – 2521S → R in CAB41450. (PubMed:11062263)Curated
Sequence conflicti258 – 2581E → K in CAB41450. (PubMed:11062263)Curated
Sequence conflicti296 – 2961L → V in CAB41450. (PubMed:11062263)Curated
Sequence conflicti564 – 5641G → E in AAH60767. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33924.1.
RefSeqiNP_036419.3. NM_012287.5.
UniGeneiHs.593373.

Genome annotation databases

EnsembliENST00000326793; ENSP00000324287; ENSG00000114331.
GeneIDi23527.
KEGGihsa:23527.
UCSCiuc003fun.4. human.

Polymorphism databases

DMDMi39932727.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33924.1.
RefSeqiNP_036419.3. NM_012287.5.
UniGeneiHs.593373.

3D structure databases

ProteinModelPortaliQ15057.
SMRiQ15057. Positions 7-360, 378-758.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117073. 4 interactions.
IntActiQ15057. 2 interactions.
STRINGi9606.ENSP00000324287.

PTM databases

PhosphoSiteiQ15057.

Polymorphism databases

DMDMi39932727.

Proteomic databases

MaxQBiQ15057.
PaxDbiQ15057.
PeptideAtlasiQ15057.
PRIDEiQ15057.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326793; ENSP00000324287; ENSG00000114331.
GeneIDi23527.
KEGGihsa:23527.
UCSCiuc003fun.4. human.

Organism-specific databases

CTDi23527.
GeneCardsiGC03M194995.
HGNCiHGNC:16469. ACAP2.
HPAiHPA034807.
HPA034808.
MIMi607766. gene.
neXtProtiNX_Q15057.
PharmGKBiPA26407.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000220815.
HOVERGENiHBG050889.
InParanoidiQ15057.
KOiK12489.
OMAiQHATDED.
OrthoDBiEOG7PVWNT.
PhylomeDBiQ15057.
TreeFamiTF318315.

Miscellaneous databases

ChiTaRSiACAP2. human.
GeneWikiiCENTB2.
GenomeRNAii23527.
NextBioi45992.
PROiQ15057.
SOURCEiSearch...

Gene expression databases

BgeeiQ15057.
CleanExiHS_ACAP2.
ExpressionAtlasiQ15057. baseline and differential.
GenevestigatoriQ15057.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.
  11. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACAP2_HUMAN
AccessioniPrimary (citable) accession number: Q15057
Secondary accession number(s): A8K2V4, Q8N5Z8, Q9UQR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 2003
Last modified: January 7, 2015
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.