CAP2_HUMAN
ID CAP2_HUMAN Reviewed; 477 AA.
AC P40123; B2R5Y3; B7Z1C4; B7Z214; Q6IAY2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Adenylyl cyclase-associated protein 2;
DE Short=CAP 2;
GN Name=CAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7962207; DOI=10.1242/jcs.107.6.1671;
RA Yu G., Swiston J., Young D.;
RT "Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-
RT associated proteins.";
RL J. Cell Sci. 107:1671-1678(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May have a regulatory bifunctional role.
CC -!- INTERACTION:
CC P40123; P60709: ACTB; NbExp=5; IntAct=EBI-1051165, EBI-353944;
CC P40123; P63261: ACTG1; NbExp=12; IntAct=EBI-1051165, EBI-351292;
CC P40123; Q96SZ5: ADO; NbExp=3; IntAct=EBI-1051165, EBI-11102284;
CC P40123; P13196: ALAS1; NbExp=3; IntAct=EBI-1051165, EBI-3905054;
CC P40123; P40123: CAP2; NbExp=4; IntAct=EBI-1051165, EBI-1051165;
CC P40123; Q549N0: CFL2; NbExp=3; IntAct=EBI-1051165, EBI-10201319;
CC P40123; A8MXD5: GRXCR1; NbExp=3; IntAct=EBI-1051165, EBI-5235612;
CC P40123; Q1KLZ0: PS1TP5BP1; NbExp=3; IntAct=EBI-1051165, EBI-9978131;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P40123-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40123-2; Sequence=VSP_055520;
CC Name=3;
CC IsoId=P40123-3; Sequence=VSP_055519;
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; U02390; AAA20587.1; -; mRNA.
DR EMBL; CR457022; CAG33303.1; -; mRNA.
DR EMBL; AK294215; BAH11700.1; -; mRNA.
DR EMBL; AL034372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK293134; BAH11460.1; -; mRNA.
DR EMBL; AK312362; BAG35280.1; -; mRNA.
DR EMBL; CH471087; EAW55380.1; -; Genomic_DNA.
DR EMBL; BC008481; AAH08481.1; -; mRNA.
DR CCDS; CCDS4539.1; -. [P40123-1]
DR PIR; I38409; I38409.
DR RefSeq; NP_006357.1; NM_006366.2. [P40123-1]
DR AlphaFoldDB; P40123; -.
DR SMR; P40123; -.
DR BioGRID; 115749; 47.
DR IntAct; P40123; 25.
DR MINT; P40123; -.
DR STRING; 9606.ENSP00000229922; -.
DR GlyGen; P40123; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40123; -.
DR MetOSite; P40123; -.
DR PhosphoSitePlus; P40123; -.
DR BioMuta; CAP2; -.
DR DMDM; 729015; -.
DR EPD; P40123; -.
DR jPOST; P40123; -.
DR MassIVE; P40123; -.
DR MaxQB; P40123; -.
DR PaxDb; P40123; -.
DR PeptideAtlas; P40123; -.
DR PRIDE; P40123; -.
DR ProteomicsDB; 55334; -. [P40123-1]
DR ProteomicsDB; 6318; -.
DR ProteomicsDB; 6395; -.
DR TopDownProteomics; P40123-1; -. [P40123-1]
DR Antibodypedia; 25070; 210 antibodies from 25 providers.
DR DNASU; 10486; -.
DR Ensembl; ENST00000229922.7; ENSP00000229922.2; ENSG00000112186.13. [P40123-1]
DR Ensembl; ENST00000465994.5; ENSP00000418604.1; ENSG00000112186.13. [P40123-2]
DR Ensembl; ENST00000493172.5; ENSP00000417208.1; ENSG00000112186.13. [P40123-3]
DR GeneID; 10486; -.
DR KEGG; hsa:10486; -.
DR MANE-Select; ENST00000229922.7; ENSP00000229922.2; NM_006366.3; NP_006357.1.
DR UCSC; uc003ncb.4; human. [P40123-1]
DR CTD; 10486; -.
DR DisGeNET; 10486; -.
DR GeneCards; CAP2; -.
DR HGNC; HGNC:20039; CAP2.
DR HPA; ENSG00000112186; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; CAP2; -.
DR MIM; 618385; gene.
DR neXtProt; NX_P40123; -.
DR OpenTargets; ENSG00000112186; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR PharmGKB; PA134989437; -.
DR VEuPathDB; HostDB:ENSG00000112186; -.
DR eggNOG; KOG2675; Eukaryota.
DR GeneTree; ENSGT00390000017955; -.
DR HOGENOM; CLU_1271928_0_0_1; -.
DR InParanoid; P40123; -.
DR OMA; QQNHAPV; -.
DR PhylomeDB; P40123; -.
DR TreeFam; TF313791; -.
DR PathwayCommons; P40123; -.
DR Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
DR SignaLink; P40123; -.
DR BioGRID-ORCS; 10486; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; CAP2; human.
DR GeneWiki; CAP2; -.
DR GenomeRNAi; 10486; -.
DR Pharos; P40123; Tbio.
DR PRO; PR:P40123; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P40123; protein.
DR Bgee; ENSG00000112186; Expressed in skeletal muscle tissue of biceps brachii and 186 other tissues.
DR ExpressionAtlas; P40123; baseline and differential.
DR Genevisible; P40123; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
DR GO; GO:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.25.40.330; -; 1.
DR Gene3D; 2.160.20.70; -; 1.
DR InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR028418; CAP2.
DR InterPro; IPR036223; CAP_C_sf.
DR InterPro; IPR028417; CAP_CS_C.
DR InterPro; IPR018106; CAP_CS_N.
DR InterPro; IPR036222; CAP_N_sf.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; PTHR10652; 1.
DR PANTHER; PTHR10652:SF2; PTHR10652:SF2; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF01213; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF101278; SSF101278; 1.
DR SUPFAM; SSF69340; SSF69340; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR PROSITE; PS01088; CAP_1; 1.
DR PROSITE; PS01089; CAP_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..477
FT /note="Adenylyl cyclase-associated protein 2"
FT /id="PRO_0000205700"
FT DOMAIN 317..455
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 225..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52481"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 75..334
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055519"
FT VAR_SEQ 149..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055520"
FT VARIANT 311
FT /note="T -> A (in dbSNP:rs34620829)"
FT /id="VAR_033717"
FT VARIANT 316
FT /note="Y -> C (in dbSNP:rs34206659)"
FT /id="VAR_033718"
SQ SEQUENCE 477 AA; 52824 MW; 2FD3950C094F5AF7 CRC64;
MANMQGLVER LERAVSRLES LSAESHRPPG NCGEVNGVIA GVAPSVEAFD KLMDSMVAEF
LKNSRILAGD VETHAEMVHS AFQAQRAFLL MASQYQQPHE NDVAALLKPI SEKIQEIQTF
RERNRGSNMF NHLSAVSESI PALGWIAVSP KPGPYVKEMN DAATFYTNRV LKDYKHSDLR
HVDWVKSYLN IWSELQAYIK EHHTTGLTWS KTGPVASTVS AFSVLSSGPG LPPPPPPLPP
PGPPPLFENE GKKEESSPSR SALFAQLNQG EAITKGLRHV TDDQKTYKNP SLRAQGGQTQ
SPTKSHTPSP TSPKSYPSQK HAPVLELEGK KWRVEYQEDR NDLVISETEL KQVAYIFKCE
KSTIQIKGKV NSIIIDNCKK LGLVFDNVVG IVEVINSQDI QIQVMGRVPT ISINKTEGCH
IYLSEDALDC EIVSAKSSEM NILIPQDGDY REFPIPEQFK TAWDGSKLIT EPAEIMA
