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 27-MAR-2024, entry version 189. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 66. DR IntAct; P40123; 28. 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; 9606-ENSP00000229922; -. DR PeptideAtlas; P40123; -. DR ProteomicsDB; 55334; -. [P40123-1] DR ProteomicsDB; 6318; -. DR ProteomicsDB; 6395; -. DR Pumba; P40123; -. DR TopDownProteomics; P40123-1; -. [P40123-1] DR Antibodypedia; 25070; 231 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 AGR; HGNC:20039; -. 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; HEDRNDL; -. DR OrthoDB; 1453907at2759; -. 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; 11 hits in 1147 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 188 other cell types or tissues. DR ExpressionAtlas; P40123; baseline and differential. 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:0007015; P:actin filament organization; IBA:GO_Central. 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:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc. DR GO; GO:0099140; P:presynaptic actin cytoskeleton organization; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR Gene3D; 2.160.20.70; -; 1. DR Gene3D; 1.25.40.330; Adenylate cyclase-associated CAP, N-terminal domain; 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; 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; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR10652:SF2; ADENYLYL CYCLASE-ASSOCIATED PROTEIN 2; 1. DR Pfam; PF08603; CAP_C; 1. DR Pfam; PF01213; CAP_N; 1. DR SMART; SM00673; CARP; 2. DR SUPFAM; SSF69340; C-terminal domain of adenylylcyclase associated protein; 1. DR SUPFAM; SSF101278; N-terminal domain of adenylylcyclase associated protein, CAP; 1. DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1. DR PROSITE; PS01088; CAP_1; 1. DR PROSITE; PS01089; CAP_2; 1. DR Genevisible; P40123; HS. 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 //