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NECP2_HUMAN
ID   NECP2_HUMAN             Reviewed;         263 AA.
AC   Q9NVZ3; B4DY19; E9PGQ8; Q5VSU4; Q5VSU5; Q9H7L1; Q9H8L1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Adaptin ear-binding coat-associated protein 2;
DE   AltName: Full=NECAP endocytosis-associated protein 2;
DE            Short=NECAP-2;
GN   Name=NECAP2;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Spleen;
RX   PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA   Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT   "Characterization of long cDNA clones from human adult spleen.";
RL   DNA Res. 7:357-366(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   TISSUE=Placenta, Spleen, and Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, and Eye;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   IDENTIFICATION BY 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).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Involved in endocytosis. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with AP1G1 and AP2A1 components of the adapter
CC       protein complexes AP-1 and AP-2. Interacts with the GAE domain proteins
CC       GGA1, GGA2 and GGA3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes
CC       with AP-2 at the plasma membrane. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9NVZ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NVZ3-2; Sequence=VSP_013236;
CC       Name=3;
CC         IsoId=Q9NVZ3-3; Sequence=VSP_013234, VSP_013235;
CC       Name=4;
CC         IsoId=Q9NVZ3-4; Sequence=VSP_041726;
CC   -!- DOMAIN: The WXXF motifs mediate binding of accessory proteins to the
CC       ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions.
CC       Selective binding to the GAE domains of AP-1 or to the alpha-ear domain
CC       of AP-2 is tuned by the acidic context surrounding the motif and the
CC       properties of the second residue of the motif itself (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NECAP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15758.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK024468; BAB15758.1; ALT_INIT; mRNA.
DR   EMBL; AK302227; BAG63581.1; -; mRNA.
DR   EMBL; AK001282; BAA91598.1; -; mRNA.
DR   EMBL; AK023545; BAB14605.1; -; mRNA.
DR   EMBL; AL137802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL669962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC017014; AAH17014.1; -; mRNA.
DR   EMBL; BC018914; AAH18914.1; -; mRNA.
DR   CCDS; CCDS173.1; -. [Q9NVZ3-1]
DR   CCDS; CCDS44066.1; -. [Q9NVZ3-2]
DR   CCDS; CCDS44067.1; -. [Q9NVZ3-4]
DR   RefSeq; NP_001138749.1; NM_001145277.1. [Q9NVZ3-2]
DR   RefSeq; NP_001138750.1; NM_001145278.1. [Q9NVZ3-4]
DR   RefSeq; NP_060560.1; NM_018090.4. [Q9NVZ3-1]
DR   AlphaFoldDB; Q9NVZ3; -.
DR   SMR; Q9NVZ3; -.
DR   BioGRID; 120832; 43.
DR   IntAct; Q9NVZ3; 23.
DR   STRING; 9606.ENSP00000391942; -.
DR   GlyGen; Q9NVZ3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NVZ3; -.
DR   MetOSite; Q9NVZ3; -.
DR   PhosphoSitePlus; Q9NVZ3; -.
DR   BioMuta; NECAP2; -.
DR   DMDM; 62287168; -.
DR   EPD; Q9NVZ3; -.
DR   jPOST; Q9NVZ3; -.
DR   MassIVE; Q9NVZ3; -.
DR   MaxQB; Q9NVZ3; -.
DR   PaxDb; Q9NVZ3; -.
DR   PeptideAtlas; Q9NVZ3; -.
DR   PRIDE; Q9NVZ3; -.
DR   ProteomicsDB; 82880; -. [Q9NVZ3-1]
DR   ProteomicsDB; 82881; -. [Q9NVZ3-2]
DR   ProteomicsDB; 82882; -. [Q9NVZ3-3]
DR   ProteomicsDB; 82883; -. [Q9NVZ3-4]
DR   Antibodypedia; 29202; 64 antibodies from 22 providers.
DR   DNASU; 55707; -.
DR   Ensembl; ENST00000337132.10; ENSP00000338746.5; ENSG00000157191.20. [Q9NVZ3-1]
DR   Ensembl; ENST00000443980.6; ENSP00000391942.2; ENSG00000157191.20. [Q9NVZ3-2]
DR   Ensembl; ENST00000457722.6; ENSP00000407091.2; ENSG00000157191.20. [Q9NVZ3-4]
DR   Ensembl; ENST00000492095.5; ENSP00000427620.1; ENSG00000157191.20. [Q9NVZ3-1]
DR   GeneID; 55707; -.
DR   KEGG; hsa:55707; -.
DR   MANE-Select; ENST00000337132.10; ENSP00000338746.5; NM_018090.5; NP_060560.1.
DR   UCSC; uc001ayo.4; human. [Q9NVZ3-1]
DR   CTD; 55707; -.
DR   DisGeNET; 55707; -.
DR   GeneCards; NECAP2; -.
DR   HGNC; HGNC:25528; NECAP2.
DR   HPA; ENSG00000157191; Low tissue specificity.
DR   MIM; 611624; gene.
DR   neXtProt; NX_Q9NVZ3; -.
DR   OpenTargets; ENSG00000157191; -.
DR   PharmGKB; PA142671268; -.
DR   VEuPathDB; HostDB:ENSG00000157191; -.
DR   eggNOG; KOG2500; Eukaryota.
DR   GeneTree; ENSGT00390000009359; -.
DR   HOGENOM; CLU_069884_1_0_1; -.
DR   InParanoid; Q9NVZ3; -.
DR   OMA; NEGHRAQ; -.
DR   OrthoDB; 1605812at2759; -.
DR   PhylomeDB; Q9NVZ3; -.
DR   TreeFam; TF314482; -.
DR   PathwayCommons; Q9NVZ3; -.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR   SignaLink; Q9NVZ3; -.
DR   BioGRID-ORCS; 55707; 6 hits in 1074 CRISPR screens.
DR   ChiTaRS; NECAP2; human.
DR   GeneWiki; NECAP2; -.
DR   GenomeRNAi; 55707; -.
DR   Pharos; Q9NVZ3; Tdark.
DR   PRO; PR:Q9NVZ3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9NVZ3; protein.
DR   Bgee; ENSG00000157191; Expressed in oocyte and 177 other tissues.
DR   ExpressionAtlas; Q9NVZ3; baseline and differential.
DR   Genevisible; Q9NVZ3; HS.
DR   GO; GO:0030125; C:clathrin vesicle coat; ISS:UniProtKB.
DR   GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd13228; PHear_NECAP; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR012466; NECAP_PHear.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   Pfam; PF07933; DUF1681; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasmic vesicle; Endocytosis;
KW   Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN           1..263
FT                   /note="Adaptin ear-binding coat-associated protein 2"
FT                   /id="PRO_0000213071"
FT   REGION          166..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           240..243
FT                   /note="WXXF motif 1"
FT   MOTIF           260..263
FT                   /note="WXXF motif 2"
FT   COMPBIAS        240..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         6..31
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041726"
FT   VAR_SEQ         164..172
FT                   /note="NMKKKEGAA -> VSSTLAWLW (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11214971"
FT                   /id="VSP_013234"
FT   VAR_SEQ         173..263
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11214971"
FT                   /id="VSP_013235"
FT   VAR_SEQ         223..263
FT                   /note="GGAPVPWPQPNPATADIWGDFTKSTGSTSSQTQPGTGWVQF -> DQLPARP
FT                   SQAQAGSSSDLSTVFPHVTSGKALPHLGQRKEDEALLSWPVFGA (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_013236"
FT   VARIANT         149
FT                   /note="D -> A (in dbSNP:rs35056694)"
FT                   /id="VAR_034154"
FT   CONFLICT        192
FT                   /note="P -> S (in Ref. 2; BAG63581)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   263 AA;  28339 MW;  6F4DE1B8335852D4 CRC64;
     MEESGYESVL CVKPDVHVYR IPPRATNRGY RAAEWQLDQP SWSGRLRITA KGQMAYIKLE
     DRTSGELFAQ APVDQFPGTA VESVTDSSRY FVIRIEDGNG RRAFIGIGFG DRGDAFDFNV
     ALQDHFKWVK QQCEFAKQAQ NPDQGPKLDL GFKEGQTIKL NIANMKKKEG AAGNPRVRPA
     STGGLSLLPP PPGGKTSTLI PPPGEQLAVG GSLVQPAVAP SSGGAPVPWP QPNPATADIW
     GDFTKSTGST SSQTQPGTGW VQF
 
 
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