Full text data of NECAP2
NECAP2
[Confidence: low (only semi-automatic identification from reviews)]
Adaptin ear-binding coat-associated protein 2 (NECAP endocytosis-associated protein 2; NECAP-2)
Adaptin ear-binding coat-associated protein 2 (NECAP endocytosis-associated protein 2; NECAP-2)
UniProt
Q9NVZ3
ID NECP2_HUMAN Reviewed; 263 AA.
AC Q9NVZ3; B4DY19; E9PGQ8; Q5VSU4; Q5VSU5; Q9H7L1; Q9H8L1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 99.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Involved in endocytosis (By similarity).
CC -!- SUBUNIT: Interacts with AP1G1 and AP2A1 components of the adapter
CC protein complexes AP-1 and AP-2. Interacts with the GAE domain
CC proteins GGA1, GGA2 and GGA3 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane (By similarity). Cell membrane (By similarity).
CC Note=Colocalizes with AP-2 at the plasma membrane (By similarity).
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 Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NVZ3-4; Sequence=VSP_041726;
CC -!- DOMAIN: The WXXF motifs mediate binding of accessory proteins to
CC the ear-domain of AP-1, GGAs and AP-2 through hydrophobic
CC interactions. Selective binding to the GAE domains of AP-1 or to
CC the alpha-ear domain of AP-2 is tuned by the acidic context
CC surrounding the motif and the properties of the second residue of
CC the motif itself (By similarity).
CC -!- SIMILARITY: Belongs to the NECAP family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15758.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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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; AL669962; CAH71454.1; -; Genomic_DNA.
DR EMBL; AL137802; CAH71454.1; JOINED; Genomic_DNA.
DR EMBL; AL137802; CAI22843.1; -; Genomic_DNA.
DR EMBL; AL669962; CAI22843.1; JOINED; Genomic_DNA.
DR EMBL; BC017014; AAH17014.1; -; mRNA.
DR EMBL; BC018914; AAH18914.1; -; mRNA.
DR RefSeq; NP_001138749.1; NM_001145277.1.
DR RefSeq; NP_001138750.1; NM_001145278.1.
DR RefSeq; NP_060560.1; NM_018090.4.
DR UniGene; Hs.437385; -.
DR ProteinModelPortal; Q9NVZ3; -.
DR SMR; Q9NVZ3; 3-132.
DR IntAct; Q9NVZ3; 7.
DR MINT; MINT-1468695; -.
DR STRING; 9606.ENSP00000263498; -.
DR PhosphoSite; Q9NVZ3; -.
DR DMDM; 62287168; -.
DR PaxDb; Q9NVZ3; -.
DR PRIDE; Q9NVZ3; -.
DR DNASU; 55707; -.
DR Ensembl; ENST00000337132; ENSP00000338746; ENSG00000157191.
DR Ensembl; ENST00000406746; ENSP00000383925; ENSG00000157191.
DR Ensembl; ENST00000443980; ENSP00000391942; ENSG00000157191.
DR Ensembl; ENST00000457722; ENSP00000407091; ENSG00000157191.
DR Ensembl; ENST00000492095; ENSP00000427620; ENSG00000157191.
DR GeneID; 55707; -.
DR KEGG; hsa:55707; -.
DR UCSC; uc001ayo.3; human.
DR CTD; 55707; -.
DR GeneCards; GC01P016767; -.
DR HGNC; HGNC:25528; NECAP2.
DR HPA; HPA028077; -.
DR MIM; 611624; gene.
DR neXtProt; NX_Q9NVZ3; -.
DR PharmGKB; PA142671268; -.
DR eggNOG; NOG329551; -.
DR HOGENOM; HOG000231188; -.
DR HOVERGEN; HBG060621; -.
DR OMA; SWPQPKP; -.
DR OrthoDB; EOG76X61J; -.
DR GeneWiki; NECAP2; -.
DR GenomeRNAi; 55707; -.
DR NextBio; 60567; -.
DR PRO; PR:Q9NVZ3; -.
DR ArrayExpress; Q9NVZ3; -.
DR Bgee; Q9NVZ3; -.
DR CleanEx; HS_NECAP2; -.
DR Genevestigator; Q9NVZ3; -.
DR GO; GO:0030125; C:clathrin vesicle coat; ISS:UniProtKB.
DR GO; GO:0005905; C:coated pit; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012466; NECAP-1.
DR InterPro; IPR011993; PH_like_dom.
DR Pfam; PF07933; DUF1681; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome;
KW Cytoplasmic vesicle; Endocytosis; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1 263 Adaptin ear-binding coat-associated
FT protein 2.
FT /FTId=PRO_0000213071.
FT MOTIF 240 243 WXXF motif 1.
FT MOTIF 260 263 WXXF motif 2.
FT VAR_SEQ 6 31 Missing (in isoform 4).
FT /FTId=VSP_041726.
FT VAR_SEQ 164 172 NMKKKEGAA -> VSSTLAWLW (in isoform 3).
FT /FTId=VSP_013234.
FT VAR_SEQ 173 263 Missing (in isoform 3).
FT /FTId=VSP_013235.
FT VAR_SEQ 223 263 GGAPVPWPQPNPATADIWGDFTKSTGSTSSQTQPGTGWVQF
FT -> DQLPARPSQAQAGSSSDLSTVFPHVTSGKALPHLGQRK
FT EDEALLSWPVFGA (in isoform 2).
FT /FTId=VSP_013236.
FT VARIANT 149 149 D -> A (in dbSNP:rs35056694).
FT /FTId=VAR_034154.
FT CONFLICT 192 192 P -> S (in Ref. 2; BAG63581).
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
//
ID NECP2_HUMAN Reviewed; 263 AA.
AC Q9NVZ3; B4DY19; E9PGQ8; Q5VSU4; Q5VSU5; Q9H7L1; Q9H8L1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 99.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Involved in endocytosis (By similarity).
CC -!- SUBUNIT: Interacts with AP1G1 and AP2A1 components of the adapter
CC protein complexes AP-1 and AP-2. Interacts with the GAE domain
CC proteins GGA1, GGA2 and GGA3 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane (By similarity). Cell membrane (By similarity).
CC Note=Colocalizes with AP-2 at the plasma membrane (By similarity).
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 Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NVZ3-4; Sequence=VSP_041726;
CC -!- DOMAIN: The WXXF motifs mediate binding of accessory proteins to
CC the ear-domain of AP-1, GGAs and AP-2 through hydrophobic
CC interactions. Selective binding to the GAE domains of AP-1 or to
CC the alpha-ear domain of AP-2 is tuned by the acidic context
CC surrounding the motif and the properties of the second residue of
CC the motif itself (By similarity).
CC -!- SIMILARITY: Belongs to the NECAP family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15758.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; AL669962; CAH71454.1; -; Genomic_DNA.
DR EMBL; AL137802; CAH71454.1; JOINED; Genomic_DNA.
DR EMBL; AL137802; CAI22843.1; -; Genomic_DNA.
DR EMBL; AL669962; CAI22843.1; JOINED; Genomic_DNA.
DR EMBL; BC017014; AAH17014.1; -; mRNA.
DR EMBL; BC018914; AAH18914.1; -; mRNA.
DR RefSeq; NP_001138749.1; NM_001145277.1.
DR RefSeq; NP_001138750.1; NM_001145278.1.
DR RefSeq; NP_060560.1; NM_018090.4.
DR UniGene; Hs.437385; -.
DR ProteinModelPortal; Q9NVZ3; -.
DR SMR; Q9NVZ3; 3-132.
DR IntAct; Q9NVZ3; 7.
DR MINT; MINT-1468695; -.
DR STRING; 9606.ENSP00000263498; -.
DR PhosphoSite; Q9NVZ3; -.
DR DMDM; 62287168; -.
DR PaxDb; Q9NVZ3; -.
DR PRIDE; Q9NVZ3; -.
DR DNASU; 55707; -.
DR Ensembl; ENST00000337132; ENSP00000338746; ENSG00000157191.
DR Ensembl; ENST00000406746; ENSP00000383925; ENSG00000157191.
DR Ensembl; ENST00000443980; ENSP00000391942; ENSG00000157191.
DR Ensembl; ENST00000457722; ENSP00000407091; ENSG00000157191.
DR Ensembl; ENST00000492095; ENSP00000427620; ENSG00000157191.
DR GeneID; 55707; -.
DR KEGG; hsa:55707; -.
DR UCSC; uc001ayo.3; human.
DR CTD; 55707; -.
DR GeneCards; GC01P016767; -.
DR HGNC; HGNC:25528; NECAP2.
DR HPA; HPA028077; -.
DR MIM; 611624; gene.
DR neXtProt; NX_Q9NVZ3; -.
DR PharmGKB; PA142671268; -.
DR eggNOG; NOG329551; -.
DR HOGENOM; HOG000231188; -.
DR HOVERGEN; HBG060621; -.
DR OMA; SWPQPKP; -.
DR OrthoDB; EOG76X61J; -.
DR GeneWiki; NECAP2; -.
DR GenomeRNAi; 55707; -.
DR NextBio; 60567; -.
DR PRO; PR:Q9NVZ3; -.
DR ArrayExpress; Q9NVZ3; -.
DR Bgee; Q9NVZ3; -.
DR CleanEx; HS_NECAP2; -.
DR Genevestigator; Q9NVZ3; -.
DR GO; GO:0030125; C:clathrin vesicle coat; ISS:UniProtKB.
DR GO; GO:0005905; C:coated pit; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012466; NECAP-1.
DR InterPro; IPR011993; PH_like_dom.
DR Pfam; PF07933; DUF1681; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome;
KW Cytoplasmic vesicle; Endocytosis; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1 263 Adaptin ear-binding coat-associated
FT protein 2.
FT /FTId=PRO_0000213071.
FT MOTIF 240 243 WXXF motif 1.
FT MOTIF 260 263 WXXF motif 2.
FT VAR_SEQ 6 31 Missing (in isoform 4).
FT /FTId=VSP_041726.
FT VAR_SEQ 164 172 NMKKKEGAA -> VSSTLAWLW (in isoform 3).
FT /FTId=VSP_013234.
FT VAR_SEQ 173 263 Missing (in isoform 3).
FT /FTId=VSP_013235.
FT VAR_SEQ 223 263 GGAPVPWPQPNPATADIWGDFTKSTGSTSSQTQPGTGWVQF
FT -> DQLPARPSQAQAGSSSDLSTVFPHVTSGKALPHLGQRK
FT EDEALLSWPVFGA (in isoform 2).
FT /FTId=VSP_013236.
FT VARIANT 149 149 D -> A (in dbSNP:rs35056694).
FT /FTId=VAR_034154.
FT CONFLICT 192 192 P -> S (in Ref. 2; BAG63581).
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
//
MIM
611624
*RECORD*
*FIELD* NO
611624
*FIELD* TI
*611624 NECAP ENDOCYTOSIS-ASSOCIATED PROTEIN 2; NECAP2
;;ADAPTIN EAR-BINDING COAT-ASSOCIATED PROTEIN 2
read more*FIELD* TX
CLONING
Through a proteomic analysis of rat brain clathrin-coated vesicles,
Ritter et al. (2003) identified Necap2. The deduced 266-amino acid
protein contains a WVQF motif that was shown in rat Necap1 (611623) to
mediate binding to the alpha-adaptin subunit (AP2A1; 601026) of the
adaptor protein-2 (AP-2) complex. Western blot analysis detected broad
Necap2 expression in rat tissues.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NECAP2
gene to chromosome 1 (TMAP SHGC-74267).
*FIELD* RF
1. Ritter, B.; Philie, J.; Girard, M.; Tung, E. C.; Blondeau, F.;
McPherson, P. S.: Identification of a family of endocytic proteins
that define a new alpha-adaptin ear-binding motif. EMBO Reports 4:
1089-1095, 2003.
*FIELD* CD
Patricia A. Hartz: 11/26/2007
*FIELD* ED
mgross: 11/26/2007
*RECORD*
*FIELD* NO
611624
*FIELD* TI
*611624 NECAP ENDOCYTOSIS-ASSOCIATED PROTEIN 2; NECAP2
;;ADAPTIN EAR-BINDING COAT-ASSOCIATED PROTEIN 2
read more*FIELD* TX
CLONING
Through a proteomic analysis of rat brain clathrin-coated vesicles,
Ritter et al. (2003) identified Necap2. The deduced 266-amino acid
protein contains a WVQF motif that was shown in rat Necap1 (611623) to
mediate binding to the alpha-adaptin subunit (AP2A1; 601026) of the
adaptor protein-2 (AP-2) complex. Western blot analysis detected broad
Necap2 expression in rat tissues.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NECAP2
gene to chromosome 1 (TMAP SHGC-74267).
*FIELD* RF
1. Ritter, B.; Philie, J.; Girard, M.; Tung, E. C.; Blondeau, F.;
McPherson, P. S.: Identification of a family of endocytic proteins
that define a new alpha-adaptin ear-binding motif. EMBO Reports 4:
1089-1095, 2003.
*FIELD* CD
Patricia A. Hartz: 11/26/2007
*FIELD* ED
mgross: 11/26/2007