Full text data of NECAP1
NECAP1
[Confidence: low (only semi-automatic identification from reviews)]
Adaptin ear-binding coat-associated protein 1 (NECAP endocytosis-associated protein 1; NECAP-1)
Adaptin ear-binding coat-associated protein 1 (NECAP endocytosis-associated protein 1; NECAP-1)
UniProt
Q8NC96
ID NECP1_HUMAN Reviewed; 275 AA.
AC Q8NC96; Q2NL73; Q5XG95; Q6NWY6; Q8N153; Q8NCB0; Q9BU52; Q9Y407;
read moreDT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 22-JAN-2014, entry version 82.
DE RecName: Full=Adaptin ear-binding coat-associated protein 1;
DE AltName: Full=NECAP endocytosis-associated protein 1;
DE Short=NECAP-1;
GN Name=NECAP1;
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 1).
RC TISSUE=Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, Lymph, and Muscle;
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 [4]
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=2;
CC Name=1;
CC IsoId=Q8NC96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NC96-2; Sequence=VSP_013232, VSP_013233;
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. The WXXF motif 1, which is preceded by an acidic
CC residue and has a glycine in second position mediates specific
CC interaction with AP-1. The WXXF motif 2, which is followed by the
CC C-terminal carboxyl group negative charge, allows specific
CC interaction with AP-2 (By similarity).
CC -!- SIMILARITY: Belongs to the NECAP family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02888.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK074858; BAC11250.1; -; mRNA.
DR EMBL; AK074880; BAC11264.1; -; mRNA.
DR EMBL; AK074923; BAC11296.1; -; mRNA.
DR EMBL; AK075013; BAC11352.1; -; mRNA.
DR EMBL; AL050272; CAB43373.2; -; mRNA.
DR EMBL; BC002888; AAH02888.1; ALT_INIT; mRNA.
DR EMBL; BC067367; AAH67367.1; -; mRNA.
DR EMBL; BC084551; AAH84551.1; -; mRNA.
DR EMBL; BC110876; AAI10877.1; -; mRNA.
DR PIR; T08719; T08719.
DR RefSeq; NP_056324.2; NM_015509.3.
DR UniGene; Hs.555927; -.
DR ProteinModelPortal; Q8NC96; -.
DR SMR; Q8NC96; 1-133.
DR IntAct; Q8NC96; 1.
DR STRING; 9606.ENSP00000341737; -.
DR PhosphoSite; Q8NC96; -.
DR DMDM; 62287155; -.
DR PaxDb; Q8NC96; -.
DR PRIDE; Q8NC96; -.
DR Ensembl; ENST00000339754; ENSP00000341737; ENSG00000089818.
DR Ensembl; ENST00000450991; ENSP00000401963; ENSG00000089818.
DR GeneID; 25977; -.
DR KEGG; hsa:25977; -.
DR UCSC; uc001qtx.2; human.
DR CTD; 25977; -.
DR GeneCards; GC12P008234; -.
DR HGNC; HGNC:24539; NECAP1.
DR MIM; 611623; gene.
DR neXtProt; NX_Q8NC96; -.
DR PharmGKB; PA142671267; -.
DR eggNOG; NOG329551; -.
DR HOVERGEN; HBG060621; -.
DR InParanoid; Q8NC96; -.
DR OMA; ESQEMDN; -.
DR OrthoDB; EOG76X61J; -.
DR PhylomeDB; Q8NC96; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; NECAP1; human.
DR GenomeRNAi; 25977; -.
DR NextBio; 47626; -.
DR PRO; PR:Q8NC96; -.
DR ArrayExpress; Q8NC96; -.
DR Bgee; Q8NC96; -.
DR CleanEx; HS_NECAP1; -.
DR Genevestigator; Q8NC96; -.
DR GO; GO:0030125; C:clathrin vesicle coat; IEA:Ensembl.
DR GO; GO:0005905; C:coated pit; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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 1 275 Adaptin ear-binding coat-associated
FT protein 1.
FT /FTId=PRO_0000213067.
FT MOTIF 252 255 WXXF motif 1.
FT MOTIF 272 275 WXXF motif 2.
FT VAR_SEQ 102 102 R -> G (in isoform 2).
FT /FTId=VSP_013232.
FT VAR_SEQ 103 275 Missing (in isoform 2).
FT /FTId=VSP_013233.
FT VARIANT 224 224 D -> N (in dbSNP:rs2231752).
FT /FTId=VAR_034153.
FT CONFLICT 77 77 Y -> F (in Ref. 2; CAB43373).
FT CONFLICT 232 232 D -> G (in Ref. 1; BAC11250).
FT CONFLICT 239 239 T -> A (in Ref. 1; BAC11264).
SQ SEQUENCE 275 AA; 29737 MW; 22FC4CCEC7E3B713 CRC64;
MATELEYESV LCVKPDVSVY RIPPRASNRG YRASDWKLDQ PDWTGRLRIT SKGKTAYIKL
EDKVSGELFA QAPVEQYPGI AVETVTDSSR YFVIRIQDGT GRSAFIGIGF TDRGDAFDFN
VSLQDHFKWV KQESEISKES QEMDARPKLD LGFKEGQTIK LCIGNITNKK GGASKPRTAR
GGGLSLLPPP PGGKVTIPPP SSSVAISNHV TPPPIPKSNH GGSDADILLD LDSPAPVTTP
APTPVSVSND LWGDFSTASS SVPNQAPQPS NWVQF
//
ID NECP1_HUMAN Reviewed; 275 AA.
AC Q8NC96; Q2NL73; Q5XG95; Q6NWY6; Q8N153; Q8NCB0; Q9BU52; Q9Y407;
read moreDT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 22-JAN-2014, entry version 82.
DE RecName: Full=Adaptin ear-binding coat-associated protein 1;
DE AltName: Full=NECAP endocytosis-associated protein 1;
DE Short=NECAP-1;
GN Name=NECAP1;
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 1).
RC TISSUE=Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, Lymph, and Muscle;
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 [4]
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=2;
CC Name=1;
CC IsoId=Q8NC96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NC96-2; Sequence=VSP_013232, VSP_013233;
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. The WXXF motif 1, which is preceded by an acidic
CC residue and has a glycine in second position mediates specific
CC interaction with AP-1. The WXXF motif 2, which is followed by the
CC C-terminal carboxyl group negative charge, allows specific
CC interaction with AP-2 (By similarity).
CC -!- SIMILARITY: Belongs to the NECAP family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02888.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK074858; BAC11250.1; -; mRNA.
DR EMBL; AK074880; BAC11264.1; -; mRNA.
DR EMBL; AK074923; BAC11296.1; -; mRNA.
DR EMBL; AK075013; BAC11352.1; -; mRNA.
DR EMBL; AL050272; CAB43373.2; -; mRNA.
DR EMBL; BC002888; AAH02888.1; ALT_INIT; mRNA.
DR EMBL; BC067367; AAH67367.1; -; mRNA.
DR EMBL; BC084551; AAH84551.1; -; mRNA.
DR EMBL; BC110876; AAI10877.1; -; mRNA.
DR PIR; T08719; T08719.
DR RefSeq; NP_056324.2; NM_015509.3.
DR UniGene; Hs.555927; -.
DR ProteinModelPortal; Q8NC96; -.
DR SMR; Q8NC96; 1-133.
DR IntAct; Q8NC96; 1.
DR STRING; 9606.ENSP00000341737; -.
DR PhosphoSite; Q8NC96; -.
DR DMDM; 62287155; -.
DR PaxDb; Q8NC96; -.
DR PRIDE; Q8NC96; -.
DR Ensembl; ENST00000339754; ENSP00000341737; ENSG00000089818.
DR Ensembl; ENST00000450991; ENSP00000401963; ENSG00000089818.
DR GeneID; 25977; -.
DR KEGG; hsa:25977; -.
DR UCSC; uc001qtx.2; human.
DR CTD; 25977; -.
DR GeneCards; GC12P008234; -.
DR HGNC; HGNC:24539; NECAP1.
DR MIM; 611623; gene.
DR neXtProt; NX_Q8NC96; -.
DR PharmGKB; PA142671267; -.
DR eggNOG; NOG329551; -.
DR HOVERGEN; HBG060621; -.
DR InParanoid; Q8NC96; -.
DR OMA; ESQEMDN; -.
DR OrthoDB; EOG76X61J; -.
DR PhylomeDB; Q8NC96; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; NECAP1; human.
DR GenomeRNAi; 25977; -.
DR NextBio; 47626; -.
DR PRO; PR:Q8NC96; -.
DR ArrayExpress; Q8NC96; -.
DR Bgee; Q8NC96; -.
DR CleanEx; HS_NECAP1; -.
DR Genevestigator; Q8NC96; -.
DR GO; GO:0030125; C:clathrin vesicle coat; IEA:Ensembl.
DR GO; GO:0005905; C:coated pit; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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 1 275 Adaptin ear-binding coat-associated
FT protein 1.
FT /FTId=PRO_0000213067.
FT MOTIF 252 255 WXXF motif 1.
FT MOTIF 272 275 WXXF motif 2.
FT VAR_SEQ 102 102 R -> G (in isoform 2).
FT /FTId=VSP_013232.
FT VAR_SEQ 103 275 Missing (in isoform 2).
FT /FTId=VSP_013233.
FT VARIANT 224 224 D -> N (in dbSNP:rs2231752).
FT /FTId=VAR_034153.
FT CONFLICT 77 77 Y -> F (in Ref. 2; CAB43373).
FT CONFLICT 232 232 D -> G (in Ref. 1; BAC11250).
FT CONFLICT 239 239 T -> A (in Ref. 1; BAC11264).
SQ SEQUENCE 275 AA; 29737 MW; 22FC4CCEC7E3B713 CRC64;
MATELEYESV LCVKPDVSVY RIPPRASNRG YRASDWKLDQ PDWTGRLRIT SKGKTAYIKL
EDKVSGELFA QAPVEQYPGI AVETVTDSSR YFVIRIQDGT GRSAFIGIGF TDRGDAFDFN
VSLQDHFKWV KQESEISKES QEMDARPKLD LGFKEGQTIK LCIGNITNKK GGASKPRTAR
GGGLSLLPPP PGGKVTIPPP SSSVAISNHV TPPPIPKSNH GGSDADILLD LDSPAPVTTP
APTPVSVSND LWGDFSTASS SVPNQAPQPS NWVQF
//
MIM
611623
*RECORD*
*FIELD* NO
611623
*FIELD* TI
*611623 NECAP ENDOCYTOSIS-ASSOCIATED PROTEIN 1; NECAP1
;;ADAPTIN EAR-BINDING COAT-ASSOCIATED PROTEIN 1
read more*FIELD* TX
CLONING
Through a proteomic analysis of rat brain clathrin-coated vesicles,
Ritter et al. (2003) identified Necap1. The deduced protein contains 275
amino acids. Western blot analysis detected Necap1 expression primarily
in brain.
GENE FUNCTION
Ritter et al. (2003) identified a motif (WVQF) in the rat Necap1 protein
that bound directly to the globular ear domain of the alpha-adaptin
subunit (AP2A1; 601026) of the adaptor protein-2 (AP-2) complex.
Mutations in this sequence blocked clathrin-mediated endocytosis.
MAPPING
Hartz (2007) mapped the NECAP1 gene to chromosome 12p13.31 based on an
alignment of the NECAP1 sequence (GenBank GENBANK AK074858) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 11/26/2007.
2. 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
611623
*FIELD* TI
*611623 NECAP ENDOCYTOSIS-ASSOCIATED PROTEIN 1; NECAP1
;;ADAPTIN EAR-BINDING COAT-ASSOCIATED PROTEIN 1
read more*FIELD* TX
CLONING
Through a proteomic analysis of rat brain clathrin-coated vesicles,
Ritter et al. (2003) identified Necap1. The deduced protein contains 275
amino acids. Western blot analysis detected Necap1 expression primarily
in brain.
GENE FUNCTION
Ritter et al. (2003) identified a motif (WVQF) in the rat Necap1 protein
that bound directly to the globular ear domain of the alpha-adaptin
subunit (AP2A1; 601026) of the adaptor protein-2 (AP-2) complex.
Mutations in this sequence blocked clathrin-mediated endocytosis.
MAPPING
Hartz (2007) mapped the NECAP1 gene to chromosome 12p13.31 based on an
alignment of the NECAP1 sequence (GenBank GENBANK AK074858) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 11/26/2007.
2. 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