Full text data of SNAP91
SNAP91
(KIAA0656)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Clathrin coat assembly protein AP180 (91 kDa synaptosomal-associated protein; Clathrin coat-associated protein AP180; Phosphoprotein F1-20)
Clathrin coat assembly protein AP180 (91 kDa synaptosomal-associated protein; Clathrin coat-associated protein AP180; Phosphoprotein F1-20)
hRBCD
IPI00006612
IPI00006612 Clathrin coat assembly protein AP180 Clathrin coat assembly protein AP180 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a membrane bound n/a found at its expected molecular weight found at molecular weight
IPI00006612 Clathrin coat assembly protein AP180 Clathrin coat assembly protein AP180 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a membrane bound n/a found at its expected molecular weight found at molecular weight
UniProt
O60641
ID AP180_HUMAN Reviewed; 907 AA.
AC O60641; A8K0L7; E5RI02; Q5JX13; Q68DL9; Q6P9D3; Q9NTY7;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1999, sequence version 2.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Clathrin coat assembly protein AP180;
DE AltName: Full=91 kDa synaptosomal-associated protein;
DE AltName: Full=Clathrin coat-associated protein AP180;
DE AltName: Full=Phosphoprotein F1-20;
GN Name=SNAP91; Synonyms=KIAA0656;
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=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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 MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-907.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH AP2B1.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for
RT clathrin-coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
CC -!- FUNCTION: Adaptins are components of the adapter complexes which
CC link clathrin to receptors in coated vesicles. Clathrin-associated
CC protein complexes are believed to interact with the cytoplasmic
CC tails of membrane proteins, leading to their selection and
CC concentration. Binding of AP180 to clathrin triskelia induces
CC their assembly into 60-70 nm coats (By similarity).
CC -!- SUBUNIT: Binds AP2A2. Interacts with AP2B1; clathrin competes with
CC SNAP91 (By similarity).
CC -!- INTERACTION:
CC Q9CR95:Necap1 (xeno); NbExp=2; IntAct=EBI-1105187, EBI-7592476;
CC -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Membrane,
CC coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Note=Component of the coat surrounding the
CC cytoplasmic face of coated vesicles in the plasma membrane (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60641-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60641-2; Sequence=VSP_020997;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC Name=3;
CC IsoId=O60641-3; Sequence=VSP_020998, VSP_020999, VSP_021000;
CC Name=4;
CC IsoId=O60641-4; Sequence=VSP_020999, VSP_047049;
CC Note=Gene prediction based on EST data;
CC -!- DOMAIN: Possesses a three domain structure: the N-terminal 300
CC residues harbor a clathrin binding site, an acidic middle domain
CC 450 residues, interrupted by an Ala-rich segment, and the C-
CC terminal domain (166 residues).
CC -!- PTM: Thr-310 can be modified by the addition of N-
CC acetylglucosamine which can be further phosphorylated. There is no
CC evidence for direct Thr-310 phosphorylation (By similarity).
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family.
CC -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31631.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAB89292.1; Type=Erroneous gene model prediction;
CC Sequence=CAH18201.1; Type=Erroneous translation; Note=Wrong choice of CDS;
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DR EMBL; AB014556; BAA31631.2; ALT_INIT; mRNA.
DR EMBL; AK289582; BAF82271.1; -; mRNA.
DR EMBL; CR749348; CAH18201.1; ALT_SEQ; mRNA.
DR EMBL; AL109915; CAB89292.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109915; CAI19453.1; -; Genomic_DNA.
DR EMBL; AL136972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF054993; AAC09352.1; -; mRNA.
DR EMBL; BC060818; AAH60818.1; -; mRNA.
DR RefSeq; NP_001229721.1; NM_001242792.1.
DR RefSeq; NP_001229722.1; NM_001242793.1.
DR RefSeq; NP_001229723.1; NM_001242794.1.
DR RefSeq; NP_001243646.1; NM_001256717.1.
DR RefSeq; NP_001243647.1; NM_001256718.1.
DR RefSeq; NP_055656.1; NM_014841.2.
DR RefSeq; XP_005248827.1; XM_005248770.1.
DR RefSeq; XP_005248828.1; XM_005248771.1.
DR UniGene; Hs.368046; -.
DR ProteinModelPortal; O60641; -.
DR SMR; O60641; 18-264.
DR IntAct; O60641; 2.
DR MINT; MINT-3000172; -.
DR STRING; 9606.ENSP00000195649; -.
DR PhosphoSite; O60641; -.
DR PaxDb; O60641; -.
DR PRIDE; O60641; -.
DR Ensembl; ENST00000369694; ENSP00000358708; ENSG00000065609.
DR Ensembl; ENST00000437520; ENSP00000413277; ENSG00000065609.
DR Ensembl; ENST00000439399; ENSP00000400459; ENSG00000065609.
DR Ensembl; ENST00000520213; ENSP00000428026; ENSG00000065609.
DR Ensembl; ENST00000520302; ENSP00000428511; ENSG00000065609.
DR Ensembl; ENST00000521743; ENSP00000428215; ENSG00000065609.
DR GeneID; 9892; -.
DR KEGG; hsa:9892; -.
DR UCSC; uc003pkb.3; human.
DR CTD; 9892; -.
DR GeneCards; GC06M084319; -.
DR H-InvDB; HIX0006038; -.
DR HGNC; HGNC:14986; SNAP91.
DR HPA; CAB009745; -.
DR HPA; HPA029632; -.
DR HPA; HPA029633; -.
DR MIM; 607923; gene.
DR neXtProt; NX_O60641; -.
DR PharmGKB; PA37956; -.
DR eggNOG; NOG267212; -.
DR HOGENOM; HOG000015763; -.
DR HOVERGEN; HBG049391; -.
DR InParanoid; O60641; -.
DR OMA; XRISGAP; -.
DR OrthoDB; EOG76QFM8; -.
DR GeneWiki; SNAP91; -.
DR GenomeRNAi; 9892; -.
DR NextBio; 37299; -.
DR PRO; PR:O60641; -.
DR ArrayExpress; O60641; -.
DR Bgee; O60641; -.
DR CleanEx; HS_SNAP91; -.
DR Genevestigator; O60641; -.
DR GO; GO:0030118; C:clathrin coat; IEA:InterPro.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; Clathrin_Pinositid-bd_GAT-like.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR013809; Epsin-like_N.
DR Pfam; PF07651; ANTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Complete proteome;
KW Glycoprotein; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 907 Clathrin coat assembly protein AP180.
FT /FTId=PRO_0000193864.
FT DOMAIN 14 145 ENTH.
FT COMPBIAS 361 583 Ala-rich.
FT COMPBIAS 536 556 Thr-rich.
FT COMPBIAS 809 897 Pro-rich.
FT MOD_RES 306 306 Phosphoserine (By similarity).
FT MOD_RES 313 313 Phosphoserine (By similarity).
FT MOD_RES 602 602 Phosphoserine (By similarity).
FT MOD_RES 623 623 Phosphoserine (By similarity).
FT MOD_RES 629 629 Phosphoserine (By similarity).
FT CARBOHYD 310 310 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 59 907 Missing (in isoform 2).
FT /FTId=VSP_020997.
FT VAR_SEQ 256 269 Missing (in isoform 3).
FT /FTId=VSP_020998.
FT VAR_SEQ 293 295 NEG -> K (in isoform 3 and isoform 4).
FT /FTId=VSP_020999.
FT VAR_SEQ 381 671 Missing (in isoform 3).
FT /FTId=VSP_021000.
FT VAR_SEQ 616 643 Missing (in isoform 4).
FT /FTId=VSP_047049.
FT CONFLICT 4 4 Q -> R (in Ref. 5; AAH60818).
SQ SEQUENCE 907 AA; 92502 MW; 23959C2B54F5EBF1 CRC64;
MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQMA
DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR NTLFNLSNFL DKSGSHGYDM
STFIRRYSRY LNEKAFSYRQ MAFDFARVKK GADGVMRTMA PEKLLKSMPI LQGQIDALLE
FDVHPNELTN GVINAAFMLL FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF
LTRMTRVSEF LKVAEQVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS
PLSKSSPATT VTSPNSTPAK TIDTSPPVDL FATASAAVPV STSKPSSDLL DLQPDFSSGG
AAAAAAPAPP PPAGGATAWG DLLGEDSLAA LSSVPSEAQI SDPFAPEPTP PTTTAEIATA
SASASTTTTV TAVTAEVDLF GDAFAASPGE APAASEGAAA PATPTPVAAA LDACSGNDPF
APSEGSAEAA PELDLFAMKP PETSVPVVTP TASTAPPVPA TAPSPAPAVA AAAAATTAAT
AAATTTTTTS AATATTAPPA LDIFGDLFES TPEVAAAPKP DAAPSIDLFS TDAFSSPPQG
ASPVPESSLT ADLLSVDAFA APSPATTASP AKVDSSGVID LFGDAFGSSA SEPQPASQAA
SSSSASADLL AGFGGSFMAP SPSPVTPAQN NLLQPNFEAA FGTTPSTSSS SSFDPSVFDG
LGDLLMPTMA PAGQPAPVSM VPPSPAMAAS KALGSDLDSS LASLVGNLGI SGTTTKKGDL
QWNAGEKKLT GGANWQPKVA PATWSAGVPP SAPLQGAVPP TSSVPPVAGA PSVGQPGAGF
GMPPAGTGMP MMPQQPVMFA QPMMRPPFGA AAVPGTQLSP SPTPASQSPK KPPAKDPLAD
LNIKDFL
//
ID AP180_HUMAN Reviewed; 907 AA.
AC O60641; A8K0L7; E5RI02; Q5JX13; Q68DL9; Q6P9D3; Q9NTY7;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1999, sequence version 2.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Clathrin coat assembly protein AP180;
DE AltName: Full=91 kDa synaptosomal-associated protein;
DE AltName: Full=Clathrin coat-associated protein AP180;
DE AltName: Full=Phosphoprotein F1-20;
GN Name=SNAP91; Synonyms=KIAA0656;
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=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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 MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-907.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH AP2B1.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for
RT clathrin-coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
CC -!- FUNCTION: Adaptins are components of the adapter complexes which
CC link clathrin to receptors in coated vesicles. Clathrin-associated
CC protein complexes are believed to interact with the cytoplasmic
CC tails of membrane proteins, leading to their selection and
CC concentration. Binding of AP180 to clathrin triskelia induces
CC their assembly into 60-70 nm coats (By similarity).
CC -!- SUBUNIT: Binds AP2A2. Interacts with AP2B1; clathrin competes with
CC SNAP91 (By similarity).
CC -!- INTERACTION:
CC Q9CR95:Necap1 (xeno); NbExp=2; IntAct=EBI-1105187, EBI-7592476;
CC -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Membrane,
CC coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Note=Component of the coat surrounding the
CC cytoplasmic face of coated vesicles in the plasma membrane (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60641-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60641-2; Sequence=VSP_020997;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC Name=3;
CC IsoId=O60641-3; Sequence=VSP_020998, VSP_020999, VSP_021000;
CC Name=4;
CC IsoId=O60641-4; Sequence=VSP_020999, VSP_047049;
CC Note=Gene prediction based on EST data;
CC -!- DOMAIN: Possesses a three domain structure: the N-terminal 300
CC residues harbor a clathrin binding site, an acidic middle domain
CC 450 residues, interrupted by an Ala-rich segment, and the C-
CC terminal domain (166 residues).
CC -!- PTM: Thr-310 can be modified by the addition of N-
CC acetylglucosamine which can be further phosphorylated. There is no
CC evidence for direct Thr-310 phosphorylation (By similarity).
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family.
CC -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31631.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAB89292.1; Type=Erroneous gene model prediction;
CC Sequence=CAH18201.1; Type=Erroneous translation; Note=Wrong choice of CDS;
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DR EMBL; AB014556; BAA31631.2; ALT_INIT; mRNA.
DR EMBL; AK289582; BAF82271.1; -; mRNA.
DR EMBL; CR749348; CAH18201.1; ALT_SEQ; mRNA.
DR EMBL; AL109915; CAB89292.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109915; CAI19453.1; -; Genomic_DNA.
DR EMBL; AL136972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF054993; AAC09352.1; -; mRNA.
DR EMBL; BC060818; AAH60818.1; -; mRNA.
DR RefSeq; NP_001229721.1; NM_001242792.1.
DR RefSeq; NP_001229722.1; NM_001242793.1.
DR RefSeq; NP_001229723.1; NM_001242794.1.
DR RefSeq; NP_001243646.1; NM_001256717.1.
DR RefSeq; NP_001243647.1; NM_001256718.1.
DR RefSeq; NP_055656.1; NM_014841.2.
DR RefSeq; XP_005248827.1; XM_005248770.1.
DR RefSeq; XP_005248828.1; XM_005248771.1.
DR UniGene; Hs.368046; -.
DR ProteinModelPortal; O60641; -.
DR SMR; O60641; 18-264.
DR IntAct; O60641; 2.
DR MINT; MINT-3000172; -.
DR STRING; 9606.ENSP00000195649; -.
DR PhosphoSite; O60641; -.
DR PaxDb; O60641; -.
DR PRIDE; O60641; -.
DR Ensembl; ENST00000369694; ENSP00000358708; ENSG00000065609.
DR Ensembl; ENST00000437520; ENSP00000413277; ENSG00000065609.
DR Ensembl; ENST00000439399; ENSP00000400459; ENSG00000065609.
DR Ensembl; ENST00000520213; ENSP00000428026; ENSG00000065609.
DR Ensembl; ENST00000520302; ENSP00000428511; ENSG00000065609.
DR Ensembl; ENST00000521743; ENSP00000428215; ENSG00000065609.
DR GeneID; 9892; -.
DR KEGG; hsa:9892; -.
DR UCSC; uc003pkb.3; human.
DR CTD; 9892; -.
DR GeneCards; GC06M084319; -.
DR H-InvDB; HIX0006038; -.
DR HGNC; HGNC:14986; SNAP91.
DR HPA; CAB009745; -.
DR HPA; HPA029632; -.
DR HPA; HPA029633; -.
DR MIM; 607923; gene.
DR neXtProt; NX_O60641; -.
DR PharmGKB; PA37956; -.
DR eggNOG; NOG267212; -.
DR HOGENOM; HOG000015763; -.
DR HOVERGEN; HBG049391; -.
DR InParanoid; O60641; -.
DR OMA; XRISGAP; -.
DR OrthoDB; EOG76QFM8; -.
DR GeneWiki; SNAP91; -.
DR GenomeRNAi; 9892; -.
DR NextBio; 37299; -.
DR PRO; PR:O60641; -.
DR ArrayExpress; O60641; -.
DR Bgee; O60641; -.
DR CleanEx; HS_SNAP91; -.
DR Genevestigator; O60641; -.
DR GO; GO:0030118; C:clathrin coat; IEA:InterPro.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; Clathrin_Pinositid-bd_GAT-like.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR013809; Epsin-like_N.
DR Pfam; PF07651; ANTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Complete proteome;
KW Glycoprotein; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 907 Clathrin coat assembly protein AP180.
FT /FTId=PRO_0000193864.
FT DOMAIN 14 145 ENTH.
FT COMPBIAS 361 583 Ala-rich.
FT COMPBIAS 536 556 Thr-rich.
FT COMPBIAS 809 897 Pro-rich.
FT MOD_RES 306 306 Phosphoserine (By similarity).
FT MOD_RES 313 313 Phosphoserine (By similarity).
FT MOD_RES 602 602 Phosphoserine (By similarity).
FT MOD_RES 623 623 Phosphoserine (By similarity).
FT MOD_RES 629 629 Phosphoserine (By similarity).
FT CARBOHYD 310 310 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 59 907 Missing (in isoform 2).
FT /FTId=VSP_020997.
FT VAR_SEQ 256 269 Missing (in isoform 3).
FT /FTId=VSP_020998.
FT VAR_SEQ 293 295 NEG -> K (in isoform 3 and isoform 4).
FT /FTId=VSP_020999.
FT VAR_SEQ 381 671 Missing (in isoform 3).
FT /FTId=VSP_021000.
FT VAR_SEQ 616 643 Missing (in isoform 4).
FT /FTId=VSP_047049.
FT CONFLICT 4 4 Q -> R (in Ref. 5; AAH60818).
SQ SEQUENCE 907 AA; 92502 MW; 23959C2B54F5EBF1 CRC64;
MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQMA
DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR NTLFNLSNFL DKSGSHGYDM
STFIRRYSRY LNEKAFSYRQ MAFDFARVKK GADGVMRTMA PEKLLKSMPI LQGQIDALLE
FDVHPNELTN GVINAAFMLL FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF
LTRMTRVSEF LKVAEQVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS
PLSKSSPATT VTSPNSTPAK TIDTSPPVDL FATASAAVPV STSKPSSDLL DLQPDFSSGG
AAAAAAPAPP PPAGGATAWG DLLGEDSLAA LSSVPSEAQI SDPFAPEPTP PTTTAEIATA
SASASTTTTV TAVTAEVDLF GDAFAASPGE APAASEGAAA PATPTPVAAA LDACSGNDPF
APSEGSAEAA PELDLFAMKP PETSVPVVTP TASTAPPVPA TAPSPAPAVA AAAAATTAAT
AAATTTTTTS AATATTAPPA LDIFGDLFES TPEVAAAPKP DAAPSIDLFS TDAFSSPPQG
ASPVPESSLT ADLLSVDAFA APSPATTASP AKVDSSGVID LFGDAFGSSA SEPQPASQAA
SSSSASADLL AGFGGSFMAP SPSPVTPAQN NLLQPNFEAA FGTTPSTSSS SSFDPSVFDG
LGDLLMPTMA PAGQPAPVSM VPPSPAMAAS KALGSDLDSS LASLVGNLGI SGTTTKKGDL
QWNAGEKKLT GGANWQPKVA PATWSAGVPP SAPLQGAVPP TSSVPPVAGA PSVGQPGAGF
GMPPAGTGMP MMPQQPVMFA QPMMRPPFGA AAVPGTQLSP SPTPASQSPK KPPAKDPLAD
LNIKDFL
//
MIM
607923
*RECORD*
*FIELD* NO
607923
*FIELD* TI
*607923 SYNAPTOSOMAL-ASSOCIATED PROTEIN, 91-KD; SNAP91
;;ASSEMBLY PROTEIN, 180-KD; AP180;;
read moreKIAA0656
*FIELD* TX
CLONING
Zhou et al. (1992) cloned 2 isoforms of Snap91, which they designated
F1-20, from mouse brain. The predominant mRNA encodes an 896-amino acid
protein with a calculated molecular mass of about 91 kD. The protein
does not contain a signal sequence or any extensive hydrophobic regions,
but it does have a number of putative phosphorylation sites. The C
terminus of Snap91 shares weak similarity with rabbit calpastatin
(114090). In mouse brain, Snap91 is a synapse-associated protein.
Expression of Snap91 is developmentally regulated in a pattern
coincident with active synaptogenesis and synaptic maturation (Zhou et
al., 1992). Biochemical analysis revealed that Snap91 is phosphorylated
in vivo and that it is a substrate for Ca(2+)-dependent proteolysis.
By sequencing clones obtained from a size-fractionated brain cDNA
library, Ishikawa et al. (1998) cloned SNAP91, which they designated
KIAA0656. The deduced full-length protein contains 907 amino acids and
shares about 83% identity with the short form of rat clathrin assembly
protein Ap180. RT-PCR detected highest expression in brain, followed by
testis, heart, and ovary. Little to no expression was detected in the
other tissues tested.
By confocal immunofluorescence microscopy of normal postmortem brains
from individuals aged 64 to 91 years, Yao et al. (2003) determined that
SNAP91 and synaptophysin (313475) showed a similar punctate staining
pattern. Staining did not, however, completely overlap.
MAPPING
By radiation hybrid analysis, Ishikawa et al. (1998) mapped the SNAP91
gene to chromosome 6.
*FIELD* RF
1. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
2. Yao, P. J.; O'Herron, T. M.; Coleman, P. D.: Immunohistochemical
characterization of clathrin assembly protein AP180 and synaptophysin
in human brain. Neurobiol. Aging 24: 173-178, 2003.
3. Zhou, S.; Sousa, R.; Tannery, N. H.; Lafer, E. M.: Characterization
of a novel synapse-specific protein. II. cDNA cloning and sequence
analysis of the F1-20 protein. J. Neurosci. 12: 2144-2155, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 7/15/2003
*FIELD* CD
Patricia A. Hartz: 6/26/2003
*FIELD* ED
carol: 08/13/2003
mgross: 7/15/2003
mgross: 6/26/2003
*RECORD*
*FIELD* NO
607923
*FIELD* TI
*607923 SYNAPTOSOMAL-ASSOCIATED PROTEIN, 91-KD; SNAP91
;;ASSEMBLY PROTEIN, 180-KD; AP180;;
read moreKIAA0656
*FIELD* TX
CLONING
Zhou et al. (1992) cloned 2 isoforms of Snap91, which they designated
F1-20, from mouse brain. The predominant mRNA encodes an 896-amino acid
protein with a calculated molecular mass of about 91 kD. The protein
does not contain a signal sequence or any extensive hydrophobic regions,
but it does have a number of putative phosphorylation sites. The C
terminus of Snap91 shares weak similarity with rabbit calpastatin
(114090). In mouse brain, Snap91 is a synapse-associated protein.
Expression of Snap91 is developmentally regulated in a pattern
coincident with active synaptogenesis and synaptic maturation (Zhou et
al., 1992). Biochemical analysis revealed that Snap91 is phosphorylated
in vivo and that it is a substrate for Ca(2+)-dependent proteolysis.
By sequencing clones obtained from a size-fractionated brain cDNA
library, Ishikawa et al. (1998) cloned SNAP91, which they designated
KIAA0656. The deduced full-length protein contains 907 amino acids and
shares about 83% identity with the short form of rat clathrin assembly
protein Ap180. RT-PCR detected highest expression in brain, followed by
testis, heart, and ovary. Little to no expression was detected in the
other tissues tested.
By confocal immunofluorescence microscopy of normal postmortem brains
from individuals aged 64 to 91 years, Yao et al. (2003) determined that
SNAP91 and synaptophysin (313475) showed a similar punctate staining
pattern. Staining did not, however, completely overlap.
MAPPING
By radiation hybrid analysis, Ishikawa et al. (1998) mapped the SNAP91
gene to chromosome 6.
*FIELD* RF
1. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
2. Yao, P. J.; O'Herron, T. M.; Coleman, P. D.: Immunohistochemical
characterization of clathrin assembly protein AP180 and synaptophysin
in human brain. Neurobiol. Aging 24: 173-178, 2003.
3. Zhou, S.; Sousa, R.; Tannery, N. H.; Lafer, E. M.: Characterization
of a novel synapse-specific protein. II. cDNA cloning and sequence
analysis of the F1-20 protein. J. Neurosci. 12: 2144-2155, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 7/15/2003
*FIELD* CD
Patricia A. Hartz: 6/26/2003
*FIELD* ED
carol: 08/13/2003
mgross: 7/15/2003
mgross: 6/26/2003