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UniProtKB/Swiss-Prot: Q6P3W7
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ID SCYL2_HUMAN Reviewed; 929 AA.
AC Q6P3W7; Q96EF4; Q96ST4; Q9H7V5; Q9NVH3; Q9P2I7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 14-APR-2009, entry version 52.
DE RecName: Full=SCY1-like protein 2;
DE AltName: Full=Coated vesicle-associated kinase of 104 kDa;
GN Name=SCYL2; Synonyms=CVAK104, KIAA1360;
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].
RC TISSUE=Carcinoma, and Leiomyosarcoma;
RX PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-929.
RC TISSUE=Brain;
RX MEDLINE=20181126; PubMed=10718198 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-929, AND VARIANT
RP LEU-357.
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]; 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 [4]
RP FUNCTION, INTERACTION WITH CLATHRIN AND AP2 COMPLEX,
RP AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=15809293 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.M502462200;
RA Conner S.D., Schmid S.L.;
RT "CVAK104 is a novel poly-L-lysine-stimulated kinase that targets the
RT beta2-subunit of AP2.";
RL J. Biol. Chem. 280:21539-21544(2005).
RN [5]
RP FUNCTION, INTERACTION WITH CLATHRIN AND AP2 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16914521 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1091/mbc.E06-05-0390;
RA Duewel M., Ungewickell E.J.;
RT "Clathrin-dependent association of CVAK104 with endosomes and the
RT trans-Golgi network.";
RL Mol. Biol. Cell 17:4513-4525(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASS
RP SPECTROMETRY.
RX PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.2116/analsci.24.161;
RA Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
RT "Automated phosphoproteome analysis for cultured cancer cells by two-
RT dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
RL Anal. Sci. 24:161-166(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438; THR-440 AND
RP SER-677, AND MASS SPECTROMETRY.
RX PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]; 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 [8]
RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA Colinge J., Superti-Furga G., Bennett K.L.;
RL Submitted (OCT-2008) to UniProtKB.
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-357; SER-720 AND HIS-863.
RX PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Component of AP2-containing clathrin coated structures
CC at the plasma membrane or of endocytic coated vesicles. According
CC to PubMed:15809293, probable serine/threonine-protein kinase that
CC phosphorylates, in vitro, the beta2-subunit of the plasma membrane
CC adapter complex AP2 and other proteins in presence of poly-L-
CC lysine. According to PubMed:16914521, has no detectable kinase
CC activity in vitro. May regulate clathrin-dependent trafficking
CC between the TGN and/or the endosomal system.
CC -!- SUBUNIT: Interacts with clathrin and plasma membrane adapter
CC complex AP2 complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasmic
CC vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi
CC network membrane. Endosome membrane. Note=According to
CC PubMed:15809293, plasma membrane-associated in clathrin-coated
CC vesicles. According to PubMed:16914521, colocalizes to the trans-
CC Golgi network (TGN) and to endosomal membranes with clathrin,
CC transferrin and plasma membrane adapter AP1 and AP3 complexes.
CC -!- PTM: According to PubMed:15809293, autophosphorylated in presence
CC of poly-L-lysine.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC -!- SIMILARITY: Contains 1 HEAT repeat.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; BC012387; AAH12387.3; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC063798; AAH63798.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AB037781; BAA92598.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AK001597; BAA91778.1; ALT_INIT; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AK024274; BAB14869.1; ALT_INIT; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AK027551; BAB55194.1; ALT_INIT; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR IPI; IPI00396218; -.
DR RefSeq; NP_060458.3; -.
DR UniGene; Hs.506481; -.
DR IntAct; Q6P3W7; 3.
DR PhosphoSite; Q6P3W7; -.
DR PRIDE; Q6P3W7; -.
DR Ensembl; ENSG00000136021; Homo_sapiens
DR GeneID; 55681; -.
DR KEGG; hsa:55681; -.
DR GeneCards; GC12P099164; -.
DR HGNC; HGNC:19286; SCYL2.
DR CleanEx; HGNC:19286; SCYL2.
DR PharmGKB; PA134887807; -.
DR HOVERGEN; Q6P3W7; -.
DR NextBio; 60474; -.
DR ArrayExpress; Q6P3W7; -.
DR Bgee; Q6P3W7; -.
DR CleanEx; HS_SCYL2; -.
DR GermOnline; ENSG00000136021; Homo_sapiens
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR InterPro; IPR000719; Prot_kinase_core.
DR InterPro; IPR017442; Se/Thr_pkinase-rel.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; Graphical view of domain structure.
DR ProDom; PD000001; Prot_kinase; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR CMR; Q6P3W7.
DR BLOCKS; Q6P3W7.
DR ProtoNet; Q6P3W7.
DR DIP; Q6P3W7.
DR ModBase; Q6P3W7.
DR HUGE; KIAA1360; -.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Endosome;
KW Golgi apparatus; Membrane; Phosphoprotein; Polymorphism.
FT CHAIN 1 929 SCY1-like protein 2.
FT /FTId=PRO_0000252446.
FT DOMAIN 32 327 Protein kinase.
FT REPEAT 443 479 HEAT.
FT REGION 699 929 Necessary for interaction with AP2
FT complex and clathrin, interaction with
FT clathrin is necessary for its targeting
FT to the TGN and endosomal membranes.
FT COILED 661 701 Potential.
FT MOD_RES 350 350 Phosphoserine.
FT MOD_RES 438 438 Phosphothreonine.
FT MOD_RES 440 440 Phosphothreonine.
FT MOD_RES 677 677 Phosphoserine.
FT VARIANT 357 357 P -> L (in dbSNP:rs33968174).
FT /FTId=VAR_041368.
FT VARIANT 720 720 T -> S.
FT /FTId=VAR_041369.
FT VARIANT 863 863 Q -> H (in a lung adenocarcinoma sample;
FT somatic mutation).
FT /FTId=VAR_041370.
FT CONFLICT 139 145 PISPDIK -> LMSGDIG (in Ref. 2; BAA92598).
FT CONFLICT 186 186 L -> S (in Ref. 3; BAB14869).
FT CONFLICT 424 424 Q -> QASNM (in Ref. 2; BAA92598).
FT CONFLICT 439 439 K -> R (in Ref. 3; BAB14869).
FT CONFLICT 554 554 F -> L (in Ref. 1; AAH12387).
FT CONFLICT 628 628 Q -> R (in Ref. 3; BAB14869).
FT CONFLICT 638 638 T -> I (in Ref. 1; AAH12387).
FT CONFLICT 747 747 T -> A (in Ref. 3; BAA91778).
SQ SEQUENCE 929 AA; 103709 MW; 980B481BF7044628 CRC64;
MESMLNKLKS TVTKVTADVT SAVMGNPVTR EFDVGRHIAS GGNGLAWKIF NGTKKSTKQE
VAVFVFDKKL IDKYQKFEKD QIIDSLKRGV QQLTRLRHPR LLTVQHPLEE SRDCLAFCTE
PVFASLANVL GNWENLPSPI SPDIKDYKLY DVETKYGLLQ VSEGLSFLHS SVKMVHGNIT
PENIILNKSG AWKIMGFDFC VSSTNPSEQE PKFPCKEWDP NLPSLCLPNP EYLAPEYILS
VSCETASDMY SLGTVMYAVF NKGKPIFEVN KQDIYKSFSR QLDQLSRLGS SSLTNIPEEV
REHVKLLLNV TPTVRPDADQ MTKIPFFDDV GAVTLQYFDT LFQRDNLQKS QFFKGLPKVL
PKLPKRVIVQ RILPCLTSEF VNPDMVPFVL PNVLLIAEEC TKEEYVKLIL PELGPVFKQQ
EPIQILLIFL QKMDLLLTKT PPDEIKNSVL PMVYRALEAP SIQIQELCLN IIPTFANLID
YPSMKNALIP RIKNACLQTS SLAVRVNSLV CLGKILEYLD KWFVLDDILP FLQQIPSKEP
AVLMGILGIY KCTFTHKKLG ITKEQLAGKV LPHLIPLSIE NNLNLNQFNS FISVIKEMLN
RLESEHKTKL EQLHIMQEQQ KSLDIGNQMN VSEEMKVTNI GNQQIDKVFN NIGADLLTGS
ESENKEDGLQ NKHKRASLTL EEKQKLAKEQ EQAQKLKSQQ PLKPQVHTPV ATVKQTKDLT
DTLMDNMSSL TSLSVSTPKS SASSTFTSVP SMGIGMMFST PTDNTKRNLT NGLNANMGFQ
TSGFNMPVNT NQNFYSSPST VGVTKMTLGT PPTLPNFNAL SVPPAGAKQT QQRPTDMSAL
NNLFGPQKPK VSMNQLSQQK PNQWLNQFVP PQGSPTMGSS VMGTQMNVIG QSAFGMQGNP
FFNPQNFAQP PTTMTNSSSA SNDLKDLFG
//

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