ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot Hosted by br flag LNCC Brazil Mirror sites: Australia Canada China Korea Switzerland Notice: This page will be replaced with www.uniprot.org. Please send us your feedback! Search for UniProtKB/Swiss-Prot: Q6P3W7 View this UniProtKB/Swiss-Prot entry on the UniProt web site 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. 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; 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 // Q6P3W7 in FASTA format NiceProt - a user-friendly view of this UniProtKB/Swiss-Prot entry View entry in raw text format (no links) Report form for errors/updates in this UniProtKB/Swiss-Prot entry BLAST logo BLAST submission on ExPASy/SIB or at NCBI (USA) Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java) PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL NPSA logo NPSA Sequence analysis tools ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot Hosted by br flag LNCC Brazil Mirror sites: Australia Canada China Korea Switzerland Notice: This page will be replaced with www.uniprot.org. 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