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MYO16_HUMAN
ID   MYO16_HUMAN             Reviewed;        1858 AA.
AC   Q9Y6X6; A6H8Y0; A8MTX3; Q5VYX4; Q5VYX5; Q5VYX6; Q6ZS13; Q8N3C2; Q8N948;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 3.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Unconventional myosin-XVI;
DE   AltName: Full=Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3;
DE   AltName: Full=Unconventional myosin-16;
GN   Name=MYO16 {ECO:0000312|HGNC:HGNC:29822};
GN   Synonyms=KIAA0865 {ECO:0000312|EMBL:BAA74888.2},
GN   MYO16B {ECO:0000312|HGNC:HGNC:29822}, NYAP3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAA74888.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-831.
RC   TISSUE=Brain {ECO:0000312|EMBL:BAA74888.2};
RX   PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAC04608.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-995 (ISOFORMS 1/3), AND VARIANTS THR-385 AND
RP   ALA-831.
RC   TISSUE=Brain {ECO:0000312|EMBL:BAC04608.1};
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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] {ECO:0000305, ECO:0000312|EMBL:CAD39107.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-831.
RC   TISSUE=Brain;
RA   Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
RT   "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
RT   recombination: preparation of full-length cDNA clones encoding motor
RT   proteins.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AL136132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-831.
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-935 (ISOFORMS 1/2/3), AND
RP   VARIANT ALA-831.
RC   TISSUE=Amygdala;
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., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   INTERACTION WITH KIRREL3.
RX   PubMed=25902260; DOI=10.1371/journal.pone.0123106;
RA   Liu Y.F., Sowell S.M., Luo Y., Chaubey A., Cameron R.S., Kim H.G.,
RA   Srivastava A.K.;
RT   "Autism and intellectual disability-associated KIRREL3 interacts with
RT   neuronal proteins MAP1B and MYO16 with potential roles in
RT   neurodevelopment.";
RL   PLoS ONE 10:E0123106-E0123106(2015).
RN   [8]
RP   VARIANT HIS-1168.
RX   PubMed=21248752; DOI=10.1038/nature09639;
RA   Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA   Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA   Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA   Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA   Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA   Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA   Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA   Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT   PBRM1 in renal carcinoma.";
RL   Nature 469:539-542(2011).
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC       Unconventional myosins serve in intracellular movements. Their highly
CC       divergent tails are presumed to bind to membranous compartments, which
CC       would be moved relative to actin filaments. May be involved in
CC       targeting of the catalytic subunit of protein phosphatase 1 during
CC       brain development. Activates PI3K and concomitantly recruits the WAVE1
CC       complex to the close vicinity of PI3K and regulates neuronal
CC       morphogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds PPP1CA and/or PPP1CC. Binds F-actin in an ATP-sensitive
CC       manner. Interacts with ACOT9, ARHGAP26 and PIK3R2. Interacts with
CC       components of the WAVE1 complex, CYFIP1 and NCKAP1; this interaction
CC       mediates PI3K-WAVE1 association and actin cytoskeleton remodeling (By
CC       similarity). Interacts with KIRREL3 (PubMed:25902260).
CC       {ECO:0000250|UniProtKB:Q5DU14, ECO:0000250|UniProtKB:Q9ERC1,
CC       ECO:0000269|PubMed:25902260}.
CC   -!- INTERACTION:
CC       Q9Y6X6; Q8IZU9: KIRREL3; NbExp=4; IntAct=EBI-310686, EBI-16427312;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ERC1}.
CC       Note=Found in puncta in soma and processes of astrocytes and
CC       dissociated cerebellar cells with the morphology of migrating granule
CC       cells. {ECO:0000250|UniProtKB:Q9ERC1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1 {ECO:0000269|PubMed:10048485};
CC         IsoId=Q9Y6X6-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:14702039};
CC         IsoId=Q9Y6X6-2; Sequence=VSP_052451;
CC       Name=3 {ECO:0000269|PubMed:15057823};
CC         IsoId=Q9Y6X6-3; Sequence=VSP_052449, VSP_052450;
CC       Name=4 {ECO:0000269|PubMed:15057823};
CC         IsoId=Q9Y6X6-4; Sequence=VSP_052447, VSP_052448, VSP_052449,
CC                                  VSP_052450;
CC   -!- PTM: Phosphorylated on tyrosine residues by FYN upon stimulation with
CC       CNTN5. {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class
CC       myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NYAP family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA74888.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC04608.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC87143.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB020672; BAA74888.2; ALT_INIT; mRNA.
DR   EMBL; AK095691; BAC04608.1; ALT_INIT; mRNA.
DR   EMBL; AB290159; BAG06713.1; -; mRNA.
DR   EMBL; AL136132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL390918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK127806; BAC87143.1; ALT_INIT; mRNA.
DR   EMBL; BC146791; AAI46792.1; -; mRNA.
DR   EMBL; AL834447; CAD39107.2; -; mRNA.
DR   CCDS; CCDS32008.1; -. [Q9Y6X6-1]
DR   RefSeq; NP_055826.1; NM_015011.1. [Q9Y6X6-1]
DR   RefSeq; XP_011519364.1; XM_011521062.1. [Q9Y6X6-1]
DR   AlphaFoldDB; Q9Y6X6; -.
DR   SMR; Q9Y6X6; -.
DR   BioGRID; 116666; 11.
DR   ELM; Q9Y6X6; -.
DR   IntAct; Q9Y6X6; 10.
DR   MINT; Q9Y6X6; -.
DR   STRING; 9606.ENSP00000401633; -.
DR   iPTMnet; Q9Y6X6; -.
DR   PhosphoSitePlus; Q9Y6X6; -.
DR   BioMuta; MYO16; -.
DR   DMDM; 152112422; -.
DR   EPD; Q9Y6X6; -.
DR   MassIVE; Q9Y6X6; -.
DR   MaxQB; Q9Y6X6; -.
DR   PaxDb; Q9Y6X6; -.
DR   PeptideAtlas; Q9Y6X6; -.
DR   PRIDE; Q9Y6X6; -.
DR   ProteomicsDB; 86817; -. [Q9Y6X6-1]
DR   ProteomicsDB; 86818; -. [Q9Y6X6-2]
DR   ProteomicsDB; 86819; -. [Q9Y6X6-3]
DR   ProteomicsDB; 86820; -. [Q9Y6X6-4]
DR   Antibodypedia; 42542; 79 antibodies from 20 providers.
DR   DNASU; 23026; -.
DR   Ensembl; ENST00000251041.10; ENSP00000251041.5; ENSG00000041515.16. [Q9Y6X6-3]
DR   Ensembl; ENST00000356711.7; ENSP00000349145.2; ENSG00000041515.16. [Q9Y6X6-1]
DR   GeneID; 23026; -.
DR   KEGG; hsa:23026; -.
DR   UCSC; uc001vqt.1; human. [Q9Y6X6-1]
DR   CTD; 23026; -.
DR   DisGeNET; 23026; -.
DR   GeneCards; MYO16; -.
DR   HGNC; HGNC:29822; MYO16.
DR   HPA; ENSG00000041515; Tissue enhanced (brain).
DR   MIM; 615479; gene.
DR   neXtProt; NX_Q9Y6X6; -.
DR   OpenTargets; ENSG00000041515; -.
DR   PharmGKB; PA162396437; -.
DR   VEuPathDB; HostDB:ENSG00000041515; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   eggNOG; KOG0515; Eukaryota.
DR   GeneTree; ENSGT00940000158920; -.
DR   HOGENOM; CLU_013794_0_0_1; -.
DR   InParanoid; Q9Y6X6; -.
DR   PhylomeDB; Q9Y6X6; -.
DR   TreeFam; TF332267; -.
DR   PathwayCommons; Q9Y6X6; -.
DR   SignaLink; Q9Y6X6; -.
DR   BioGRID-ORCS; 23026; 9 hits in 1071 CRISPR screens.
DR   ChiTaRS; MYO16; human.
DR   GenomeRNAi; 23026; -.
DR   Pharos; Q9Y6X6; Tbio.
DR   PRO; PR:Q9Y6X6; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q9Y6X6; protein.
DR   Bgee; ENSG00000041515; Expressed in cortical plate and 98 other tissues.
DR   ExpressionAtlas; Q9Y6X6; baseline and differential.
DR   Genevisible; Q9Y6X6; HS.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR   GO; GO:0016459; C:myosin complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HGNC-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISS:HGNC-UCL.
DR   GO; GO:0051015; F:actin filament binding; ISS:HGNC-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR   GO; GO:0021549; P:cerebellum development; ISS:HGNC-UCL.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:HGNC-UCL.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:HGNC.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR   CDD; cd14878; MYSc_Myo16; 1.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036042; MYSc_Myo16.
DR   InterPro; IPR039482; NYAP_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF15439; NYAP_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; ANK repeat; ATP-binding; Cytoplasm;
KW   Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1858
FT                   /note="Unconventional myosin-XVI"
FT                   /id="PRO_0000289136"
FT   REPEAT          59..88
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          92..121
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          125..154
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          158..189
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          191..217
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          221..250
FT                   /note="ANK 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          254..283
FT                   /note="ANK 7"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          401..1145
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          1147..1176
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          373..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1111..1377
FT                   /note="Involved in CYFIP1- and NCKAP1-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1219..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1326..1409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1448..1674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1697..1731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1747..1778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1821..1844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1219..1248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1329..1346
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1474..1498
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1529..1548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1568..1596
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1702..1731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1763..1778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         497..504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   VAR_SEQ         1..192
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15057823"
FT                   /id="VSP_052447"
FT   VAR_SEQ         206..225
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15057823"
FT                   /id="VSP_052448"
FT   VAR_SEQ         936..940
FT                   /note="TSENV -> RGRCF (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15057823"
FT                   /id="VSP_052449"
FT   VAR_SEQ         941..1858
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15057823"
FT                   /id="VSP_052450"
FT   VAR_SEQ         1091..1858
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_052451"
FT   VARIANT         181
FT                   /note="D -> E (in dbSNP:rs911973)"
FT                   /id="VAR_050214"
FT   VARIANT         339
FT                   /note="V -> I (in dbSNP:rs405397)"
FT                   /id="VAR_050215"
FT   VARIANT         385
FT                   /note="M -> T (in dbSNP:rs16973313)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_032584"
FT   VARIANT         831
FT                   /note="P -> A (in dbSNP:rs3825491)"
FT                   /evidence="ECO:0000269|PubMed:10048485,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17974005, ECO:0000269|Ref.3"
FT                   /id="VAR_032585"
FT   VARIANT         1168
FT                   /note="L -> H (found in a renal cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21248752"
FT                   /id="VAR_064737"
FT   VARIANT         1171
FT                   /note="I -> M (in dbSNP:rs157024)"
FT                   /id="VAR_050216"
FT   CONFLICT        555
FT                   /note="K -> E (in Ref. 6; CAD39107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        953
FT                   /note="T -> A (in Ref. 2; BAC87143)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1858 AA;  206129 MW;  B2D821DD53BD109E CRC64;
     MEIDQCLLES LPLGQRQRLV KRMRCEQIKA YYEREKAFQK QEGFLKRLKH AKNPKVHFNL
     TDMLQDAIIH HNDKEVLRLL KEGADPHTLV SSGGSLLHLC ARYDNAFIAE ILIDRGVNVN
     HQDEDFWTPM HIACACDNPD IVLLLVLAGA NVLLQDVNGN IPLDYAVEGT ESSSILLTYL
     DENGVDLTSL RQMKLQRPMS MLTDVKHFLS SGGNVNEKND EGVTLLHMAC ASGYKEVVSL
     ILEHGGDLNI VDDQYWTPLH LAAKYGQTNL VKLLLMHQAN PHLVNCNEEK ASDIAASEFI
     EEMLLKAEIA WEEKMKEPLS ASTLAQEEPY EEIIHDLPVL SSKLSPLVLP IAKQDSLLEK
     DIMFKDATKG LCKQQSQDSI PENPMMSGST KPEQVKLMPP APNDDLATLS ELNDGSLLYE
     IQKRFGNNQI YTFIGDILLL VNPYKELPIY SSMVSQLYFS SSGKLCSSLP PHLFSCVERA
     FHQLFREQRP QCFILSGERG SGKSEASKQI IRHLTCRAGA SRATLDSRFK HVVCILEAFG
     HAKTTLNDLS SCFIKYFELQ FCERKQQLTG ARIYTYLLEK SRLVSQPLGQ SNFLIFYLLM
     DGLSAEEKYG LHLNNLCAHR YLNQTIQDDA STGERSLNRE KLAVLKRALN VVGFSSLEVE
     NLFVILAAIL HLGDIRFTAL NEGNSAFVSD LQLLEQVAGM LQVSTDELAS ALTTDIQYFK
     GDMIIRRHTI QIAEFFRDLL AKSLYSRLFS FLVNTMNSCL HSQDEQKSMQ TLDIGILDIF
     GFEEFQKNEF EQLCVNMTNE KMHHYINEVL FLHEQVECVQ EGVTMETAYS PGNQNGVLDF
     FFQKPSGFLT LLDEESQMIW SVESNFPKKL QSLLESSNTN AVYSPMKDGN GNVALKDHGT
     AFTIMHYAGR VMYDVVGAIE KNKDSLSQNL LFVMKTSENV VINHLFQSKL SQTGSLVSAY
     PSFKFRGHKS ALLSKKMTAS SIIGENKNYL ELSKLLKKKG TSTFLQRLER GDPVTIASQL
     RKSLMDIIGK LQKCTPHFIH CIRPNNSKLP DTFDNFYVSA QLQYIGVLEM VKIFRYGYPV
     RLSFSDFLSR YKPLADTFLR EKKEQSAAER CRLVLQQCKL QGWQMGVRKV FLKYWHADQL
     NDLCLQLQRK IITCQKVIRG FLARQHLLQR ISIRQQEVTS INSFLQNTED MGLKTYDALV
     IQNASDIARE NDRLRSEMNA PYHKEKLEVR NMQEEGSKRT DDKSGPRHFH PSSMSVCAAV
     DGLGQCLVGP SIWSPSLHSV FSMDDSSSLP SPRKQPPPKP KRDPNTRLSA SYEAVSACLS
     AAREAANEAL ARPRPHSDDY STMKKIPPRK PKRSPNTKLS GSYEEISGSR PGDARPAGAP
     GAAARVLTPG TPQCALPPAA PPGDEDDSEP VYIEMLGHAA RPDSPDPGES VYEEMKCCLP
     DDGGPGAGSF LLHGASPPLL HRAPEDEAAG PPGDACDIPP PFPNLLPHRP PLLVFPPTPV
     TCSPASDESP LTPLEVKKLP VLETNLKYPV QPEGSSPLSP QYSKSQKGDG DRPASPGLAL
     FNGSGRASPP STPPPPPPPP GPPPAPYRPC AHLAFPPEPA PVNAGKAGPS AEAPKVHPKP
     NSAPVAGPCS SFPKIPYSPV KATRADARKA GSSASPPAPY SPPSSRPLSS PLDELASLFN
     SGRSVLRKSA AGRKIREAEG FETNMNISSR DDPSTSEITS ETQDRNANNH GIQLSNSLSS
     AITAENGNSI SNGLPEEDGY SRLSISGTGT STFQRHRDSH TTQVIHQLRL SENESVALQE
     LLDWRRKLCE EGQDWQQILH HAEPRVPPPP PCKKPSLLKK PEGASCNRLP SELWDTTI
 
 
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