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TM245_HUMAN
ID   TM245_HUMAN             Reviewed;         879 AA.
AC   Q9H330; B4DSW7; Q5JTQ5; Q5SS43; Q6ZME3; Q8NDJ5; Q96CG6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 3.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Transmembrane protein 245;
DE   AltName: Full=Protein CG-2;
GN   Name=TMEM245; Synonyms=C9orf5;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT
RP   GLU-9.
RX   PubMed=10564813; DOI=10.1016/s0378-1119(99)00432-1;
RA   Chadwick B.P., Gill S., Leyne M., Mull J., Liebert C.B., Robbins C.M.,
RA   Pinkett H.W., Makalowska I., Maayan C., Blumenfeld A., Axelrod F.B.,
RA   Brownstein M., Slaugenhaupt S.A.;
RT   "Cloning, genomic organization and expression of a putative human
RT   transmembrane protein related to the Caenorhabditis elegans M01F1.4 gene.";
RL   Gene 240:67-73(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 222-511 (ISOFORM 4).
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., 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 540-879 (ISOFORMS 2/3).
RC   TISSUE=Eye;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36; SER-332 AND THR-334, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; 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   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-551.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
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., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-327, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2;
CC         IsoId=Q9H330-2; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q9H330-3; Sequence=VSP_014680;
CC       Name=4;
CC         IsoId=Q9H330-4; Sequence=VSP_059402, VSP_059403, VSP_059404;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10564813}.
CC   -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG43365.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF153415; AAG43365.1; ALT_FRAME; mRNA.
DR   EMBL; AK299952; BAG61779.1; -; mRNA.
DR   EMBL; AK172815; BAD18785.1; -; mRNA.
DR   EMBL; AL669894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL358815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014248; AAH14248.2; -; mRNA.
DR   EMBL; AL833960; CAD38810.1; -; mRNA.
DR   CCDS; CCDS43858.1; -. [Q9H330-2]
DR   RefSeq; NP_114401.2; NM_032012.3. [Q9H330-2]
DR   AlphaFoldDB; Q9H330; -.
DR   BioGRID; 117237; 45.
DR   IntAct; Q9H330; 14.
DR   MINT; Q9H330; -.
DR   STRING; 9606.ENSP00000363714; -.
DR   GlyConnect; 1853; 7 N-Linked glycans (2 sites).
DR   GlyGen; Q9H330; 6 sites, 7 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9H330; -.
DR   PhosphoSitePlus; Q9H330; -.
DR   SwissPalm; Q9H330; -.
DR   BioMuta; TMEM245; -.
DR   DMDM; 71152403; -.
DR   EPD; Q9H330; -.
DR   jPOST; Q9H330; -.
DR   MassIVE; Q9H330; -.
DR   MaxQB; Q9H330; -.
DR   PaxDb; Q9H330; -.
DR   PeptideAtlas; Q9H330; -.
DR   PRIDE; Q9H330; -.
DR   ProteomicsDB; 80660; -. [Q9H330-2]
DR   ProteomicsDB; 80661; -. [Q9H330-3]
DR   ProteomicsDB; 80662; -. [Q9H330-4]
DR   Antibodypedia; 7137; 40 antibodies from 9 providers.
DR   DNASU; 23731; -.
DR   Ensembl; ENST00000374586.8; ENSP00000363714.3; ENSG00000106771.13. [Q9H330-2]
DR   GeneID; 23731; -.
DR   KEGG; hsa:23731; -.
DR   MANE-Select; ENST00000374586.8; ENSP00000363714.3; NM_032012.4; NP_114401.2.
DR   UCSC; uc004bdt.5; human. [Q9H330-2]
DR   CTD; 23731; -.
DR   DisGeNET; 23731; -.
DR   GeneCards; TMEM245; -.
DR   HGNC; HGNC:1363; TMEM245.
DR   HPA; ENSG00000106771; Low tissue specificity.
DR   neXtProt; NX_Q9H330; -.
DR   OpenTargets; ENSG00000106771; -.
DR   PharmGKB; PA25980; -.
DR   VEuPathDB; HostDB:ENSG00000106771; -.
DR   eggNOG; KOG2365; Eukaryota.
DR   GeneTree; ENSGT00390000001667; -.
DR   HOGENOM; CLU_005960_0_0_1; -.
DR   InParanoid; Q9H330; -.
DR   OMA; CVHFFWK; -.
DR   OrthoDB; 228524at2759; -.
DR   PhylomeDB; Q9H330; -.
DR   TreeFam; TF315224; -.
DR   PathwayCommons; Q9H330; -.
DR   SignaLink; Q9H330; -.
DR   BioGRID-ORCS; 23731; 12 hits in 1080 CRISPR screens.
DR   ChiTaRS; TMEM245; human.
DR   GenomeRNAi; 23731; -.
DR   Pharos; Q9H330; Tdark.
DR   PRO; PR:Q9H330; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9H330; protein.
DR   Bgee; ENSG00000106771; Expressed in cardiac muscle of right atrium and 197 other tissues.
DR   ExpressionAtlas; Q9H330; baseline and differential.
DR   Genevisible; Q9H330; HS.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   InterPro; IPR002549; AI-2E-like.
DR   PANTHER; PTHR21716; PTHR21716; 1.
DR   Pfam; PF01594; AI-2E_transport; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZA5"
FT   CHAIN           2..879
FT                   /note="Transmembrane protein 245"
FT                   /id="PRO_0000089670"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        626..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        650..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        732..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        776..796
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        815..835
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZA5"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZA5"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZA5"
FT   MOD_RES         36
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3ZXD8"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         334
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         877
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        575
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..448
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_014680"
FT   VAR_SEQ         440..447
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_059402"
FT   VAR_SEQ         511
FT                   /note="N -> K (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_059403"
FT   VAR_SEQ         512..879
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_059404"
FT   VARIANT         9
FT                   /note="D -> E (in dbSNP:rs12001627)"
FT                   /evidence="ECO:0000269|PubMed:10564813"
FT                   /id="VAR_059604"
FT   VARIANT         314
FT                   /note="A -> T (in dbSNP:rs2271877)"
FT                   /id="VAR_056815"
FT   VARIANT         787
FT                   /note="T -> A (in dbSNP:rs3750455)"
FT                   /id="VAR_056816"
FT   CONFLICT        785
FT                   /note="L -> V (in Ref. 2; BAG61779)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        855
FT                   /note="N -> I (in Ref. 2; BAD18785)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   879 AA;  97357 MW;  AD26DE952B1D94AE CRC64;
     MADGGGPKDA PSLRSSPGPA PRVPRAVGPS GGGGETPRTA ALALRFDKPI KQAFYNTGAV
     LFVCLCCGAA VLVYFILEAF LRPLLWAVLC GTFLHPFKSS LTRLGRHWLQ RLHRAHTPIV
     LAALLLPLCF VDYGVEALGE QALRRRRLLL LLGAGGPLLY GLYCLGSYLG VQVLLVHAAT
     LICRGLDYFS SLWIWTLVVG YVLTVSFKWN ASTERYLRAV SIPVWIILLF HLASLAGSWR
     IPVFLVIVFL MSVGTLYEKQ NGKESSGAEL PGQVISMAAS TLANLAISIT GYESSSEDQP
     STQPAEAVDR GESAPTLSTS PSPSSPSPTS PSPTLGRRRP EIGTFLRKKK TSDIYFVSLV
     WAIVVMQIWL NLWIVQLLPV PIAVWILKKL VIHFGVVDFL EKRYHVWWGI IESFLKERQG
     ALAPWPIVGL GKFLLKVDSK LWHWLNKKMI IWLEKMLDKI ISIFIIFLLV IGTLLLALLL
     TAKVHQESVH MIEVTSNLIN ETLANHPEWA NWLPEAQVVQ RALNSAANNV YQYGREWITH
     KLHKILGDKV NNTAVIEKQV LELWDRLYHS WFVKNVTHSG RHKGQKLHVS RQNSWLGDIL
     DWQDIVSFVH ENIETFLSIL ESLWIVMSRN VSLLFTTVTT LLTILFYSGT ALLNFVLSLI
     IFLTTLFYLL SSSDEYYKPV KWVISLTPLS QPGPSSNIIG QSVEEAIRGV FDASLKMAGF
     YGLYTWLTHT MFGINIVFIP SALAAILGAV PFLGTYWAAV PAVLDLWLTQ GLGCKAILLL
     IFHLLPTYFV DTAIYSDISG GGHPYLTGLA VAGGAYYLGL EGAIIGPILL CILVVASNIY
     SAMLVSPTNS VPTPNQTPWP AQPQRTFRDI SEDLKSSVG
 
 
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