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ADA29_HUMAN
ID   ADA29_HUMAN             Reviewed;         820 AA.
AC   Q9UKF5; Q4W5F3; Q9UHP1; Q9UKF3; Q9UKF4;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 3.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 29;
DE            Short=ADAM 29;
DE   AltName: Full=Cancer/testis antigen 73;
DE            Short=CT73;
DE   Flags: Precursor;
GN   Name=ADAM29;
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] (ISOFORMS ALPHA; BETA AND GAMMA).
RC   TISSUE=Testis;
RX   PubMed=10512762; DOI=10.1006/bbrc.1999.1322;
RA   Cerretti D.P., DuBose R.F., Black R.A., Nelson N.;
RT   "Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that
RT   show testis-specific gene expression.";
RL   Biochem. Biophys. Res. Commun. 263:810-815(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC   TISSUE=Testis;
RX   PubMed=10644455; DOI=10.1006/geno.1999.6029;
RA   Xu R., Cai J., Xu T., Zhou W., Ying B., Deng K., Zhao S., Li C.;
RT   "Molecular cloning and mapping of a novel ADAM gene (ADAM29) to human
RT   chromosome 4.";
RL   Genomics 62:537-539(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC   TISSUE=Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INVOLVEMENT IN CUTANEOUS MELANOMA, VARIANTS PHE-72; MET-89; LYS-111;
RP   PHE-112; PHE-115; ASN-131; LYS-176; PHE-234; PHE-257; GLU-305; ASN-345;
RP   ASP-403; ASP-434; LYS-503 AND TYR-533, AND CHARACTERIZATION OF VARIANTS
RP   LYS-111; PHE-112; PHE-115; PHE-257; ASP-434 AND LYS-503.
RX   PubMed=21618342; DOI=10.1002/humu.21477;
RA   Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U.,
RA   Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.;
RT   "Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and
RT   ADAM7 are often mutated in melanoma.";
RL   Hum. Mutat. 32:E2148-E2175(2011).
RN   [7]
RP   VARIANTS [LARGE SCALE ANALYSIS] LEU-31 AND ILE-205.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May be involved in spermatogenesis and fertilization. Seems
CC       to be a non catalytic metalloprotease-like protein.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Alpha;
CC         IsoId=Q9UKF5-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=Q9UKF5-2; Sequence=VSP_005491;
CC       Name=Gamma;
CC         IsoId=Q9UKF5-3; Sequence=VSP_005492, VSP_005493;
CC   -!- TISSUE SPECIFICITY: Expressed specifically in testes.
CC   -!- DISEASE: Note=Has been found to be frequently mutated in melanoma.
CC       ADAM7 mutations may play a role in melanoma progression and metastasis.
CC       {ECO:0000269|PubMed:21618342}.
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DR   EMBL; AF171929; AAF03777.1; -; mRNA.
DR   EMBL; AF171930; AAF03778.1; -; mRNA.
DR   EMBL; AF171931; AAF03779.1; -; mRNA.
DR   EMBL; AF134708; AAF22163.1; -; mRNA.
DR   EMBL; AK292410; BAF85099.1; -; mRNA.
DR   EMBL; AC105914; AAY41055.1; -; Genomic_DNA.
DR   EMBL; CH471056; EAX04727.1; -; Genomic_DNA.
DR   EMBL; CH471056; EAX04728.1; -; Genomic_DNA.
DR   CCDS; CCDS3823.1; -. [Q9UKF5-1]
DR   RefSeq; NP_001124175.1; NM_001130703.1. [Q9UKF5-1]
DR   RefSeq; NP_001124176.1; NM_001130704.1. [Q9UKF5-1]
DR   RefSeq; NP_001124177.1; NM_001130705.1. [Q9UKF5-1]
DR   RefSeq; NP_001265054.1; NM_001278125.1. [Q9UKF5-1]
DR   RefSeq; NP_001265055.1; NM_001278126.1. [Q9UKF5-1]
DR   RefSeq; NP_001265056.1; NM_001278127.1. [Q9UKF5-1]
DR   RefSeq; NP_055084.3; NM_014269.4. [Q9UKF5-1]
DR   RefSeq; XP_011529858.1; XM_011531556.1. [Q9UKF5-1]
DR   RefSeq; XP_011529859.1; XM_011531557.1. [Q9UKF5-1]
DR   RefSeq; XP_011529861.1; XM_011531559.1. [Q9UKF5-1]
DR   RefSeq; XP_011529862.1; XM_011531560.1. [Q9UKF5-1]
DR   RefSeq; XP_011529863.1; XM_011531561.1. [Q9UKF5-1]
DR   AlphaFoldDB; Q9UKF5; -.
DR   SMR; Q9UKF5; -.
DR   BioGRID; 116268; 1.
DR   IntAct; Q9UKF5; 1.
DR   STRING; 9606.ENSP00000484862; -.
DR   MEROPS; M12.981; -.
DR   GlyGen; Q9UKF5; 9 sites.
DR   iPTMnet; Q9UKF5; -.
DR   PhosphoSitePlus; Q9UKF5; -.
DR   BioMuta; ADAM29; -.
DR   DMDM; 145559438; -.
DR   MassIVE; Q9UKF5; -.
DR   MaxQB; Q9UKF5; -.
DR   PaxDb; Q9UKF5; -.
DR   PeptideAtlas; Q9UKF5; -.
DR   PRIDE; Q9UKF5; -.
DR   ProteomicsDB; 84779; -. [Q9UKF5-1]
DR   ProteomicsDB; 84780; -. [Q9UKF5-2]
DR   ProteomicsDB; 84781; -. [Q9UKF5-3]
DR   Antibodypedia; 2608; 93 antibodies from 27 providers.
DR   DNASU; 11086; -.
DR   Ensembl; ENST00000359240.7; ENSP00000352177.3; ENSG00000168594.15. [Q9UKF5-1]
DR   Ensembl; ENST00000404450.8; ENSP00000384229.3; ENSG00000168594.15. [Q9UKF5-1]
DR   Ensembl; ENST00000445694.5; ENSP00000414544.1; ENSG00000168594.15. [Q9UKF5-1]
DR   Ensembl; ENST00000514159.1; ENSP00000423517.1; ENSG00000168594.15. [Q9UKF5-1]
DR   Ensembl; ENST00000615367.4; ENSP00000484862.1; ENSG00000168594.15. [Q9UKF5-1]
DR   Ensembl; ENST00000618444.1; ENSP00000478469.1; ENSG00000168594.15. [Q9UKF5-1]
DR   GeneID; 11086; -.
DR   KEGG; hsa:11086; -.
DR   MANE-Select; ENST00000359240.7; ENSP00000352177.3; NM_014269.4; NP_055084.3.
DR   UCSC; uc003iuc.3; human. [Q9UKF5-1]
DR   CTD; 11086; -.
DR   DisGeNET; 11086; -.
DR   GeneCards; ADAM29; -.
DR   HGNC; HGNC:207; ADAM29.
DR   HPA; ENSG00000168594; Tissue enriched (testis).
DR   MIM; 604778; gene.
DR   neXtProt; NX_Q9UKF5; -.
DR   OpenTargets; ENSG00000168594; -.
DR   PharmGKB; PA24524; -.
DR   VEuPathDB; HostDB:ENSG00000168594; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000163394; -.
DR   HOGENOM; CLU_012714_4_0_1; -.
DR   InParanoid; Q9UKF5; -.
DR   OMA; TSHMCPD; -.
DR   PhylomeDB; Q9UKF5; -.
DR   TreeFam; TF314733; -.
DR   PathwayCommons; Q9UKF5; -.
DR   BioGRID-ORCS; 11086; 9 hits in 1070 CRISPR screens.
DR   ChiTaRS; ADAM29; human.
DR   GenomeRNAi; 11086; -.
DR   Pharos; Q9UKF5; Tbio.
DR   PRO; PR:Q9UKF5; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9UKF5; protein.
DR   Bgee; ENSG00000168594; Expressed in sperm and 79 other tissues.
DR   ExpressionAtlas; Q9UKF5; baseline and differential.
DR   Genevisible; Q9UKF5; HS.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1990913; C:sperm head plasma membrane; IBA:GO_Central.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..193
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029134"
FT   CHAIN           194..820
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 29"
FT                   /id="PRO_0000029135"
FT   TOPO_DOM        194..674
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        675..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        696..820
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          198..390
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          397..483
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          625..654
FT                   /note="EGF-like"
FT   REPEAT          739..747
FT                   /note="1"
FT   REPEAT          748..756
FT                   /note="2"
FT   REPEAT          757..765
FT                   /note="3"
FT   REPEAT          766..774
FT                   /note="4"
FT   REPEAT          775..783
FT                   /note="5"
FT   REPEAT          784..792
FT                   /note="6"
FT   REPEAT          793..801
FT                   /note="7"
FT   REPEAT          802..810
FT                   /note="8"
FT   REPEAT          811..819
FT                   /note="9"
FT   REGION          706..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..819
FT                   /note="9 X 9 AA approximate repeats"
FT   COMPBIAS        706..726
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        538
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        558
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        307..384
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..354
FT                   /evidence="ECO:0000250"
FT   DISULFID        455..475
FT                   /evidence="ECO:0000250"
FT   DISULFID        625..636
FT                   /evidence="ECO:0000250"
FT   DISULFID        630..642
FT                   /evidence="ECO:0000250"
FT   DISULFID        644..653
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         750..803
FT                   /note="Missing (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:10512762"
FT                   /id="VSP_005491"
FT   VAR_SEQ         763..787
FT                   /note="VTPSQSQPRVMPSQSQPPVMPSQSH -> QNLFLFSFSISDCVLNFRLLYLQ
FT                   AT (in isoform Gamma)"
FT                   /evidence="ECO:0000303|PubMed:10512762"
FT                   /id="VSP_005492"
FT   VAR_SEQ         788..820
FT                   /note="Missing (in isoform Gamma)"
FT                   /evidence="ECO:0000303|PubMed:10512762"
FT                   /id="VSP_005493"
FT   VARIANT         31
FT                   /note="P -> L (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs544557652)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036148"
FT   VARIANT         72
FT                   /note="L -> F (in a melanoma cell line)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066322"
FT   VARIANT         89
FT                   /note="I -> M (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066323"
FT   VARIANT         111
FT                   /note="E -> K (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; increases the adhesion of melanoma cells
FT                   to collagens I and IV; dbSNP:rs267600087)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066324"
FT   VARIANT         112
FT                   /note="S -> F (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; increases the adhesion of melanoma cells
FT                   to collagens I and IV)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066325"
FT   VARIANT         115
FT                   /note="S -> F (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; increases the adhesion of melanoma cells
FT                   to collagens I and IV)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066326"
FT   VARIANT         131
FT                   /note="D -> N (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066327"
FT   VARIANT         176
FT                   /note="E -> K (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs899870236)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066328"
FT   VARIANT         205
FT                   /note="V -> I (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs772388824)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036149"
FT   VARIANT         234
FT                   /note="S -> F (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs866380131)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066329"
FT   VARIANT         257
FT                   /note="I -> F (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; increases the adhesion of melanoma cells
FT                   to collagens I and IV; dbSNP:rs140083180)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066330"
FT   VARIANT         305
FT                   /note="G -> E (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs267600089)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066331"
FT   VARIANT         345
FT                   /note="D -> N (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs267600090)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066332"
FT   VARIANT         403
FT                   /note="G -> D (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs150047888)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066333"
FT   VARIANT         434
FT                   /note="G -> D (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; increases the adhesion of melanoma cells
FT                   to collagens I and IV; dbSNP:rs267600091)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066334"
FT   VARIANT         503
FT                   /note="E -> K (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; increases the adhesion of melanoma cells
FT                   to collagens I and IV)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066335"
FT   VARIANT         533
FT                   /note="H -> Y (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs267600093)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066336"
FT   CONFLICT        196
FT                   /note="H -> Y (in Ref. 2; AAF22163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        744
FT                   /note="P -> H (in Ref. 2; AAF22163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        748
FT                   /note="S -> Y (in Ref. 2; AAF22163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        753
FT                   /note="Q -> R (in Ref. 1; AAF03777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        764
FT                   /note="T -> M (in Ref. 1; AAF03777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        769..773
FT                   /note="QPRVM -> HPQLT (in Ref. 1; AAF03777)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   820 AA;  92759 MW;  AA2FB11342A884C9 CRC64;
     MKMLLLLHCL GVFLSCSGHI QDEHPQYHSP PDVVIPVRIT GTTRGMTPPG WLSYILPFGG
     QKHIIHIKVK KLLFSKHLPV FTYTDQGAIL EDQPFVQNNC YYHGYVEGDP ESLVSLSTCF
     GGFQGILQIN DFAYEIKPLA FSTTFEHLVY KMDSEEKQFS TMRSGFMQNE ITCRMEFEEI
     DNSTQKQSSY VGWWIHFRIV EIVVVIDNYL YIRYERNDSK LLEDLYVIVN IVDSILDVIG
     VKVLLFGLEI WTNKNLIVVD DVRKSVHLYC KWKSENITPR MQHDTSHLFT TLGLRGLSGI
     GAFRGMCTPH RSCAIVTFMN KTLGTFSIAV AHHLGHNLGM NHDEDTCRCS QPRCIMHEGN
     PPITKFSNCS YGDFWEYTVE RTKCLLETVH TKDIFNVKRC GNGVVEEGEE CDCGPLKHCA
     KDPCCLSNCT LTDGSTCAFG LCCKDCKFLP SGKVCRKEVN ECDLPEWCNG TSHKCPDDFY
     VEDGIPCKER GYCYEKSCHD RNEQCRRIFG AGANTASETC YKELNTLGDR VGHCGIKNAT
     YIKCNISDVQ CGRIQCENVT EIPNMSDHTT VHWARFNDIM CWSTDYHLGM KGPDIGEVKD
     GTECGIDHIC IHRHCVHITI LNSNCSPAFC NKRGICNNKH HCHCNYLWDP PNCLIKGYGG
     SVDSGPPPKR KKKKKFCYLC ILLLIVLFIL LCCLYRLCKK SKPIKKQQDV QTPSAKEEEK
     IQRRPHELPP QSQPWVMPSQ SQPPVTPSQS HPQVMPSQSQ PPVTPSQSQP RVMPSQSQPP
     VMPSQSHPQL TPSQSQPPVT PSQRQPQLMP SQSQPPVTPS
 
 
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