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RMD2_HUMAN
ID   RMD2_HUMAN              Reviewed;         410 AA.
AC   Q96LZ7; A9UMZ7; A9UN00; Q4ZG33; Q6UXN4; Q8N657; Q8N9A2; Q8NCV6; Q8NHM0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Regulator of microtubule dynamics protein 2;
DE            Short=RMD-2;
DE            Short=hRMD-2;
DE   AltName: Full=Protein FAM82A1;
GN   Name=RMDN2; Synonyms=FAM82A, FAM82A1; ORFNames=BLOCK18, UNQ9371/PRO34163;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP   ASP-259.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA   Guo J.H., Yu L.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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.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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-410.
RA   Gorry M.C., Zhang Y., Marks J.J., Suppe B., Hart P.S., Cortelli J.R.,
RA   Pallos D., Hart T.C.;
RT   "Physical/genetic map of the 2p22-2p21 region on chromosome 2.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   IDENTIFICATION (ISOFORM 1), INTERACTION WITH MICROTUBULES, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=18070910; DOI=10.1083/jcb.200705108;
RA   Oishi K., Okano H., Sawa H.;
RT   "RMD-1, a novel microtubule-associated protein, functions in chromosome
RT   segregation in Caenorhabditis elegans.";
RL   J. Cell Biol. 179:1149-1162(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139; TYR-152; THR-154 AND
RP   THR-157, AND 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   -!- SUBUNIT: Interacts with microtubules. {ECO:0000269|PubMed:18070910}.
CC   -!- INTERACTION:
CC       Q96LZ7; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-2806908, EBI-741181;
CC       Q96LZ7; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2806908, EBI-11522760;
CC       Q96LZ7; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-2806908, EBI-2548702;
CC       Q96LZ7; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2806908, EBI-11522780;
CC       Q96LZ7; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-2806908, EBI-517508;
CC       Q96LZ7; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-2806908, EBI-1052304;
CC       Q96LZ7; Q8IZV5: RDH10; NbExp=3; IntAct=EBI-2806908, EBI-11913715;
CC       Q96LZ7; O95197-3: RTN3; NbExp=3; IntAct=EBI-2806908, EBI-11525735;
CC       Q96LZ7; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-2806908, EBI-3920694;
CC       Q96LZ7; Q16623: STX1A; NbExp=3; IntAct=EBI-2806908, EBI-712466;
CC       Q96LZ7; Q8WY91: THAP4; NbExp=3; IntAct=EBI-2806908, EBI-726691;
CC       Q96LZ7; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-2806908, EBI-1044859;
CC       Q96LZ7; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-2806908, EBI-1059156;
CC       Q96LZ7; O95292: VAPB; NbExp=4; IntAct=EBI-2806908, EBI-1188298;
CC       Q96LZ7; Q53XM7: VAPB; NbExp=3; IntAct=EBI-2806908, EBI-10178947;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:18070910}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18070910}.
CC       Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18070910}.
CC       Note=In interphase localizes in the cytoplasm, and during mitosis
CC       localizes to the spindle microtubules and spindle poles. Also detected
CC       as large dots in the perinuclear region.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q96LZ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96LZ7-2; Sequence=VSP_025524, VSP_025527;
CC       Name=3;
CC         IsoId=Q96LZ7-3; Sequence=VSP_025525, VSP_025526;
CC       Name=4;
CC         IsoId=Q96LZ7-4; Sequence=VSP_025525;
CC   -!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM81211.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK057516; BAB71517.1; -; mRNA.
DR   EMBL; AK095462; BAC04551.1; -; mRNA.
DR   EMBL; AY358269; AAQ88636.1; -; mRNA.
DR   EMBL; AF435956; AAM20907.1; -; mRNA.
DR   EMBL; AC009229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016689; AAX88865.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00385.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00387.1; -; Genomic_DNA.
DR   EMBL; BC024243; AAH24243.3; -; mRNA.
DR   EMBL; AH011736; AAM81211.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BR000689; FAA00414.1; -; mRNA.
DR   EMBL; BR000692; FAA00417.1; -; mRNA.
DR   CCDS; CCDS1792.1; -. [Q96LZ7-2]
DR   CCDS; CCDS54351.1; -. [Q96LZ7-1]
DR   CCDS; CCDS54352.1; -. [Q96LZ7-4]
DR   RefSeq; NP_001164262.1; NM_001170791.2. [Q96LZ7-1]
DR   RefSeq; NP_001164263.1; NM_001170792.2. [Q96LZ7-1]
DR   RefSeq; NP_001164264.1; NM_001170793.2. [Q96LZ7-4]
DR   RefSeq; NP_001309140.1; NM_001322211.1. [Q96LZ7-1]
DR   RefSeq; NP_653314.3; NM_144713.4.
DR   RefSeq; XP_016858964.1; XM_017003475.1.
DR   AlphaFoldDB; Q96LZ7; -.
DR   SMR; Q96LZ7; -.
DR   BioGRID; 127373; 34.
DR   IntAct; Q96LZ7; 22.
DR   STRING; 9606.ENSP00000234195; -.
DR   iPTMnet; Q96LZ7; -.
DR   PhosphoSitePlus; Q96LZ7; -.
DR   BioMuta; RMDN2; -.
DR   DMDM; 147643051; -.
DR   EPD; Q96LZ7; -.
DR   jPOST; Q96LZ7; -.
DR   MassIVE; Q96LZ7; -.
DR   MaxQB; Q96LZ7; -.
DR   PaxDb; Q96LZ7; -.
DR   PeptideAtlas; Q96LZ7; -.
DR   PRIDE; Q96LZ7; -.
DR   ProteomicsDB; 77272; -. [Q96LZ7-1]
DR   ProteomicsDB; 77273; -. [Q96LZ7-2]
DR   ProteomicsDB; 77274; -. [Q96LZ7-3]
DR   ProteomicsDB; 77275; -. [Q96LZ7-4]
DR   Antibodypedia; 29456; 165 antibodies from 22 providers.
DR   DNASU; 151393; -.
DR   Ensembl; ENST00000354545.8; ENSP00000346549.3; ENSG00000115841.21. [Q96LZ7-1]
DR   Ensembl; ENST00000406384.5; ENSP00000386004.1; ENSG00000115841.21. [Q96LZ7-1]
DR   Ensembl; ENST00000417700.6; ENSP00000392977.2; ENSG00000115841.21. [Q96LZ7-4]
DR   GeneID; 151393; -.
DR   KEGG; hsa:151393; -.
DR   MANE-Select; ENST00000354545.8; ENSP00000346549.3; NM_001170791.3; NP_001164262.1.
DR   UCSC; uc002rql.4; human. [Q96LZ7-1]
DR   CTD; 151393; -.
DR   DisGeNET; 151393; -.
DR   GeneCards; RMDN2; -.
DR   HGNC; HGNC:26567; RMDN2.
DR   HPA; ENSG00000115841; Tissue enhanced (adrenal).
DR   MIM; 611872; gene.
DR   neXtProt; NX_Q96LZ7; -.
DR   OpenTargets; ENSG00000115841; -.
DR   PharmGKB; PA162387925; -.
DR   VEuPathDB; HostDB:ENSG00000115841; -.
DR   eggNOG; ENOG502QS2U; Eukaryota.
DR   GeneTree; ENSGT00950000182992; -.
DR   HOGENOM; CLU_046369_0_0_1; -.
DR   InParanoid; Q96LZ7; -.
DR   OMA; DLGQKNN; -.
DR   OrthoDB; 1380644at2759; -.
DR   PhylomeDB; Q96LZ7; -.
DR   TreeFam; TF315854; -.
DR   PathwayCommons; Q96LZ7; -.
DR   SignaLink; Q96LZ7; -.
DR   BioGRID-ORCS; 151393; 8 hits in 1073 CRISPR screens.
DR   ChiTaRS; RMDN2; human.
DR   GenomeRNAi; 151393; -.
DR   Pharos; Q96LZ7; Tbio.
DR   PRO; PR:Q96LZ7; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q96LZ7; protein.
DR   Bgee; ENSG00000115841; Expressed in adrenal tissue and 133 other tissues.
DR   ExpressionAtlas; Q96LZ7; baseline and differential.
DR   Genevisible; Q96LZ7; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR   GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR   GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW   Microtubule; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..410
FT                   /note="Regulator of microtubule dynamics protein 2"
FT                   /id="PRO_0000287504"
FT   TRANSMEM        9..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          122..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          68..110
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        132..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BSE0"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q498D5"
FT   MOD_RES         139
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         152
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         154
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         157
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..151
FT                   /note="MPYSTNKELILGIMVGTAGISLLLLWYHKVRKPGIAMKLPEFLSLGNTFNSI
FT                   TLQDEIHDDQGTTVIFQERQLQILEKLNELLTNMEELKEEIRFLKEAIPKLEEYIQDEL
FT                   GGKITVHKISPQHRARKRRLPTIQSSATSNSSEEAESEGG -> MGKCLSCCKEDQSFQ
FT                   RCSPEDQVSTDAQHRGASSISQPSISLGHKTSYSPVTHKVNAAKASRRLLSVSSPSFSE
FT                   RRYSLFVGFQKRNASPYWQQSRANFDSEEDTGFTDIKSSSDHCGSFISRRRRFSSRKLS
FT                   IVSYYKSAIFFDPQASGQNVFNLNEIEIFSKTSSNTDAKKHITISAPEYNTKNFKNFET
FT                   NTTSPAFGNTIDTASYQQSTSSFFSLASDISSPDQQNGIANDIQQRGQLCKDLKDFLHP
FT                   RPESYSTGHSPIMIPQHPSQSGTFPFLHKAGFSSSYKNSGCFIPPQSELTSGLFEDEDF
FT                   AVLFQDEDRSSPIEIPKIR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_025524"
FT   VAR_SEQ         1..151
FT                   /note="MPYSTNKELILGIMVGTAGISLLLLWYHKVRKPGIAMKLPEFLSLGNTFNSI
FT                   TLQDEIHDDQGTTVIFQERQLQILEKLNELLTNMEELKEEIRFLKEAIPKLEEYIQDEL
FT                   GGKITVHKISPQHRARKRRLPTIQSSATSNSSEEAESEGG -> MGKCLR (in
FT                   isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT                   /id="VSP_025525"
FT   VAR_SEQ         349..410
FT                   /note="AEELCPGYSNPNYMYLAKCYTDLEENQNALKFCNLALLLPTVTKEDKEAQKE
FT                   MQKIMTSLKR -> VHFVYPLF (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_025526"
FT   VAR_SEQ         394..410
FT                   /note="DKEAQKEMQKIMTSLKR -> EL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_025527"
FT   VARIANT         259
FT                   /note="G -> D (in dbSNP:rs4670800)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_032316"
FT   CONFLICT        Q96LZ7-2:259
FT                   /note="G -> D (in Ref. 1; BAB71517)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   410 AA;  47399 MW;  DE5249E5808CA42A CRC64;
     MPYSTNKELI LGIMVGTAGI SLLLLWYHKV RKPGIAMKLP EFLSLGNTFN SITLQDEIHD
     DQGTTVIFQE RQLQILEKLN ELLTNMEELK EEIRFLKEAI PKLEEYIQDE LGGKITVHKI
     SPQHRARKRR LPTIQSSATS NSSEEAESEG GYITANTDTE EQSFPVPKAF NTRVEELNLD
     VLLQKVDHLR MSESGKSESF ELLRDHKEKF RDEIEFMWRF ARAYGDMYEL STNTQEKKHY
     ANIGKTLSER AINRAPMNGH CHLWYAVLCG YVSEFEGLQN KINYGHLFKE HLDIAIKLLP
     EEPFLYYLKG RYCYTVSKLS WIEKKMAATL FGKIPSSTVQ EALHNFLKAE ELCPGYSNPN
     YMYLAKCYTD LEENQNALKF CNLALLLPTV TKEDKEAQKE MQKIMTSLKR
 
 
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