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KAZRN_HUMAN
ID   KAZRN_HUMAN             Reviewed;         775 AA.
AC   Q674X7; B0QYQ0; B1AJZ1; B1AK78; Q5TGF1; Q674X4; Q674X6; Q6ZUD1; Q8IYN7;
AC   Q8N409; Q9UIL2; Q9UPX4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Kazrin;
GN   Name=KAZN {ECO:0000312|HGNC:HGNC:29173};
GN   Synonyms=C1orf196 {ECO:0000312|HGNC:HGNC:29173}, KAZ, KIAA1026;
GN   ORFNames=HRIHFB2003;
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 2; 3 AND 4), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH PPL.
RC   TISSUE=Spinal ganglion;
RX   PubMed=15337775; DOI=10.1083/jcb.200312123;
RA   Groot K.R., Sevilla L.M., Nishi K., DiColandrea T., Watt F.M.;
RT   "Kazrin, a novel periplakin-interacting protein associated with desmosomes
RT   and the keratinocyte plasma membrane.";
RL   J. Cell Biol. 166:653-659(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Uterus;
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 109-775 (ISOFORM 4), AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Fetal brain;
RX   PubMed=9853615; DOI=10.1038/4315;
RA   Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT   "Selection system for genes encoding nuclear-targeted proteins.";
RL   Nat. Biotechnol. 16:1338-1342(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 536-775 (ISOFORM 1), AND VARIANT
RP   THR-706.
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352 AND SER-387, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
CC   -!- FUNCTION: Component of the cornified envelope of keratinocytes. May be
CC       involved in the interplay between adherens junctions and desmosomes.
CC       The function in the nucleus is not known.
CC       {ECO:0000269|PubMed:15337775}.
CC   -!- SUBUNIT: Isoform 2, isoform 3 and isoform 4 interact with PPL N-
CC       terminus.
CC   -!- INTERACTION:
CC       Q674X7; P51114: FXR1; NbExp=2; IntAct=EBI-949239, EBI-713291;
CC       Q674X7; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-949239, EBI-741037;
CC       Q674X7; Q92574: TSC1; NbExp=2; IntAct=EBI-949239, EBI-1047085;
CC       Q674X7-2; Q03989: ARID5A; NbExp=3; IntAct=EBI-12024294, EBI-948603;
CC       Q674X7-2; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-12024294, EBI-12357161;
CC       Q674X7-2; Q92997: DVL3; NbExp=3; IntAct=EBI-12024294, EBI-739789;
CC       Q674X7-2; P25791-3: LMO2; NbExp=3; IntAct=EBI-12024294, EBI-11959475;
CC       Q674X7-2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-12024294, EBI-1216080;
CC       Q674X7-2; P25786: PSMA1; NbExp=6; IntAct=EBI-12024294, EBI-359352;
CC       Q674X7-2; Q8IZW8: TNS4; NbExp=3; IntAct=EBI-12024294, EBI-7543499;
CC       Q674X7-2; Q99757: TXN2; NbExp=3; IntAct=EBI-12024294, EBI-2932492;
CC       Q674X7-2; O75604: USP2; NbExp=3; IntAct=EBI-12024294, EBI-743272;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Cell junction, desmosome.
CC       Nucleus. Note=Observed at the apical plasma membrane of keratinocytes.
CC       Partially colocalizes with PPL and DP at desmosomes, and with PP at the
CC       interdesmosomal plasma membrane. Colocalizes with cortical actin-based
CC       membrane structures.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Cell junction, desmosome.
CC       Nucleus. Note=Observed at the apical plasma membrane of keratinocytes.
CC       Partially colocalizes with PPL and DP at desmosomes, and with PP at the
CC       interdesmosomal plasma membrane. Colocalizes with cortical actin-based
CC       membrane structures.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Cell junction, desmosome.
CC       Nucleus. Note=Observed at the apical plasma membrane of keratinocytes.
CC       Partially colocalizes with PPL and DP at desmosomes, and with PP at the
CC       interdesmosomal plasma membrane. Colocalizes with cortical actin-based
CC       membrane structures.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q674X7-1; Sequence=Displayed;
CC       Name=2; Synonyms=A;
CC         IsoId=Q674X7-2; Sequence=VSP_031901, VSP_031903;
CC       Name=3; Synonyms=B;
CC         IsoId=Q674X7-3; Sequence=VSP_031899, VSP_031901, VSP_031903;
CC       Name=4; Synonyms=C, D;
CC         IsoId=Q674X7-4; Sequence=VSP_031898, VSP_031901, VSP_031903;
CC       Name=5;
CC         IsoId=Q674X7-5; Sequence=VSP_031900, VSP_031902;
CC   -!- TISSUE SPECIFICITY: Isoform 2, isoform 3 and isoform 4 are expressed in
CC       several cell lines including keratinocytes and bladder and epidermoid
CC       carcinoma (at protein level). Isoform 2, isoform 3 and isoform 4 are
CC       expressed in hair follicle and interfollicular epidermis (at protein
CC       level). {ECO:0000269|PubMed:15337775}.
CC   -!- SIMILARITY: Belongs to the kazrin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH36877.1; Type=Miscellaneous discrepancy; Note=The cDNA sequence has been translated in the reverse direction.; Evidence={ECO:0000305};
CC       Sequence=AAI01638.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI13622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA82978.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA88115.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC86294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY505119; AAS86434.1; -; mRNA.
DR   EMBL; AY505120; AAS86435.1; -; mRNA.
DR   EMBL; AY505121; AAS86436.1; -; mRNA.
DR   EMBL; AY505122; AAS86437.1; -; mRNA.
DR   EMBL; AB028949; BAA82978.1; ALT_INIT; mRNA.
DR   EMBL; AL034395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL035405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471167; EAW51704.1; -; Genomic_DNA.
DR   EMBL; BC035501; AAH35501.3; -; mRNA.
DR   EMBL; BC036877; AAH36877.1; ALT_SEQ; mRNA.
DR   EMBL; BC101637; AAI01638.1; ALT_INIT; mRNA.
DR   EMBL; BC113621; AAI13622.1; ALT_INIT; mRNA.
DR   EMBL; AB015329; BAA88115.1; ALT_FRAME; mRNA.
DR   EMBL; AK125794; BAC86294.1; ALT_INIT; mRNA.
DR   CCDS; CCDS152.2; -. [Q674X7-1]
DR   CCDS; CCDS30604.1; -. [Q674X7-3]
DR   CCDS; CCDS41267.1; -. [Q674X7-2]
DR   CCDS; CCDS41268.1; -. [Q674X7-4]
DR   RefSeq; NP_001017999.1; NM_001017999.2. [Q674X7-4]
DR   RefSeq; NP_001018000.1; NM_001018000.3. [Q674X7-3]
DR   RefSeq; NP_001018001.1; NM_001018001.2. [Q674X7-4]
DR   RefSeq; NP_056024.1; NM_015209.2. [Q674X7-2]
DR   RefSeq; NP_963922.2; NM_201628.2. [Q674X7-1]
DR   RefSeq; XP_016856260.1; XM_017000771.1. [Q674X7-2]
DR   AlphaFoldDB; Q674X7; -.
DR   SMR; Q674X7; -.
DR   BioGRID; 116858; 27.
DR   IntAct; Q674X7; 16.
DR   MINT; Q674X7; -.
DR   STRING; 9606.ENSP00000365198; -.
DR   GlyGen; Q674X7; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q674X7; -.
DR   PhosphoSitePlus; Q674X7; -.
DR   BioMuta; HGNC:32336; -.
DR   BioMuta; KAZN; -.
DR   DMDM; 172044653; -.
DR   EPD; Q674X7; -.
DR   jPOST; Q674X7; -.
DR   MassIVE; Q674X7; -.
DR   MaxQB; Q674X7; -.
DR   PaxDb; Q674X7; -.
DR   PeptideAtlas; Q674X7; -.
DR   PRIDE; Q674X7; -.
DR   ProteomicsDB; 3001; -.
DR   ProteomicsDB; 65976; -. [Q674X7-1]
DR   ProteomicsDB; 65977; -. [Q674X7-2]
DR   ProteomicsDB; 65978; -. [Q674X7-3]
DR   ProteomicsDB; 65979; -. [Q674X7-4]
DR   ProteomicsDB; 65980; -. [Q674X7-5]
DR   Antibodypedia; 28740; 109 antibodies from 19 providers.
DR   DNASU; 23254; -.
DR   Ensembl; ENST00000361144.9; ENSP00000354727.5; ENSG00000189337.17. [Q674X7-3]
DR   Ensembl; ENST00000376030.7; ENSP00000365198.2; ENSG00000189337.17. [Q674X7-1]
DR   Ensembl; ENST00000400797.3; ENSP00000383601.3; ENSG00000189337.17. [Q674X7-4]
DR   Ensembl; ENST00000400798.6; ENSP00000383602.2; ENSG00000189337.17. [Q674X7-4]
DR   Ensembl; ENST00000503743.5; ENSP00000426015.1; ENSG00000189337.17. [Q674X7-2]
DR   GeneID; 23254; -.
DR   KEGG; hsa:23254; -.
DR   MANE-Select; ENST00000376030.7; ENSP00000365198.2; NM_201628.3; NP_963922.2.
DR   UCSC; uc001avm.5; human. [Q674X7-1]
DR   CTD; 23254; -.
DR   DisGeNET; 23254; -.
DR   GeneCards; KAZN; -.
DR   HGNC; HGNC:29173; KAZN.
DR   HPA; ENSG00000189337; Tissue enhanced (lymphoid).
DR   MIM; 618301; gene.
DR   neXtProt; NX_Q674X7; -.
DR   OpenTargets; ENSG00000189337; -.
DR   VEuPathDB; HostDB:ENSG00000189337; -.
DR   eggNOG; KOG0249; Eukaryota.
DR   GeneTree; ENSGT00940000154570; -.
DR   HOGENOM; CLU_010768_2_0_1; -.
DR   InParanoid; Q674X7; -.
DR   OrthoDB; 558442at2759; -.
DR   PhylomeDB; Q674X7; -.
DR   TreeFam; TF331216; -.
DR   TreeFam; TF343181; -.
DR   PathwayCommons; Q674X7; -.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   SignaLink; Q674X7; -.
DR   BioGRID-ORCS; 23254; 10 hits in 1079 CRISPR screens.
DR   ChiTaRS; KAZN; human.
DR   GenomeRNAi; 23254; -.
DR   Pharos; Q674X7; Tbio.
DR   PRO; PR:Q674X7; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q674X7; protein.
DR   Bgee; ENSG00000189337; Expressed in cerebellar vermis and 197 other tissues.
DR   ExpressionAtlas; Q674X7; baseline and differential.
DR   Genevisible; Q674X7; HS.
DR   GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0030057; C:desmosome; IDA:MGI.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   CDD; cd09564; SAM_kazrin_repeat1; 1.
DR   CDD; cd09567; SAM_kazrin_repeat2; 1.
DR   CDD; cd09570; SAM_kazrin_repeat3; 1.
DR   Gene3D; 1.10.150.50; -; 3.
DR   InterPro; IPR037614; Kazrin.
DR   InterPro; IPR037613; Kazrin_SAM_rpt_1.
DR   InterPro; IPR037615; Kazrin_SAM_rpt_2.
DR   InterPro; IPR037616; Kazrin_SAM_rpt_3.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR12776; PTHR12776; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SSF47769; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Keratinization; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..775
FT                   /note="Kazrin"
FT                   /id="PRO_0000322453"
FT   DOMAIN          446..511
FT                   /note="SAM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          524..588
FT                   /note="SAM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          612..679
FT                   /note="SAM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          38..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..333
FT                   /note="Interaction with PPL"
FT                   /evidence="ECO:0000269|PubMed:15337775"
FT   REGION          290..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          688..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          74..256
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        311..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..760
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69ZS8"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..94
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15337775,
FT                   ECO:0000303|PubMed:9853615"
FT                   /id="VSP_031898"
FT   VAR_SEQ         1..75
FT                   /note="MMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGA
FT                   AASASAAGDSAATNMENPQLGAQ -> MRAADSGSWERVRQLAAQGEPAPSCGAGAGPA
FT                   RPPGPAACEQCVDAAGPGDRPRAGVPRVRADGDCSQP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15337775,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031899"
FT   VAR_SEQ         350..421
FT                   /note="GDSPGPVQKNLHNPIVQSLEDLEDQKRKKKKEKMGFGSISRVFARGKQRKSL
FT                   DPGLFDDSDSQCSPTRQSLS -> VRPAAAGPGPLGPAQKLQGRGWRGEAILAVSSRPP
FT                   REHSGECISCSVLSFCKKRWMWGEKGMRPVCSLCPGG (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10470851"
FT                   /id="VSP_031900"
FT   VAR_SEQ         408..422
FT                   /note="DSDSQCSPTRQSLSL -> GTAPDYYIEEDADW (in isoform 2,
FT                   isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15337775,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9853615"
FT                   /id="VSP_031901"
FT   VAR_SEQ         422..775
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10470851"
FT                   /id="VSP_031902"
FT   VAR_SEQ         423..775
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15337775,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9853615"
FT                   /id="VSP_031903"
FT   VARIANT         706
FT                   /note="A -> T (in dbSNP:rs10803354)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_060168"
FT   VARIANT         763
FT                   /note="R -> C (in dbSNP:rs12048768)"
FT                   /id="VAR_060169"
FT   CONFLICT        348..349
FT                   /note="CN -> S (in Ref. 6; BAA88115)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   775 AA;  86351 MW;  7A13B7F262C79294 CRC64;
     MMEDNKQLAL RIDGAVQSAS QEVTNLRAEL TATNRRLAEL SGGGGPGPGP GAAASASAAG
     DSAATNMENP QLGAQVLLRE EVSRLQEEVH LLRQMKEMLA KDLEESQGGK SSEVLSATEL
     RVQLAQKEQE LARAKEALQA MKADRKRLKG EKTDLVSQMQ QLYATLESRE EQLRDFIRNY
     EQHRKESEDA VKALAKEKDL LEREKWELRR QAKEATDHAT ALRSQLDLKD NRMKELEAEL
     AMAKQSLATL TKDVPKRHSL AMPGETVLNG NQEWVVQADL PLTAAIRQSQ QTLYHSHPPH
     PADRQAVRVS PCHSRQPSVI SDASAAEGDR SSTPSDINSP RHRTHSLCNG DSPGPVQKNL
     HNPIVQSLED LEDQKRKKKK EKMGFGSISR VFARGKQRKS LDPGLFDDSD SQCSPTRQSL
     SLSEGEEQMD RLQQVELVRT TPMSHWKAGT VQAWLEVVMA MPMYVKACTE NVKSGKVLLS
     LSDEDLQLGL GVCSSLHRRK LRLAIEDYRD AEAGRSLSKA AELDHHWVAK AWLNDIGLSQ
     YSQAFQNHLV DGRMLNSLMK RDLEKHLNVS KKFHQVSILL GIELLYQVNF SREALQERRA
     RCETQNIDPV VWTNQRVLKW VRDIDLKEYA DNLTNSGVHG AVLVLEPTFN AEAMATALGI
     PSGKHILRRH LAEEMSAVFH PANSTGIREA ERFGTPPGRA SSVTRAGKEE NSSGLKYKAG
     RLPLGKIGRG FSSKDPDFHD DYGSLQNEDC GDDDPQSRLE QCRLEGYNSL EVTNV
 
 
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