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KRT82_HUMAN
ID   KRT82_HUMAN             Reviewed;         513 AA.
AC   Q9NSB4;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 3.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Keratin, type II cuticular Hb2;
DE   AltName: Full=Keratin-82;
DE            Short=K82;
DE   AltName: Full=Type II hair keratin Hb2;
DE   AltName: Full=Type-II keratin Kb22;
GN   Name=KRT82; Synonyms=KRTHB2;
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 [GENOMIC DNA].
RX   PubMed=10692104; DOI=10.1046/j.1523-1747.2000.00910.x;
RA   Rogers M.A., Winter H., Langbein L., Wolf C., Schweizer J.;
RT   "Characterization of a 300 kbp region of human DNA containing the type II
RT   hair keratin.";
RL   J. Invest. Dermatol. 114:464-472(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC   -!- INTERACTION:
CC       Q9NSB4; P27658: COL8A1; NbExp=3; IntAct=EBI-1045341, EBI-747133;
CC       Q9NSB4; O14964: HGS; NbExp=3; IntAct=EBI-1045341, EBI-740220;
CC       Q9NSB4; P49639: HOXA1; NbExp=3; IntAct=EBI-1045341, EBI-740785;
CC       Q9NSB4; P19012: KRT15; NbExp=3; IntAct=EBI-1045341, EBI-739566;
CC       Q9NSB4; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1045341, EBI-3044087;
CC       Q9NSB4; Q15323: KRT31; NbExp=3; IntAct=EBI-1045341, EBI-948001;
CC       Q9NSB4; Q14525: KRT33B; NbExp=3; IntAct=EBI-1045341, EBI-1049638;
CC       Q9NSB4; O76011: KRT34; NbExp=3; IntAct=EBI-1045341, EBI-1047093;
CC       Q9NSB4; Q92764: KRT35; NbExp=3; IntAct=EBI-1045341, EBI-1058674;
CC       Q9NSB4; Q6A162: KRT40; NbExp=3; IntAct=EBI-1045341, EBI-10171697;
CC       Q9NSB4; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-1045341, EBI-769257;
CC       Q9NSB4; Q08AM6: VAC14; NbExp=3; IntAct=EBI-1045341, EBI-2107455;
CC   -!- MISCELLANEOUS: There are two types of hair/microfibrillar keratin, I
CC       (acidic) and II (neutral to basic).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; Y19207; CAB76827.2; -; Genomic_DNA.
DR   EMBL; AC078865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS8826.1; -.
DR   RefSeq; NP_149022.3; NM_033033.3.
DR   AlphaFoldDB; Q9NSB4; -.
DR   SMR; Q9NSB4; -.
DR   BioGRID; 110086; 31.
DR   ComplexPortal; CPX-5664; Keratin-80- Keratin-82 dimer complex.
DR   IntAct; Q9NSB4; 16.
DR   STRING; 9606.ENSP00000257974; -.
DR   iPTMnet; Q9NSB4; -.
DR   PhosphoSitePlus; Q9NSB4; -.
DR   BioMuta; KRT82; -.
DR   DMDM; 148887391; -.
DR   EPD; Q9NSB4; -.
DR   jPOST; Q9NSB4; -.
DR   MassIVE; Q9NSB4; -.
DR   PaxDb; Q9NSB4; -.
DR   PeptideAtlas; Q9NSB4; -.
DR   PRIDE; Q9NSB4; -.
DR   ProteomicsDB; 82524; -.
DR   Antibodypedia; 55914; 104 antibodies from 23 providers.
DR   DNASU; 3888; -.
DR   Ensembl; ENST00000257974.3; ENSP00000257974.3; ENSG00000161850.3.
DR   GeneID; 3888; -.
DR   KEGG; hsa:3888; -.
DR   MANE-Select; ENST00000257974.3; ENSP00000257974.3; NM_033033.4; NP_149022.3.
DR   UCSC; uc001sai.2; human.
DR   CTD; 3888; -.
DR   GeneCards; KRT82; -.
DR   HGNC; HGNC:6459; KRT82.
DR   HPA; ENSG00000161850; Tissue enriched (skin).
DR   MIM; 601078; gene.
DR   neXtProt; NX_Q9NSB4; -.
DR   OpenTargets; ENSG00000161850; -.
DR   PharmGKB; PA30248; -.
DR   VEuPathDB; HostDB:ENSG00000161850; -.
DR   eggNOG; ENOG502QWIE; Eukaryota.
DR   GeneTree; ENSGT00940000161849; -.
DR   HOGENOM; CLU_012560_6_1_1; -.
DR   InParanoid; Q9NSB4; -.
DR   OMA; CQSNIEP; -.
DR   OrthoDB; 904619at2759; -.
DR   PhylomeDB; Q9NSB4; -.
DR   TreeFam; TF317854; -.
DR   PathwayCommons; Q9NSB4; -.
DR   Reactome; R-HSA-6805567; Keratinization.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   SignaLink; Q9NSB4; -.
DR   BioGRID-ORCS; 3888; 12 hits in 1060 CRISPR screens.
DR   GenomeRNAi; 3888; -.
DR   Pharos; Q9NSB4; Tdark.
DR   PRO; PR:Q9NSB4; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9NSB4; protein.
DR   Bgee; ENSG00000161850; Expressed in zone of skin and 22 other tissues.
DR   Genevisible; Q9NSB4; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
DR   GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..513
FT                   /note="Keratin, type II cuticular Hb2"
FT                   /id="PRO_0000063697"
FT   DOMAIN          120..431
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..120
FT                   /note="Head"
FT   REGION          121..155
FT                   /note="Coil 1A"
FT   REGION          156..165
FT                   /note="Linker 1"
FT   REGION          166..266
FT                   /note="Coil 1B"
FT   REGION          267..283
FT                   /note="Linker 12"
FT   REGION          284..427
FT                   /note="Coil 2"
FT   REGION          428..513
FT                   /note="Tail"
FT   VARIANT         219
FT                   /note="E -> Q (in dbSNP:rs1791634)"
FT                   /id="VAR_032786"
FT   VARIANT         452
FT                   /note="E -> D (in dbSNP:rs1732263)"
FT                   /id="VAR_032787"
FT   VARIANT         458
FT                   /note="T -> M (in dbSNP:rs2658658)"
FT                   /id="VAR_018118"
SQ   SEQUENCE   513 AA;  56653 MW;  69BB9256BB3B6587 CRC64;
     MSYHSFQPGS RCGSQSFSSY SAVMPRMVTH YAVSKGPCRP GGGRGLRALG CLGSRSLCNV
     GFGRPRVASR CGGTLPGFGY RLGATCGPSA CITPVTINES LLVPLALEID PTVQRVKRDE
     KEQIKCLNNR FASFINKVRF LEQKNKLLET KWNFMQQQRC CQTNIEPIFE GYISALRRQL
     DCVSGDRVRL ESELCSLQAA LEGYKKKYEE ELSLRPCVEN EFVALKKDVD TAFLMKADLE
     TNAEALVQEI DFLKSLYEEE ICLLQSQISE TSVIVKMDNS RELDVDGIIA EIKAQYDDIA
     SRSKAEAEAW YQCRYEELRV TAGNHCDNLR NRKNEILEMN KLIQRLQQET ENVKAQRCKL
     EGAIAEAEQQ GEAALNDAKC KLAGLEEALQ KAKQDMACLL KEYQEVMNSK LGLDIEIATY
     RRLLEGEEHR LCEGIGPVNI SVSSSKGAFL YEPCGVSTPV LSTGVLRSNG GCSIVGTGEL
     YVPCEPQGLL SCGSGRKSSM TLGAGGSSPS HKH
 
 
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