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K2C6C_HUMAN
ID   K2C6C_HUMAN             Reviewed;         564 AA.
AC   P48668; A1L4L5; P48666; Q2TAZ9; Q7RTN9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 189.
DE   RecName: Full=Keratin, type II cytoskeletal 6C;
DE   AltName: Full=Cytokeratin-6C;
DE            Short=CK-6C;
DE   AltName: Full=Cytokeratin-6E;
DE            Short=CK-6E;
DE   AltName: Full=Keratin K6h;
DE   AltName: Full=Keratin-6C;
DE            Short=K6C;
DE   AltName: Full=Type-II keratin Kb12;
GN   Name=KRT6C; Synonyms=KRT6E;
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 / MRNA], AND VARIANTS ASN-227 AND ILE-481.
RC   TISSUE=Skin;
RX   PubMed=7543104; DOI=10.1074/jbc.270.31.18581;
RA   Takahashi K., Paladini R.D., Coulombe P.A.;
RT   "Cloning and characterization of multiple human genes and cDNAs encoding
RT   highly related type II keratin 6 isoforms.";
RL   J. Biol. Chem. 270:18581-18592(1995).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-182.
RC   TISSUE=Skin;
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   [4]
RP   PROTEIN SEQUENCE OF 2-9; 16-24; 31-40; 43-86; 169-189; 195-204; 208-222;
RP   224-369; 376-386; 425-436; 456-475 AND 534-550, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lung carcinoma;
RA   Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=11683385; DOI=10.1242/jcs.114.14.2569;
RA   Hesse M., Magin T.M., Weber K.;
RT   "Genes for intermediate filament proteins and the draft sequence of the
RT   human genome: novel keratin genes and a surprisingly high number of
RT   pseudogenes related to keratin genes 8 and 18.";
RL   J. Cell Sci. 114:2569-2575(2001).
RN   [6]
RP   PHOSPHORYLATION AT SER-60.
RX   PubMed=9054461; DOI=10.1074/jbc.272.11.7556;
RA   Ku N.-O., Omary M.B.;
RT   "Phosphorylation of human keratin 8 in vivo at conserved head domain serine
RT   23 and at epidermal growth factor-stimulated tail domain serine 431.";
RL   J. Biol. Chem. 272:7556-7564(1997).
RN   [7]
RP   INVOLVEMENT IN PPKNEFD, AND VARIANT PPKNEFD ASN-172 DEL.
RX   PubMed=19609311; DOI=10.1038/jid.2009.215;
RA   Wilson N.J., Messenger A.G., Leachman S.A., O'Toole E.A., Lane E.B.,
RA   McLean W.H., Smith F.J.;
RT   "Keratin K6c mutations cause focal palmoplantar keratoderma.";
RL   J. Invest. Dermatol. 130:425-429(2010).
RN   [8]
RP   INVOLVEMENT IN PPKNEFD, AND VARIANT PPKNEFD LYS-472.
RX   PubMed=21801157; DOI=10.1111/j.1365-2133.2011.10552.x;
RA   Akasaka E., Nakano H., Nakano A., Toyomaki Y., Takiyoshi N., Rokunohe D.,
RA   Nishikawa Y., Korekawa A., Matsuzaki Y., Mitsuhashi Y., Sawamura D.;
RT   "Diffuse and focal palmoplantar keratoderma can be caused by a keratin 6c
RT   mutation.";
RL   Br. J. Dermatol. 165:1290-1292(2011).
RN   [9]
RP   VARIANT PPKNEFD LYS-472, AND CHARACTERIZATION OF VARIANT PPKNEFD LYS-472.
RX   PubMed=23662636; DOI=10.1111/1346-8138.12185;
RA   Kubo A., Oura Y., Hirano T., Aoyama Y., Sato S., Nakamura K., Takae Y.,
RA   Amagai M.;
RT   "Collapse of the keratin filament network through the expression of mutant
RT   keratin 6c observed in a case of focal plantar keratoderma.";
RL   J. Dermatol. 40:553-557(2013).
CC   -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT6 isomers
CC       associate with KRT16 and/or KRT17.
CC   -!- INTERACTION:
CC       P48668; Q08043: ACTN3; NbExp=3; IntAct=EBI-2564105, EBI-2880652;
CC       P48668; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2564105, EBI-618309;
CC       P48668; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-2564105, EBI-2125614;
CC       P48668; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2564105, EBI-14069005;
CC       P48668; A1A4E9: KRT13; NbExp=3; IntAct=EBI-2564105, EBI-10171552;
CC       P48668; P02533: KRT14; NbExp=3; IntAct=EBI-2564105, EBI-702178;
CC       P48668; P19012: KRT15; NbExp=3; IntAct=EBI-2564105, EBI-739566;
CC       P48668; P08779: KRT16; NbExp=3; IntAct=EBI-2564105, EBI-356410;
CC       P48668; P05783: KRT18; NbExp=4; IntAct=EBI-2564105, EBI-297888;
CC       P48668; P08727: KRT19; NbExp=3; IntAct=EBI-2564105, EBI-742756;
CC       P48668; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-2564105, EBI-2952736;
CC       P48668; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-2564105, EBI-11980019;
CC       P48668; Q7Z3Y9: KRT26; NbExp=5; IntAct=EBI-2564105, EBI-12084444;
CC       P48668; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2564105, EBI-3044087;
CC       P48668; Q15323: KRT31; NbExp=6; IntAct=EBI-2564105, EBI-948001;
CC       P48668; Q14525: KRT33B; NbExp=3; IntAct=EBI-2564105, EBI-1049638;
CC       P48668; O76011: KRT34; NbExp=3; IntAct=EBI-2564105, EBI-1047093;
CC       P48668; Q92764: KRT35; NbExp=3; IntAct=EBI-2564105, EBI-1058674;
CC       P48668; O76013-2: KRT36; NbExp=3; IntAct=EBI-2564105, EBI-11958506;
CC       P48668; O76014: KRT37; NbExp=3; IntAct=EBI-2564105, EBI-1045716;
CC       P48668; O76015: KRT38; NbExp=6; IntAct=EBI-2564105, EBI-1047263;
CC       P48668; Q6A162: KRT40; NbExp=6; IntAct=EBI-2564105, EBI-10171697;
CC       P48668; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2564105, EBI-1105213;
CC       P48668; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-2564105, EBI-2130429;
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in distinct types of
CC       epithelia such as those in oral mucosa, esophagus, papillae of tongue
CC       and hair follicle outer root sheath.
CC   -!- DISEASE: Palmoplantar keratoderma, non-epidermolytic, focal or diffuse
CC       (PPKNEFD) [MIM:615735]: A dermatological disorder characterized by non-
CC       epidermolytic abnormal thickening of the skin on the palms and soles.
CC       Diffuse palmoplantar keratoderma is characterized by uniform
CC       involvement of the palmoplantar surface, while the focal form consists
CC       of localized areas of hyperkeratosis located mainly on pressure points
CC       and sites of recurrent friction. {ECO:0000269|PubMed:19609311,
CC       ECO:0000269|PubMed:21801157, ECO:0000269|PubMed:23662636}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: There are at least six isoforms of human type II
CC       keratin-6 (K6).
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC       respectively).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; L42611; AAC41770.1; -; mRNA.
DR   EMBL; L42601; AAC41769.1; -; Genomic_DNA.
DR   EMBL; L42593; AAC41769.1; JOINED; Genomic_DNA.
DR   EMBL; L42594; AAC41769.1; JOINED; Genomic_DNA.
DR   EMBL; L42595; AAC41769.1; JOINED; Genomic_DNA.
DR   EMBL; L42596; AAC41769.1; JOINED; Genomic_DNA.
DR   EMBL; L42597; AAC41769.1; JOINED; Genomic_DNA.
DR   EMBL; L42598; AAC41769.1; JOINED; Genomic_DNA.
DR   EMBL; L42599; AAC41769.1; JOINED; Genomic_DNA.
DR   EMBL; AC055736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC110639; AAI10640.1; -; mRNA.
DR   EMBL; BC130583; AAI30584.1; -; mRNA.
DR   EMBL; BC130585; AAI30586.1; -; mRNA.
DR   EMBL; BK000962; DAA01484.1; -; Genomic_DNA.
DR   CCDS; CCDS8829.1; -.
DR   PIR; I61768; I61768.
DR   PIR; I61770; I61770.
DR   RefSeq; NP_775109.2; NM_173086.4.
DR   AlphaFoldDB; P48668; -.
DR   SMR; P48668; -.
DR   BioGRID; 130423; 54.
DR   IntAct; P48668; 47.
DR   STRING; 9606.ENSP00000252250; -.
DR   Allergome; 415; Hom s 5.
DR   GlyGen; P48668; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P48668; -.
DR   PhosphoSitePlus; P48668; -.
DR   SwissPalm; P48668; -.
DR   BioMuta; KRT6C; -.
DR   DMDM; 59803089; -.
DR   jPOST; P48668; -.
DR   MassIVE; P48668; -.
DR   PaxDb; P48668; -.
DR   PeptideAtlas; P48668; -.
DR   PRIDE; P48668; -.
DR   ProteomicsDB; 55922; -.
DR   TopDownProteomics; P48668; -.
DR   Antibodypedia; 14621; 118 antibodies from 23 providers.
DR   DNASU; 286887; -.
DR   Ensembl; ENST00000252250.7; ENSP00000252250.6; ENSG00000170465.10.
DR   GeneID; 286887; -.
DR   KEGG; hsa:286887; -.
DR   MANE-Select; ENST00000252250.7; ENSP00000252250.6; NM_173086.5; NP_775109.2.
DR   UCSC; uc001sal.4; human.
DR   CTD; 286887; -.
DR   DisGeNET; 286887; -.
DR   GeneCards; KRT6C; -.
DR   GeneReviews; KRT6C; -.
DR   HGNC; HGNC:20406; KRT6C.
DR   HPA; ENSG00000170465; Tissue enhanced (esophagus, vagina).
DR   MalaCards; KRT6C; -.
DR   MIM; 612315; gene.
DR   MIM; 615735; phenotype.
DR   neXtProt; NX_P48668; -.
DR   OpenTargets; ENSG00000170465; -.
DR   Orphanet; 402003; Autosomal dominant focal non-epidermolytic palmoplantar keratoderma with plantar blistering.
DR   PharmGKB; PA134891227; -.
DR   VEuPathDB; HostDB:ENSG00000170465; -.
DR   eggNOG; ENOG502QURK; Eukaryota.
DR   GeneTree; ENSGT00940000154600; -.
DR   HOGENOM; CLU_012560_6_1_1; -.
DR   InParanoid; P48668; -.
DR   OMA; DNIFEER; -.
DR   OrthoDB; 824246at2759; -.
DR   PhylomeDB; P48668; -.
DR   TreeFam; TF317854; -.
DR   PathwayCommons; P48668; -.
DR   Reactome; R-HSA-6805567; Keratinization.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   SignaLink; P48668; -.
DR   BioGRID-ORCS; 286887; 10 hits in 1000 CRISPR screens.
DR   ChiTaRS; KRT6C; human.
DR   GenomeRNAi; 286887; -.
DR   Pharos; P48668; Tbio.
DR   PRO; PR:P48668; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P48668; protein.
DR   Bgee; ENSG00000170465; Expressed in esophagus mucosa and 71 other tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
DR   GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR   GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:UniProtKB.
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   Acetylation; Coiled coil; Direct protein sequencing; Disease variant;
KW   Intermediate filament; Keratin; Palmoplantar keratoderma; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CHAIN           2..564
FT                   /note="Keratin, type II cytoskeletal 6C"
FT                   /id="PRO_0000063735"
FT   DOMAIN          163..476
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..162
FT                   /note="Head"
FT   REGION          163..198
FT                   /note="Coil 1A"
FT   REGION          199..217
FT                   /note="Linker 1"
FT   REGION          218..309
FT                   /note="Coil 1B"
FT   REGION          310..333
FT                   /note="Linker 12"
FT   REGION          334..472
FT                   /note="Coil 2"
FT   REGION          473..564
FT                   /note="Tail"
FT   SITE            414
FT                   /note="Stutter"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9054461"
FT   VARIANT         172
FT                   /note="Missing (in PPKNEFD; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:19609311"
FT                   /id="VAR_071308"
FT   VARIANT         182
FT                   /note="R -> Q (in dbSNP:rs11608915)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_035031"
FT   VARIANT         227
FT                   /note="S -> N (in dbSNP:rs17099602)"
FT                   /evidence="ECO:0000269|PubMed:7543104"
FT                   /id="VAR_035032"
FT   VARIANT         472
FT                   /note="E -> K (in PPKNEFD; collapsed of the keratin
FT                   filament network in a dose-dependent manner;
FT                   dbSNP:rs587777292)"
FT                   /evidence="ECO:0000269|PubMed:21801157,
FT                   ECO:0000269|PubMed:23662636"
FT                   /id="VAR_071309"
FT   VARIANT         481
FT                   /note="V -> I (in dbSNP:rs412533)"
FT                   /evidence="ECO:0000269|PubMed:7543104"
FT                   /id="VAR_035033"
FT   CONFLICT        88
FT                   /note="G -> R (in Ref. 1; AAC41770/AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        89
FT                   /note="G -> A (in Ref. 1; AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="G -> D (in Ref. 1; AAC41770/AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="D -> E (in Ref. 1; AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="N -> G (in Ref. 1; AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="L -> F (in Ref. 1; AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404
FT                   /note="S -> N (in Ref. 1; AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        486
FT                   /note="V -> I (in Ref. 1; AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        493
FT                   /note="I -> V (in Ref. 1; AAC41769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        523
FT                   /note="I -> V (in Ref. 1; AAC41769)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   564 AA;  60025 MW;  FABEABD829A75612 CRC64;
     MASTSTTIRS HSSSRRGFSA NSARLPGVSR SGFSSISVSR SRGSGGLGGA CGGAGFGSRS
     LYGLGGSKRI SIGGGSCAIS GGYGSRAGGS YGFGGAGSGF GFGGGAGIGF GLGGGAGLAG
     GFGGPGFPVC PPGGIQEVTV NQSLLTPLNL QIDPAIQRVR AEEREQIKTL NNKFASFIDK
     VRFLEQQNKV LDTKWTLLQE QGTKTVRQNL EPLFEQYINN LRRQLDSIVG ERGRLDSELR
     NMQDLVEDLK NKYEDEINKR TAAENEFVTL KKDVDAAYMN KVELQAKADT LTDEINFLRA
     LYDAELSQMQ THISDTSVVL SMDNNRNLDL DSIIAEVKAQ YEEIAQRSRA EAESWYQTKY
     EELQVTAGRH GDDLRNTKQE IAEINRMIQR LRSEIDHVKK QCASLQAAIA DAEQRGEMAL
     KDAKNKLEGL EDALQKAKQD LARLLKEYQE LMNVKLALDV EIATYRKLLE GEECRLNGEG
     VGQVNVSVVQ STISSGYGGA SGVGSGLGLG GGSSYSYGSG LGIGGGFSSS SGRAIGGGLS
     SVGGGSSTIK YTTTSSSSRK SYKH
 
 
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