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PARI_HUMAN
ID   PARI_HUMAN              Reviewed;         579 AA.
AC   Q9NWS1; B4E0Y0; Q05C00; Q499L8; Q4FZA0; Q4KMW7; Q6NSC6; Q6PJA1; Q86W36;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=PCNA-interacting partner;
DE            Short=PARI;
DE   AltName: Full=PARP-1 binding protein;
DE   AltName: Full=PARP1-binding protein;
DE            Short=PARPBP;
GN   Name=PARPBP; Synonyms=C12orf48, PARI;
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 1 AND 2).
RC   TISSUE=Thymus;
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 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] (ISOFORMS 4 AND 5), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-416 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-501 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE
RP   MRNA] OF 30-579 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF
RP   34-579 (ISOFORMS 6 AND 7).
RC   TISSUE=Ovary, and Testis;
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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP   PARP1.
RX   PubMed=20931645; DOI=10.1002/gcc.20828;
RA   Piao L., Nakagawa H., Ueda K., Chung S., Kashiwaya K., Eguchi H.,
RA   Ohigashi H., Ishikawa O., Daigo Y., Matsuda K., Nakamura Y.;
RT   "C12orf48, termed PARP-1 binding protein, enhances poly(ADP-ribose)
RT   polymerase-1 (PARP-1) activity and protects pancreatic cancer cells from
RT   DNA damage.";
RL   Genes Chromosomes Cancer 50:13-24(2011).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAD51 AND PCNA.
RX   PubMed=22153967; DOI=10.1016/j.molcel.2011.11.010;
RA   Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S.,
RA   Boulton S.J., D'Andrea A.D.;
RT   "Inhibition of homologous recombination by the PCNA-interacting protein
RT   PARI.";
RL   Mol. Cell 45:75-86(2012).
CC   -!- FUNCTION: Required to suppress inappropriate homologous recombination,
CC       thereby playing a central role DNA repair and in the maintenance of
CC       genomic stability. Antagonizes homologous recombination by interfering
CC       with the formation of the RAD51-DNA homologous recombination structure.
CC       Binds single-strand DNA and poly(A) homopolymers. Positively regulate
CC       the poly(ADP-ribosyl)ation activity of PARP1; however such function may
CC       be indirect. {ECO:0000269|PubMed:20931645,
CC       ECO:0000269|PubMed:22153967}.
CC   -!- SUBUNIT: Interacts with RAD51 and PCNA (PubMed:22153967). Interacts
CC       with PARP1 (PubMed:20931645). Interacts with TASOR (By similarity).
CC       {ECO:0000250|UniProtKB:Q6IRT3, ECO:0000269|PubMed:20931645,
CC       ECO:0000269|PubMed:22153967}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000269|PubMed:20931645, ECO:0000269|PubMed:22153967}.
CC       Note=Localizes to chromatin in response to S phase arrest but not in
CC       mitosis. Targeted to chromatin via its interaction with PCNA.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q9NWS1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NWS1-2; Sequence=VSP_023588;
CC       Name=3;
CC         IsoId=Q9NWS1-3; Sequence=VSP_023591, VSP_023592;
CC       Name=4;
CC         IsoId=Q9NWS1-4; Sequence=VSP_023589, VSP_023590;
CC       Name=5;
CC         IsoId=Q9NWS1-5; Sequence=VSP_023587;
CC       Name=6;
CC         IsoId=Q9NWS1-6; Sequence=VSP_023594, VSP_023595;
CC       Name=7;
CC         IsoId=Q9NWS1-7; Sequence=VSP_023593, VSP_023596, VSP_023597;
CC   -!- TISSUE SPECIFICITY: Restricted to testis. Overexpressed in multiple
CC       cancer cells. {ECO:0000269|PubMed:20931645}.
CC   -!- DOMAIN: Although it shares some sequence similarity with SRS2 yeast
CC       helicase, does not contain a functional ATPase domain suggesting it has
CC       no helicase activity. {ECO:0000269|PubMed:20931645}.
CC   -!- SIMILARITY: Belongs to the PARI family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18903.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH30962.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAH50696.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH70270.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH70270.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AK000648; BAA91306.1; -; mRNA.
DR   EMBL; AK303571; BAG64592.1; -; mRNA.
DR   EMBL; AC087882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC018903; AAH18903.1; ALT_INIT; mRNA.
DR   EMBL; BC030962; AAH30962.1; ALT_SEQ; mRNA.
DR   EMBL; BC050696; AAH50696.1; ALT_INIT; mRNA.
DR   EMBL; BC070270; AAH70270.1; ALT_SEQ; mRNA.
DR   EMBL; BC098313; AAH98313.1; -; mRNA.
DR   EMBL; BC099734; AAH99734.2; -; mRNA.
DR   EMBL; BC099844; AAH99844.2; -; mRNA.
DR   CCDS; CCDS81729.1; -. [Q9NWS1-4]
DR   CCDS; CCDS81730.1; -. [Q9NWS1-2]
DR   CCDS; CCDS9090.2; -. [Q9NWS1-1]
DR   RefSeq; NP_001306917.1; NM_001319988.1.
DR   RefSeq; NP_001306922.1; NM_001319993.1. [Q9NWS1-2]
DR   RefSeq; NP_001306923.1; NM_001319994.1. [Q9NWS1-2]
DR   RefSeq; NP_001306924.1; NM_001319995.1.
DR   RefSeq; NP_001306925.1; NM_001319996.1. [Q9NWS1-4]
DR   RefSeq; NP_060385.3; NM_017915.4. [Q9NWS1-1]
DR   RefSeq; XP_016875032.1; XM_017019543.1.
DR   RefSeq; XP_016875033.1; XM_017019544.1.
DR   AlphaFoldDB; Q9NWS1; -.
DR   BioGRID; 120342; 15.
DR   IntAct; Q9NWS1; 3.
DR   MINT; Q9NWS1; -.
DR   STRING; 9606.ENSP00000332915; -.
DR   iPTMnet; Q9NWS1; -.
DR   PhosphoSitePlus; Q9NWS1; -.
DR   BioMuta; PARPBP; -.
DR   DMDM; 308153618; -.
DR   EPD; Q9NWS1; -.
DR   MassIVE; Q9NWS1; -.
DR   MaxQB; Q9NWS1; -.
DR   PaxDb; Q9NWS1; -.
DR   PeptideAtlas; Q9NWS1; -.
DR   PRIDE; Q9NWS1; -.
DR   ProteomicsDB; 82965; -. [Q9NWS1-1]
DR   ProteomicsDB; 82966; -. [Q9NWS1-2]
DR   ProteomicsDB; 82967; -. [Q9NWS1-3]
DR   ProteomicsDB; 82968; -. [Q9NWS1-4]
DR   ProteomicsDB; 82969; -. [Q9NWS1-5]
DR   ProteomicsDB; 82970; -. [Q9NWS1-6]
DR   ProteomicsDB; 82971; -. [Q9NWS1-7]
DR   Antibodypedia; 49085; 85 antibodies from 15 providers.
DR   DNASU; 55010; -.
DR   Ensembl; ENST00000327680.7; ENSP00000332915.3; ENSG00000185480.12. [Q9NWS1-1]
DR   Ensembl; ENST00000392911.6; ENSP00000376643.2; ENSG00000185480.12. [Q9NWS1-2]
DR   Ensembl; ENST00000537257.5; ENSP00000442549.1; ENSG00000185480.12. [Q9NWS1-4]
DR   GeneID; 55010; -.
DR   KEGG; hsa:55010; -.
DR   MANE-Select; ENST00000327680.7; ENSP00000332915.3; NM_017915.5; NP_060385.3.
DR   UCSC; uc001tjd.4; human. [Q9NWS1-1]
DR   CTD; 55010; -.
DR   DisGeNET; 55010; -.
DR   GeneCards; PARPBP; -.
DR   HGNC; HGNC:26074; PARPBP.
DR   HPA; ENSG00000185480; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 613687; gene.
DR   neXtProt; NX_Q9NWS1; -.
DR   OpenTargets; ENSG00000185480; -.
DR   PharmGKB; PA143485378; -.
DR   VEuPathDB; HostDB:ENSG00000185480; -.
DR   eggNOG; ENOG502QR2U; Eukaryota.
DR   GeneTree; ENSGT00390000006088; -.
DR   HOGENOM; CLU_120746_0_0_1; -.
DR   InParanoid; Q9NWS1; -.
DR   OrthoDB; 355941at2759; -.
DR   PhylomeDB; Q9NWS1; -.
DR   TreeFam; TF332230; -.
DR   PathwayCommons; Q9NWS1; -.
DR   SignaLink; Q9NWS1; -.
DR   BioGRID-ORCS; 55010; 12 hits in 1081 CRISPR screens.
DR   ChiTaRS; PARPBP; human.
DR   GenomeRNAi; 55010; -.
DR   Pharos; Q9NWS1; Tbio.
DR   PRO; PR:Q9NWS1; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9NWS1; protein.
DR   Bgee; ENSG00000185480; Expressed in ventricular zone and 109 other tissues.
DR   ExpressionAtlas; Q9NWS1; baseline and differential.
DR   Genevisible; Q9NWS1; HS.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038932; PARPBP.
DR   PANTHER; PTHR32121; PTHR32121; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..579
FT                   /note="PCNA-interacting partner"
FT                   /id="PRO_0000280269"
FT   REGION          480..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..285
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023587"
FT   VAR_SEQ         1..81
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023588"
FT   VAR_SEQ         130..133
FT                   /note="SQLL -> VSIF (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023589"
FT   VAR_SEQ         134..579
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023590"
FT   VAR_SEQ         166..172
FT                   /note="VQLLARK -> ALPVLKR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023591"
FT   VAR_SEQ         173..579
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023592"
FT   VAR_SEQ         274..394
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023593"
FT   VAR_SEQ         274..297
FT                   /note="SIAGGQILSVIKMQLIKGQNSRDP -> RGCKSICWKINNWNEFWKCSSGQK
FT                   (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023594"
FT   VAR_SEQ         298..579
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023595"
FT   VAR_SEQ         422..423
FT                   /note="MK -> RV (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023596"
FT   VAR_SEQ         424..579
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023597"
FT   VARIANT         400
FT                   /note="V -> M (in dbSNP:rs12227879)"
FT                   /id="VAR_031105"
FT   CONFLICT        76
FT                   /note="N -> K (in Ref. 3; AAH99844)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="P -> L (in Ref. 3; AAH30962)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="G -> A (in Ref. 3; AAH98313)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="H -> R (in Ref. 3; AAH70270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        381
FT                   /note="N -> D (in Ref. 1; BAA91306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403
FT                   /note="S -> L (in Ref. 1; BAA91306)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   579 AA;  65054 MW;  DC576A868DD1F331 CRC64;
     MAVFNQKSVS DMIKEFRKNW RALCNSERTT LCGADSMLLA LQLSMAENNK QHSGEFTVSL
     SDVLLTWKYL LHEKLNLPVE NMDVTDHYED VRKIYDDFLK NSNMLDLIDV YQKCRALTSN
     CENYNTVSPS QLLDFLSGKQ YAVGDETDLS IPTSPTSKYN RDNEKVQLLA RKIIFSYLNL
     LVNSKNDLAV AYILNIPDRG LGREAFTDLK HAAREKQMSI FLVATSFIRT IELGGKGYAP
     PPSDPLRTHV KGLSNFINFI DKLDEILGEI PNPSIAGGQI LSVIKMQLIK GQNSRDPFCK
     AIEEVAQDLD LRIKNIINSQ EGVVALSTTD ISPARPKSHA INHGTAYCGR DTVKALLVLL
     DEEAANAPTK NKAELLYDEE NTIHHHGTSI LTLFRSPTQV NNSIKPLRER ICVSMQEKKI
     KMKQTLIRSQ FACTYKDDYM ISKDNWNNVN LASKPLCVLY MENDLSEGVN PSVGRSTIGT
     SFGNVHLDRS KNEKVSRKST SQTGNKSSKR KQVDLDGENI LCDNRNEPPQ HKNAKIPKKS
     NDSQNRLYGK LAKVAKSNKC TAKDKLISGQ AKLTQFFRL
 
 
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