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N4BP2_HUMAN
ID   N4BP2_HUMAN             Reviewed;        1770 AA.
AC   Q86UW6; A0AVR3; Q9NVK2; Q9P2D4;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=NEDD4-binding protein 2;
DE            Short=N4BP2;
DE            EC=3.-.-.-;
DE   AltName: Full=BCL-3-binding protein;
GN   Name=N4BP2; Synonyms=B3BP, KIAA1413;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH BCL3 AND
RP   CREBBP, AND VARIANT ASN-611.
RC   TISSUE=T-cell;
RX   PubMed=12730195; DOI=10.1074/jbc.m303518200;
RA   Watanabe N., Wachi S., Fujita T.;
RT   "Identification and characterization of BCL-3-binding protein: implications
RT   for transcription and DNA repair or recombination.";
RL   J. Biol. Chem. 278:26102-26110(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-611.
RC   TISSUE=Lung;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-659.
RC   TISSUE=Teratocarcinoma;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-1770 (ISOFORM 2), AND VARIANT
RP   ASN-611.
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 AND THR-1210, 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).
RN   [7]
RP   STRUCTURE BY NMR OF 1688-1770.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SMR domain of NEDD4-binding protein 2.";
RL   Submitted (JUN-2006) to the PDB data bank.
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] ALA-283.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Has 5'-polynucleotide kinase and nicking endonuclease
CC       activity. May play a role in DNA repair or recombination.
CC       {ECO:0000269|PubMed:12730195}.
CC   -!- SUBUNIT: Binds NEDD4 (By similarity). Binds BCL3 and CREBBP.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86UW6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86UW6-2; Sequence=VSP_009721;
CC   -!- DOMAIN: The Smr domain has nicking endonuclease activity, but no
CC       significant double strand cleavage or exonuclease activity.
CC   -!- PTM: Ubiquitinated; this targets the protein for degradation by the
CC       proteasome. {ECO:0000250}.
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DR   EMBL; AY267013; AAP22172.1; -; mRNA.
DR   EMBL; BC126466; AAI26467.1; -; mRNA.
DR   EMBL; AK001542; BAA91748.1; -; mRNA.
DR   EMBL; AB037834; BAA92651.1; -; mRNA.
DR   CCDS; CCDS3457.1; -. [Q86UW6-1]
DR   RefSeq; NP_001305288.1; NM_001318359.1.
DR   RefSeq; NP_060647.2; NM_018177.5. [Q86UW6-1]
DR   RefSeq; XP_011512020.1; XM_011513718.2. [Q86UW6-1]
DR   RefSeq; XP_016863887.1; XM_017008398.1. [Q86UW6-1]
DR   PDB; 2D9I; NMR; -; A=1688-1770.
DR   PDB; 2VKC; NMR; -; A=1657-1770.
DR   PDB; 3BHB; X-ray; 2.20 A; C=129-138.
DR   PDB; 3FAU; X-ray; 1.90 A; A/B/C/D=1691-1770.
DR   PDBsum; 2D9I; -.
DR   PDBsum; 2VKC; -.
DR   PDBsum; 3BHB; -.
DR   PDBsum; 3FAU; -.
DR   AlphaFoldDB; Q86UW6; -.
DR   SMR; Q86UW6; -.
DR   BioGRID; 120848; 75.
DR   CORUM; Q86UW6; -.
DR   IntAct; Q86UW6; 12.
DR   STRING; 9606.ENSP00000261435; -.
DR   iPTMnet; Q86UW6; -.
DR   PhosphoSitePlus; Q86UW6; -.
DR   BioMuta; N4BP2; -.
DR   DMDM; 145559498; -.
DR   EPD; Q86UW6; -.
DR   jPOST; Q86UW6; -.
DR   MassIVE; Q86UW6; -.
DR   MaxQB; Q86UW6; -.
DR   PaxDb; Q86UW6; -.
DR   PeptideAtlas; Q86UW6; -.
DR   PRIDE; Q86UW6; -.
DR   ProteomicsDB; 69917; -. [Q86UW6-1]
DR   ProteomicsDB; 69918; -. [Q86UW6-2]
DR   Antibodypedia; 23545; 27 antibodies from 12 providers.
DR   DNASU; 55728; -.
DR   Ensembl; ENST00000261435.11; ENSP00000261435.6; ENSG00000078177.14. [Q86UW6-1]
DR   GeneID; 55728; -.
DR   KEGG; hsa:55728; -.
DR   MANE-Select; ENST00000261435.11; ENSP00000261435.6; NM_018177.6; NP_060647.2.
DR   UCSC; uc003guy.5; human. [Q86UW6-1]
DR   CTD; 55728; -.
DR   DisGeNET; 55728; -.
DR   GeneCards; N4BP2; -.
DR   HGNC; HGNC:29851; N4BP2.
DR   HPA; ENSG00000078177; Tissue enhanced (lymphoid).
DR   MIM; 619139; gene.
DR   neXtProt; NX_Q86UW6; -.
DR   OpenTargets; ENSG00000078177; -.
DR   PharmGKB; PA162396580; -.
DR   VEuPathDB; HostDB:ENSG00000078177; -.
DR   eggNOG; KOG2401; Eukaryota.
DR   GeneTree; ENSGT00940000160604; -.
DR   InParanoid; Q86UW6; -.
DR   OMA; SICYGEN; -.
DR   OrthoDB; 76267at2759; -.
DR   PhylomeDB; Q86UW6; -.
DR   TreeFam; TF327016; -.
DR   PathwayCommons; Q86UW6; -.
DR   SignaLink; Q86UW6; -.
DR   BioGRID-ORCS; 55728; 31 hits in 1075 CRISPR screens.
DR   ChiTaRS; N4BP2; human.
DR   EvolutionaryTrace; Q86UW6; -.
DR   GenomeRNAi; 55728; -.
DR   Pharos; Q86UW6; Tbio.
DR   PRO; PR:Q86UW6; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q86UW6; protein.
DR   Bgee; ENSG00000078177; Expressed in tibia and 164 other tissues.
DR   ExpressionAtlas; Q86UW6; baseline and differential.
DR   Genevisible; Q86UW6; HS.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IDA:MGI.
DR   GO; GO:0004519; F:endonuclease activity; IDA:MGI.
DR   GO; GO:0046404; F:polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IDA:MGI.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   CDD; cd14365; CUE_N4BP2; 1.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR013899; DUF1771.
DR   InterPro; IPR041801; N4BP2_CUE.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   InterPro; IPR009060; UBA-like_sf.
DR   Pfam; PF08590; DUF1771; 1.
DR   Pfam; PF01713; Smr; 1.
DR   SMART; SM01162; DUF1771; 1.
DR   SMART; SM00463; SMR; 1.
DR   SUPFAM; SSF160443; SSF160443; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51140; CUE; 1.
DR   PROSITE; PS50828; SMR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW   Hydrolase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..1770
FT                   /note="NEDD4-binding protein 2"
FT                   /id="PRO_0000096681"
FT   DOMAIN          46..89
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   DOMAIN          1691..1770
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00321"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1580..1606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          90..177
FT                   /evidence="ECO:0000255"
FT   COILED          218..259
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        113..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..749
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1587..1606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         447..454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         906
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1210
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1596..1612
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10718198"
FT                   /id="VSP_009721"
FT   VARIANT         101
FT                   /note="S -> I (in dbSNP:rs17511668)"
FT                   /id="VAR_051215"
FT   VARIANT         196
FT                   /note="M -> V (in dbSNP:rs10014170)"
FT                   /id="VAR_051216"
FT   VARIANT         283
FT                   /note="P -> A (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035474"
FT   VARIANT         611
FT                   /note="D -> N (in dbSNP:rs794001)"
FT                   /evidence="ECO:0000269|PubMed:10718198,
FT                   ECO:0000269|PubMed:12730195, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_051217"
FT   VARIANT         1587
FT                   /note="T -> A (in dbSNP:rs2271395)"
FT                   /id="VAR_051218"
FT   CONFLICT        118
FT                   /note="E -> K (in Ref. 2; AAI26467)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        428
FT                   /note="S -> F (in Ref. 3; BAA91748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        660
FT                   /note="K -> Q (in Ref. 1; AAP22172)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        778
FT                   /note="K -> E (in Ref. 4; BAA92651)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1353
FT                   /note="S -> R (in Ref. 2; AAI26467 and 4; BAA92651)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1524
FT                   /note="L -> V (in Ref. 1; AAP22172)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1591
FT                   /note="S -> F (in Ref. 1; AAP22172)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1669..1685
FT                   /evidence="ECO:0007829|PDB:2VKC"
FT   HELIX           1686..1688
FT                   /evidence="ECO:0007829|PDB:2VKC"
FT   STRAND          1690..1692
FT                   /evidence="ECO:0007829|PDB:2D9I"
FT   HELIX           1698..1719
FT                   /evidence="ECO:0007829|PDB:3FAU"
FT   STRAND          1724..1728
FT                   /evidence="ECO:0007829|PDB:3FAU"
FT   STRAND          1734..1736
FT                   /evidence="ECO:0007829|PDB:3FAU"
FT   HELIX           1742..1752
FT                   /evidence="ECO:0007829|PDB:3FAU"
FT   STRAND          1757..1761
FT                   /evidence="ECO:0007829|PDB:3FAU"
FT   STRAND          1764..1768
FT                   /evidence="ECO:0007829|PDB:3FAU"
SQ   SEQUENCE   1770 AA;  198801 MW;  9A49FAB19C1BD56D CRC64;
     MPRRRKNLGG NPFRKTANPK EVVVSSVASR EEPTTTLPSM GETKVDQEEL FTSISEIFSD
     LDPDVVYLML SECDFKVENA MDCLLELSAT DTKIEESSSQ SFVASENQVG AAESKIMEKR
     PEEESEDSKM DSFLDMQLTE DLDSLIQNAF EKLNSSPDDQ VYSFLPSQDV NSFNDSSEFI
     NPDSSNMTPI FSTQNMNLNG ENLENSGSTL SLNPLPSHSV LNESKCFIKD NTLALESNYP
     EDSLLSSSLN VASDSIAGCS SLNQKQKELL ESECVEAQFS EAPVDLDASE PQACLNLPGL
     DLPGTGGDQK STRVSDVFLP SEGFNFKPHK HPELPTKGKD VSYCPVLAPL PLLLPPPPPP
     PMWNPMIPAF DLFQGNHGFV APVVTTAAHW RSVNYTFPPS VISHTSPTKV WRNKDGTSAY
     QVQETPVSQV VRKKTSYVGL VLVLLRGLPG SGKSFLARTL QEDNPSGVIL STDDYFYING
     QYQFDVKYLG EAHEWNQNRA KEAFEKKISP IIIDNTNLQA WEMKPYVALS QKHKYKVLFR
     EPDTWWKFKP KELARRNIHG VSKEKITRML EHYQRFVSVP IIMSSSVPEK IERIELCAYS
     CEDRSTSPRD DEDIISEKEE NILSLSLKHL EFTEEKNLDV TKETMLPENV AYLSNADLNK
     RRKEISDMNP SIQSALILET PHMYFSDSES KLQATDKSEN EQIEMVAVKG YSKTDTDSSM
     ERVSPSTCCS ENNQEDCDLA NSGPLQNEKS SPGEIVEERA TVTKKAFGKQ KSKSTLEKFP
     RHELSNFVGD WPVDKTIGQR TKRNRKTEKT SSVQSDKKYN YPQSHKLVNS VSVNTDCVQQ
     RGSPHESVED GRKSQCDDAS EPLNSYKYDA YKNIDKNSFN IMGDWPSSDS LAQREHRSRM
     PKTGLSEPNL EIGTNDKMNE ISLSTAHEAC WGTSSQKLKT LGSSNLGSSE MLLSEMTCES
     QTCLSKKSHG QHTSLPLTFT NSAPTVSGVV EPQTLAECQE QMPKRDPGKE VGMCTQTEPQ
     DFALLWKIEK NKISISDSIK VLTGRLDGFK PKVFNINTKS DVQEAIPYRV MYDKSTFVEE
     SELTSADESE NLNILCKLFG SFSLEALKDL YERCNKDIIW ATSLLLDSET KLCEDTEFEN
     FQKSCDGSQI GPFSLGLNLK EIISQRGTLE NSNSPVPEFS HGIGISNADS QSTCDAERGN
     SEQAEMRAVT PENHESMTSI FPSAAVGLKN NNDILPNSQE ELLYSSKQSF PGILKATTPK
     DMSETEKNLV VTETGDNIHS PSHFSDIFNF VSSTSNLELN EEIYFTDSLE IKRNENFPKD
     YVKFSDEEEF MNEDEKEMKE ILMAGSSLSA GVSGEDKTEI LNPTPAMAKS LTIDCLELAL
     PPELAFQLNE LFGPVGIDSG SLTVEDCVVH IDLNLAKVIH EKWKESVMER QRQEEVSCGK
     FMQDPSLVGH TGLDNPEQKS SQRTGKKLLK TLTASEMLPL LDHWNTQTKK VSLREIMSEE
     IALQEKHNLK RETLMFEKDC ATKLKEKQLF KIFPAINQNF LVDIFKDHNY SLEHTVQFLN
     CVLEGDPVKT VVAQEFVHQN ENVTSHTGQK SKEKKPKKLK ETEETPSELS FQDFEYPDYD
     DYRAEAFLHQ QKRMECYSKA KEAYRIGKKN VATFYAQQGT LHEQKMKEAN HLAAIEIFEK
     VNASLLPQNV LDLHGLHVDE ALEHLMRVLE KKTEEFKQNG GKPYLSVITG RGNHSQGGVA
     RIKPAVIKYL ISHSFRFSEI KPGCLKVMLK
 
 
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