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RNF38_HUMAN
ID   RNF38_HUMAN             Reviewed;         515 AA.
AC   Q9H0F5; A6PVP9; B1AM81; B1AM82; B3KSG4; E7EVL3; Q7LB33; Q8N0Y0; Q9H748;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 4.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF38 {ECO:0000305};
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger protein 38;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF38 {ECO:0000305};
GN   Name=RNF38 {ECO:0000312|HGNC:HGNC:18052};
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 3), TISSUE SPECIFICITY, AND VARIANT
RP   THR-206.
RX   PubMed=12074600; DOI=10.1016/s0006-291x(02)00584-3;
RA   Eisenberg I., Hochner H., Levi T., Yelin R., Kahan T.,
RA   Mitrani-Rosenbaum S.;
RT   "Cloning and characterization of a novel human gene RNF38 encoding a
RT   conserved putative protein with a RING finger domain.";
RL   Biochem. Biophys. Res. Commun. 294:1169-1176(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   TISSUE=Colon, and 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [7]
RP   FUNCTION, NUCLEAR LOCALIZATION SIGNAL, AND SUBCELLULAR LOCATION.
RX   PubMed=23973461; DOI=10.1016/j.bbrc.2013.08.031;
RA   Sheren J.E., Kassenbrock C.K.;
RT   "RNF38 encodes a nuclear ubiquitin protein ligase that modifies p53.";
RL   Biochem. Biophys. Res. Commun. 440:473-478(2013).
RN   [8]
RP   STRUCTURE BY NMR OF 445-506.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RING finger in RING finger protein 38.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase able to ubiquitinate
CC       p53/TP53 which promotes its relocalization to discrete foci associated
CC       with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme.
CC       {ECO:0000269|PubMed:23973461}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- INTERACTION:
CC       Q9H0F5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2341200, EBI-3867333;
CC       Q9H0F5; Q5T749: KPRP; NbExp=3; IntAct=EBI-2341200, EBI-10981970;
CC       Q9H0F5; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2341200, EBI-10171774;
CC       Q9H0F5; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-2341200, EBI-1052037;
CC       Q9H0F5; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-2341200, EBI-1048945;
CC       Q9H0F5; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-2341200, EBI-18395721;
CC       Q9H0F5; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-2341200, EBI-11962084;
CC       Q9H0F5; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-2341200, EBI-18394498;
CC       Q9H0F5; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-2341200, EBI-10261141;
CC       Q9H0F5; Q14847-2: LASP1; NbExp=3; IntAct=EBI-2341200, EBI-9088686;
CC       Q9H0F5; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-2341200, EBI-12813389;
CC       Q9H0F5; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-2341200, EBI-751555;
CC       Q9H0F5-2; P54253: ATXN1; NbExp=6; IntAct=EBI-25866807, EBI-930964;
CC       Q9H0F5-2; P48643: CCT5; NbExp=3; IntAct=EBI-25866807, EBI-355710;
CC       Q9H0F5-2; P42858: HTT; NbExp=21; IntAct=EBI-25866807, EBI-466029;
CC       Q9H0F5-2; O76024: WFS1; NbExp=3; IntAct=EBI-25866807, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23973461}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9H0F5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H0F5-2; Sequence=VSP_012243;
CC       Name=3;
CC         IsoId=Q9H0F5-3; Sequence=VSP_037337;
CC       Name=4;
CC         IsoId=Q9H0F5-4; Sequence=VSP_053846, VSP_053847;
CC       Name=5;
CC         IsoId=Q9H0F5-5; Sequence=VSP_053845;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis.
CC       {ECO:0000269|PubMed:12074600}.
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DR   EMBL; AF394047; AAM73697.1; -; mRNA.
DR   EMBL; AL136817; CAB66751.3; -; mRNA.
DR   EMBL; AK024996; BAB15050.1; -; mRNA.
DR   EMBL; AK093480; BAG52726.1; -; mRNA.
DR   EMBL; AL161792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58305.1; -; Genomic_DNA.
DR   EMBL; BC033786; AAH33786.2; -; mRNA.
DR   CCDS; CCDS6603.1; -. [Q9H0F5-1]
DR   CCDS; CCDS6604.1; -. [Q9H0F5-2]
DR   RefSeq; NP_073618.3; NM_022781.4. [Q9H0F5-1]
DR   RefSeq; NP_919309.1; NM_194328.2. [Q9H0F5-3]
DR   RefSeq; NP_919310.1; NM_194329.2. [Q9H0F5-2]
DR   RefSeq; NP_919311.1; NM_194330.2. [Q9H0F5-3]
DR   RefSeq; NP_919313.1; NM_194332.2. [Q9H0F5-3]
DR   RefSeq; XP_005251423.1; XM_005251366.3. [Q9H0F5-3]
DR   RefSeq; XP_005251424.1; XM_005251367.3. [Q9H0F5-3]
DR   RefSeq; XP_005251425.1; XM_005251368.3.
DR   RefSeq; XP_006716784.1; XM_006716721.3. [Q9H0F5-3]
DR   RefSeq; XP_011516014.1; XM_011517712.2. [Q9H0F5-3]
DR   RefSeq; XP_011516015.1; XM_011517713.2. [Q9H0F5-3]
DR   RefSeq; XP_016869784.1; XM_017014295.1.
DR   PDB; 1X4J; NMR; -; A=445-506.
DR   PDB; 4V3K; X-ray; 2.04 A; C/F=439-515.
DR   PDB; 4V3L; X-ray; 1.53 A; C=439-515.
DR   PDB; 7OJX; X-ray; 2.40 A; A=439-515.
DR   PDBsum; 1X4J; -.
DR   PDBsum; 4V3K; -.
DR   PDBsum; 4V3L; -.
DR   PDBsum; 7OJX; -.
DR   AlphaFoldDB; Q9H0F5; -.
DR   SMR; Q9H0F5; -.
DR   BioGRID; 127416; 39.
DR   IntAct; Q9H0F5; 30.
DR   MINT; Q9H0F5; -.
DR   STRING; 9606.ENSP00000259605; -.
DR   iPTMnet; Q9H0F5; -.
DR   PhosphoSitePlus; Q9H0F5; -.
DR   BioMuta; RNF38; -.
DR   DMDM; 56749664; -.
DR   PaxDb; Q9H0F5; -.
DR   PeptideAtlas; Q9H0F5; -.
DR   PRIDE; Q9H0F5; -.
DR   ProteomicsDB; 3188; -.
DR   ProteomicsDB; 80269; -. [Q9H0F5-1]
DR   ProteomicsDB; 80270; -. [Q9H0F5-2]
DR   ProteomicsDB; 80271; -. [Q9H0F5-3]
DR   Antibodypedia; 2887; 89 antibodies from 21 providers.
DR   DNASU; 152006; -.
DR   Ensembl; ENST00000259605.11; ENSP00000259605.6; ENSG00000137075.18. [Q9H0F5-1]
DR   Ensembl; ENST00000350199.8; ENSP00000343947.4; ENSG00000137075.18. [Q9H0F5-3]
DR   Ensembl; ENST00000353739.8; ENSP00000335239.5; ENSG00000137075.18. [Q9H0F5-2]
DR   Ensembl; ENST00000357058.7; ENSP00000349566.3; ENSG00000137075.18. [Q9H0F5-3]
DR   Ensembl; ENST00000377877.4; ENSP00000367109.3; ENSG00000137075.18. [Q9H0F5-4]
DR   Ensembl; ENST00000377885.6; ENSP00000367117.2; ENSG00000137075.18. [Q9H0F5-3]
DR   Ensembl; ENST00000611646.4; ENSP00000483536.1; ENSG00000137075.18. [Q9H0F5-4]
DR   GeneID; 152006; -.
DR   KEGG; hsa:152006; -.
DR   MANE-Select; ENST00000259605.11; ENSP00000259605.6; NM_022781.5; NP_073618.3.
DR   UCSC; uc003zzh.5; human. [Q9H0F5-1]
DR   CTD; 152006; -.
DR   DisGeNET; 152006; -.
DR   GeneCards; RNF38; -.
DR   HGNC; HGNC:18052; RNF38.
DR   HPA; ENSG00000137075; Low tissue specificity.
DR   MIM; 612488; gene.
DR   neXtProt; NX_Q9H0F5; -.
DR   OpenTargets; ENSG00000137075; -.
DR   PharmGKB; PA34438; -.
DR   VEuPathDB; HostDB:ENSG00000137075; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   GeneTree; ENSGT00940000156228; -.
DR   HOGENOM; CLU_024578_0_0_1; -.
DR   InParanoid; Q9H0F5; -.
DR   OMA; PPMIQAC; -.
DR   OrthoDB; 1570520at2759; -.
DR   PhylomeDB; Q9H0F5; -.
DR   TreeFam; TF325756; -.
DR   PathwayCommons; Q9H0F5; -.
DR   SignaLink; Q9H0F5; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 152006; 9 hits in 1114 CRISPR screens.
DR   ChiTaRS; RNF38; human.
DR   EvolutionaryTrace; Q9H0F5; -.
DR   GeneWiki; RNF38; -.
DR   GenomeRNAi; 152006; -.
DR   Pharos; Q9H0F5; Tbio.
DR   PRO; PR:Q9H0F5; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9H0F5; protein.
DR   Bgee; ENSG00000137075; Expressed in sperm and 207 other tissues.
DR   Genevisible; Q9H0F5; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Metal-binding; Nucleus;
KW   Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..515
FT                   /note="E3 ubiquitin-protein ligase RNF38"
FT                   /id="PRO_0000056078"
FT   ZN_FING         463..504
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          73..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           57..71
FT                   /note="Bipartite nuclear localization signal 1"
FT   MOTIF           115..131
FT                   /note="Bipartite nuclear localization signal 2"
FT   COMPBIAS        87..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..183
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_053845"
FT   VAR_SEQ         1..83
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12074600"
FT                   /id="VSP_037337"
FT   VAR_SEQ         1..44
FT                   /note="MACKISPGANSASLPGHPNKVICERVRLQSLFPLLPSDQNTTVQ -> MQHT
FT                   CTQQKKVTYKHIARFSPRNRLCQADAVFNNNLAGFQLQSP (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_053846"
FT   VAR_SEQ         5..54
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012243"
FT   VAR_SEQ         45..120
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_053847"
FT   VARIANT         206
FT                   /note="A -> T (in dbSNP:rs183475137)"
FT                   /evidence="ECO:0000269|PubMed:12074600"
FT                   /id="VAR_055400"
FT   CONFLICT        308
FT                   /note="I -> K (in Ref. 2; CAB66751)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="E -> G (in Ref. 3; BAG52726)"
FT                   /evidence="ECO:0000305"
FT   HELIX           441..445
FT                   /evidence="ECO:0007829|PDB:4V3K"
FT   STRAND          448..450
FT                   /evidence="ECO:0007829|PDB:4V3L"
FT   STRAND          453..455
FT                   /evidence="ECO:0007829|PDB:1X4J"
FT   STRAND          457..459
FT                   /evidence="ECO:0007829|PDB:4V3L"
FT   TURN            464..467
FT                   /evidence="ECO:0007829|PDB:4V3L"
FT   STRAND          475..478
FT                   /evidence="ECO:0007829|PDB:4V3L"
FT   TURN            480..482
FT                   /evidence="ECO:0007829|PDB:1X4J"
FT   STRAND          484..486
FT                   /evidence="ECO:0007829|PDB:4V3L"
FT   HELIX           487..496
FT                   /evidence="ECO:0007829|PDB:4V3L"
FT   TURN            501..503
FT                   /evidence="ECO:0007829|PDB:4V3L"
SQ   SEQUENCE   515 AA;  57595 MW;  ABFE9486CA732AFA CRC64;
     MACKISPGAN SASLPGHPNK VICERVRLQS LFPLLPSDQN TTVQEDAHFK AFFQSEDSPS
     PKRQRLSHSV FDYTSASPAP SPPMRPWEMT SNRQPPSVRP SQHHFSGERC NTPARNRRSP
     PVRRQRGRRD RLSRHNSISQ DENYHHLPYA QQQAIEEPRA FHPPNVSPRL LHPAAHPPQQ
     NAVMVDIHDQ LHQGTVPVSY TVTTVAPHGI PLCTGQHIPA CSTQQVPGCS VVFSGQHLPV
     CSVPPPMLQA CSVQHLPVPY AAFPPLISSD PFLIHPPHLS PHHPPHLPPP GQFVPFQTQQ
     SRSPLQRIEN EVELLGEHLP VGGFTYPPSA HPPTLPPSAP LQFLTHDPLH QEVSFGVPYP
     PFMPRRLTGR SRYRSQQPIP PPPYHPSLLP YVLSMLPVPP AVGPTFSFEL DVEDGEVENY
     EALLNLAERL GEAKPRGLTK ADIEQLPSYR FNPNNHQSEQ TLCVVCMCDF ESRQLLRVLP
     CNHEFHAKCV DKWLKANRTC PICRADASEV HRDSE
 
 
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