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APBB3_HUMAN
ID   APBB3_HUMAN             Reviewed;         486 AA.
AC   O95704; B3KQN9; Q08AG4; Q96Q18; Q9BYD4; Q9NYX6; Q9NYX7; Q9NYX8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Amyloid-beta A4 precursor protein-binding family B member 3;
DE   AltName: Full=Protein Fe65-like 2;
DE            Short=Fe65L2;
GN   Name=APBB3 {ECO:0000312|HGNC:HGNC:20708};
GN   Synonyms=FE65L2 {ECO:0000312|HGNC:HGNC:20708};
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] (ISOFORMS I AND II), INTERACTION WITH APP; APLP1
RP   AND APLP2, AND VARIANT ARG-231.
RC   TISSUE=Brain;
RX   PubMed=10081969; DOI=10.1016/s0304-3940(98)00995-1;
RA   Tanahashi H.;
RT   "Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's
RT   beta-amyloid precursor protein.";
RL   Neurosci. Lett. 261:143-146(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-231.
RX   PubMed=10329396; DOI=10.1006/bbrc.1999.0639;
RA   Tanahashi H., Tabira T.;
RT   "Genome structure and chromosomal mapping of the gene for Fe65L2
RT   interacting with Alzheimer's beta-amyloid precursor protein.";
RL   Biochem. Biophys. Res. Commun. 258:385-389(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I-214 AND I-245), SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=12153398; DOI=10.1042/bj20020562;
RA   Tanahashi H., Tabira T.;
RT   "Characterization of an amyloid precursor protein-binding protein Fe65L2
RT   and its novel isoforms lacking phosphotyrosine-interaction domains.";
RL   Biochem. J. 367:687-695(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I; II; III AND IV), AND VARIANT
RP   ARG-231.
RA   Mao Y.M., Xie Y., Sun Z., Chen X.M., Ying K., Dai J.L., Lin S., Wu C.Q.,
RA   Li Y.;
RT   "Molecular cloning of the full-length cDNA and novel splicing isoforms of
RT   Fe65L2 gene.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II), AND VARIANT ARG-231.
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-231.
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
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   [9]
RP   STRUCTURE BY NMR OF 30-61.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the WW domain from the human amyloid beta A4
RT   precursor protein-binding family B member 3, APBB3.";
RL   Submitted (APR-2008) to the PDB data bank.
CC   -!- FUNCTION: May modulate the internalization of amyloid-beta precursor
CC       protein.
CC   -!- SUBUNIT: Interacts with APP (via intracellular domain)
CC       (PubMed:10081969). Interacts with APLP1 and APLP2 (via intracellular
CC       domain) (PubMed:10081969). {ECO:0000269|PubMed:10081969}.
CC   -!- INTERACTION:
CC       O95704; P05067: APP; NbExp=5; IntAct=EBI-286427, EBI-77613;
CC       O95704; Q9UN19: DAPP1; NbExp=2; IntAct=EBI-286427, EBI-3918199;
CC       O95704; P00533: EGFR; NbExp=2; IntAct=EBI-286427, EBI-297353;
CC       O95704; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-286427, EBI-9090282;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12153398}. Nucleus
CC       {ECO:0000269|PubMed:12153398}.
CC   -!- SUBCELLULAR LOCATION: [Isoform I-214]: Nucleus.
CC   -!- SUBCELLULAR LOCATION: [Isoform I-245]: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=II;
CC         IsoId=O95704-1; Sequence=Displayed;
CC       Name=I;
CC         IsoId=O95704-2; Sequence=VSP_006799;
CC       Name=III;
CC         IsoId=O95704-3; Sequence=VSP_006800;
CC       Name=IV;
CC         IsoId=O95704-4; Sequence=VSP_006801;
CC       Name=I-214;
CC         IsoId=O95704-5; Sequence=VSP_047811, VSP_047813;
CC       Name=I-245;
CC         IsoId=O95704-6; Sequence=VSP_047812, VSP_047814;
CC   -!- TISSUE SPECIFICITY: Expressed in various tissues, highest expression in
CC       brain. {ECO:0000269|PubMed:12153398}.
CC   -!- MISCELLANEOUS: [Isoform I-214]: Increased expression upon apoptotic
CC       stimuli. {ECO:0000305}.
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DR   EMBL; AB018247; BAA35188.1; -; mRNA.
DR   EMBL; AB024745; BAA78674.1; -; Genomic_DNA.
DR   EMBL; AB049618; BAB40806.1; -; mRNA.
DR   EMBL; AB061224; BAB71767.1; -; mRNA.
DR   EMBL; AF224708; AAF65172.1; -; mRNA.
DR   EMBL; AF224709; AAF65173.1; -; mRNA.
DR   EMBL; AF224710; AAF65174.1; -; mRNA.
DR   EMBL; AF224711; AAF65175.1; -; mRNA.
DR   EMBL; AK075280; BAG52101.1; -; mRNA.
DR   EMBL; AC011399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471062; EAW62041.1; -; Genomic_DNA.
DR   EMBL; BC125187; AAI25188.1; -; mRNA.
DR   CCDS; CCDS4227.1; -. [O95704-4]
DR   CCDS; CCDS4228.1; -. [O95704-3]
DR   CCDS; CCDS4229.1; -. [O95704-1]
DR   CCDS; CCDS47279.1; -. [O95704-2]
DR   RefSeq; NP_006042.3; NM_006051.3. [O95704-4]
DR   RefSeq; NP_573418.2; NM_133172.2. [O95704-3]
DR   RefSeq; NP_573419.2; NM_133173.2. [O95704-1]
DR   RefSeq; NP_573420.2; NM_133174.2. [O95704-2]
DR   PDB; 2DYQ; X-ray; 3.10 A; A=281-417.
DR   PDB; 2YSC; NMR; -; A=30-61.
DR   PDBsum; 2DYQ; -.
DR   PDBsum; 2YSC; -.
DR   AlphaFoldDB; O95704; -.
DR   SMR; O95704; -.
DR   BioGRID; 115593; 26.
DR   IntAct; O95704; 24.
DR   MINT; O95704; -.
DR   STRING; 9606.ENSP00000346378; -.
DR   iPTMnet; O95704; -.
DR   PhosphoSitePlus; O95704; -.
DR   BioMuta; APBB3; -.
DR   MassIVE; O95704; -.
DR   PaxDb; O95704; -.
DR   PeptideAtlas; O95704; -.
DR   PRIDE; O95704; -.
DR   ProteomicsDB; 51002; -. [O95704-1]
DR   ProteomicsDB; 51003; -. [O95704-2]
DR   ProteomicsDB; 51004; -. [O95704-3]
DR   ProteomicsDB; 51005; -. [O95704-4]
DR   ProteomicsDB; 77814; -.
DR   ProteomicsDB; 79619; -.
DR   Antibodypedia; 1613; 192 antibodies from 23 providers.
DR   DNASU; 10307; -.
DR   Ensembl; ENST00000354402.9; ENSP00000346378.5; ENSG00000113108.20. [O95704-4]
DR   Ensembl; ENST00000356738.6; ENSP00000349177.2; ENSG00000113108.20. [O95704-3]
DR   Ensembl; ENST00000357560.9; ENSP00000350171.4; ENSG00000113108.20. [O95704-1]
DR   Ensembl; ENST00000412920.7; ENSP00000402591.3; ENSG00000113108.20. [O95704-2]
DR   Ensembl; ENST00000467078.5; ENSP00000422718.1; ENSG00000113108.20. [O95704-6]
DR   Ensembl; ENST00000509914.5; ENSP00000426107.1; ENSG00000113108.20. [O95704-5]
DR   GeneID; 10307; -.
DR   KEGG; hsa:10307; -.
DR   MANE-Select; ENST00000357560.9; ENSP00000350171.4; NM_133173.3; NP_573419.2.
DR   UCSC; uc003lgd.2; human. [O95704-1]
DR   CTD; 10307; -.
DR   DisGeNET; 10307; -.
DR   GeneCards; APBB3; -.
DR   HGNC; HGNC:20708; APBB3.
DR   HPA; ENSG00000113108; Tissue enhanced (brain).
DR   MIM; 602711; gene.
DR   neXtProt; NX_O95704; -.
DR   OpenTargets; ENSG00000113108; -.
DR   PharmGKB; PA134958636; -.
DR   VEuPathDB; HostDB:ENSG00000113108; -.
DR   eggNOG; ENOG502QR5N; Eukaryota.
DR   GeneTree; ENSGT00390000000002; -.
DR   HOGENOM; CLU_093354_0_0_1; -.
DR   InParanoid; O95704; -.
DR   OMA; LYMGILP; -.
DR   PhylomeDB; O95704; -.
DR   TreeFam; TF314331; -.
DR   PathwayCommons; O95704; -.
DR   SignaLink; O95704; -.
DR   BioGRID-ORCS; 10307; 10 hits in 1075 CRISPR screens.
DR   ChiTaRS; APBB3; human.
DR   EvolutionaryTrace; O95704; -.
DR   GeneWiki; APBB3; -.
DR   GenomeRNAi; 10307; -.
DR   Pharos; O95704; Tbio.
DR   PRO; PR:O95704; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; O95704; protein.
DR   Bgee; ENSG00000113108; Expressed in right hemisphere of cerebellum and 96 other tissues.
DR   ExpressionAtlas; O95704; baseline and differential.
DR   Genevisible; O95704; HS.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:ARUK-UCL.
DR   GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR   GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IDA:ARUK-UCL.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR039576; APBB1/2/3.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR14058; PTHR14058; 1.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00462; PTB; 2.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; SSF51045; 1.
DR   PROSITE; PS01179; PID; 2.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN           1..486
FT                   /note="Amyloid-beta A4 precursor protein-binding family B
FT                   member 3"
FT                   /id="PRO_0000076054"
FT   DOMAIN          29..61
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          113..280
FT                   /note="PID 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          285..440
FT                   /note="PID 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   VAR_SEQ         196..214
FT                   /note="VHIRVWGVGSSKGRDRDFA -> AVIPTDADPQYLNPWTQIL (in
FT                   isoform I-214)"
FT                   /evidence="ECO:0000303|PubMed:12153398"
FT                   /id="VSP_047811"
FT   VAR_SEQ         210..245
FT                   /note="DRDFAFVASDKDSCMLKCHVFCCDVPAKAIASALHG -> SSDVDPGLLPLP
FT                   GPALVGEGGPSSAGTVWGESERLG (in isoform I-245)"
FT                   /evidence="ECO:0000303|PubMed:12153398"
FT                   /id="VSP_047812"
FT   VAR_SEQ         210..211
FT                   /note="Missing (in isoform I)"
FT                   /evidence="ECO:0000303|PubMed:10081969, ECO:0000303|Ref.4"
FT                   /id="VSP_006799"
FT   VAR_SEQ         210
FT                   /note="D -> PISAPA (in isoform III)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_006800"
FT   VAR_SEQ         210
FT                   /note="D -> DSPISAPA (in isoform IV)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_006801"
FT   VAR_SEQ         215..486
FT                   /note="Missing (in isoform I-214)"
FT                   /evidence="ECO:0000303|PubMed:12153398"
FT                   /id="VSP_047813"
FT   VAR_SEQ         246..486
FT                   /note="Missing (in isoform I-245)"
FT                   /evidence="ECO:0000303|PubMed:12153398"
FT                   /id="VSP_047814"
FT   VARIANT         165
FT                   /note="G -> R (in dbSNP:rs7715021)"
FT                   /id="VAR_029518"
FT   VARIANT         231
FT                   /note="C -> R (in dbSNP:rs250430)"
FT                   /evidence="ECO:0000269|PubMed:10081969,
FT                   ECO:0000269|PubMed:10329396, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15372022, ECO:0000269|Ref.4"
FT                   /id="VAR_024702"
FT   STRAND          35..40
FT                   /evidence="ECO:0007829|PDB:2YSC"
FT   STRAND          43..51
FT                   /evidence="ECO:0007829|PDB:2YSC"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:2YSC"
FT   STRAND          292..304
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   HELIX           307..318
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   STRAND          327..333
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   STRAND          335..342
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   STRAND          354..358
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   HELIX           359..361
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   STRAND          362..367
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   STRAND          373..379
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   STRAND          381..383
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   STRAND          385..391
FT                   /evidence="ECO:0007829|PDB:2DYQ"
FT   HELIX           397..415
FT                   /evidence="ECO:0007829|PDB:2DYQ"
SQ   SEQUENCE   486 AA;  52585 MW;  553DFB4D8655EFA1 CRC64;
     MLGKDYMLAI ILVNCDDDLW GDHSLEVEAG LPPGWRKIHD AAGTYYWHVP SGSTQWQRPT
     WELGDAEDPG TGTEGIWGLR PPKGRSFSSL ESSLDRSNSL SWYGGESYIQ SMEPGAKCFA
     VRSLGWVEVP EEDLAPGKSS IAVNNCIQQL AQTRSRSQPP DGAWGEGQNM LMILKKDAMS
     LVNPLDHSLI HCQPLVHIRV WGVGSSKGRD RDFAFVASDK DSCMLKCHVF CCDVPAKAIA
     SALHGLCAQI LSERVEVSGD ASCCSPDPIS PEDLPRQVEL LDAVSQAAQK YEALYMGTLP
     VTKAMGMDVL NEAIGTLTAR GDRNAWVPTM LSVSDSLMTA HPIQAEASTE EEPLWQCPVR
     LVTFIGVGRD PHTFGLIADL GRQSFQCAAF WCQPHAGGLS EAVQAACMVQ YQKCLVASAA
     RGKAWGAQAR ARLRLKRTSS MDSPGGPLPL PLLKGGVGGA GATPRKRGVF SFLDAFRLKP
     SLLHMP
 
 
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