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P20L1_HUMAN
ID   P20L1_HUMAN             Reviewed;        1017 AA.
AC   A8MW92; A8MZC9; Q86U89; Q86W43; Q96BT0; Q9H702; Q9HBK3; Q9NYR3; Q9Y381;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=PHD finger protein 20-like protein 1;
GN   Name=PHF20L1; ORFNames=CGI-72;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 755-1017 (ISOFORM 1).
RC   TISSUE=Brain, and Colon;
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=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 613-1017 (ISOFORM 1).
RC   TISSUE=Uterus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-1017 (ISOFORM 4).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 555-1017 (ISOFORM 1).
RA   Shan Y.X., Huang C.Q., Yu L.;
RT   "Cloning and characterization of a novel PHD finger gene.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-909, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-79; LYS-530 AND LYS-851,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [10]
RP   STRUCTURE BY NMR OF 1-181 (ISOFORM 2).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the tudor domain of PHD finger protein 20-like 1.";
RL   Submitted (OCT-2007) to the PDB data bank.
CC   -!- INTERACTION:
CC       A8MW92; P68431: H3C12; NbExp=2; IntAct=EBI-2560834, EBI-79722;
CC       A8MW92; P62805: H4C9; NbExp=2; IntAct=EBI-2560834, EBI-302023;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A8MW92-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A8MW92-2; Sequence=VSP_033781, VSP_033782, VSP_033783;
CC       Name=4;
CC         IsoId=A8MW92-4; Sequence=VSP_040407, VSP_040408;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD34067.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAP33690.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB15098.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAW92152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK025268; BAB15098.1; ALT_INIT; mRNA.
DR   EMBL; AK290506; BAF83195.1; -; mRNA.
DR   EMBL; AF228727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471060; EAW92148.1; -; Genomic_DNA.
DR   EMBL; CH471060; EAW92152.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC015211; AAH15211.1; -; mRNA.
DR   EMBL; BC050655; AAH50655.4; -; mRNA.
DR   EMBL; BC056413; AAH56413.2; -; mRNA.
DR   EMBL; AF151830; AAD34067.1; ALT_INIT; mRNA.
DR   EMBL; AY279109; AAP33690.1; ALT_INIT; mRNA.
DR   CCDS; CCDS6367.2; -. [A8MW92-1]
DR   CCDS; CCDS6368.1; -. [A8MW92-2]
DR   RefSeq; NP_057102.4; NM_016018.4. [A8MW92-1]
DR   RefSeq; NP_940915.1; NM_198513.1. [A8MW92-2]
DR   RefSeq; XP_016869006.1; XM_017013517.1. [A8MW92-2]
DR   PDB; 2EQM; NMR; -; A=1-81.
DR   PDB; 2EQU; NMR; -; A=85-177.
DR   PDB; 2JTF; NMR; -; A=1-74.
DR   PDB; 6L0X; X-ray; 1.30 A; A/B=5-70.
DR   PDB; 6L10; X-ray; 1.60 A; A/B/C/D=5-70.
DR   PDB; 6L1C; X-ray; 1.58 A; A=5-70.
DR   PDB; 6L1F; X-ray; 1.90 A; B=5-70.
DR   PDB; 6L1I; X-ray; 1.85 A; B=5-70.
DR   PDB; 6L1P; X-ray; 1.23 A; A/B/C/D=5-70.
DR   PDBsum; 2EQM; -.
DR   PDBsum; 2EQU; -.
DR   PDBsum; 2JTF; -.
DR   PDBsum; 6L0X; -.
DR   PDBsum; 6L10; -.
DR   PDBsum; 6L1C; -.
DR   PDBsum; 6L1F; -.
DR   PDBsum; 6L1I; -.
DR   PDBsum; 6L1P; -.
DR   AlphaFoldDB; A8MW92; -.
DR   SMR; A8MW92; -.
DR   BioGRID; 119294; 69.
DR   IntAct; A8MW92; 31.
DR   MINT; A8MW92; -.
DR   STRING; 9606.ENSP00000378784; -.
DR   iPTMnet; A8MW92; -.
DR   PhosphoSitePlus; A8MW92; -.
DR   BioMuta; PHF20L1; -.
DR   EPD; A8MW92; -.
DR   jPOST; A8MW92; -.
DR   MassIVE; A8MW92; -.
DR   MaxQB; A8MW92; -.
DR   PaxDb; A8MW92; -.
DR   PeptideAtlas; A8MW92; -.
DR   PRIDE; A8MW92; -.
DR   ProteomicsDB; 2228; -. [A8MW92-1]
DR   ProteomicsDB; 2229; -. [A8MW92-2]
DR   ProteomicsDB; 2230; -. [A8MW92-4]
DR   ABCD; A8MW92; 1 sequenced antibody.
DR   Antibodypedia; 27384; 135 antibodies from 17 providers.
DR   DNASU; 51105; -.
DR   Ensembl; ENST00000337920.8; ENSP00000338269.4; ENSG00000129292.21. [A8MW92-2]
DR   Ensembl; ENST00000395386.7; ENSP00000378784.2; ENSG00000129292.21. [A8MW92-1]
DR   Ensembl; ENST00000622263.4; ENSP00000482945.1; ENSG00000129292.21. [A8MW92-1]
DR   GeneID; 51105; -.
DR   KEGG; hsa:51105; -.
DR   MANE-Select; ENST00000395386.7; ENSP00000378784.2; NM_016018.5; NP_057102.4.
DR   UCSC; uc003ytr.4; human. [A8MW92-1]
DR   CTD; 51105; -.
DR   DisGeNET; 51105; -.
DR   GeneCards; PHF20L1; -.
DR   HGNC; HGNC:24280; PHF20L1.
DR   HPA; ENSG00000129292; Low tissue specificity.
DR   neXtProt; NX_A8MW92; -.
DR   OpenTargets; ENSG00000129292; -.
DR   PharmGKB; PA134874888; -.
DR   VEuPathDB; HostDB:ENSG00000129292; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   GeneTree; ENSGT00940000156215; -.
DR   InParanoid; A8MW92; -.
DR   OMA; KFKCQIP; -.
DR   OrthoDB; 147824at2759; -.
DR   PhylomeDB; A8MW92; -.
DR   TreeFam; TF106475; -.
DR   PathwayCommons; A8MW92; -.
DR   SignaLink; A8MW92; -.
DR   BioGRID-ORCS; 51105; 9 hits in 1077 CRISPR screens.
DR   ChiTaRS; PHF20L1; human.
DR   EvolutionaryTrace; A8MW92; -.
DR   GenomeRNAi; 51105; -.
DR   Pharos; A8MW92; Tbio.
DR   PRO; PR:A8MW92; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; A8MW92; protein.
DR   Bgee; ENSG00000129292; Expressed in adrenal tissue and 190 other tissues.
DR   ExpressionAtlas; A8MW92; baseline and differential.
DR   Genevisible; A8MW92; HS.
DR   GO; GO:0044545; C:NSL complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd04508; TUDOR; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR014002; Agenet_dom_plant.
DR   InterPro; IPR022255; DUF3776.
DR   InterPro; IPR040477; KDM4_Tudor_2.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR043449; PHF20-like.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15856; PTHR15856; 1.
DR   Pfam; PF12618; DUF3776; 1.
DR   Pfam; PF02820; MBT; 1.
DR   Pfam; PF18104; Tudor_2; 1.
DR   SMART; SM00743; Agenet; 2.
DR   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Isopeptide bond;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1017
FT                   /note="PHD finger protein 20-like protein 1"
FT                   /id="PRO_0000336001"
FT   DOMAIN          11..71
FT                   /note="Tudor 1"
FT   DOMAIN          85..141
FT                   /note="Tudor 2"
FT   ZN_FING         681..729
FT                   /note="PHD-type"
FT   REGION          183..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..579
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         368
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CCJ9"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         909
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   CROSSLNK        75
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        79
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        530
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        851
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         144..169
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033781"
FT   VAR_SEQ         311
FT                   /note="A -> V (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033782"
FT   VAR_SEQ         312..1017
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033783"
FT   VAR_SEQ         547..573
FT                   /note="KRKEKDKERREKRDKDHYRPKQKKKKK -> IRSWDFSALLMKIPSYSPISL
FT                   SGLPES (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10810093"
FT                   /id="VSP_040407"
FT   VAR_SEQ         574..1017
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10810093"
FT                   /id="VSP_040408"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:6L1P"
FT   TURN            24..26
FT                   /evidence="ECO:0007829|PDB:2JTF"
FT   STRAND          28..37
FT                   /evidence="ECO:0007829|PDB:6L1P"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:6L1P"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:6L1P"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:6L1P"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:6L1P"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:2JTF"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:2JTF"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:2EQU"
FT   STRAND          98..111
FT                   /evidence="ECO:0007829|PDB:2EQU"
FT   STRAND          114..120
FT                   /evidence="ECO:0007829|PDB:2EQU"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:2EQU"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:2EQU"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:2EQU"
SQ   SEQUENCE   1017 AA;  115010 MW;  6FF33736EE712836 CRC64;
     MSKKPPNRPG ITFEIGARLE ALDYLQKWYP SRIEKIDYEE GKMLVHFERW SHRYDEWIYW
     DSNRLRPLER PALRKEGLKD EEDFFDFKAG EEVLARWTDC RYYPAKIEAI NKEGTFTVQF
     YDGVIRCLKR MHIKAMPEDA KGQVKSQHPL SWCCPIDPAG SCNQSMGSED WIALVKAAAA
     AAAKNKTGSK PRTSANSNKD KDKDERKWFK VPSKKEETST CIATPDVEKK EDLPTSSETF
     GLHVENVPKM VFPQPESTLS NKRKNNQGNS FQAKRARLNK ITGLLASKAV GVDGAEKKED
     YNETAPMLEQ AISPKPQSQK KNEADISSSA NTQKPALLSS TLSSGKARSK KCKHESGDSS
     GCIKPPKSPL SPELIQVEDL TLVSQLSSSV INKTSPPQPV NPPRPFKHSE RRRRSQRLAT
     LPMPDDSVEK VSSPSPATDG KVFSISSQNQ QESSVPEVPD VAHLPLEKLG PCLPLDLSRG
     SEVTAPVASD SSYRNECPRA EKEDTQMLPN PSSKAIADGR GAPAAAGISK TEKKVKLEDK
     SSTAFGKRKE KDKERREKRD KDHYRPKQKK KKKKKKKSKQ HDYSDYEDSS LEFLERCSSP
     LTRSSGSSLA SRSMFTEKTT TYQYPRAILS VDLSGENLSD VDFLDDSSTE SLLLSGDEYN
     QDFDSTNFEE SQDEDDALNE IVRCICEMDE ENGFMIQCEE CLCWQHSVCM GLLEESIPEQ
     YICYICRDPP GQRWSAKYRY DKEWLNNGRM CGLSFFKENY SHLNAKKIVS THHLLADVYG
     VTEVLHGLQL KIGILKNKHH PDLHLWACSG KRKDQDQIIA GVEKKIAQDT VNREEKKYVQ
     NHKEPPRLPL KMEGTYITSE HSYQKPQSFG QDCKSLADPG SSDDDDVSSL EEEQEFHMRS
     KNSLQYSAKE HGMPEKNPAE GNTVFVYNDK KGTEDPGDSH LQWQLNLLTH IENVQNEVTS
     RMDLIEKEVD VLESWLDFTG ELEPPDPLAR LPQLKRHIKQ LLIDMGKVQQ IATLCSV
 
 
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