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PEF1_HUMAN
ID   PEF1_HUMAN              Reviewed;         284 AA.
AC   Q9UBV8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=Peflin {ECO:0000303|PubMed:10486255};
DE   AltName: Full=PEF protein with a long N-terminal hydrophobic domain {ECO:0000303|PubMed:10486255};
DE   AltName: Full=Penta-EF hand domain-containing protein 1 {ECO:0000312|HGNC:HGNC:30009};
GN   Name=PEF1 {ECO:0000312|HGNC:HGNC:30009}; Synonyms=ABP32;
GN   ORFNames=UNQ1845/PRO3573 {ECO:0000303|PubMed:12975309};
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].
RX   PubMed=10486255; DOI=10.1006/bbrc.1999.1189;
RA   Kitaura Y., Watanabe M., Satoh H., Kawai T., Hitomi K., Maki M.;
RT   "Peflin, a novel member of the five-EF-hand-protein family, is similar to
RT   the apoptosis-linked gene 2 (ALG-2) protein but possesses nonapeptide
RT   repeats in the N-terminal hydrophobic region.";
RL   Biochem. Biophys. Res. Commun. 263:68-75(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RA   Shibata M., Noguchi J.;
RT   "A putative calcium binding protein that has five EF-hand motifs.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate, and Skin;
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, SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6.
RX   PubMed=11278427; DOI=10.1074/jbc.m008649200;
RA   Kitaura Y., Matsumoto S., Satoh H., Hitomi K., Maki M.;
RT   "Peflin and ALG-2, members of the penta-EF-hand protein family, form a
RT   heterodimer that dissociates in a Ca2+-dependent manner.";
RL   J. Biol. Chem. 276:14053-14058(2001).
RN   [8]
RP   INTERACTION WITH PDCD6.
RX   PubMed=11883899; DOI=10.1006/abbi.2001.2736;
RA   Kitaura Y., Satoh H., Takahashi H., Shibata H., Maki M.;
RT   "Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized by
RT   dimerization through their fifth EF-hand regions.";
RL   Arch. Biochem. Biophys. 399:12-18(2002).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PDCD6, UBIQUITINATION AT
RP   LYS-137, AND MUTAGENESIS OF LYS-137; LYS-165 AND LYS-167.
RX   PubMed=27716508; DOI=10.1016/j.cell.2016.09.026;
RA   McGourty C.A., Akopian D., Walsh C., Gorur A., Werner A., Schekman R.,
RA   Bautista D., Rape M.;
RT   "Regulation of the CUL3 ubiquitin ligase by a calcium-dependent co-
RT   adaptor.";
RL   Cell 167:525-538(2016).
CC   -!- FUNCTION: Calcium-binding protein that acts as an adapter that bridges
CC       unrelated proteins or stabilizes weak protein-protein complexes in
CC       response to calcium. Together with PDCD6, acts as calcium-dependent
CC       adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic
CC       reticulum (ER)-Golgi transport by regulating the size of COPII coats
CC       (PubMed:27716508). In response to cytosolic calcium increase, the
CC       heterodimer formed with PDCD6 interacts with, and bridges together the
CC       BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting
CC       monoubiquitination of SEC31 and subsequent collagen export, which is
CC       required for neural crest specification (PubMed:27716508). Its role in
CC       the heterodimer formed with PDCD6 is however unclear: some evidence
CC       shows that PEF1 and PDCD6 work together and promote association between
CC       PDCD6 and SEC31 in presence of calcium (PubMed:27716508). Other reports
CC       show that PEF1 dissociates from PDCD6 in presence of calcium, and may
CC       act as a negative regulator of PDCD6 (PubMed:11278427). Also acts as a
CC       negative regulator of ER-Golgi transport; possibly by inhibiting
CC       interaction between PDCD6 and SEC31 (By similarity).
CC       {ECO:0000250|UniProtKB:Q641Z8, ECO:0000269|PubMed:11278427,
CC       ECO:0000269|PubMed:27716508}.
CC   -!- SUBUNIT: Heterodimer; heterodimerizes (via the EF-hand 5) with PDCD6
CC       (PubMed:11278427, PubMed:11883899, PubMed:27716508). Dissociates from
CC       PDCD6 in presence of calcium (PubMed:11278427).
CC       {ECO:0000269|PubMed:11278427, ECO:0000269|PubMed:11883899,
CC       ECO:0000269|PubMed:27716508}.
CC   -!- INTERACTION:
CC       Q9UBV8; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-724639, EBI-357530;
CC       Q9UBV8; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-724639, EBI-12102070;
CC       Q9UBV8; O95429: BAG4; NbExp=5; IntAct=EBI-724639, EBI-2949658;
CC       Q9UBV8; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-724639, EBI-953896;
CC       Q9UBV8; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-724639, EBI-718615;
CC       Q9UBV8; Q13137: CALCOCO2; NbExp=4; IntAct=EBI-724639, EBI-739580;
CC       Q9UBV8; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-724639, EBI-747776;
CC       Q9UBV8; P78358: CTAG1B; NbExp=3; IntAct=EBI-724639, EBI-1188472;
CC       Q9UBV8; Q15038: DAZAP2; NbExp=6; IntAct=EBI-724639, EBI-724310;
CC       Q9UBV8; Q04637-9: EIF4G1; NbExp=3; IntAct=EBI-724639, EBI-12012124;
CC       Q9UBV8; Q01844: EWSR1; NbExp=3; IntAct=EBI-724639, EBI-739737;
CC       Q9UBV8; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-724639, EBI-11978259;
CC       Q9UBV8; Q6PJQ5: FOXR2; NbExp=7; IntAct=EBI-724639, EBI-8468543;
CC       Q9UBV8; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-724639, EBI-10329202;
CC       Q9UBV8; O14964: HGS; NbExp=3; IntAct=EBI-724639, EBI-740220;
CC       Q9UBV8; Q4G0P3-6: HYDIN; NbExp=3; IntAct=EBI-724639, EBI-14748124;
CC       Q9UBV8; Q0VD86: INCA1; NbExp=3; IntAct=EBI-724639, EBI-6509505;
CC       Q9UBV8; Q53G59: KLHL12; NbExp=8; IntAct=EBI-724639, EBI-740929;
CC       Q9UBV8; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-724639, EBI-10210845;
CC       Q9UBV8; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-724639, EBI-11992140;
CC       Q9UBV8; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-724639, EBI-12811111;
CC       Q9UBV8; Q71SY5: MED25; NbExp=3; IntAct=EBI-724639, EBI-394558;
CC       Q9UBV8; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-724639, EBI-10174029;
CC       Q9UBV8; O75340: PDCD6; NbExp=10; IntAct=EBI-724639, EBI-352915;
CC       Q9UBV8; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-724639, EBI-724639;
CC       Q9UBV8; O95486-2: SEC24A; NbExp=3; IntAct=EBI-724639, EBI-12320085;
CC       Q9UBV8; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-724639, EBI-12275818;
CC       Q9UBV8; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-724639, EBI-12288855;
CC       Q9UBV8; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-724639, EBI-11959123;
CC       Q9UBV8; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-724639, EBI-742688;
CC       Q9UBV8; Q8IWL8: STH; NbExp=3; IntAct=EBI-724639, EBI-12843506;
CC       Q9UBV8; Q92734: TFG; NbExp=6; IntAct=EBI-724639, EBI-357061;
CC       Q9UBV8; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-724639, EBI-2559305;
CC       Q9UBV8; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-724639, EBI-12040603;
CC       Q9UBV8; Q15915: ZIC1; NbExp=3; IntAct=EBI-724639, EBI-11963196;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278427}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:Q641Z8}. Membrane
CC       {ECO:0000269|PubMed:11278427}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:11278427}. Cytoplasmic vesicle, COPII-coated
CC       vesicle membrane {ECO:0000269|PubMed:27716508}; Peripheral membrane
CC       protein {ECO:0000305}. Note=Membrane-associated in the presence of
CC       Ca(2+) (PubMed:11278427). Localizes to endoplasmic reticulum exit site
CC       (ERES) (By similarity). {ECO:0000250|UniProtKB:Q641Z8,
CC       ECO:0000269|PubMed:11278427}.
CC   -!- PTM: Ubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex.
CC       {ECO:0000269|PubMed:27716508}.
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DR   EMBL; AB026628; BAA85163.1; -; mRNA.
DR   EMBL; AB018357; BAA84922.1; -; mRNA.
DR   EMBL; AY359011; AAQ89370.1; -; mRNA.
DR   EMBL; AK001420; BAA91680.1; -; mRNA.
DR   EMBL; CR542139; CAG46936.1; -; mRNA.
DR   EMBL; BC002773; AAH02773.1; -; mRNA.
DR   EMBL; BC012561; AAH12561.1; -; mRNA.
DR   CCDS; CCDS345.1; -.
DR   RefSeq; NP_036524.1; NM_012392.3.
DR   AlphaFoldDB; Q9UBV8; -.
DR   SMR; Q9UBV8; -.
DR   BioGRID; 139275; 90.
DR   CORUM; Q9UBV8; -.
DR   IntAct; Q9UBV8; 50.
DR   MINT; Q9UBV8; -.
DR   STRING; 9606.ENSP00000362807; -.
DR   ChEMBL; CHEMBL4105771; -.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   GlyGen; Q9UBV8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UBV8; -.
DR   PhosphoSitePlus; Q9UBV8; -.
DR   BioMuta; PEF1; -.
DR   DMDM; 74761895; -.
DR   REPRODUCTION-2DPAGE; IPI00018235; -.
DR   EPD; Q9UBV8; -.
DR   jPOST; Q9UBV8; -.
DR   MassIVE; Q9UBV8; -.
DR   MaxQB; Q9UBV8; -.
DR   PaxDb; Q9UBV8; -.
DR   PeptideAtlas; Q9UBV8; -.
DR   PRIDE; Q9UBV8; -.
DR   ProteomicsDB; 84082; -.
DR   Antibodypedia; 31143; 169 antibodies from 28 providers.
DR   DNASU; 553115; -.
DR   Ensembl; ENST00000373703.5; ENSP00000362807.4; ENSG00000162517.13.
DR   GeneID; 553115; -.
DR   KEGG; hsa:553115; -.
DR   MANE-Select; ENST00000373703.5; ENSP00000362807.4; NM_012392.4; NP_036524.1.
DR   UCSC; uc001bth.3; human.
DR   CTD; 553115; -.
DR   DisGeNET; 553115; -.
DR   GeneCards; PEF1; -.
DR   HGNC; HGNC:30009; PEF1.
DR   HPA; ENSG00000162517; Low tissue specificity.
DR   MIM; 610033; gene.
DR   neXtProt; NX_Q9UBV8; -.
DR   OpenTargets; ENSG00000162517; -.
DR   PharmGKB; PA142671184; -.
DR   VEuPathDB; HostDB:ENSG00000162517; -.
DR   eggNOG; KOG0037; Eukaryota.
DR   GeneTree; ENSGT00940000155722; -.
DR   HOGENOM; CLU_051357_1_0_1; -.
DR   InParanoid; Q9UBV8; -.
DR   OMA; MAYQGGY; -.
DR   OrthoDB; 1330600at2759; -.
DR   PhylomeDB; Q9UBV8; -.
DR   TreeFam; TF314682; -.
DR   PathwayCommons; Q9UBV8; -.
DR   SignaLink; Q9UBV8; -.
DR   BioGRID-ORCS; 553115; 92 hits in 1079 CRISPR screens.
DR   ChiTaRS; PEF1; human.
DR   GeneWiki; PEF1; -.
DR   GenomeRNAi; 553115; -.
DR   Pharos; Q9UBV8; Tbio.
DR   PRO; PR:Q9UBV8; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UBV8; protein.
DR   Bgee; ENSG00000162517; Expressed in left lobe of thyroid gland and 199 other tissues.
DR   ExpressionAtlas; Q9UBV8; baseline and differential.
DR   Genevisible; Q9UBV8; HS.
DR   GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IMP:GO_Central.
DR   GO; GO:0048208; P:COPII vesicle coating; IMP:UniProtKB.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR   GO; GO:0014032; P:neural crest cell development; IMP:UniProtKB.
DR   GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
DR   GO; GO:1902527; P:positive regulation of protein monoubiquitination; IMP:UniProtKB.
DR   GO; GO:0051592; P:response to calcium ion; IPI:UniProtKB.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13405; EF-hand_6; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW   Isopeptide bond; Membrane; Metal-binding; Reference proteome; Repeat;
KW   Ubl conjugation.
FT   CHAIN           1..284
FT                   /note="Peflin"
FT                   /id="PRO_0000247045"
FT   REPEAT          21..29
FT                   /note="1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          31..39
FT                   /note="2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          41..49
FT                   /note="3"
FT                   /evidence="ECO:0000305"
FT   REPEAT          50..58
FT                   /note="4"
FT                   /evidence="ECO:0000305"
FT   REPEAT          59..67
FT                   /note="5"
FT                   /evidence="ECO:0000305"
FT   REPEAT          76..84
FT                   /note="6"
FT                   /evidence="ECO:0000305"
FT   REPEAT          85..92
FT                   /note="7"
FT                   /evidence="ECO:0000305"
FT   REPEAT          93..100
FT                   /note="8"
FT                   /evidence="ECO:0000305"
FT   REPEAT          101..109
FT                   /note="9"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          114..149
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          155..183
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          181..216
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          217..253
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          254..283
FT                   /note="EF-hand 5"
FT                   /evidence="ECO:0000305"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          21..109
FT                   /note="9 X 9 AA approximate tandem repeat of [AP]-P-G-G-P-
FT                   Y-G-G-P-P"
FT                   /evidence="ECO:0000305"
FT   REGION          204..284
FT                   /note="Required for interaction with PDCD6"
FT                   /evidence="ECO:0000269|PubMed:11883899"
FT   COMPBIAS        47..64
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         127
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         129
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         131
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         138
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         196
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         198
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CROSSLNK        137
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000305|PubMed:27716508"
FT   MUTAGEN         137
FT                   /note="K->R: Decreased ubiquitination by the BCR(KLHL12) E3
FT                   ubiquitin ligase complex."
FT                   /evidence="ECO:0000269|PubMed:27716508"
FT   MUTAGEN         165
FT                   /note="K->R: Does not affect ubiquitination by the
FT                   BCR(KLHL12) E3 ubiquitin ligase complex."
FT                   /evidence="ECO:0000269|PubMed:27716508"
FT   MUTAGEN         167
FT                   /note="K->R: Does not affect ubiquitination by the
FT                   BCR(KLHL12) E3 ubiquitin ligase complex."
FT                   /evidence="ECO:0000269|PubMed:27716508"
SQ   SEQUENCE   284 AA;  30381 MW;  2E9AA5750CB7A68A CRC64;
     MASYPYRQGC PGAAGQAPGA PPGSYYPGPP NSGGQYGSGL PPGGGYGGPA PGGPYGPPAG
     GGPYGHPNPG MFPSGTPGGP YGGAAPGGPY GQPPPSSYGA QQPGLYGQGG APPNVDPEAY
     SWFQSVDSDH SGYISMKELK QALVNCNWSS FNDETCLMMI NMFDKTKSGR IDVYGFSALW
     KFIQQWKNLF QQYDRDRSGS ISYTELQQAL SQMGYNLSPQ FTQLLVSRYC PRSANPAMQL
     DRFIQVCTQL QVLTEAFREK DTAVQGNIRL SFEDFVTMTA SRML
 
 
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