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
