ID VCIP1_HUMAN Reviewed; 1222 AA. AC Q96JH7; Q504T4; Q86T93; Q86W01; Q8N3A9; Q9H5R8; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 2. DT 12-OCT-2022, entry version 165. DE RecName: Full=Deubiquitinating protein VCPIP1 {ECO:0000305}; DE EC=3.4.19.12 {ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:32649882}; DE AltName: Full=Valosin-containing protein p97/p47 complex-interacting protein 1 {ECO:0000305}; DE AltName: Full=Valosin-containing protein p97/p47 complex-interacting protein p135 {ECO:0000250|UniProtKB:Q8CF97}; DE Short=VCP/p47 complex-interacting 135-kDa protein {ECO:0000250|UniProtKB:Q8CF97}; GN Name=VCPIP1 {ECO:0000303|PubMed:32649882, ECO:0000312|HGNC:HGNC:30897}; GN Synonyms=KIAA1850 {ECO:0000303|PubMed:11347906}, GN VCIP135 {ECO:0000303|PubMed:23827681}; 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]. RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis, and 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1184. RC TISSUE=Lung; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747; THR-763; SER-994 AND RP SER-1198, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-408, 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-1198, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046; RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., RA Ovaa H., Komander D.; RT "OTU deubiquitinases reveal mechanisms of linkage specificity and enable RT ubiquitin chain restriction analysis."; RL Cell 154:169-184(2013). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747; SER-757; SER-768; RP SER-994; SER-998; SER-1077 AND SER-1198, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP IDENTIFICATION BY 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 [14] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=28584101; DOI=10.1073/pnas.1621076114; RA Tsai Y.C., Kotiya A., Kiris E., Yang M., Bavari S., Tessarollo L., RA Oyler G.A., Weissman A.M.; RT "Deubiquitinating enzyme VCIP135 dictates the duration of botulinum RT neurotoxin type A intoxication."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E5158-E5166(2017). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-219 RP AND SER-1207, AND PHOSPHORYLATION AT SER-1207. RX PubMed=32649882; DOI=10.1016/j.molcel.2020.06.027; RA Huang J., Zhou Q., Gao M., Nowsheen S., Zhao F., Kim W., Zhu Q., Kojima Y., RA Yin P., Zhang Y., Guo G., Tu X., Deng M., Luo K., Qin B., Machida Y., RA Lou Z.; RT "Tandem deubiquitination and acetylation of SPRTN promotes DNA-protein RT crosslink repair and protects against aging."; RL Mol. Cell 0:0-0(2020). CC -!- FUNCTION: Deubiquitinating enzyme involved in DNA repair and reassembly CC of the Golgi apparatus and the endoplasmic reticulum following mitosis CC (PubMed:32649882). Necessary for VCP-mediated reassembly of Golgi CC stacks after mitosis (By similarity). Plays a role in VCP-mediated CC formation of transitional endoplasmic reticulum (tER) (By similarity). CC Mediates dissociation of the ternary complex containing STX5A, NSFL1C CC and VCP (By similarity). Also involved in DNA repair following CC phosphorylation by ATM or ATR: acts by catalyzing deubiquitination of CC SPRTN, thereby promoting SPRTN recruitment to chromatin and subsequent CC proteolytic cleavage of covalent DNA-protein cross-links (DPCs) CC (PubMed:32649882). Hydrolyzes 'Lys-11'- and 'Lys-48'-linked CC polyubiquitin chains (PubMed:23827681). {ECO:0000250|UniProtKB:Q8CF97, CC ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:32649882}. CC -!- FUNCTION: (Microbial infection) Regulates the duration of C.botulinum CC neurotoxin type A (BoNT/A) intoxication by catalyzing deubiquitination CC of Botulinum neurotoxin A light chain (LC), thereby preventing LC CC degradation by the proteasome, and accelerating botulinum neurotoxin CC intoxication in patients. {ECO:0000269|PubMed:28584101}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:23827681, CC ECO:0000269|PubMed:32649882}; CC -!- SUBUNIT: Binds VCP and the ternary complex containing STX5A, NSFL1C and CC VCP. {ECO:0000250|UniProtKB:Q8CF97}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32649882}. Cytoplasm CC {ECO:0000269|PubMed:32649882}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:Q8CF97}. Golgi apparatus, Golgi stack CC {ECO:0000250|UniProtKB:Q8CF97}. Note=Associated with Golgi stacks and CC endoplasmic reticulum (By similarity). Displays cytoplasmic to nuclear CC translocation in response to DNA-protein cross-links (DPCs)-inducing CC agents (PubMed:32649882). {ECO:0000250|UniProtKB:Q8CF97, CC ECO:0000269|PubMed:32649882}. CC -!- PTM: Phosphorylated at Ser-1207 by ATM or ATR following induction of CC covalent DNA-protein cross-links (DPCs). {ECO:0000269|PubMed:32649882}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15552.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB47479.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB058753; BAB47479.1; ALT_INIT; mRNA. DR EMBL; AL834476; CAD39135.1; -; mRNA. DR EMBL; AL832606; CAD89944.1; -; mRNA. DR EMBL; BC049379; AAH49379.1; -; mRNA. DR EMBL; BC094799; AAH94799.1; -; mRNA. DR EMBL; AK026785; BAB15552.1; ALT_FRAME; mRNA. DR CCDS; CCDS6192.1; -. DR RefSeq; NP_079330.2; NM_025054.4. DR AlphaFoldDB; Q96JH7; -. DR SMR; Q96JH7; -. DR BioGRID; 123125; 153. DR IntAct; Q96JH7; 45. DR MINT; Q96JH7; -. DR STRING; 9606.ENSP00000309031; -. DR BindingDB; Q96JH7; -. DR ChEMBL; CHEMBL4630849; -. DR MEROPS; C64.006; -. DR GlyGen; Q96JH7; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q96JH7; -. DR MetOSite; Q96JH7; -. DR PhosphoSitePlus; Q96JH7; -. DR BioMuta; VCPIP1; -. DR DMDM; 42560002; -. DR EPD; Q96JH7; -. DR jPOST; Q96JH7; -. DR MassIVE; Q96JH7; -. DR MaxQB; Q96JH7; -. DR PaxDb; Q96JH7; -. DR PeptideAtlas; Q96JH7; -. DR PRIDE; Q96JH7; -. DR ProteomicsDB; 76963; -. DR Antibodypedia; 24885; 102 antibodies from 26 providers. DR DNASU; 80124; -. DR Ensembl; ENST00000310421.5; ENSP00000309031.4; ENSG00000175073.8. DR GeneID; 80124; -. DR KEGG; hsa:80124; -. DR MANE-Select; ENST00000310421.5; ENSP00000309031.4; NM_025054.5; NP_079330.2. DR UCSC; uc003xwn.4; human. DR CTD; 80124; -. DR DisGeNET; 80124; -. DR GeneCards; VCPIP1; -. DR HGNC; HGNC:30897; VCPIP1. DR HPA; ENSG00000175073; Tissue enhanced (bone). DR MIM; 611745; gene. DR neXtProt; NX_Q96JH7; -. DR OpenTargets; ENSG00000175073; -. DR PharmGKB; PA142670629; -. DR VEuPathDB; HostDB:ENSG00000175073; -. DR eggNOG; KOG4345; Eukaryota. DR GeneTree; ENSGT00390000002854; -. DR HOGENOM; CLU_009674_0_0_1; -. DR InParanoid; Q96JH7; -. DR OMA; VPMGLRN; -. DR OrthoDB; 222681at2759; -. DR PhylomeDB; Q96JH7; -. DR TreeFam; TF329469; -. DR PathwayCommons; Q96JH7; -. DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases. DR SignaLink; Q96JH7; -. DR SIGNOR; Q96JH7; -. DR BioGRID-ORCS; 80124; 89 hits in 1135 CRISPR screens. DR ChiTaRS; VCPIP1; human. DR GeneWiki; VCPIP1; -. DR GenomeRNAi; 80124; -. DR Pharos; Q96JH7; Tbio. DR PRO; PR:Q96JH7; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q96JH7; protein. DR Bgee; ENSG00000175073; Expressed in tendon of biceps brachii and 142 other tissues. DR Genevisible; Q96JH7; HS. DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB. DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central. DR GO; GO:0090168; P:Golgi reassembly; IBA:GO_Central. DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl. DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB. DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB. DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IDA:UniProtKB. DR GO; GO:1905634; P:regulation of protein localization to chromatin; IDA:UniProtKB. DR InterPro; IPR003323; OTU_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR039087; VCPIP1. DR InterPro; IPR045827; VCPIP1_N. DR PANTHER; PTHR14843; PTHR14843; 1. DR Pfam; PF02338; OTU; 1. DR Pfam; PF19437; VCIP135_N; 1. DR SUPFAM; SSF54236; SSF54236; 1. DR PROSITE; PS50802; OTU; 1. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; DNA damage; DNA repair; Endoplasmic reticulum; KW Golgi apparatus; Hydrolase; Nucleus; Phosphoprotein; Protease; KW Reference proteome; Thiol protease; Ubl conjugation pathway. FT CHAIN 1..1222 FT /note="Deubiquitinating protein VCPIP1" FT /id="PRO_0000065769" FT DOMAIN 208..361 FT /note="OTU" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 725..776 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 989..1009 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1024..1074 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1113..1175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1188..1222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..23 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 741..775 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1054..1074 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1130..1175 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 216 FT /evidence="ECO:0000250|UniProtKB:Q96FW1" FT ACT_SITE 219 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:32649882" FT ACT_SITE 354 FT /evidence="ECO:0000250|UniProtKB:Q96FW1" FT MOD_RES 408 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 747 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 757 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 763 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 768 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 994 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 998 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1077 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1198 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1207 FT /note="Phosphoserine; by ATM" FT /evidence="ECO:0000269|PubMed:32649882" FT MUTAGEN 219 FT /note="C->A: Loss of deubiquitinating activity and ability FT to deubiquitinate SPRTN." FT /evidence="ECO:0000269|PubMed:32649882" FT MUTAGEN 1207 FT /note="S->A: Abolished phosphorylation in response to FT covalent DNA-protein cross-links (DPCs)." FT /evidence="ECO:0000269|PubMed:32649882" FT CONFLICT 169 FT /note="L -> P (in Ref. 2; CAD89944)" FT /evidence="ECO:0000305" FT CONFLICT 437 FT /note="Q -> R (in Ref. 2; CAD89944)" FT /evidence="ECO:0000305" FT CONFLICT 811 FT /note="P -> F (in Ref. 3; AAH49379)" FT /evidence="ECO:0000305" FT CONFLICT 927 FT /note="Missing (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 988 FT /note="A -> S (in Ref. 3; AAH49379)" FT /evidence="ECO:0000305" SQ SEQUENCE 1222 AA; 134321 MW; 5CE99D723386782D CRC64; MSQPPPPPPP LPPPPPPPEA PQTPSSLASA AASGGLLKRR DRRILSGSCP DPKCQARLFF PASGSVSIEC TECGQRHEQQ QLLGVEEVTD PDVVLHNLLR NALLGVTGAP KKNTELVKVM GLSNYHCKLL SPILARYGMD KQTGRAKLLR DMNQGELFDC ALLGDRAFLI EPEHVNTVGY GKDRSGSLLY LHDTLEDIKR ANKSQECLIP VHVDGDGHCL VHAVSRALVG RELFWHALRE NLKQHFQQHL ARYQALFHDF IDAAEWEDII NECDPLFVPP EGVPLGLRNI HIFGLANVLH RPIILLDSLS GMRSSGDYSA TFLPGLIPAE KCTGKDGHLN KPICIAWSSS GRNHYIPLVG IKGAALPKLP MNLLPKAWGV PQDLIKKYIK LEEDGGCVIG GDRSLQDKYL LRLVAAMEEV FMDKHGIHPS LVADVHQYFY RRTGVIGVQP EEVTAAAKKA VMDNRLHKCL LCGALSELHV PPEWLAPGGK LYNLAKSTHG QLRTDKNYSF PLNNLVCSYD SVKDVLVPDY GMSNLTACNW CHGTSVRKVR GDGSIVYLDG DRTNSRSTGG KCGCGFKHFW DGKEYDNLPE AFPITLEWGG RVVRETVYWF QYESDSSLNS NVYDVAMKLV TKHFPGEFGS EILVQKVVHT ILHQTAKKNP DDYTPVNIDG AHAQRVGDVQ GQESESQLPT KIILTGQKTK TLHKEELNMS KTERTIQQNI TEQASVMQKR KTEKLKQEQK GQPRTVSPST IRDGPSSAPA TPTKAPYSPT TSKEKKIRIT TNDGRQSMVT LKSSTTFFEL QESIAREFNI PPYLQCIRYG FPPKELMPPQ AGMEKEPVPL QHGDRITIEI LKSKAEGGQS AAAHSAHTVK QEDIAVTGKL SSKELQEQAE KEMYSLCLLA TLMGEDVWSY AKGLPHMFQQ GGVFYSIMKK TMGMADGKHC TFPHLPGKTF VYNASEDRLE LCVDAAGHFP IGPDVEDLVK EAVSQVRAEA TTRSRESSPS HGLLKLGSGG VVKKKSEQLH NVTAFQGKGH SLGTASGNPH LDPRARETSV VRKHNTGTDF SNSSTKTEPS VFTASSSNSE LIRIAPGVVT MRDGRQLDPD LVEAQRKKLQ EMVSSIQASM DRHLRDQSTE QSPSDLPQRK TEVVSSSAKS GSLQTGLPES FPLTGGTENL NTETTDGCVA DALGAAFATR SKAQRGNSVE ELEEMDSQDA EMTNTTEPMD HS //