VCIP1_HUMAN
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 03-AUG-2022, entry version 164.
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; 150.
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
