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SprT-like domain-containing protein Spartan (DNA damage protein targeting VCP) (DVC1) (Protein with SprT-like domain at the N terminus) (Spartan)

 SPRTN_HUMAN             Reviewed;         489 AA.
Q9H040; B1AKT0; B5MEF7; Q5TE78; Q6UWW6; Q96BC5; Q96KA0;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 2.
27-SEP-2017, entry version 132.
RecName: Full=SprT-like domain-containing protein Spartan;
AltName: Full=DNA damage protein targeting VCP;
Short=DVC1;
AltName: Full=Protein with SprT-like domain at the N terminus;
Short=Spartan;
Name=SPRTN; Synonyms=C1orf124, DVC1; ORFNames=UNQ1880/PRO4323;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
LEU-296.
TISSUE=Embryo, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-296.
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-243 (ISOFORM 2), AND VARIANT LEU-296.
TISSUE=Colon, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA, AND MUTAGENESIS
OF ASP-473 AND 331-TYR-PHE-332.
PubMed=22894931; DOI=10.4161/cc.21694;
Machida Y., Kim M.S., Machida Y.J.;
"Spartan/C1orf124 is important to prevent UV-induced mutagenesis.";
Cell Cycle 11:3395-3402(2012).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KCTD13; PCNA;
POLD3 AND VCP.
PubMed=22902628; DOI=10.1074/jbc.M112.400135;
Ghosal G., Leung J.W., Nair B.C., Fong K.W., Chen J.;
"Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is
a regulator of translesion synthesis.";
J. Biol. Chem. 287:34225-34233(2012).
[10]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH PCNA AND
RAD18, AND MUTAGENESIS OF 456-CYS--CYS-459.
PubMed=22681887; DOI=10.1016/j.molcel.2012.05.020;
Centore R.C., Yazinski S.A., Tse A., Zou L.;
"Spartan/C1orf124, a reader of PCNA ubiquitylation and a regulator of
UV-induced DNA damage response.";
Mol. Cell 46:625-635(2012).
[11]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH PCNA AND VCP,
AND MUTAGENESIS OF 325-GLN--PHE-332 AND 456-CYS--CYS-459.
PubMed=23042607; DOI=10.1038/nsmb.2394;
Davis E.J., Lachaud C., Appleton P., Macartney T.J., Nathke I.,
Rouse J.;
"DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA
damage.";
Nat. Struct. Mol. Biol. 19:1093-1100(2012).
[12]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DEVELOPMENTAL STAGE,
INTERACTION WITH PCNA AND VCP, AND MUTAGENESIS OF PHE-253; LEU-260;
331-TYR-PHE-332 AND 456-CYS--CYS-459.
PubMed=23042605; DOI=10.1038/nsmb.2395;
Mosbech A., Gibbs-Seymour I., Kagias K., Thorslund T., Beli P.,
Povlsen L., Nielsen S.V., Smedegaard S., Sedgwick G., Lukas C.,
Hartmann-Petersen R., Lukas J., Choudhary C., Pocock R.,
Bekker-Jensen S., Mailand N.;
"DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes
ubiquitin-dependent responses to replication blocks.";
Nat. Struct. Mol. Biol. 19:1084-1092(2012).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PCNA.
PubMed=22987070; DOI=10.1093/nar/gks850;
Juhasz S., Balogh D., Hajdu I., Burkovics P., Villamil M.A.,
Zhuang Z., Haracska L.;
"Characterization of human Spartan/C1orf124, an ubiquitin-PCNA
interacting regulator of DNA damage tolerance.";
Nucleic Acids Res. 40:10795-10808(2012).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
INVOLVEMENT IN RJALS, VARIANT RJALS CYS-117, AND CHARACTERIZATION OF
VARIANT RJALS CYS-117.
PubMed=25261934; DOI=10.1038/ng.3103;
Lessel D., Vaz B., Halder S., Lockhart P.J., Marinovic-Terzic I.,
Lopez-Mosqueda J., Philipp M., Sim J.C., Smith K.R., Oehler J.,
Cabrera E., Freire R., Pope K., Nahid A., Norris F., Leventer R.J.,
Delatycki M.B., Barbi G., von Ameln S., Hoegel J., Degoricija M.,
Fertig R., Burkhalter M.D., Hofmann K., Thiele H., Altmueller J.,
Nuernberg G., Nuernberg P., Bahlo M., Martin G.M., Aalfs C.M.,
Oshima J., Terzic J., Amor D.J., Dikic I., Ramadan K., Kubisch C.;
"Mutations in SPRTN cause early onset hepatocellular carcinoma,
genomic instability and progeroid features.";
Nat. Genet. 46:1239-1244(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-484, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-423, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-303; LYS-341; LYS-361;
LYS-376; LYS-423 AND LYS-424, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Regulator of UV-induced DNA damage response: acts as a
'reader' of ubiquitinated PCNA that enhances RAD18-mediated PCNA
ubiquitination and translesion DNA synthesis (TLS). Recruited to
sites of UV damage and interacts with ubiquitinated PCNA and
RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA.
Facilitates chromatin association of RAD18 and is required for
efficient PCNA monoubiquitination, promoting a feed-forward loop
to enhance PCNA ubiquitination and translesion DNA synthesis. Acts
as a regulator of TLS by recruiting VCP/p97 to sites of DNA
damage, possibly leading to extraction of DNA polymerase eta
(POLH) by VCP/p97 to prevent excessive translesion DNA synthesis
and limit the incidence of mutations induced by DNA damage.
{ECO:0000269|PubMed:22681887, ECO:0000269|PubMed:22894931,
ECO:0000269|PubMed:22902628, ECO:0000269|PubMed:22987070,
ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:23042607}.
-!- SUBUNIT: Interacts with PCNA (when ubiquitinated). Interacts with
RAD18. Interacts (via its SHP-box) with VCP/p97. Interacts with
KCTD13 and POLD3. {ECO:0000269|PubMed:22681887,
ECO:0000269|PubMed:22894931, ECO:0000269|PubMed:22902628,
ECO:0000269|PubMed:22987070, ECO:0000269|PubMed:23042605,
ECO:0000269|PubMed:23042607}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to sites
of UV damage via the PIP-box. Recruited to stalled replication
forks at sites of replication stress.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H040-1; Sequence=Displayed;
Name=2;
IsoId=Q9H040-2; Sequence=VSP_029891, VSP_029892;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9H040-3; Sequence=VSP_046925, VSP_029891, VSP_029892;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Predominantly expressed during S- and G2-
phases and early M-phase. It then drops, and is probably degraded
by the APC/C complex. {ECO:0000269|PubMed:23042605}.
-!- DOMAIN: The PIP-box mediates the interaction with PCNA, while the
UBZ-type zinc finger mediates binding to 'Lys-48'- and 'Lys-63'-
linked polyubiquitin (PubMed:22894931, PubMed:22681887,
PubMed:23042607, PubMed:23042605 and PubMed:22987070).
{ECO:0000269|PubMed:22681887, ECO:0000269|PubMed:23042605,
ECO:0000269|PubMed:23042607}.
-!- DISEASE: Ruijs-Aalfs syndrome (RJALS) [MIM:616200]: A syndrome
characterized by genomic instability, progeroid features, and
susceptibility toward early onset hepatocellular carcinoma.
{ECO:0000269|PubMed:25261934}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the Spartan family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB55037.1; Type=Frameshift; Positions=224; Evidence={ECO:0000305};
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EMBL; AY358611; AAQ88974.1; -; mRNA.
EMBL; AK027613; BAB55232.1; -; mRNA.
EMBL; AK027317; BAB55037.1; ALT_FRAME; mRNA.
EMBL; AL512744; CAC21670.1; -; mRNA.
EMBL; AL117352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471098; EAW69956.1; -; Genomic_DNA.
EMBL; BC015740; AAH15740.1; -; mRNA.
EMBL; BC068478; AAH68478.1; -; mRNA.
CCDS; CCDS1594.1; -. [Q9H040-1]
CCDS; CCDS31054.1; -. [Q9H040-2]
CCDS; CCDS58066.1; -. [Q9H040-3]
RefSeq; NP_001010984.1; NM_001010984.3. [Q9H040-2]
RefSeq; NP_001248391.1; NM_001261462.2. [Q9H040-3]
RefSeq; NP_114407.3; NM_032018.6. [Q9H040-1]
UniGene; Hs.554892; -.
PDB; 5IY4; X-ray; 2.94 A; B/D/F=321-336.
PDBsum; 5IY4; -.
ProteinModelPortal; Q9H040; -.
SMR; Q9H040; -.
BioGrid; 123817; 97.
IntAct; Q9H040; 4.
MINT; MINT-4719711; -.
STRING; 9606.ENSP00000295050; -.
iPTMnet; Q9H040; -.
PhosphoSitePlus; Q9H040; -.
BioMuta; SPRTN; -.
DMDM; 162416221; -.
EPD; Q9H040; -.
MaxQB; Q9H040; -.
PaxDb; Q9H040; -.
PeptideAtlas; Q9H040; -.
PRIDE; Q9H040; -.
DNASU; 83932; -.
Ensembl; ENST00000008440; ENSP00000008440; ENSG00000010072. [Q9H040-3]
Ensembl; ENST00000295050; ENSP00000295050; ENSG00000010072. [Q9H040-1]
Ensembl; ENST00000391858; ENSP00000375731; ENSG00000010072. [Q9H040-2]
GeneID; 83932; -.
KEGG; hsa:83932; -.
UCSC; uc001hur.5; human. [Q9H040-1]
CTD; 83932; -.
DisGeNET; 83932; -.
EuPathDB; HostDB:ENSG00000010072.15; -.
GeneCards; SPRTN; -.
H-InvDB; HIX0001695; -.
HGNC; HGNC:25356; SPRTN.
HPA; HPA025073; -.
MalaCards; SPRTN; -.
MIM; 616086; gene.
MIM; 616200; phenotype.
neXtProt; NX_Q9H040; -.
OpenTargets; ENSG00000010072; -.
PharmGKB; PA142672442; -.
eggNOG; KOG3931; Eukaryota.
eggNOG; ENOG410XPXU; LUCA.
GeneTree; ENSGT00390000003585; -.
HOGENOM; HOG000031496; -.
HOVERGEN; HBG101206; -.
InParanoid; Q9H040; -.
OMA; NEHLDWC; -.
OrthoDB; EOG091G02ZI; -.
PhylomeDB; Q9H040; -.
TreeFam; TF314762; -.
Reactome; R-HSA-110320; Translesion Synthesis by POLH.
GeneWiki; C1orf124; -.
GenomeRNAi; 83932; -.
PRO; PR:Q9H040; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000010072; -.
CleanEx; HS_C1orf124; -.
ExpressionAtlas; Q9H040; baseline and differential.
Genevisible; Q9H040; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:LIFEdb.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0019985; P:translesion synthesis; IDA:UniProtKB.
InterPro; IPR006640; SprT-like_domain.
InterPro; IPR006642; Znf_Rad18_put.
Pfam; PF10263; SprT-like; 1.
SMART; SM00731; SprT; 1.
SMART; SM00734; ZnF_Rad18; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromosome;
Complete proteome; Disease mutation; DNA damage; DNA repair;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 489 SprT-like domain-containing protein
Spartan.
/FTId=PRO_0000312748.
DOMAIN 45 212 SprT-like.
ZN_FING 453 476 UBZ-type.
MOTIF 253 261 SHP-box.
MOTIF 325 332 PIP-box.
COMPBIAS 444 451 Poly-Ser.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 303 303 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 341 341 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 361 361 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 376 376 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 423 423 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 424 424 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 484 484 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
VAR_SEQ 108 150 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046925.
VAR_SEQ 240 250 DKPNRGEAQLV -> GTFVYILLIFM (in isoform 2
and isoform 3).
{ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_029891.
VAR_SEQ 251 489 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_029892.
VARIANT 117 117 Y -> C (in RJALS; cells ectopically
expressing the mutant are completely
unable to restore DNA replication fork
progression; dbSNP:rs527236213).
{ECO:0000269|PubMed:25261934}.
/FTId=VAR_072708.
VARIANT 296 296 P -> L (in dbSNP:rs2437150).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_037556.
MUTAGEN 253 253 F->A: Abolishes binding to VCP/p97; when
associated with A-260.
{ECO:0000269|PubMed:23042605}.
MUTAGEN 260 260 L->A: Abolishes binding to VCP/p97; when
associated with A-253.
{ECO:0000269|PubMed:23042605}.
MUTAGEN 325 332 QNVLSNYF->ANVASNAA: Abolishes binding to
PCNA. {ECO:0000269|PubMed:23042607}.
MUTAGEN 331 332 YF->AA: Abolishes binding to PCNA.
{ECO:0000269|PubMed:22894931,
ECO:0000269|PubMed:23042605}.
MUTAGEN 456 459 CPVC->APVA: Abolishes binding to
ubiquitin. {ECO:0000269|PubMed:22681887,
ECO:0000269|PubMed:23042605,
ECO:0000269|PubMed:23042607}.
MUTAGEN 473 473 D->A: Abolishes binding to ubiquitin.
{ECO:0000269|PubMed:22894931}.
HELIX 328 330 {ECO:0000244|PDB:5IY4}.
SEQUENCE 489 AA; 55134 MW; 9CF437C057B2BA2B CRC64;
MDDDLMLALR LQEEWNLQEA ERDHAQESLS LVDASWELVD PTPDLQALFV QFNDQFFWGQ
LEAVEVKWSV RMTLCAGICS YEGKGGMCSI RLSEPLLKLR PRKDLVETLL HEMIHAYLFV
TNNDKDREGH GPEFCKHMHR INSLTGANIT VYHTFHDEVD EYRRHWWRCN GPCQHRPPYY
GYVKRATNRE PSAHDYWWAE HQKTCGGTYI KIKEPENYSK KGKGKAKLGK EPVLAAENKD
KPNRGEAQLV IPFSGKGYVL GETSNLPSPG KLITSHAINK TQDLLNQNHS ANAVRPNSKI
KVKFEQNGSS KNSHLVSPAV SNSHQNVLSN YFPRVSFANQ KAFRGVNGSP RISVTVGNIP
KNSVSSSSQR RVSSSKISLR NSSKVTESAS VMPSQDVSGS EDTFPNKRPR LEDKTVFDNF
FIKKEQIKSS GNDPKYSTTT AQNSSSSSSQ SKMVNCPVCQ NEVLESQINE HLDWCLEGDS
IKVKSEESL


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