CPLM-021198

Genbank Nucleotide ID

SprT-like domain-containing protein Spartan

Protein Synonyms/Alias

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

C1orf124; DVC1; UNQ1880/PRO4323

Homo sapiens (Human)

Position	Peptide	Type	References
84	GICSYEGKGGMCSIR	ubiquitination	[1, 2]
98	RLSEPLLKLRPRKDL	ubiquitination	[2, 3, 4, 5, 6]
136	GHGPEFCKHMHRINS	ubiquitination	[2]
184	PPYYGYVKRATNREP	ubiquitination	[2]
203	YWWAEHQKTCGGTYI	ubiquitination	[2]
211	TCGGTYIKIKEPENY	ubiquitination	[2]
213	GGTYIKIKEPENYSK	ubiquitination	[2]
220	KEPENYSKKGKGKAK	ubiquitination	[4]
221	EPENYSKKGKGKAKL	ubiquitination	[2]
230	KGKAKLGKEPVLAAE	ubiquitination	[2, 4]
256	LVIPFSGKGYVLGET	ubiquitination	[4]
271	SNLPSPGKLITSHAI	ubiquitination	[2, 3, 5]
280	ITSHAINKTQDLLNQ	ubiquitination	[2, 6, 7]
341	RVSFANQKAFRGVNG	ubiquitination	[1, 2, 3, 5, 7, 8]
361	VTVGNIPKNSVSSSS	ubiquitination	[1, 2, 3, 4, 5, 6, 8, 9]
376	QRRVSSSKISLRNSS	ubiquitination	[2]
384	ISLRNSSKVTESASV	ubiquitination	[4, 7, 9]
407	SEDTFPNKRPRLEDK	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
414	KRPRLEDKTVFDNFF	ubiquitination	[1, 2, 3, 4, 5, 6, 8, 9]
423	VFDNFFIKKEQIKSS	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9]
424	FDNFFIKKEQIKSSG	ubiquitination	[2, 6]
428	FIKKEQIKSSGNDPK	ubiquitination	[2, 4, 9]
435	KSSGNDPKYSTTTAQ	ubiquitination	[1, 2, 4, 6, 8, 9]
484	EGDSIKVKSEESL**	ubiquitination	[2, 4]

[1] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]

Functional Description

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.

DOMAIN 45 212 SprT-like.
ZN_FING 453 476 UBZ-type.
MOTIF 253 261 SHP-box.
MOTIF 325 332 PIP-box.

Alternative splicing; Chromosome; Complete proteome; DNA damage; DNA repair; Metal-binding; Nucleus; Polymorphism; Reference proteome; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO:0016607; C:nuclear speck; IDA:LIFEdb.
GO:0003677; F:DNA binding; IEA:InterPro.
GO:0070530; F:K63-linked polyubiquitin binding; IDA:UniProtKB.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO:0009411; P:response to UV; IDA:UniProtKB.
GO:0019985; P:translesion synthesis; IDA:UniProtKB.

IPR006640; SprT-like_domain.
IPR006642; Znf_Rad18_put.

SM00731; SprT
SM00734; ZnF_Rad18

PS00142; ZINC_PROTEASE