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Protein

SprT-like domain-containing protein Spartan

Gene

SPRTN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri453 – 47624UBZ-typeAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: InterPro
  • K63-linked polyubiquitin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: Reactome
  • error-free translesion synthesis Source: Reactome
  • positive regulation of protein ubiquitination Source: UniProtKB
  • response to UV Source: UniProtKB
  • translesion synthesis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-110320. Translesion Synthesis by POLH.

Names & Taxonomyi

Protein namesi
Recommended name:
SprT-like domain-containing protein Spartan
Alternative name(s):
DNA damage protein targeting VCP
Short name:
DVC1
Protein with SprT-like domain at the N terminus
Short name:
Spartan
Gene namesi
Name:SPRTN
Synonyms:C1orf124, DVC1
ORF Names:UNQ1880/PRO4323
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25356. SPRTN.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Localizes to sites of UV damage via the PIP-box. Recruited to stalled relication forks at sites of replication stress.

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • nuclear speck Source: LIFEdb
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Ruijs-Aalfs syndrome (RJALS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by genomic instability, progeroid features, and susceptibility toward early onset hepatocellular carcinoma.
See also OMIM:616200
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti117 – 1171Y → C in RJALS; cells ectopically expressing the mutant are completely unable to restore DNA replication fork progression. 1 Publication
VAR_072708

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi253 – 2531F → A: Abolishes binding to VCP/p97; when associated with A-260. 1 Publication
Mutagenesisi260 – 2601L → A: Abolishes binding to VCP/p97; when associated with A-253. 1 Publication
Mutagenesisi325 – 3328QNVLSNYF → ANVASNAA: Abolishes binding to PCNA. 1 Publication
Mutagenesisi331 – 3322YF → AA: Abolishes binding to PCNA. 2 Publications
Mutagenesisi456 – 4594CPVC → APVA: Abolishes binding to ubiquitin. 3 Publications
Mutagenesisi473 – 4731D → A: Abolishes binding to ubiquitin. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiSPRTN.
MIMi616200. phenotype.
PharmGKBiPA142672442.

Polymorphism and mutation databases

BioMutaiSPRTN.
DMDMi162416221.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489SprT-like domain-containing protein SpartanPRO_0000312748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Cross-linki423 – 423Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki484 – 484Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9H040.
PaxDbiQ9H040.
PRIDEiQ9H040.

PTM databases

iPTMnetiQ9H040.
PhosphoSiteiQ9H040.

Expressioni

Developmental stagei

Predominantly expressed during S- and G2-phases and early M-phase. It then drops, and is probably degraded by the APC/C complex.1 Publication

Gene expression databases

BgeeiQ9H040.
CleanExiHS_C1orf124.
ExpressionAtlasiQ9H040. baseline and differential.
GenevisibleiQ9H040. HS.

Organism-specific databases

HPAiHPA025073.

Interactioni

Subunit structurei

Interacts with PCNA (when ubiquitinated). Interacts with RAD18. Interacts (via its SHP-box) with VCP/p97. Interacts with KCTD13 and POLD3.6 Publications

GO - Molecular functioni

  • K63-linked polyubiquitin binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123817. 95 interactions.
IntActiQ9H040. 4 interactions.
MINTiMINT-4719711.
STRINGi9606.ENSP00000295050.

Structurei

3D structure databases

ProteinModelPortaliQ9H040.
SMRiQ9H040. Positions 449-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 212168SprT-likeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi253 – 2619SHP-box
Motifi325 – 3328PIP-box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi444 – 4518Poly-Ser

Domaini

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).3 Publications

Sequence similaritiesi

Belongs to the Spartan family.Curated
Contains 1 SprT-like domain.Curated
Contains 1 UBZ-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri453 – 47624UBZ-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3931. Eukaryota.
ENOG410XPXU. LUCA.
GeneTreeiENSGT00390000003585.
HOGENOMiHOG000031496.
HOVERGENiHBG101206.
InParanoidiQ9H040.
OMAiNEHLDWC.
OrthoDBiEOG7TMZS3.
PhylomeDBiQ9H040.
TreeFamiTF314762.

Family and domain databases

InterProiIPR006640. SprT-like_domain.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamiPF10263. SprT-like. 1 hit.
[Graphical view]
SMARTiSM00731. SprT. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H040-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDDDLMLALR LQEEWNLQEA ERDHAQESLS LVDASWELVD PTPDLQALFV
60 70 80 90 100
QFNDQFFWGQ LEAVEVKWSV RMTLCAGICS YEGKGGMCSI RLSEPLLKLR
110 120 130 140 150
PRKDLVETLL HEMIHAYLFV TNNDKDREGH GPEFCKHMHR INSLTGANIT
160 170 180 190 200
VYHTFHDEVD EYRRHWWRCN GPCQHRPPYY GYVKRATNRE PSAHDYWWAE
210 220 230 240 250
HQKTCGGTYI KIKEPENYSK KGKGKAKLGK EPVLAAENKD KPNRGEAQLV
260 270 280 290 300
IPFSGKGYVL GETSNLPSPG KLITSHAINK TQDLLNQNHS ANAVRPNSKI
310 320 330 340 350
KVKFEQNGSS KNSHLVSPAV SNSHQNVLSN YFPRVSFANQ KAFRGVNGSP
360 370 380 390 400
RISVTVGNIP KNSVSSSSQR RVSSSKISLR NSSKVTESAS VMPSQDVSGS
410 420 430 440 450
EDTFPNKRPR LEDKTVFDNF FIKKEQIKSS GNDPKYSTTT AQNSSSSSSQ
460 470 480
SKMVNCPVCQ NEVLESQINE HLDWCLEGDS IKVKSEESL
Length:489
Mass (Da):55,134
Last modified:December 4, 2007 - v2
Checksum:i9CF437C057B2BA2B
GO
Isoform 2 (identifier: Q9H040-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     240-250: DKPNRGEAQLV → GTFVYILLIFM
     251-489: Missing.

Note: No experimental confirmation available.
Show »
Length:250
Mass (Da):29,191
Checksum:iF06A426627CF2473
GO
Isoform 3 (identifier: Q9H040-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     108-150: Missing.
     240-250: DKPNRGEAQLV → GTFVYILLIFM
     251-489: Missing.

Note: No experimental confirmation available.
Show »
Length:207
Mass (Da):24,247
Checksum:i18733A05FD49D4B1
GO

Sequence cautioni

The sequence BAB55037.1 differs from that shown. Reason: Frameshift at position 224. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti117 – 1171Y → C in RJALS; cells ectopically expressing the mutant are completely unable to restore DNA replication fork progression. 1 Publication
VAR_072708
Natural varianti296 – 2961P → L.3 Publications
Corresponds to variant rs2437150 [ dbSNP | Ensembl ].
VAR_037556

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei108 – 15043Missing in isoform 3. 1 PublicationVSP_046925Add
BLAST
Alternative sequencei240 – 25011DKPNRGEAQLV → GTFVYILLIFM in isoform 2 and isoform 3. 3 PublicationsVSP_029891Add
BLAST
Alternative sequencei251 – 489239Missing in isoform 2 and isoform 3. 3 PublicationsVSP_029892Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358611 mRNA. Translation: AAQ88974.1.
AK027613 mRNA. Translation: BAB55232.1.
AK027317 mRNA. Translation: BAB55037.1. Frameshift.
AL512744 mRNA. Translation: CAC21670.1.
AL117352 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW69956.1.
BC015740 mRNA. Translation: AAH15740.1.
BC068478 mRNA. Translation: AAH68478.1.
CCDSiCCDS1594.1. [Q9H040-1]
CCDS31054.1. [Q9H040-2]
CCDS58066.1. [Q9H040-3]
RefSeqiNP_001010984.1. NM_001010984.3. [Q9H040-2]
NP_001248391.1. NM_001261462.2. [Q9H040-3]
NP_114407.3. NM_032018.6. [Q9H040-1]
UniGeneiHs.554892.

Genome annotation databases

EnsembliENST00000008440; ENSP00000008440; ENSG00000010072. [Q9H040-3]
ENST00000295050; ENSP00000295050; ENSG00000010072. [Q9H040-1]
ENST00000391858; ENSP00000375731; ENSG00000010072. [Q9H040-2]
GeneIDi83932.
KEGGihsa:83932.
UCSCiuc001hur.5. human. [Q9H040-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358611 mRNA. Translation: AAQ88974.1.
AK027613 mRNA. Translation: BAB55232.1.
AK027317 mRNA. Translation: BAB55037.1. Frameshift.
AL512744 mRNA. Translation: CAC21670.1.
AL117352 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW69956.1.
BC015740 mRNA. Translation: AAH15740.1.
BC068478 mRNA. Translation: AAH68478.1.
CCDSiCCDS1594.1. [Q9H040-1]
CCDS31054.1. [Q9H040-2]
CCDS58066.1. [Q9H040-3]
RefSeqiNP_001010984.1. NM_001010984.3. [Q9H040-2]
NP_001248391.1. NM_001261462.2. [Q9H040-3]
NP_114407.3. NM_032018.6. [Q9H040-1]
UniGeneiHs.554892.

3D structure databases

ProteinModelPortaliQ9H040.
SMRiQ9H040. Positions 449-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123817. 95 interactions.
IntActiQ9H040. 4 interactions.
MINTiMINT-4719711.
STRINGi9606.ENSP00000295050.

PTM databases

iPTMnetiQ9H040.
PhosphoSiteiQ9H040.

Polymorphism and mutation databases

BioMutaiSPRTN.
DMDMi162416221.

Proteomic databases

MaxQBiQ9H040.
PaxDbiQ9H040.
PRIDEiQ9H040.

Protocols and materials databases

DNASUi83932.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000008440; ENSP00000008440; ENSG00000010072. [Q9H040-3]
ENST00000295050; ENSP00000295050; ENSG00000010072. [Q9H040-1]
ENST00000391858; ENSP00000375731; ENSG00000010072. [Q9H040-2]
GeneIDi83932.
KEGGihsa:83932.
UCSCiuc001hur.5. human. [Q9H040-1]

Organism-specific databases

CTDi83932.
GeneCardsiSPRTN.
H-InvDBHIX0001695.
HGNCiHGNC:25356. SPRTN.
HPAiHPA025073.
MalaCardsiSPRTN.
MIMi616086. gene.
616200. phenotype.
neXtProtiNX_Q9H040.
PharmGKBiPA142672442.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3931. Eukaryota.
ENOG410XPXU. LUCA.
GeneTreeiENSGT00390000003585.
HOGENOMiHOG000031496.
HOVERGENiHBG101206.
InParanoidiQ9H040.
OMAiNEHLDWC.
OrthoDBiEOG7TMZS3.
PhylomeDBiQ9H040.
TreeFamiTF314762.

Enzyme and pathway databases

ReactomeiR-HSA-110320. Translesion Synthesis by POLH.

Miscellaneous databases

GeneWikiiC1orf124.
GenomeRNAii83932.
NextBioi73047.
PROiQ9H040.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H040.
CleanExiHS_C1orf124.
ExpressionAtlasiQ9H040. baseline and differential.
GenevisibleiQ9H040. HS.

Family and domain databases

InterProiIPR006640. SprT-like_domain.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamiPF10263. SprT-like. 1 hit.
[Graphical view]
SMARTiSM00731. SprT. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT LEU-296.
    Tissue: Embryo and Teratocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-296.
    Tissue: Brain.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-243 (ISOFORM 2), VARIANT LEU-296.
    Tissue: Colon and Testis.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Spartan/C1orf124 is important to prevent UV-induced mutagenesis."
    Machida Y., Kim M.S., Machida Y.J.
    Cell Cycle 11:3395-3402(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA, MUTAGENESIS OF ASP-473 AND 331-TYR-PHE-332.
  9. "Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a regulator of translesion synthesis."
    Ghosal G., Leung J.W., Nair B.C., Fong K.W., Chen J.
    J. Biol. Chem. 287:34225-34233(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCTD13; PCNA; POLD3 AND VCP.
  10. "Spartan/C1orf124, a reader of PCNA ubiquitylation and a regulator of UV-induced DNA damage response."
    Centore R.C., Yazinski S.A., Tse A., Zou L.
    Mol. Cell 46:625-635(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH PCNA AND RAD18, MUTAGENESIS OF 456-CYS--CYS-459.
  11. "DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA damage."
    Davis E.J., Lachaud C., Appleton P., Macartney T.J., Nathke I., Rouse J.
    Nat. Struct. Mol. Biol. 19:1093-1100(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH PCNA AND VCP, MUTAGENESIS OF 325-GLN--PHE-332 AND 456-CYS--CYS-459.
  12. Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DEVELOPMENTAL STAGE, INTERACTION WITH PCNA AND VCP, MUTAGENESIS OF PHE-253; LEU-260; 331-TYR-PHE-332 AND 456-CYS--CYS-459.
  13. "Characterization of human Spartan/C1orf124, an ubiquitin-PCNA interacting regulator of DNA damage tolerance."
    Juhasz S., Balogh D., Hajdu I., Burkovics P., Villamil M.A., Zhuang Z., Haracska L.
    Nucleic Acids Res. 40:10795-10808(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA.
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: INVOLVEMENT IN RJALS, VARIANT RJALS CYS-117, CHARACTERIZATION OF VARIANT RJALS CYS-117.
  16. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPRTN_HUMAN
AccessioniPrimary (citable) accession number: Q9H040
Secondary accession number(s): B1AKT0
, B5MEF7, Q5TE78, Q6UWW6, Q96BC5, Q96KA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: April 13, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.