SPRTN_HUMAN - dbPTM
SPRTN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPRTN_HUMAN
UniProt AC Q9H040
Protein Name SprT-like domain-containing protein Spartan
Gene Name SPRTN
Organism Homo sapiens (Human).
Sequence Length 489
Subcellular Localization Nucleus. Chromosome. Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress.
Protein 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..
Protein Sequence MDDDLMLALRLQEEWNLQEAERDHAQESLSLVDASWELVDPTPDLQALFVQFNDQFFWGQLEAVEVKWSVRMTLCAGICSYEGKGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINSLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHRPPYYGYVKRATNREPSAHDYWWAEHQKTCGGTYIKIKEPENYSKKGKGKAKLGKEPVLAAENKDKPNRGEAQLVIPFSGKGYVLGETSNLPSPGKLITSHAINKTQDLLNQNHSANAVRPNSKIKVKFEQNGSSKNSHLVSPAVSNSHQNVLSNYFPRVSFANQKAFRGVNGSPRISVTVGNIPKNSVSSSSQRRVSSSKISLRNSSKVTESASVMPSQDVSGSEDTFPNKRPRLEDKTVFDNFFIKKEQIKSSGNDPKYSTTTAQNSSSSSSQSKMVNCPVCQNEVLESQINEHLDWCLEGDSIKVKSEESL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MDDDLMLA
-------CCHHHHHH
22814378
73PhosphorylationVKWSVRMTLCAGICS
CCCHHEEEEEEECCC
-
80PhosphorylationTLCAGICSYEGKGGM
EEEEECCCCCCCCCE
-
84UbiquitinationGICSYEGKGGMCSIR
ECCCCCCCCCEEEEE
-
98UbiquitinationRLSEPLLKLRPRKDL
EECCCHHHCCCCHHH
21890473
98UbiquitinationRLSEPLLKLRPRKDL
EECCCHHHCCCCHHH
21890473
98UbiquitinationRLSEPLLKLRPRKDL
EECCCHHHCCCCHHH
21890473
98 (in isoform 1)Ubiquitination-21890473
98 (in isoform 2)Ubiquitination-21890473
136UbiquitinationGHGPEFCKHMHRINS
CCCHHHHHHHHHHHH
-
145PhosphorylationMHRINSLTGANITVY
HHHHHHCCCCEEEEE
-
154PhosphorylationANITVYHTFHDEVDE
CEEEEEEECCHHHHH
-
179PhosphorylationPCQHRPPYYGYVKRA
CCCCCCCCCCEEEEC
24043423
180PhosphorylationCQHRPPYYGYVKRAT
CCCCCCCCCEEEECC
24043423
182PhosphorylationHRPPYYGYVKRATNR
CCCCCCCEEEECCCC
24043423
184UbiquitinationPPYYGYVKRATNREP
CCCCCEEEECCCCCC
-
203UbiquitinationYWWAEHQKTCGGTYI
CHHHHCCCCCCCEEE
-
211UbiquitinationTCGGTYIKIKEPENY
CCCCEEEEECCCCCC
-
213SumoylationGGTYIKIKEPENYSK
CCEEEEECCCCCCCC
-
213SumoylationGGTYIKIKEPENYSK
CCEEEEECCCCCCCC
-
213UbiquitinationGGTYIKIKEPENYSK
CCEEEEECCCCCCCC
-
220UbiquitinationKEPENYSKKGKGKAK
CCCCCCCCCCCCCCC
21906983
220 (in isoform 1)Ubiquitination-21890473
220 (in isoform 2)Ubiquitination-21890473
221UbiquitinationEPENYSKKGKGKAKL
CCCCCCCCCCCCCCC
-
227UbiquitinationKKGKGKAKLGKEPVL
CCCCCCCCCCCCCEE
-
230SumoylationKGKAKLGKEPVLAAE
CCCCCCCCCCEEEEC
-
230UbiquitinationKGKAKLGKEPVLAAE
CCCCCCCCCCEEEEC
21906983
230SumoylationKGKAKLGKEPVLAAE
CCCCCCCCCCEEEEC
-
230 (in isoform 2)Ubiquitination-21890473
230AcetylationKGKAKLGKEPVLAAE
CCCCCCCCCCEEEEC
32649882
230 (in isoform 1)Ubiquitination-21890473
241SumoylationLAAENKDKPNRGEAQ
EEECCCCCCCCCCCE
-
241SumoylationLAAENKDKPNRGEAQ
EEECCCCCCCCCCCE
-
256UbiquitinationLVIPFSGKGYVLGET
EEEECCCCCEEEECC
-
263PhosphorylationKGYVLGETSNLPSPG
CCEEEECCCCCCCCC
29978859
264PhosphorylationGYVLGETSNLPSPGK
CEEEECCCCCCCCCC
22167270
268PhosphorylationGETSNLPSPGKLITS
ECCCCCCCCCCEEHH
22167270
271UbiquitinationSNLPSPGKLITSHAI
CCCCCCCCEEHHHHH
21890473
271AcetylationSNLPSPGKLITSHAI
CCCCCCCCEEHHHHH
25953088
271 (in isoform 1)Ubiquitination-21890473
280UbiquitinationITSHAINKTQDLLNQ
EHHHHHHHHHHHHHC
-
290PhosphorylationDLLNQNHSANAVRPN
HHHHCCCCCCCCCCC
28555341
298PhosphorylationANAVRPNSKIKVKFE
CCCCCCCCCEEEEEE
28555341
303SumoylationPNSKIKVKFEQNGSS
CCCCEEEEEEECCCC
-
303SumoylationPNSKIKVKFEQNGSS
CCCCEEEEEEECCCC
28112733
317PhosphorylationSKNSHLVSPAVSNSH
CCCCEEECCCCCCCC
28555341
341SumoylationRVSFANQKAFRGVNG
CHHCCCCHHHCCCCC
-
341UbiquitinationRVSFANQKAFRGVNG
CHHCCCCHHHCCCCC
21890473
341SumoylationRVSFANQKAFRGVNG
CHHCCCCHHHCCCCC
28112733
341 (in isoform 1)Ubiquitination-21890473
349PhosphorylationAFRGVNGSPRISVTV
HHCCCCCCCCEEEEE
29978859
353PhosphorylationVNGSPRISVTVGNIP
CCCCCCEEEEECCCC
29978859
355PhosphorylationGSPRISVTVGNIPKN
CCCCEEEEECCCCCC
29978859
361SumoylationVTVGNIPKNSVSSSS
EEECCCCCCCCCCHH
-
361UbiquitinationVTVGNIPKNSVSSSS
EEECCCCCCCCCCHH
21890473
361SumoylationVTVGNIPKNSVSSSS
EEECCCCCCCCCCHH
28112733
361 (in isoform 1)Ubiquitination-21890473
363PhosphorylationVGNIPKNSVSSSSQR
ECCCCCCCCCCHHCC
29978859
365PhosphorylationNIPKNSVSSSSQRRV
CCCCCCCCCHHCCCC
29052541
366PhosphorylationIPKNSVSSSSQRRVS
CCCCCCCCHHCCCCC
29978859
367PhosphorylationPKNSVSSSSQRRVSS
CCCCCCCHHCCCCCC
29978859
368PhosphorylationKNSVSSSSQRRVSSS
CCCCCCHHCCCCCCC
29978859
373PhosphorylationSSSQRRVSSSKISLR
CHHCCCCCCCCEECC
31316063
374PhosphorylationSSQRRVSSSKISLRN
HHCCCCCCCCEECCC
31316063
375PhosphorylationSQRRVSSSKISLRNS
HCCCCCCCCEECCCC
21712546
376UbiquitinationQRRVSSSKISLRNSS
CCCCCCCCEECCCCC
-
376SumoylationQRRVSSSKISLRNSS
CCCCCCCCEECCCCC
28112733
382PhosphorylationSKISLRNSSKVTESA
CCEECCCCCCCCCCE
-
383PhosphorylationKISLRNSSKVTESAS
CEECCCCCCCCCCEE
31316063
384UbiquitinationISLRNSSKVTESASV
EECCCCCCCCCCEEE
21906983
384 (in isoform 1)Ubiquitination-21890473
386PhosphorylationLRNSSKVTESASVMP
CCCCCCCCCCEEECC
-
398PhosphorylationVMPSQDVSGSEDTFP
ECCCCCCCCCCCCCC
28555341
407UbiquitinationSEDTFPNKRPRLEDK
CCCCCCCCCCCCCCC
21890473
407 (in isoform 1)Ubiquitination-21890473
414UbiquitinationKRPRLEDKTVFDNFF
CCCCCCCCCEECCEE
21890473
414 (in isoform 1)Ubiquitination-21890473
423SumoylationVFDNFFIKKEQIKSS
EECCEEEEHHHHHCC
-
423UbiquitinationVFDNFFIKKEQIKSS
EECCEEEEHHHHHCC
21890473
423SumoylationVFDNFFIKKEQIKSS
EECCEEEEHHHHHCC
28112733
423 (in isoform 1)Ubiquitination-21890473
424UbiquitinationFDNFFIKKEQIKSSG
ECCEEEEHHHHHCCC
-
424SumoylationFDNFFIKKEQIKSSG
ECCEEEEHHHHHCCC
28112733
428SumoylationFIKKEQIKSSGNDPK
EEEHHHHHCCCCCCC
-
428UbiquitinationFIKKEQIKSSGNDPK
EEEHHHHHCCCCCCC
21906983
428SumoylationFIKKEQIKSSGNDPK
EEEHHHHHCCCCCCC
-
428 (in isoform 1)Ubiquitination-21890473
435SumoylationKSSGNDPKYSTTTAQ
HCCCCCCCCCCCCCC
-
435UbiquitinationKSSGNDPKYSTTTAQ
HCCCCCCCCCCCCCC
2190698
435SumoylationKSSGNDPKYSTTTAQ
HCCCCCCCCCCCCCC
-
435 (in isoform 1)Ubiquitination-21890473
436PhosphorylationSSGNDPKYSTTTAQN
CCCCCCCCCCCCCCC
29496907
437PhosphorylationSGNDPKYSTTTAQNS
CCCCCCCCCCCCCCC
-
444PhosphorylationSTTTAQNSSSSSSQS
CCCCCCCCCCCCCCC
-
446PhosphorylationTTAQNSSSSSSQSKM
CCCCCCCCCCCCCEE
28985074
451PhosphorylationSSSSSSQSKMVNCPV
CCCCCCCCEECCCHH
-
484SumoylationEGDSIKVKSEESL--
CCCEEEECCCCCC--
-
484UbiquitinationEGDSIKVKSEESL--
CCCEEEECCCCCC--
-
484SumoylationEGDSIKVKSEESL--
CCCEEEECCCCCC--
25218447
484 (in isoform 1)Ubiquitination-21890473

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
373SPhosphorylationKinaseCHEK1O14757
Uniprot
374SPhosphorylationKinaseCHEK1O14757
Uniprot
383SPhosphorylationKinaseCHEK1O14757
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPRTN_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SPRTN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_HUMANPCNAphysical
22681887
RAD18_HUMANRAD18physical
22681887
PCNA_HUMANPCNAphysical
22902628
VCIP1_HUMANVCPIP1physical
22902628
TERA_HUMANVCPphysical
22902628
UBXN1_HUMANUBXN1physical
22902628
DPOD3_HUMANPOLD3physical
22902628
BACD1_HUMANKCTD13physical
22902628
HLTF_HUMANHLTFphysical
22902628
CAND1_HUMANCAND1physical
22902628
RAD18_HUMANRAD18physical
22902628
SLX4_HUMANSLX4physical
22902628
POLH_HUMANPOLHphysical
22902628
UBC_HUMANUBCphysical
22894931
PCNA_HUMANPCNAphysical
22894931
TERA_HUMANVCPphysical
23042607
PCNA_HUMANPCNAphysical
23042607
UFD1_HUMANUFD1Lphysical
23042607
NSF1C_HUMANNSFL1Cphysical
23042607
NPL4_HUMANNPLOC4physical
23042607
PCNA_HUMANPCNAphysical
22987070
UBC_HUMANUBCphysical
23042605
PCNA_HUMANPCNAphysical
23042605
MLH1_HUMANMLH1physical
23042605
TERA_HUMANVCPphysical
23042605
LACTB_HUMANLACTBphysical
23042605
SSBP_HUMANSSBP1physical
23042605
HSP7C_HUMANHSPA8physical
23042605
TBB6_HUMANTUBB6physical
23042605
AGM1_HUMANPGM3physical
23042605
DNJA2_HUMANDNAJA2physical
23042605
TBB4B_HUMANTUBB4Bphysical
23042605
ATX3_HUMANATXN3physical
23042605
CLIC4_HUMANCLIC4physical
23042605
PMS2_HUMANPMS2physical
23042605
FZR1_HUMANFZR1physical
23042605
DPOD1_HUMANPOLD1physical
23254330
DPOD2_HUMANPOLD2physical
23254330
DPOD3_HUMANPOLD3physical
23254330
DPOD4_HUMANPOLD4physical
23254330
ATPA_HUMANATP5A1physical
23254330
TIF1B_HUMANTRIM28physical
23254330
DYHC1_HUMANDYNC1H1physical
23254330
YBOX1_HUMANYBX1physical
23254330
RCN2_HUMANRCN2physical
23254330
HUWE1_HUMANHUWE1physical
23254330
MAGD2_HUMANMAGED2physical
23254330
F120A_HUMANFAM120Aphysical
23254330
AKA12_HUMANAKAP12physical
23254330
ANXA2_HUMANANXA2physical
23254330
VIME_HUMANVIMphysical
23254330
STAU1_HUMANSTAU1physical
23254330
PSMD3_HUMANPSMD3physical
23254330
PRS7_HUMANPSMC2physical
23254330
LAP2A_HUMANTMPOphysical
23254330
LAP2B_HUMANTMPOphysical
23254330
PHB_HUMANPHBphysical
23254330
DNJC7_HUMANDNAJC7physical
23254330
DDX17_HUMANDDX17physical
23254330
GRP75_HUMANHSPA9physical
23254330
AT1A1_HUMANATP1A1physical
23254330
AT2A2_HUMANATP2A2physical
23254330
ZCCHV_HUMANZC3HAV1physical
23254330
UBB_HUMANUBBphysical
23254330
PYR1_HUMANCADphysical
23254330
ATPB_HUMANATP5Bphysical
23254330
H1X_HUMANH1FXphysical
23254330
H2B1K_HUMANHIST1H2BKphysical
23254330
H2B1N_HUMANHIST1H2BNphysical
23254330
H2B1H_HUMANHIST1H2BHphysical
23254330
H2B1L_HUMANHIST1H2BLphysical
23254330
H2B1M_HUMANHIST1H2BMphysical
23254330
H2B2F_HUMANHIST2H2BFphysical
23254330
H2B1D_HUMANHIST1H2BDphysical
23254330
H2B1C_HUMANHIST1H2BDphysical
23254330
VDAC1_HUMANVDAC1physical
23254330
SRSF1_HUMANSRSF1physical
23254330
SRSF5_HUMANSRSF5physical
23254330
HNRDL_HUMANHNRNPDLphysical
23254330
PSMD4_HUMANPSMD4physical
23254330
RBM39_HUMANRBM39physical
23254330
HNRPQ_HUMANSYNCRIPphysical
23254330
STRAP_HUMANSTRAPphysical
23254330
DDX5_HUMANDDX5physical
23254330
SYDC_HUMANDARSphysical
23254330
LMNB1_HUMANLMNB1physical
23254330
CTBP2_HUMANCTBP2physical
23254330
CKAP4_HUMANCKAP4physical
23254330
LPPRC_HUMANLRPPRCphysical
23254330
RFC1_HUMANRFC1physical
23254330
UBR5_HUMANUBR5physical
23254330
EFTU_HUMANTUFMphysical
23254330
UBC_HUMANUBCphysical
22681887
UBC_HUMANUBCphysical
23042607
BRAP_HUMANBRAPphysical
26496610
BCL7C_HUMANBCL7Cphysical
26496610
RGPA2_HUMANRALGAPA2physical
26496610
T2FA_HUMANGTF2F1physical
28514442
IF4E2_HUMANEIF4E2physical
28514442
SNAG_HUMANNAPGphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616200Ruijs-Aalfs syndrome (RJALS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPRTN_HUMAN

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Related Literatures of Post-Translational Modification

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