TIM_HUMAN - dbPTM
TIM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIM_HUMAN
UniProt AC Q9UNS1
Protein Name Protein timeless homolog
Gene Name TIMELESS {ECO:0000312|EMBL:AAH50557.1}
Organism Homo sapiens (Human).
Sequence Length 1208
Subcellular Localization Nucleus .
Protein Description Plays an important role in the control of DNA replication, maintenance of replication fork stability, maintenance of genome stability throughout normal DNA replication and in the regulation of the circadian clock. Involved in the determination of period length and in the DNA damage-dependent phase advancing of the circadian clock. Negatively regulates CLOCK|NPAS2-ARTNL/BMAL1|ARTNL2/BMAL2-induced transactivation of PER1 possibly via translocation of PER1 into the nucleus. Forms a complex with TIPIN and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress. Timeless promotes TIPIN nuclear localization. Involved in cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. May also play an important role in epithelial cell morphogenesis and formation of branching tubules..
Protein Sequence MDLHMMNCELLATCSALGYLEGDTYHKEPDCLESVKDLIRYLRHEDETRDVRQQLGAAQILQSDLLPILTQHHQDKPLFDAVIRLMVNLTQPALLCFGNLPKEPSFRHHFLQVLTYLQAYKEAFASEKAFGVLSETLYELLQLGWEERQEEDNLLIERILLLVRNILHVPADLDQEKKIDDDASAHDQLLWAIHLSGLDDLLLFLASSSAEEQWSLHVLEIVSLMFRDQNPEQLAGVGQGRLAQERSADFAELEVLRQREMAEKKTRALQRGNRHSRFGGSYIVQGLKSIGERDLIFHKGLHNLRNYSSDLGKQPKKVPKRRQAARELSIQRRSALNVRLFLRDFCSEFLENCYNRLMGSVKDHLLREKAQQHDETYYMWALAFFMAFNRAASFRPGLVSETLSVRTFHFIEQNLTNYYEMMLTDRKEAASWARRMHLALKAYQELLATVNEMDISPDEAVRESSRIIKNNIFYVMEYRELFLALFRKFDERCQPRSFLRDLVETTHLFLKMLERFCRSRGNLVVQNKQKKRRKKKKKVLDQAIVSGNVPSSPEEVEAVWPALAEQLQCCAQNSELSMDSVVPFDAASEVPVEEQRAEAMVRIQDCLLAGQAPQALTLLRSAREVWPEGDVFGSQDISPEEEIQLLKQILSAPLPRQQGPEERGAEEEEEEEEEEEEELQVVQVSEKEFNFLDYLKRFACSTVVRAYVLLLRSYQQNSAHTNHCIVKMLHRLAHDLKMEALLFQLSVFCLFNRLLSDPAAGAYKELVTFAKYILGKFFALAAVNQKAFVELLFWKNTAVVREMTEGYGSLDDRSSSRRAPTWSPEEEAHLRELYLANKDVEGQDVVEAILAHLNTVPRTRKQIIHHLVQMGLADSVKDFQRKGTHIVLWTGDQELELQRLFEEFRDSDDVLGHIMKNITAKRSRARIVDKLLALGLVAERRELYKKRQKKLASSILPNGAESLKDFCQEDLEEEENLPEEDSEEEEEGGSEAEQVQGSLVLSNENLGQSLHQEGFSIPLLWLQNCLIRAADDREEDGCSQAVPLVPLTEENEEAMENEQFQQLLRKLGVRPPASGQETFWRIPAKLSPTQLRRAAASLSQPEEEQKLQPELQPKVPGEQGSDEEHCKEHRAQALRALLLAHKKKAGLASPEEEDAVGKEPLKAAPKKRQLLDSDEEQEEDEGRNRAPELGAPGIQKKKRYQIEDDEDD
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
13PhosphorylationMNCELLATCSALGYL
CCHHHHHHHHHHCCC		13.6326552605
15PhosphorylationCELLATCSALGYLEG
HHHHHHHHHHCCCCC		23.3626552605
19PhosphorylationATCSALGYLEGDTYH
HHHHHHCCCCCCCCC		11.4826552605
24PhosphorylationLGYLEGDTYHKEPDC
HCCCCCCCCCCCCCH		38.0826552605
25PhosphorylationGYLEGDTYHKEPDCL
CCCCCCCCCCCCCHH		18.6826552605
34PhosphorylationKEPDCLESVKDLIRY
CCCCHHHHHHHHHHH		22.8626552605
41PhosphorylationSVKDLIRYLRHEDET
HHHHHHHHHHCCHHH		10.90-
105PhosphorylationGNLPKEPSFRHHFLQ
CCCCCCCCHHHHHHH		35.6823898821
115PhosphorylationHHFLQVLTYLQAYKE
HHHHHHHHHHHHHHH		24.2720860994
116PhosphorylationHFLQVLTYLQAYKEA
HHHHHHHHHHHHHHH		7.8323898821
120PhosphorylationVLTYLQAYKEAFASE
HHHHHHHHHHHHHCC		9.0823898821
126PhosphorylationAYKEAFASEKAFGVL
HHHHHHHCCHHHHHH		32.9323898821
223PhosphorylationLHVLEIVSLMFRDQN
HHHHHHHHHHCCCCC		21.5624719451
246MethylationQGRLAQERSADFAEL
CCHHHHHHCCCHHHH		25.68115918481
267MethylationEMAEKKTRALQRGNR
HHHHHHHHHHHHCCC		42.0354560221
271MethylationKKTRALQRGNRHSRF
HHHHHHHHCCCCCCC		45.2454560227
281PhosphorylationRHSRFGGSYIVQGLK
CCCCCCCCHHHHCCH		16.4427134283
282PhosphorylationHSRFGGSYIVQGLKS
CCCCCCCHHHHCCHH		14.3719835603
287UbiquitinationGSYIVQGLKSIGERD
CCHHHHCCHHHCCCH		1.8921890473
287 (in isoform 2)Ubiquitination-1.8921890473
288 (in isoform 1)Ubiquitination-47.0221890473
288AcetylationSYIVQGLKSIGERDL
CHHHHCCHHHCCCHH		47.0225953088
288UbiquitinationSYIVQGLKSIGERDL
CHHHHCCHHHCCCHH		47.0222817900
289PhosphorylationYIVQGLKSIGERDLI
HHHHCCHHHCCCHHH		40.6528555341
298 (in isoform 2)Ubiquitination-19.1121890473
298UbiquitinationGERDLIFHKGLHNLR
CCCHHHCCHHHHHHH		19.1123000965
299AcetylationERDLIFHKGLHNLRN
CCHHHCCHHHHHHHH		53.0419608861
299 (in isoform 1)Ubiquitination-53.0421890473
299UbiquitinationERDLIFHKGLHNLRN
CCHHHCCHHHHHHHH		53.0423000965
305MethylationHKGLHNLRNYSSDLG
CHHHHHHHHCCCCCC		45.41115918485
308PhosphorylationLHNLRNYSSDLGKQP
HHHHHHCCCCCCCCC		22.4130576142
309PhosphorylationHNLRNYSSDLGKQPK
HHHHHCCCCCCCCCC		26.88-
312UbiquitinationRNYSSDLGKQPKKVP
HHCCCCCCCCCCCCC		31.3833845483
313AcetylationNYSSDLGKQPKKVPK
HCCCCCCCCCCCCCH		71.3925953088
313UbiquitinationNYSSDLGKQPKKVPK
HCCCCCCCCCCCCCH		71.3933845483
315UbiquitinationSSDLGKQPKKVPKRR
CCCCCCCCCCCCHHH		41.7524816145
316UbiquitinationSDLGKQPKKVPKRRQ
CCCCCCCCCCCHHHH		65.0024816145
329PhosphorylationRQAARELSIQRRSAL
HHHHHHHHHHHHHHH		16.3625999147
497PhosphorylationDERCQPRSFLRDLVE
HHHCCCHHHHHHHHH		35.0020860994
505PhosphorylationFLRDLVETTHLFLKM
HHHHHHHHHHHHHHH		16.4320860994
530UbiquitinationLVVQNKQKKRRKKKK
HHCCCHHHHHHHHHH		50.2724816145
531UbiquitinationVVQNKQKKRRKKKKK
HCCCHHHHHHHHHHH		55.7424816145
606GlutathionylationAMVRIQDCLLAGQAP
HHHHHHHHHHCCCCC		1.6022555962
634PhosphorylationPEGDVFGSQDISPEE
CCCCCCCCCCCCHHH		17.1420873877
638PhosphorylationVFGSQDISPEEEIQL
CCCCCCCCHHHHHHH		34.2520873877
687UbiquitinationQVVQVSEKEFNFLDY
HEEECCHHHHCHHHH		61.16-
702PhosphorylationLKRFACSTVVRAYVL
HHHHHHHHHHHHHHH		23.9324719451
804PhosphorylationTAVVREMTEGYGSLD
HHHHHHHHCCCCCCC		22.85-
807PhosphorylationVREMTEGYGSLDDRS
HHHHHCCCCCCCCCC		9.4122817900
809PhosphorylationEMTEGYGSLDDRSSS
HHHCCCCCCCCCCCC		21.8227499020
813MethylationGYGSLDDRSSSRRAP
CCCCCCCCCCCCCCC		37.80115918489
815PhosphorylationGSLDDRSSSRRAPTW
CCCCCCCCCCCCCCC		28.85-
816PhosphorylationSLDDRSSSRRAPTWS
CCCCCCCCCCCCCCC		27.34-
821PhosphorylationSSSRRAPTWSPEEEA
CCCCCCCCCCHHHHH		37.2726270265
823PhosphorylationSRRAPTWSPEEEAHL
CCCCCCCCHHHHHHH		25.5525159151
837UbiquitinationLRELYLANKDVEGQD
HHHHHHHCCCCCCHH		38.1629967540
838UbiquitinationRELYLANKDVEGQDV
HHHHHHCCCCCCHHH		58.5029967540
860UbiquitinationLNTVPRTRKQIIHHL
CCCCCHHHHHHHHHH		30.1129967540
861UbiquitinationNTVPRTRKQIIHHLV
CCCCHHHHHHHHHHH		45.2829967540
919PhosphorylationGHIMKNITAKRSRAR
HHHHHHHCCHHHHHH		35.2020860994
953PhosphorylationKRQKKLASSILPNGA
HHHHHHHHCCCCCCH		28.4826546556
962PhosphorylationILPNGAESLKDFCQE
CCCCCHHHHHHHHHH		39.9425850435
1074PhosphorylationLGVRPPASGQETFWR
HCCCCCCCCCCCEEE		46.9427732954
1078PhosphorylationPPASGQETFWRIPAK
CCCCCCCCEEECCCC		22.1727732954
1084UbiquitinationETFWRIPAKLSPTQL
CCEEECCCCCCHHHH		24.0533845483
1085AcetylationTFWRIPAKLSPTQLR
CEEECCCCCCHHHHH		44.1123749302
1085UbiquitinationTFWRIPAKLSPTQLR
CEEECCCCCCHHHHH		44.1133845483
1087PhosphorylationWRIPAKLSPTQLRRA
EECCCCCCHHHHHHH		25.7922167270
1089PhosphorylationIPAKLSPTQLRRAAA
CCCCCCHHHHHHHHH		36.5423927012
1097PhosphorylationQLRRAAASLSQPEEE
HHHHHHHHCCCHHHH		24.6722617229
1099PhosphorylationRRAAASLSQPEEEQK
HHHHHHCCCHHHHHH		40.9930576142
1105UbiquitinationLSQPEEEQKLQPELQ
CCCHHHHHHCCHHHC		55.8529967540
1106UbiquitinationSQPEEEQKLQPELQP
CCHHHHHHCCHHHCC		52.9829967540
1121PhosphorylationKVPGEQGSDEEHCKE
CCCCCCCCCHHHHHH		41.3623401153
1126UbiquitinationQGSDEEHCKEHRAQA
CCCCHHHHHHHHHHH		6.6429967540
1127UbiquitinationGSDEEHCKEHRAQAL
CCCHHHHHHHHHHHH		59.4729967540
1142AcetylationRALLLAHKKKAGLAS
HHHHHHHHHHCCCCC		50.8125953088
1149PhosphorylationKKKAGLASPEEEDAV
HHHCCCCCHHHHCCC		37.5819664994
1158AcetylationEEEDAVGKEPLKAAP
HHHCCCCCCCCCCCC		49.9526051181
1172PhosphorylationPKKRQLLDSDEEQEE
CCHHCCCCCHHHHHH		63.7432645325
1173PhosphorylationKKRQLLDSDEEQEED
CHHCCCCCHHHHHHH		47.0629255136
1195UbiquitinationELGAPGIQKKKRYQI
HHCCCCCCCCCCCCC		58.3824816145
1196UbiquitinationLGAPGIQKKKRYQIE
HCCCCCCCCCCCCCC		59.3424816145
1200PhosphorylationGIQKKKRYQIEDDED
CCCCCCCCCCCCCCC		23.79-
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

Oops, there are no upstream regulatory protein records of TIM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIM_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 TIM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIPIN_HUMANTIPINphysical
17296725
CRY2_HUMANCRY2physical
15798197
CHK1_HUMANCHEK1physical
15798197
ATRIP_HUMANATRIPphysical
15798197
PER1_MOUSEPer1physical
9856465
PER2_MOUSEPer2physical
9856465
PCNA_HUMANPCNAphysical
18451105
TIPIN_HUMANTIPINphysical
17102137
ZSCA1_HUMANZSCAN1physical
20211142
XRCC1_HUMANXRCC1physical
22939629
STPAP_HUMANTUT1physical
22863883
NASP_HUMANNASPphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TIM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149 AND SER-1173, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1089, AND MASSSPECTROMETRY.

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