DPOLL_HUMAN - dbPTM
DPOLL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOLL_HUMAN
UniProt AC Q9UGP5
Protein Name DNA polymerase lambda {ECO:0000305}
Gene Name POLL {ECO:0000312|HGNC:HGNC:9184}
Organism Homo sapiens (Human).
Sequence Length 575
Subcellular Localization Nucleus .
Protein Description DNA polymerase that functions in several pathways of DNA repair. [PubMed: 11457865]
Protein Sequence MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQKAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWVCAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLPGPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNTHGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
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
23UbiquitinationIHADASSKVLAKIPR
CCCCCCCHHHHCCCC		38.48-
27UbiquitinationASSKVLAKIPRREEG
CCCHHHHCCCCHHCC		49.43-
42PhosphorylationEEAEEWLSSLRAHVV
HHHHHHHHHHHHHHH		28.5330301811
43PhosphorylationEAEEWLSSLRAHVVR
HHHHHHHHHHHHHHH		21.5025954137
51PhosphorylationLRAHVVRTGIGRARA
HHHHHHHHCCHHHHH		22.8828555341
152PhosphorylationSKAEQDASIPPGTHE
CHHHCCCCCCCCCHH		43.8727080861
157PhosphorylationDASIPPGTHEALLQT
CCCCCCCCHHHHHHH		23.4727080861
164PhosphorylationTHEALLQTALSPPPP
CHHHHHHHHCCCCCC		29.5427080861
167PhosphorylationALLQTALSPPPPPTR
HHHHHHCCCCCCCCC		32.6630108239
173PhosphorylationLSPPPPPTRPVSPPQ
CCCCCCCCCCCCCCH		54.0723401153
177PhosphorylationPPPTRPVSPPQKAKE
CCCCCCCCCCHHHCC		33.2825159151
204PhosphorylationEASDGEETQVSAADL
CCCCCCCEECCHHHH		29.93-
230PhosphorylationLEGDCEPSPAPAVLD
CCCCCCCCCCCCHHC		16.0522817900
246PhosphorylationWVCAQPSSQKATNHN
EEECCCCCCCCCCCC		42.2417525332
248UbiquitinationCAQPSSQKATNHNLH
ECCCCCCCCCCCCCC		60.16-
273UbiquitinationAYSVQGDKWRALGYA
HHHCCCHHHHHHHHH		45.46-
294PhosphorylationKSFHKPVTSYQEACS
HHCCCCCCCHHHHHC		30.1829888752
295PhosphorylationSFHKPVTSYQEACSI
HCCCCCCCHHHHHCC		25.6729888752
296PhosphorylationFHKPVTSYQEACSIP
CCCCCCCHHHHHCCC		10.8729888752
301PhosphorylationTSYQEACSIPGIGKR
CCHHHHHCCCCHHHH		38.5829888752
359PhosphorylationWYQQGFRSLEDIRSQ
HHHHCCCCHHHHHHH		33.5721815630
380PhosphorylationQAIGLKHYSDFLERM
HHHCHHHHHHHHHHC		14.35-
381PhosphorylationAIGLKHYSDFLERMP
HHCHHHHHHHHHHCC		22.9328188228
398PhosphorylationEATEIEQTVQKAAQA
HHHHHHHHHHHHHHH		16.4723403867
526PhosphorylationLAKTKGMSLSEHALS
HHHHCCCCCCHHHHH		37.0922210691
528PhosphorylationKTKGMSLSEHALSTA
HHCCCCCCHHHHHHH		21.7422210691
553PhosphorylationGPGRVLPTPTEKDVF
CCCCCCCCCCHHHHH		38.3922817900
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
167SPhosphorylationKinaseCDK2P24941
PSP
177SPhosphorylationKinaseCDK2P24941
PSP
204TPhosphorylationKinaseATMQ13315
PSP
204TPhosphorylationKinasePRKDCP78527
GPS
230SPhosphorylationKinaseCDK2P24941
PSP
553TPhosphorylationKinaseCDK2P24941
PSP
-KUbiquitinationE3 ubiquitin ligaseHUWE1Q7Z6Z7
PMID:22203964
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPOLL_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 DPOLL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_HUMANPCNAphysical
11784855
PCNA_HUMANPCNAphysical
12081642
A4_HUMANAPPphysical
21832049
ADIP_HUMANSSX2IPphysical
25416956
FSD2_HUMANFSD2physical
25416956
K1C40_HUMANKRT40physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
QSPP_HUMANC9orf64physical
26186194
SG1D1_HUMANSCGB1D1physical
26186194
SEMG2_HUMANSEMG2physical
26186194
SEMG1_HUMANSEMG1physical
26186194
IMDH1_HUMANIMPDH1physical
26186194
TRFL_HUMANLTFphysical
26186194
NOSIP_HUMANNOSIPphysical
26186194
RIOX2_HUMANMINAphysical
26186194
LACRT_HUMANLACRTphysical
26186194
MED1_HUMANMED1physical
26186194
ST1C2_HUMANSULT1C2physical
26186194
SYN2_HUMANSYN2physical
26186194
CYTS_HUMANCST4physical
26186194
QSPP_HUMANC9orf64physical
28514442
SEMG2_HUMANSEMG2physical
28514442
SEMG1_HUMANSEMG1physical
28514442
LACRT_HUMANLACRTphysical
28514442
SYN2_HUMANSYN2physical
28514442
TRFL_HUMANLTFphysical
28514442
ST1C2_HUMANSULT1C2physical
28514442
RIOX2_HUMANMINAphysical
28514442
SG1D1_HUMANSCGB1D1physical
28514442
CYTS_HUMANCST4physical
28514442
MED1_HUMANMED1physical
28514442
SPB4_HUMANSERPINB4physical
28514442
NOSIP_HUMANNOSIPphysical
28514442
SP16H_HUMANSUPT16Hphysical
27173435
RFA3_HUMANRPA3physical
27173435
WRN_HUMANWRNphysical
27173435
SSRP1_HUMANSSRP1physical
27173435
ODBB_HUMANBCKDHBphysical
27173435
RFA2_HUMANRPA2physical
27173435
RFA1_HUMANRPA1physical
27173435
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 DPOLL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND MASSSPECTROMETRY.

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