PRI2_HUMAN - dbPTM
PRI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRI2_HUMAN
UniProt AC P49643
Protein Name DNA primase large subunit
Gene Name PRIM2
Organism Homo sapiens (Human).
Sequence Length 509
Subcellular Localization
Protein Description DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication..
Protein Sequence MEFSGRKWRKLRLAGDQRNASYPHCLQFYLQPPSENISLIEFENLAIDRVKLLKSVENLGVSYVKGTEQYQSKLESELRKLKFSYRENLEDEYEPRRRDHISHFILRLAYCQSEELRRWFIQQEMDLLRFRFSILPKDKIQDFLKDSQLQFEAISDEEKTLREQEIVASSPSLSGLKLGFESIYKIPFADALDLFRGRKVYLEDGFAYVPLKDIVAIILNEFRAKLSKALALTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQGNVGKISLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLEQALQFWKQEFIKGKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKIILSNPPSQGDYHGCPFRHSDPELLKQKLQSYKISPGGISQILDLVKGTHYQVACQKYFEMIHNVDDCGFSLNHPNQFFCESQRILNGGKDIKKEPIQPETPQPKPSVQKTKDASSALASLNSSLEMDMEGLEDYFSEDS
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
4Phosphorylation----MEFSGRKWRKL
----CCCCCCCCCCC		25.1220068231
54 (in isoform 1)Ubiquitination-63.9921890473
54 (in isoform 2)Ubiquitination-63.9921890473
54UbiquitinationIDRVKLLKSVENLGV
HHHHHHHHHHHHHCC		63.9921906983
55PhosphorylationDRVKLLKSVENLGVS
HHHHHHHHHHHHCCC		34.3321406692
62PhosphorylationSVENLGVSYVKGTEQ
HHHHHCCCEECCHHH		23.5521406692
63PhosphorylationVENLGVSYVKGTEQY
HHHHCCCEECCHHHH		12.0821406692
65 (in isoform 1)Ubiquitination-52.4621890473
65 (in isoform 2)Ubiquitination-52.4621890473
65UbiquitinationNLGVSYVKGTEQYQS
HHCCCEECCHHHHHH		52.4621906983
73 (in isoform 2)Ubiquitination-40.5221890473
73UbiquitinationGTEQYQSKLESELRK
CHHHHHHHHHHHHHH		40.5221906983
73 (in isoform 1)Ubiquitination-40.5221890473
82UbiquitinationESELRKLKFSYRENL
HHHHHHHCCHHHHCC		34.99-
102PhosphorylationPRRRDHISHFILRLA
HHHHHHHHHHHHHHH		14.6620860994
139 (in isoform 1)Ubiquitination-48.6821890473
139UbiquitinationFSILPKDKIQDFLKD
HCCCCHHHHHHHHHH		48.6821890473
1392-HydroxyisobutyrylationFSILPKDKIQDFLKD
HCCCCHHHHHHHHHH		48.68-
139 (in isoform 2)Ubiquitination-48.6821890473
145UbiquitinationDKIQDFLKDSQLQFE
HHHHHHHHHCCCHHE		56.1621906983
145 (in isoform 1)Ubiquitination-56.1621890473
147PhosphorylationIQDFLKDSQLQFEAI
HHHHHHHCCCHHEEC		31.0728387310
155PhosphorylationQLQFEAISDEEKTLR
CCHHEECCHHHHHHH		46.1229449344
159 (in isoform 1)Ubiquitination-51.3021890473
159UbiquitinationEAISDEEKTLREQEI
EECCHHHHHHHHHHH		51.3021906983
170PhosphorylationEQEIVASSPSLSGLK
HHHHHHCCCCCCCCC		14.5821815630
177 (in isoform 1)Ubiquitination-50.5221890473
177UbiquitinationSPSLSGLKLGFESIY
CCCCCCCCCCCEEEE		50.5221906983
201PhosphorylationLFRGRKVYLEDGFAY
HHCCCEEEECCCCEE		13.8624114839
208PhosphorylationYLEDGFAYVPLKDIV
EECCCCEEEEHHHHH		10.59-
227PhosphorylationNEFRAKLSKALALTA
HHHHHHHHHHHHHHH		18.3822210691
228UbiquitinationEFRAKLSKALALTAR
HHHHHHHHHHHHHHH		58.83-
257PhosphorylationLNHLSHSYTGQDYST
HHHHHCCCCCCCCCC		14.9527642862
262PhosphorylationHSYTGQDYSTQGNVG
CCCCCCCCCCCCCCE		13.0127642862
272PhosphorylationQGNVGKISLDQIDLL
CCCCEEEEHHHHHHH		29.4020068231
280PhosphorylationLDQIDLLSTKSFPPC
HHHHHHHCCCCCCHH		40.8824719451
282UbiquitinationQIDLLSTKSFPPCMR
HHHHHCCCCCCHHHH		46.88-
335UbiquitinationKQEFIKGKMDPDKFD
HHHHHCCCCCHHHCC		34.82-
340UbiquitinationKGKMDPDKFDKGYSY
CCCCCHHHCCCCCCC		61.93-
343UbiquitinationMDPDKFDKGYSYNIR
CCHHHCCCCCCCCCC		63.98-
345PhosphorylationPDKFDKGYSYNIRHS
HHHCCCCCCCCCCCC		17.4529496907
360PhosphorylationFGKEGKRTDYTPFSC
CCCCCCCCCCCCCCE		36.5228152594
362PhosphorylationKEGKRTDYTPFSCLK
CCCCCCCCCCCCEEE		18.7228152594
363PhosphorylationEGKRTDYTPFSCLKI
CCCCCCCCCCCEEEH		22.2228152594
377PhosphorylationIILSNPPSQGDYHGC
HHHCCCCCCCCCCCC		48.3128152594
381PhosphorylationNPPSQGDYHGCPFRH
CCCCCCCCCCCCCCC		13.6128152594
389PhosphorylationHGCPFRHSDPELLKQ
CCCCCCCCCHHHHHH		51.0824719451
395UbiquitinationHSDPELLKQKLQSYK
CCCHHHHHHHHHHCC		58.99-
400PhosphorylationLLKQKLQSYKISPGG
HHHHHHHHCCCCCCH		38.5424719451
401PhosphorylationLKQKLQSYKISPGGI
HHHHHHHCCCCCCHH		10.2024719451
402UbiquitinationKQKLQSYKISPGGIS
HHHHHHCCCCCCHHH		41.7921890473
402 (in isoform 1)Ubiquitination-41.7921890473
404PhosphorylationKLQSYKISPGGISQI
HHHHCCCCCCHHHHH		17.2225159151
409PhosphorylationKISPGGISQILDLVK
CCCCCHHHHHHHHHC		17.9127362937
416UbiquitinationSQILDLVKGTHYQVA
HHHHHHHCCCHHHHH		66.44-
463UbiquitinationNGGKDIKKEPIQPET
CCCCCCCCCCCCCCC		69.89-
470PhosphorylationKEPIQPETPQPKPSV
CCCCCCCCCCCCCCC		33.6325159151
474AcetylationQPETPQPKPSVQKTK
CCCCCCCCCCCCCCC		44.6826051181
476PhosphorylationETPQPKPSVQKTKDA
CCCCCCCCCCCCCCH		43.2225159151
484PhosphorylationVQKTKDASSALASLN
CCCCCCHHHHHHHHH		26.6921406692
485PhosphorylationQKTKDASSALASLNS
CCCCCHHHHHHHHHH		29.0821406692
489PhosphorylationDASSALASLNSSLEM
CHHHHHHHHHHHHCC		29.0021406692
492PhosphorylationSALASLNSSLEMDME
HHHHHHHHHHCCCCC		41.4121406692
493PhosphorylationALASLNSSLEMDMEG
HHHHHHHHHCCCCCH		27.5521406692
504PhosphorylationDMEGLEDYFSEDS--
CCCHHHHHHCCCC--		10.3021406692
506PhosphorylationEGLEDYFSEDS----
CHHHHHHCCCC----		33.9820873877
509PhosphorylationEDYFSEDS-------
HHHHCCCC-------		37.7620873877
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 PRI2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRI2_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 PRI2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
DPOLA_HUMANPOLA1physical
22863883
DPOA2_HUMANPOLA2physical
22863883
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 PRI2_HUMAN

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Related Literatures of Post-Translational Modification
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 THR-470, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, AND MASSSPECTROMETRY.

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