PRI1_HUMAN - dbPTM
PRI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRI1_HUMAN
UniProt AC P49642
Protein Name DNA primase small subunit
Gene Name PRIM1
Organism Homo sapiens (Human).
Sequence Length 420
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 METFDPTELPELLKLYYRRLFPYSQYYRWLNYGGVIKNYFQHREFSFTLKDDIYIRYQSFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKELVFDIDMTDYDDVRRCCSSADICPKCWTLMTMAIRIIDRALKEDFGFKHRLWVYSGRRGVHCWVCDESVRKLSSAVRSGIVEYLSLVKGGQDVKKKVHLSEKIHPFIRKSINIIKKYFEEYALVNQDILENKESWDKILALVPETIHDELQQSFQKSHNSLQRWEHLKKVASRYQNNIKNDKYGPWLEWEIMLQYCFPRLDINVSKGINHLLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICRELDAISTNEEEKEENEAESDVKHRTRDYKKTSLAPYVKVFEHFLENLDKSRKGELLKKSDLQKDF
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-------METFDPTE
-------CCCCCCCH		11.1922223895
3Phosphorylation-----METFDPTELP
-----CCCCCCCHHH		31.8520068231
7Phosphorylation-METFDPTELPELLK
-CCCCCCCHHHHHHH		52.5820068231
16PhosphorylationLPELLKLYYRRLFPY
HHHHHHHHHHHHCCH		8.0420068231
17PhosphorylationPELLKLYYRRLFPYS
HHHHHHHHHHHCCHH		10.3320068231
23PhosphorylationYYRRLFPYSQYYRWL
HHHHHCCHHHHHHHH		10.8923663014
24PhosphorylationYRRLFPYSQYYRWLN
HHHHCCHHHHHHHHH		16.3723663014
26PhosphorylationRLFPYSQYYRWLNYG
HHCCHHHHHHHHHHC		6.7823663014
27PhosphorylationLFPYSQYYRWLNYGG
HCCHHHHHHHHHHCC		6.4123663014
32PhosphorylationQYYRWLNYGGVIKNY
HHHHHHHHCCHHCCE		17.0623663014
57PhosphorylationKDDIYIRYQSFNNQS
CCCEEEEEECCCCHH		10.0329496907
59PhosphorylationDIYIRYQSFNNQSDL
CEEEEEECCCCHHHH		22.4720873877
68UbiquitinationNNQSDLEKEMQKMNP
CCHHHHHHHHHHHCC		66.8221906983
72UbiquitinationDLEKEMQKMNPYKID
HHHHHHHHHCCCEEE		39.0622817900
76PhosphorylationEMQKMNPYKIDIGAV
HHHHHCCCEEEEEEE		18.6426546556
77UbiquitinationMQKMNPYKIDIGAVY
HHHHCCCEEEEEEEE		34.85-
95UbiquitinationPNQHNTVKLGAFQAQ
CCCCCCEEECCCHHC		38.8823000965
104UbiquitinationGAFQAQEKELVFDID
CCCHHCCCEEEEEEC		44.2421906983
123PhosphorylationDDVRRCCSSADICPK
HHHHHHHCCCCCCHH		31.99-
124PhosphorylationDVRRCCSSADICPKC
HHHHHHCCCCCCHHH		18.95-
130UbiquitinationSSADICPKCWTLMTM
CCCCCCHHHHHHHHH		37.68-
147UbiquitinationRIIDRALKEDFGFKH
HHHHHHHHHHCCCCE		55.0121906983
153UbiquitinationLKEDFGFKHRLWVYS
HHHHCCCCEEEEEEE		28.3527667366
183PhosphorylationKLSSAVRSGIVEYLS
HHHHHHHHCHHHHHH		26.6920068231
188PhosphorylationVRSGIVEYLSLVKGG
HHHCHHHHHHHHCCC		7.2420068231
190PhosphorylationSGIVEYLSLVKGGQD
HCHHHHHHHHCCCCC		30.1621406692
193UbiquitinationVEYLSLVKGGQDVKK
HHHHHHHCCCCCHHH		63.7221906983
193AcetylationVEYLSLVKGGQDVKK
HHHHHHHCCCCCHHH		63.7219413330
201UbiquitinationGGQDVKKKVHLSEKI
CCCCHHHHHCHHHHH		29.2123000965
207UbiquitinationKKVHLSEKIHPFIRK
HHHCHHHHHHHHHHH		42.8323000965
214UbiquitinationKIHPFIRKSINIIKK
HHHHHHHHHHHHHHH		51.3629967540
215PhosphorylationIHPFIRKSINIIKKY
HHHHHHHHHHHHHHH		15.8328060719
221UbiquitinationKSINIIKKYFEEYAL
HHHHHHHHHHHHHHC		44.7729967540
237UbiquitinationNQDILENKESWDKIL
CHHHHHCCCHHHHHH		43.6921906983
242UbiquitinationENKESWDKILALVPE
HCCCHHHHHHHHCHH		33.1022817900
250PhosphorylationILALVPETIHDELQQ
HHHHCHHHHHHHHHH		19.9720873877
258PhosphorylationIHDELQQSFQKSHNS
HHHHHHHHHHHHCHH		19.3820873877
261UbiquitinationELQQSFQKSHNSLQR
HHHHHHHHHCHHHHH		52.2321963094
273UbiquitinationLQRWEHLKKVASRYQ
HHHHHHHHHHHHHHH		47.3027667366
284UbiquitinationSRYQNNIKNDKYGPW
HHHHHHCCCCCCCHH		62.3127667366
310PhosphorylationPRLDINVSKGINHLL
CCCCEEECHHHHHHH		22.22-
311UbiquitinationRLDINVSKGINHLLK
CCCEEECHHHHHHHC		60.5721906983
318UbiquitinationKGINHLLKSPFSVHP
HHHHHHHCCCCCCCC		63.5429967540
319PhosphorylationGINHLLKSPFSVHPK
HHHHHHCCCCCCCCC		31.0225159151
326UbiquitinationSPFSVHPKTGRISVP
CCCCCCCCCCEEECE		49.0522817900
327PhosphorylationPFSVHPKTGRISVPI
CCCCCCCCCEEECEE		35.8228555341
331PhosphorylationHPKTGRISVPIDLQK
CCCCCEEECEECHHH		22.0821406692
351PhosphorylationPFTVPTISFICRELD
CCCCCHHHHHHHHHC		15.8424719451
354GlutathionylationVPTISFICRELDAIS
CCHHHHHHHHHCCCC		2.3222555962
361PhosphorylationCRELDAISTNEEEKE
HHHHCCCCCCHHHHH		27.2220363803
362PhosphorylationRELDAISTNEEEKEE
HHHCCCCCCHHHHHH		40.3020363803
367UbiquitinationISTNEEEKEENEAES
CCCCHHHHHHHHHHH		73.8733845483
377UbiquitinationNEAESDVKHRTRDYK
HHHHHHHCHHHHCHH		32.1533845483
385UbiquitinationHRTRDYKKTSLAPYV
HHHHCHHHHCCHHHH		36.8029967540
386PhosphorylationRTRDYKKTSLAPYVK
HHHCHHHHCCHHHHH		25.48-
387PhosphorylationTRDYKKTSLAPYVKV
HHCHHHHCCHHHHHH		31.26-
391PhosphorylationKKTSLAPYVKVFEHF
HHHCCHHHHHHHHHH		13.8029496907
404UbiquitinationHFLENLDKSRKGELL
HHHHCCCHHHCCHHH		56.1629967540
412UbiquitinationSRKGELLKKSDLQKD
HHCCHHHHHHHHCCC		63.9624816145
414PhosphorylationKGELLKKSDLQKDF-
CCHHHHHHHHCCCC-		41.8028555341
418UbiquitinationLKKSDLQKDF-----
HHHHHHCCCC-----		69.29-
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 PRI1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRI1_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
1Acetylation5 (4)D ⇒ Ars2277339
  • Menopause (age at onset)
  • Mean corpuscular volume
  • Plateletcrit
22267201
27863252
26414677
3Phosphorylation5 (2)D ⇒ Ars2277339
  • Menopause (age at onset)
  • Mean corpuscular volume
  • Plateletcrit
22267201
27863252
26414677
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRI2_HUMANPRIM2physical
22939629
RFA2_HUMANRPA2physical
26344197
DPOA2_HUMANPOLA2physical
28514442
PRI2_HUMANPRIM2physical
28514442
DPOLA_HUMANPOLA1physical
28514442
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 PRI1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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