CINP_HUMAN - dbPTM
CINP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CINP_HUMAN
UniProt AC Q9BW66
Protein Name Cyclin-dependent kinase 2-interacting protein
Gene Name CINP
Organism Homo sapiens (Human).
Sequence Length 212
Subcellular Localization Nucleus . Binds to nuclear under G1 conditions, and dissociates from chromatin with the start of DNA replication.
Protein Description Interacts with the components of the replication complex and 2 kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling..
Protein Sequence MEAKTLGTVTPRKPVLSVSARKIKDNAADWHNLILKWETLNDAGFTTANNIANLKISLLNKDKIELDSSSPASKENEEKVCLEYNEELEKLCEELQATLDGLTKIQVKMEKLSSTTKGICELENYHYGEESKRPPLFHTWPTTHFYEVSHKLLEMYRKELLLKRTVAKELAHTGDPDLTLSYLSMWLHQPYVESDSRLHLESMLLETGHRAL
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-------MEAKTLGT
-------CCCCCCCC		11.5922814378
4Ubiquitination----MEAKTLGTVTP
----CCCCCCCCCCC		30.86-
8PhosphorylationMEAKTLGTVTPRKPV
CCCCCCCCCCCCCCE		25.0721815630
10PhosphorylationAKTLGTVTPRKPVLS
CCCCCCCCCCCCEEE		19.7422617229
13UbiquitinationLGTVTPRKPVLSVSA
CCCCCCCCCEEEEEE		40.45-
24UbiquitinationSVSARKIKDNAADWH
EEEEEEHHCCHHHHH		48.22-
39PhosphorylationNLILKWETLNDAGFT
HHEEEEEECCCCCCC		29.7320068231
46PhosphorylationTLNDAGFTTANNIAN
ECCCCCCCCHHHHHH		24.8720068231
47PhosphorylationLNDAGFTTANNIANL
CCCCCCCCHHHHHHC		25.7320068231
57PhosphorylationNIANLKISLLNKDKI
HHHHCEEEECCCCCE		25.8024719451
61AcetylationLKISLLNKDKIELDS
CEEEECCCCCEECCC		61.4412432655
61UbiquitinationLKISLLNKDKIELDS
CEEEECCCCCEECCC		61.44-
63MethylationISLLNKDKIELDSSS
EEECCCCCEECCCCC		39.42-
63UbiquitinationISLLNKDKIELDSSS
EEECCCCCEECCCCC		39.42-
68PhosphorylationKDKIELDSSSPASKE
CCCEECCCCCCCCCC		45.3925159151
69PhosphorylationDKIELDSSSPASKEN
CCEECCCCCCCCCCC		39.7525159151
70PhosphorylationKIELDSSSPASKENE
CEECCCCCCCCCCCH		28.5625159151
73PhosphorylationLDSSSPASKENEEKV
CCCCCCCCCCCHHHH		43.8428450419
117UbiquitinationEKLSSTTKGICELEN
HHHCCCCCCCEEECC		46.49-
163UbiquitinationYRKELLLKRTVAKEL
HHHHHHHHHHHHHHH		46.09-
173PhosphorylationVAKELAHTGDPDLTL
HHHHHHHHCCCCHHH		37.3622210691
202PhosphorylationDSRLHLESMLLETGH
CCHHHHHHHHHHCCC		22.5322210691
207PhosphorylationLESMLLETGHRAL--
HHHHHHHCCCCCC--		37.9522210691
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 CINP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CINP_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 CINP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ATRIP_HUMANATRIPphysical
19889979
CA109_HUMANC1orf109physical
25416956
ATRIP_HUMANATRIPphysical
25416956
FBF1_HUMANFBF1physical
25416956
SYCE1_HUMANSYCE1physical
25416956
SPA5L_HUMANSPATA5L1physical
28514442
CA109_HUMANC1orf109physical
28514442
KIF7_HUMANKIF7physical
28514442
POTEE_HUMANPOTEEphysical
28514442
SPAT5_HUMANSPATA5physical
28514442
HECD1_HUMANHECTD1physical
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 CINP_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 SER-70, AND MASSSPECTROMETRY.

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