dbPTM

INCA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	INCA1_HUMAN
UniProt AC	Q0VD86
Protein Name	Protein INCA1
Gene Name	INCA1
Organism	Homo sapiens (Human).
Sequence Length	236
Subcellular Localization	Nucleus .
Protein Description
Protein Sequence	MQVQDDGVNLIPFAKCSRVVSRSPPPRLPSQSLRPMPQRYGDVFWKNLNQRPTPTWLEEQHIPPMLRATGCSQLGLYPPEQLPPPEMLWRRKKRRPCLEGMQQQGLGGVPARVRAVTYHLEDLRRRQSIINELKKAQWGSSGAASEPVVLGEEGCGFPSTNEYPDLEEERATYPQEEDRFLTPGRAQLLWSPWSPLDQEEACASRQLHSLASFSTVTARRNPLHNPWGMELAASEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Phosphorylation	CSRVVSRSPPPRLPS CCCCCCCCCCCCCCC	33.96	26699800
92	Acetylation	PEMLWRRKKRRPCLE HHHHHCCCCCCCCHH	41.90	12433563
93	Acetylation	EMLWRRKKRRPCLEG HHHHCCCCCCCCHHH	52.40	12433573
182	Phosphorylation	QEEDRFLTPGRAQLL CHHHCCCCCCCCCEE	22.45	22817900
191	Phosphorylation	GRAQLLWSPWSPLDQ CCCCEECCCCCCCCH	19.23	22817900
194	Phosphorylation	QLLWSPWSPLDQEEA CEECCCCCCCCHHHH	20.97	15159402
209	Phosphorylation	CASRQLHSLASFSTV HHHHHHHHHHCCCCC	33.93	28270605
212	Phosphorylation	RQLHSLASFSTVTAR HHHHHHHCCCCCCCC	25.64	28270605
214	Phosphorylation	LHSLASFSTVTARRN HHHHHCCCCCCCCCC	21.33	28270605
215	Phosphorylation	HSLASFSTVTARRNP HHHHCCCCCCCCCCC	21.62	28270605
217	Phosphorylation	LASFSTVTARRNPLH HHCCCCCCCCCCCCC	17.97	28270605

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
23	S	Phosphorylation	Kinase	CDK2	P24941	PSP
182	T	Phosphorylation	Kinase	CDK2	P24941	PSP
191	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of INCA1_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 INCA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CCNA1_HUMAN	CCNA1	physical	15159402

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 INCA1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Identification of interaction partners and substrates of the cyclinA1-CDK2 complex."; Diederichs S., Baeumer N., Ji P., Metzelder S.K., Idos G.E.,Cauvet T., Wang W., Moeller M., Pierschalski S., Gromoll J.,Schrader M.G., Koeffler H.P., Berdel W.E., Serve H., Mueller-Tidow C.; J. Biol. Chem. 279:33727-33741(2004). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CCNA1,IDENTIFICATION IN A COMPLEX WITH CCNA1 AND CDK2, PHOSPHORYLATION ATSER-23; THR-182; SER-191 AND SER-194, MUTAGENESIS OF SER-23; THR-182;SER-191 AND SER-194, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.	15159402 [Abstract]