dbPTM

KCRB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCRB_MOUSE
UniProt AC	Q04447
Protein Name	Creatine kinase B-type
Gene Name	Ckb
Organism	Mus musculus (Mouse).
Sequence Length	381
Subcellular Localization	Cytoplasm.
Protein Description	Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa..
Protein Sequence	MPFSNSHNTQKLRFPAEDEFPDLSSHNNHMAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGHPYIMTVGAVAGDEESYDVFKDLFDPIIEERHGGYQPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQAIDDLMPAQK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPFSNSHNTQK ----CCCCCCCCCCC	31.39	24899341
6	Phosphorylation	--MPFSNSHNTQKLR --CCCCCCCCCCCCC	19.54	29550500
9	Phosphorylation	PFSNSHNTQKLRFPA CCCCCCCCCCCCCCC	22.96	22817900
24	Phosphorylation	EDEFPDLSSHNNHMA CCCCCCCCCCCCCHH	36.61	29899451
35	Phosphorylation	NHMAKVLTPELYAEL CCHHHHCCHHHHHHH	20.08	25521595
39	Nitration	KVLTPELYAELRAKC HHCCHHHHHHHHHHC	9.07	-
39	Phosphorylation	KVLTPELYAELRAKC HHCCHHHHHHHHHHC	9.07	24925903
82	Phosphorylation	VAGDEESYDVFKDLF EECCHHHHHHHHHHH	21.29	30387612
100	Phosphorylation	IEERHGGYQPSDEHK HHHHCCCCCCCCCCC	23.11	29899451
103	Phosphorylation	RHGGYQPSDEHKTDL HCCCCCCCCCCCCCC	39.85	29899451
107	Ubiquitination	YQPSDEHKTDLNPDN CCCCCCCCCCCCCCC	41.51	22790023
125	Phosphorylation	GDDLDPNYVLSSRVR CCCCCHHCEEECCCC	14.25	24899341
128	Phosphorylation	LDPNYVLSSRVRTGR CCHHCEEECCCCCCC	13.17	23737553
129	Phosphorylation	DPNYVLSSRVRTGRS CHHCEEECCCCCCCC	30.54	24899341
156	Ubiquitination	GERRAIEKLAVEALS HHHHHHHHHHHHHHH	35.32	22790023
163	Phosphorylation	KLAVEALSSLDGDLS HHHHHHHHCCCCCCH	35.58	22817900
164	Phosphorylation	LAVEALSSLDGDLSG HHHHHHHCCCCCCHH	31.18	22817900
170	Phosphorylation	SSLDGDLSGRYYALK HCCCCCCHHHHHHHH	26.43	29899451
178	Phosphorylation	GRYYALKSMTEAEQQ HHHHHHHCCCHHHHH	31.61	22817900
180	Phosphorylation	YYALKSMTEAEQQQL HHHHHCCCHHHHHHH	38.85	22942356
196	Ubiquitination	DDHFLFDKPVSPLLL CCCCCCCCCCHHHHH	39.73	22790023
199	Phosphorylation	FLFDKPVSPLLLASG CCCCCCCHHHHHHHC	20.54	26824392
205	Phosphorylation	VSPLLLASGMARDWP CHHHHHHHCCCCCCC	29.13	29899451
242	Ubiquitination	LRVISMQKGGNMKEV EEEEEEEECCCHHHH	61.21	22790023
247	Ubiquitination	MQKGGNMKEVFTRFC EEECCCHHHHHHHHH	55.51	27667366
251	Phosphorylation	GNMKEVFTRFCTGLT CCHHHHHHHHHHCHH	28.19	-
254	S-nitrosylation	KEVFTRFCTGLTQIE HHHHHHHHHCHHHHH	2.38	24895380
254	S-palmitoylation	KEVFTRFCTGLTQIE HHHHHHHHHCHHHHH	2.38	28680068
254	S-nitrosocysteine	KEVFTRFCTGLTQIE HHHHHHHHHCHHHHH	2.38	-
255	Phosphorylation	EVFTRFCTGLTQIET HHHHHHHHCHHHHHH	32.30	29899451
258	Phosphorylation	TRFCTGLTQIETLFK HHHHHCHHHHHHHHH	28.92	22006019
265	Ubiquitination	TQIETLFKSKNYEFM HHHHHHHHCCCCEEC	64.73	22790023
269	Nitration	TLFKSKNYEFMWNPH HHHHCCCCEECCCCC	17.80	16800626
269	Nitration	TLFKSKNYEFMWNPH HHHHCCCCEECCCCC	17.80	16800626
269	Nitrated tyrosine	TLFKSKNYEFMWNPH HHHHCCCCEECCCCC	17.80	-
279	Phosphorylation	MWNPHLGYILTCPSN CCCCCCEEEEECCCC	10.10	27742792
282	Phosphorylation	PHLGYILTCPSNLGT CCCEEEEECCCCCCC	16.89	27742792
283	Glutathionylation	HLGYILTCPSNLGTG CCEEEEECCCCCCCC	2.89	24333276
283	S-nitrosylation	HLGYILTCPSNLGTG CCEEEEECCCCCCCC	2.89	24895380
283	S-palmitoylation	HLGYILTCPSNLGTG CCEEEEECCCCCCCC	2.89	28680068
285	Phosphorylation	GYILTCPSNLGTGLR EEEEECCCCCCCCCC	47.00	20495213
289	Phosphorylation	TCPSNLGTGLRAGVH ECCCCCCCCCCCEEE	35.89	24925903
298	Ubiquitination	LRAGVHIKLPHLGKH CCCEEEEECCCCCCC	40.88	22790023
304	Ubiquitination	IKLPHLGKHEKFSEV EECCCCCCCHHHHHH	55.75	22790023
307	Ubiquitination	PHLGKHEKFSEVLKR CCCCCCHHHHHHHHH	54.64	22790023
309	Phosphorylation	LGKHEKFSEVLKRLR CCCCHHHHHHHHHHH	37.55	29899451
313	Acetylation	EKFSEVLKRLRLQKR HHHHHHHHHHHHHHC	55.34	7666031
313	Ubiquitination	EKFSEVLKRLRLQKR HHHHHHHHHHHHHHC	55.34	22790023
322	Phosphorylation	LRLQKRGTGGVDTAA HHHHHCCCCCCCCCC	34.49	25521595
327	Phosphorylation	RGTGGVDTAAVGGVF CCCCCCCCCCCCCEE	17.70	22817900

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
-	K	Ubiquitination	E3 ubiquitin ligase	Asb9	Q91ZT8	PMID:22199232

Functions of PTM Sites

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

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 KCRB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KCRB_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KCRB_MOUSE

Related Literatures of Post-Translational Modification

Nitration
Reference	PubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease."; Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.; Biochemistry 45:8009-8022(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, AND MASS SPECTROMETRY.	16800626 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASSSPECTROMETRY.	15648052 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39 AND TYR-125, AND MASSSPECTROMETRY.	18034455 [Abstract]