dbPTM

KCRB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCRB_HUMAN
UniProt AC	P12277
Protein Name	Creatine kinase B-type {ECO:0000305}
Gene Name	CKB
Organism	Homo sapiens (Human).
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	MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTGVDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQAIDDLMPAQK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPFSNSHNALK ----CCCCCCCCCEE	31.39	25159151
6	Phosphorylation	--MPFSNSHNALKLR --CCCCCCCCCEECC	19.54	22496350
11	Ubiquitination	SNSHNALKLRFPAED CCCCCCEECCCCCCC	34.89	21906983
13	Methylation	SHNALKLRFPAEDEF CCCCEECCCCCCCCC	33.64	-
24	Phosphorylation	EDEFPDLSAHNNHMA CCCCCCCHHCCCHHH	34.56	26437602
32	Ubiquitination	AHNNHMAKVLTPELY HCCCHHHHHCCHHHH	30.15	-
35	Phosphorylation	NHMAKVLTPELYAEL CHHHHHCCHHHHHHH	20.08	21945579
39	Phosphorylation	KVLTPELYAELRAKS HHCCHHHHHHHHCCC	9.07	21945579
43	Methylation	PELYAELRAKSTPSG HHHHHHHHCCCCCCC	31.32	-
45	Ubiquitination	LYAELRAKSTPSGFT HHHHHHCCCCCCCCC	48.72	-
82	Phosphorylation	VAGDEESYEVFKDLF EECCHHHHHHHHHHH	21.28	-
86	Ubiquitination	EESYEVFKDLFDPII HHHHHHHHHHHHHHH	59.71	-
96	Methylation	FDPIIEDRHGGYKPS HHHHHCCCCCCCCCC	19.98	-
101	Ubiquitination	EDRHGGYKPSDEHKT CCCCCCCCCCHHCCC	41.12	-
107	Acetylation	YKPSDEHKTDLNPDN CCCCHHCCCCCCCCC	41.51	26051181
107	Ubiquitination	YKPSDEHKTDLNPDN CCCCHHCCCCCCCCC	41.51	-
108	Phosphorylation	KPSDEHKTDLNPDNL CCCHHCCCCCCCCCC	47.85	21406692
125	Phosphorylation	GDDLDPNYVLSSRVR CCCCCHHCEEECCCC	14.25	20068231
128	Phosphorylation	LDPNYVLSSRVRTGR CCHHCEEECCCCCCC	13.17	20068231
129	Phosphorylation	DPNYVLSSRVRTGRS CHHCEEECCCCCCCC	30.54	20068231
133	Phosphorylation	VLSSRVRTGRSIRGF EEECCCCCCCCCCCE	33.81	21406692
136	Phosphorylation	SRVRTGRSIRGFCLP CCCCCCCCCCCEECC	20.27	21406692
138	Methylation	VRTGRSIRGFCLPPH CCCCCCCCCEECCCC	33.12	-
156	2-Hydroxyisobutyrylation	GERRAIEKLAVEALS HHHHHHHHHHHHHHH	35.32	-
156	Ubiquitination	GERRAIEKLAVEALS HHHHHHHHHHHHHHH	35.32	21890473
163	Phosphorylation	KLAVEALSSLDGDLA HHHHHHHHCCCCCHH	35.58	20873877
164	Phosphorylation	LAVEALSSLDGDLAG HHHHHHHCCCCCHHH	31.18	21082442
172	Methylation	LDGDLAGRYYALKSM CCCCHHHHHHHHHCC	18.71	-
173	Phosphorylation	DGDLAGRYYALKSMT CCCHHHHHHHHHCCC	7.68	-
174	Phosphorylation	GDLAGRYYALKSMTE CCHHHHHHHHHCCCH	12.23	-
178	Phosphorylation	GRYYALKSMTEAEQQ HHHHHHHCCCHHHHH	31.61	22496350
180	Phosphorylation	YYALKSMTEAEQQQL HHHHHCCCHHHHHHH	38.85	28857561
196	Acetylation	DDHFLFDKPVSPLLL CCCCCCCCCCHHHHH	39.73	27452117
196	Ubiquitination	DDHFLFDKPVSPLLL CCCCCCCCCCHHHHH	39.73	-
199	Phosphorylation	FLFDKPVSPLLLASG CCCCCCCHHHHHHHC	20.54	22617229
205	Phosphorylation	VSPLLLASGMARDWP CHHHHHHHCCCCCCC	29.13	22210691
215	Methylation	ARDWPDARGIWHNDN CCCCCCCCCEEECCC	44.50	-
223	Ubiquitination	GIWHNDNKTFLVWVN CEEECCCCCEEEEEC	43.44	21890473
223	Sumoylation	GIWHNDNKTFLVWVN CEEECCCCCEEEEEC	43.44	-
242	Acetylation	LRVISMQKGGNMKEV EEEEEEEECCCHHHH	61.21	26051181
242	2-Hydroxyisobutyrylation	LRVISMQKGGNMKEV EEEEEEEECCCHHHH	61.21	-
242	Ubiquitination	LRVISMQKGGNMKEV EEEEEEEECCCHHHH	61.21	21890473
247	Ubiquitination	MQKGGNMKEVFTRFC EEECCCHHHHHHHHH	55.51	-
247	2-Hydroxyisobutyrylation	MQKGGNMKEVFTRFC EEECCCHHHHHHHHH	55.51	-
247	Acetylation	MQKGGNMKEVFTRFC EEECCCHHHHHHHHH	55.51	27452117
247	Succinylation	MQKGGNMKEVFTRFC EEECCCHHHHHHHHH	55.51	23954790
254	Glutathionylation	KEVFTRFCTGLTQIE HHHHHHHHHCHHHHH	2.38	22555962
254	S-nitrosylation	KEVFTRFCTGLTQIE HHHHHHHHHCHHHHH	2.38	19483679
254	S-palmitoylation	KEVFTRFCTGLTQIE HHHHHHHHHCHHHHH	2.38	29575903
254	S-nitrosocysteine	KEVFTRFCTGLTQIE HHHHHHHHHCHHHHH	2.38	-
255	Phosphorylation	EVFTRFCTGLTQIET HHHHHHHHCHHHHHH	32.30	24076635
258	Phosphorylation	TRFCTGLTQIETLFK HHHHHCHHHHHHHHH	28.92	24076635
262	Phosphorylation	TGLTQIETLFKSKDY HCHHHHHHHHHCCCC	38.84	24076635
265	Acetylation	TQIETLFKSKDYEFM HHHHHHHHCCCCCCC	60.76	26051181
265	Ubiquitination	TQIETLFKSKDYEFM HHHHHHHHCCCCCCC	60.76	21906983
267	Acetylation	IETLFKSKDYEFMWN HHHHHHCCCCCCCCC	65.99	7825031
269	Nitration	TLFKSKDYEFMWNPH HHHHCCCCCCCCCCC	18.14	-
269	Nitration	TLFKSKDYEFMWNPH HHHHCCCCCCCCCCC	18.14	-
269	Phosphorylation	TLFKSKDYEFMWNPH HHHHCCCCCCCCCCC	18.14	-
269	Nitrated tyrosine	TLFKSKDYEFMWNPH HHHHCCCCCCCCCCC	18.14	-
279	Phosphorylation	MWNPHLGYILTCPSN CCCCCCEEEEECCCC	10.10	28152594
282	Phosphorylation	PHLGYILTCPSNLGT CCCEEEEECCCCCCC	16.89	27251275
283	Glutathionylation	HLGYILTCPSNLGTG CCEEEEECCCCCCCC	2.89	10769188
285	Phosphorylation	GYILTCPSNLGTGLR EEEEECCCCCCCCCC	47.00	27499020
289	Phosphorylation	TCPSNLGTGLRAGVH ECCCCCCCCCCCEEE	35.89	27251275
298	Ubiquitination	LRAGVHIKLPNLGKH CCCEEEEECCCCCCC	42.91	21906983
298	Acetylation	LRAGVHIKLPNLGKH CCCEEEEECCCCCCC	42.91	26051181
304	Ubiquitination	IKLPNLGKHEKFSEV EECCCCCCCHHHHHH	52.32	21906983
304	Acetylation	IKLPNLGKHEKFSEV EECCCCCCCHHHHHH	52.32	27452117
307	Sumoylation	PNLGKHEKFSEVLKR CCCCCCHHHHHHHHH	54.64	-
307	Ubiquitination	PNLGKHEKFSEVLKR CCCCCCHHHHHHHHH	54.64	21890473
307	2-Hydroxyisobutyrylation	PNLGKHEKFSEVLKR CCCCCCHHHHHHHHH	54.64	-
307	Sumoylation	PNLGKHEKFSEVLKR CCCCCCHHHHHHHHH	54.64	-
307	Acetylation	PNLGKHEKFSEVLKR CCCCCCHHHHHHHHH	54.64	23236377
309	Phosphorylation	LGKHEKFSEVLKRLR CCCCHHHHHHHHHHH	37.55	20886841
313	Acetylation	EKFSEVLKRLRLQKR HHHHHHHHHHHHHHC	55.34	26051181
313	Ubiquitination	EKFSEVLKRLRLQKR HHHHHHHHHHHHHHC	55.34	21890473
313	Succinylation	EKFSEVLKRLRLQKR HHHHHHHHHHHHHHC	55.34	23954790
320	Methylation	KRLRLQKRGTGGVDT HHHHHHHCCCCCCCC	34.64	-
322	Phosphorylation	LRLQKRGTGGVDTAA HHHHHCCCCCCCCCC	34.49	26657352
327	Phosphorylation	RGTGGVDTAAVGGVF CCCCCCCCCCCCCEE	17.70	25307156
337	Phosphorylation	VGGVFDVSNADRLGF CCCEEECCCCCCCCC	28.30	25307156
381	Ubiquitination	DDLMPAQK------- HHHCCCCC-------	65.50	-

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	Q96DX5	PMID:17148442

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASB9_HUMAN	ASB9	physical	16189514
SERP2_HUMAN	SERP2	physical	16189514
ASB9_HUMAN	ASB9	physical	20302626
PA24A_HUMAN	PLA2G4A	physical	22939629
G6PD_HUMAN	G6PD	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
SIAS_HUMAN	NANS	physical	22863883
PSA_HUMAN	NPEPPS	physical	22863883
PAK2_HUMAN	PAK2	physical	22863883
PUR4_HUMAN	PFAS	physical	22863883
SCLY_HUMAN	SCLY	physical	22863883
TGM2_HUMAN	TGM2	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
ASB9_HUMAN	ASB9	physical	25416956
KCRM_HUMAN	CKM	physical	26186194
ABCB7_HUMAN	ABCB7	physical	26344197
ACON_HUMAN	ACO2	physical	26344197
DDX10_HUMAN	DDX10	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
TPM4_HUMAN	TPM4	physical	26344197
KCRM_HUMAN	CKM	physical	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
DB00148	Creatine

Regulatory Network of KCRB_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-4, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35 AND SER-199, AND MASSSPECTROMETRY.	18669648 [Abstract]