CARME_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CARME_HUMAN
• UniProt AC: Q8N4J0
• Protein Name: Carnosine N-methyltransferase {ECO:0000303|PubMed:26001783, ECO:0000312|HGNC:HGNC:23435}
• Gene Name: CARNMT1 {ECO:0000312|HGNC:HGNC:23435}
• Organism: Homo sapiens (Human).
• Sequence Length: 409
• Subcellular Localization: Cytoplasm, cytosol . Nucleus .
• Protein Description: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His)..
• Protein Sequence: MQRRRRPPPPTSRLPEGCGGGGGGSEEVEVQFSAGRWGSAAAVSAAAAAATRSTEEEEERLEREHFWKIINAFRYYGTSMHERVNRTERQFRSLPANQQKLLPQFLLHLDKIRKCIDHNQEILLTIVNDCIHMFENKEYGEDGNGKIMPASTFDMDKLKSTLKQFVRDWSETGKAERDACYQPIIKEILKNFPKERWDPSKVNILVPGAGLGRLAWEIAMLGYACQGNEWSFFMLFSSNFVLNRCSEINKYKLYPWIHQFSNNRRSADQIRPIFFPDVDPHSLPPGSNFSMTAGDFQEIYSECNTWDCIATCFFIDTAHNVIDYIDTIWKILKPGGIWINLGPLLYHFENLANELSIELSYEDIKNVVLQYGFKVEVEKESVLSTYTVNDLSMMKYYYECVLFVVRKPQ

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
21	Ubiquitination	LPEGCGGGGGGSEEV CCCCCCCCCCCCCEE		21890473
32	Ubiquitination	SEEVEVQFSAGRWGS CCEEEEEEECCCCHH		21890473
44	Phosphorylation	WGSAAAVSAAAAAAT CHHHHHHHHHHHHHH		21406692
51	Phosphorylation	SAAAAAATRSTEEEE HHHHHHHHCCCHHHH		21406692
78	Ubiquitination	NAFRYYGTSMHERVN HHHHHHCCCHHHHHC		29967540
84	Ubiquitination	GTSMHERVNRTERQF CCCHHHHHCHHHHHH		29967540
100	Ubiquitination	SLPANQQKLLPQFLL CCCHHHHHHHHHHHH		23000965
107	Ubiquitination	KLLPQFLLHLDKIRK HHHHHHHHHHHHHHH		29967540
139	Phosphorylation	HMFENKEYGEDGNGK HHHCCCCCCCCCCCC		24425749
151	O-linked_Glycosylation	NGKIMPASTFDMDKL CCCEEECHHCCHHHH		29351928
151	Phosphorylation	NGKIMPASTFDMDKL CCCEEECHHCCHHHH		-
152	Phosphorylation	GKIMPASTFDMDKLK CCEEECHHCCHHHHH		-
157	Ubiquitination	ASTFDMDKLKSTLKQ CHHCCHHHHHHHHHH		29967540
157	Acetylation	ASTFDMDKLKSTLKQ CHHCCHHHHHHHHHH		25953088
161	Phosphorylation	DMDKLKSTLKQFVRD CHHHHHHHHHHHHHH		-
163	Ubiquitination	DKLKSTLKQFVRDWS HHHHHHHHHHHHHHH		29967540
163	Acetylation	DKLKSTLKQFVRDWS HHHHHHHHHHHHHHH		25953088
166	Ubiquitination	KSTLKQFVRDWSETG HHHHHHHHHHHHHHC		21890473
170	Phosphorylation	KQFVRDWSETGKAER HHHHHHHHHHCHHHH		-
174	Ubiquitination	RDWSETGKAERDACY HHHHHHCHHHHHHHH		-
186	Ubiquitination	ACYQPIIKEILKNFP HHHHHHHHHHHHHCC		29967540
252	Acetylation	CSEINKYKLYPWIHQ CHHHHHHHCHHHHHH		25953088
386	Phosphorylation	KESVLSTYTVNDLSM ECEEEEEEEECCHHH		22817900
398	Phosphorylation	LSMMKYYYECVLFVV HHHHHHHEEEEEEEE		22817900

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CARME_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CARME_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CARME_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
DTL_HUMAN	DTL	physical	26186194
MAP7_HUMAN	MAP7	physical	26186194
MKRN2_HUMAN	MKRN2	physical	26186194
ZCH18_HUMAN	ZC3H18	physical	26186194
TAB1_HUMAN	TAB1	physical	26186194
FANCJ_HUMAN	BRIP1	physical	26186194
CK5P1_HUMAN	CDK5RAP1	physical	26186194
R113A_HUMAN	RNF113A	physical	26186194
CUL4A_HUMAN	CUL4A	physical	26186194
LENG9_HUMAN	LENG9	physical	26186194
NUPL2_HUMAN	NUPL2	physical	26186194
TAB2_HUMAN	TAB2	physical	26186194
CNTLN_HUMAN	CNTLN	physical	26186194
PARN_HUMAN	PARN	physical	26186194
ZBTB2_HUMAN	ZBTB2	physical	26186194
GLE1_HUMAN	GLE1	physical	26186194
M3K7_HUMAN	MAP3K7	physical	26186194
KIF11_HUMAN	KIF11	physical	26186194
LUZP1_HUMAN	LUZP1	physical	26186194
MCR_HUMAN	NR3C2	physical	26186194
TPP2_HUMAN	TPP2	physical	26186194
ZBT25_HUMAN	ZBTB25	physical	26186194
SARM1_HUMAN	SARM1	physical	26186194
KLHL7_HUMAN	KLHL7	physical	26186194
OSBL1_HUMAN	OSBPL1A	physical	26186194
RBM22_HUMAN	RBM22	physical	26186194
KCTD3_HUMAN	KCTD3	physical	26186194
DTL_HUMAN	DTL	physical	28514442
MKRN2_HUMAN	MKRN2	physical	28514442
ZBTB2_HUMAN	ZBTB2	physical	28514442
M3K7_HUMAN	MAP3K7	physical	28514442
ZBT25_HUMAN	ZBTB25	physical	28514442
SARM1_HUMAN	SARM1	physical	28514442
TAB2_HUMAN	TAB2	physical	28514442
LUZP1_HUMAN	LUZP1	physical	28514442
CK5P1_HUMAN	CDK5RAP1	physical	28514442
TAB1_HUMAN	TAB1	physical	28514442
KLHL7_HUMAN	KLHL7	physical	28514442
ZCH18_HUMAN	ZC3H18	physical	28514442
FANCJ_HUMAN	BRIP1	physical	28514442
OSBL1_HUMAN	OSBPL1A	physical	28514442
MAP7_HUMAN	MAP7	physical	28514442
MCR_HUMAN	NR3C2	physical	28514442
NUPL2_HUMAN	NUPL2	physical	28514442
LENG9_HUMAN	LENG9	physical	28514442
GLE1_HUMAN	GLE1	physical	28514442
TPP2_HUMAN	TPP2	physical	28514442
PARN_HUMAN	PARN	physical	28514442
KCTD3_HUMAN	KCTD3	physical	28514442
HDAC1_HUMAN	HDAC1	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
• There are no disease associations of PTM sites.