TCO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TCO1_HUMAN
• UniProt AC: P20061
• Protein Name: Transcobalamin-1
• Gene Name: TCN1
• Organism: Homo sapiens (Human).
• Sequence Length: 433
• Subcellular Localization: Secreted.
• Protein Description: Binds vitamin B12 with femtomolar affinity and protects it from the acidic environment of the stomach..
• Protein Sequence: MRQSHQLPLVGLLLFSFIPSQLCEICEVSEENYIRLKPLLNTMIQSNYNRGTSAVNVVLSLKLVGIQIQTLMQKMIQQIKYNVKSRLSDVSSGELALIILALGVCRNAEENLIYDYHLIDKLENKFQAEIENMEAHNGTPLTNYYQLSLDVLALCLFNGNYSTAEVVNHFTPENKNYYFGSQFSVDTGAMAVLALTCVKKSLINGQIKADEGSLKNISIYTKSLVEKILSEKKENGLIGNTFSTGEAMQALFVSSDYYNENDWNCQQTLNTVLTEISQGAFSNPNAAAQVLPALMGKTFLDINKDSSCVSASGNFNISADEPITVTPPDSQSYISVNYSVRINETYFTNVTVLNGSVFLSVMEKAQKMNDTIFGFTMEERSWGPYITCIQGLCANNNDRTYWELLSGGEPLSQGAGSYVVRNGENLEVRWSKY

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
42	Phosphorylation	RLKPLLNTMIQSNYN EHHHHHHHHHHHCCC	18.67	-
46	Phosphorylation	LLNTMIQSNYNRGTS HHHHHHHHCCCCCCH	30.29	-
48	Phosphorylation	NTMIQSNYNRGTSAV HHHHHHCCCCCCHHH	16.10	-
60	Phosphorylation	SAVNVVLSLKLVGIQ HHHHHHHHHHHHCHH	16.31	24719451
160	N-linked_Glycosylation	ALCLFNGNYSTAEVV HHHHHCCCCCHHHHH	28.78	UniProtKB CARBOHYD
216	N-linked_Glycosylation	ADEGSLKNISIYTKS ECCCCCCCEEEECHH	38.23	23846701
216	N-linked_Glycosylation	ADEGSLKNISIYTKS ECCCCCCCEEEECHH	38.23	16740002
230	Phosphorylation	SLVEKILSEKKENGL HHHHHHHHHHHHCCC	51.33	24719451
316	N-linked_Glycosylation	VSASGNFNISADEPI EECCCCEEECCCCCE	31.16	23846701
337	N-linked_Glycosylation	SQSYISVNYSVRINE CCCEEEEEEEEEECC	19.30	23846701
343	N-linked_Glycosylation	VNYSVRINETYFTNV EEEEEEECCCEEEEE	25.62	23846701
349	N-linked_Glycosylation	INETYFTNVTVLNGS ECCCEEEEEEEECCE	19.98	23846701
354	N-linked_Glycosylation	FTNVTVLNGSVFLSV EEEEEEECCEEHHHH	36.04	23846701
369	N-linked_Glycosylation	MEKAQKMNDTIFGFT HHHHHHHCCCCCCEE	50.76	23846701
369	N-linked_Glycosylation	MEKAQKMNDTIFGFT HHHHHHHCCCCCCEE	50.76	16740002

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

Oops, there are no upstream regulatory protein records of TCO1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TCO1_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 TCO1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TCO1_HUMAN !!

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-216 AND ASN-369, AND MASSSPECTROMETRY.
PubMed: 16740002

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-216, AND MASSSPECTROMETRY.
PubMed: 16335952