TIP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TIP_HUMAN
• UniProt AC: Q8TB96
• Protein Name: T-cell immunomodulatory protein
• Gene Name: ITFG1 {ECO:0000312|HGNC:HGNC:30697}
• Organism: Homo sapiens (Human).
• Sequence Length: 612
• Subcellular Localization: Secreted . Membrane ; Single-pass type I membrane protein .
• Protein Description: Modulator of T-cell function. Has a protective effect in graft versus host disease model (By similarity)..
• Protein Sequence: MAAAGRLPSSWALFSPLLAGLALLGVGPVPARALHNVTAELFGAEAWGTLAAFGDLNSDKQTDLFVLRERNDLIVFLADQNAPYFKPKVKVSFKNHSALITSVVPGDYDGDSQMDVLLTYLPKNYAKSELGAVIFWGQNQTLDPNNMTILNRTFQDEPLIMDFNGDLIPDIFGITNESNQPQILLGGNLSWHPALTTTSKMRIPHSHAFIDLTEDFTADLFLTTLNATTSTFQFEIWENLDGNFSVSTILEKPQNMMVVGQSAFADFDGDGHMDHLLPGCEDKNCQKSTIYLVRSGMKQWVPVLQDFSNKGTLWGFVPFVDEQQPTEIPIPITLHIGDYNMDGYPDALVILKNTSGSNQQAFLLENVPCNNASCEEARRMFKVYWELTDLNQIKDAMVATFFDIYEDGILDIVVLSKGYTKNDFAIHTLKNNFEADAYFVKVIVLSGLCSNDCPRKITPFGVNQPGPYIMYTTVDANGYLKNGSAGQLSQSAHLALQLPYNVLGLGRSANFLDHLYVGIPRPSGEKSIRKQEWTAIIPNSQLIVIPYPHNVPRSWSAKLYLTPSNIVLLTAIALIGVCVFILAIIGILHWQEKKADDREKRQEAHRFHFDAM

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
36	N-linked_Glycosylation	VPARALHNVTAELFG CCHHHHHHHHHHHHC	33.41	UniProtKB CARBOHYD
86	Ubiquitination	DQNAPYFKPKVKVSF CCCCCCCCCEEEEEE	37.78	2190698
95	N-linked_Glycosylation	KVKVSFKNHSALITS EEEEEECCCCEEEEE	32.13	UniProtKB CARBOHYD
139	N-linked_Glycosylation	AVIFWGQNQTLDPNN CEEEEECCCCCCCCC	32.63	UniProtKB CARBOHYD
146	N-linked_Glycosylation	NQTLDPNNMTILNRT CCCCCCCCCEEECCC	34.07	UniProtKB CARBOHYD
151	N-linked_Glycosylation	PNNMTILNRTFQDEP CCCCEEECCCCCCCC	36.78	UniProtKB CARBOHYD
176	N-linked_Glycosylation	PDIFGITNESNQPQI CCHHCCCCCCCCCEE	49.10	UniProtKB CARBOHYD
188	N-linked_Glycosylation	PQILLGGNLSWHPAL CEEEECCCEEECCCC	29.15	19159218
226	N-linked_Glycosylation	DLFLTTLNATTSTFQ HEEEECCCCCCCEEE	32.90	UniProtKB CARBOHYD
243	N-linked_Glycosylation	IWENLDGNFSVSTIL EEECCCCCEEEEEEE	26.20	UniProtKB CARBOHYD
298	Ubiquitination	YLVRSGMKQWVPVLQ EEEECCCCHHEEEEE	44.53	-
353	N-linked_Glycosylation	DALVILKNTSGSNQQ CEEEEEECCCCCCCE	35.71	UniProtKB CARBOHYD
371	N-linked_Glycosylation	LENVPCNNASCEEAR EECCCCCCCCHHHHH	39.69	UniProtKB CARBOHYD
421	Ubiquitination	VLSKGYTKNDFAIHT EECCCCCCCCEEEHH	46.14	-
450	Phosphorylation	IVLSGLCSNDCPRKI EEHHCCCCCCCCCCC	40.52	29255136
482	N-linked_Glycosylation	DANGYLKNGSAGQLS CCCCEECCCCCCCCC	47.24	UniProtKB CARBOHYD
526	Ubiquitination	IPRPSGEKSIRKQEW CCCCCCCCCCCCEEE	55.50	-
530	Ubiquitination	SGEKSIRKQEWTAII CCCCCCCCEEEEEEE	51.39	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TIP_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 TIP_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TIP_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

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-188, AND MASSSPECTROMETRY.
PubMed: 19159218