KTAP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KTAP2_HUMAN
• UniProt AC: Q8N6L1
• Protein Name: Keratinocyte-associated protein 2
• Gene Name: KRTCAP2
• Organism: Homo sapiens (Human).
• Sequence Length: 136
• Subcellular Localization: Endoplasmic reticulum . Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Required for efficient substrate-specific N-glycosylation probably involving the STT3A-containing OST complex. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1..
• Protein Sequence: MVVGTGTSLALSSLLSLLLFAGMQMYSRQLASTEWLTIQGGLLGSGLFVFSLTAFNNLENLVFGKGFQAKIFPEILLCLLLALFASGLIHRVCVTTCFIFSMVGLYYINKISSTLYQAAAPVLTPAKVTGKSKKRN

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
31 (in isoform 2)	Phosphorylation	-	26.19	24043423
33 (in isoform 2)	Phosphorylation	-	22.02	24043423
34 (in isoform 2)	Phosphorylation	-	17.00	24043423
38 (in isoform 2)	Phosphorylation	-	17.21	24043423
39 (in isoform 2)	Phosphorylation	-	33.89	24043423
42 (in isoform 2)	Phosphorylation	-	23.43	24043423
52 (in isoform 2)	Phosphorylation	-	5.47	24043423
53 (in isoform 2)	Phosphorylation	-	14.28	24043423
101	Phosphorylation	VTTCFIFSMVGLYYI HHHHHHHHHHHHHHH	3.47	-
106	Phosphorylation	IFSMVGLYYINKISS HHHHHHHHHHHHHHC	2.28	-
107	Phosphorylation	FSMVGLYYINKISST HHHHHHHHHHHHHCH	2.22	-
112	Phosphorylation	LYYINKISSTLYQAA HHHHHHHHCHHHHHH	27.14	23312004
113	Phosphorylation	YYINKISSTLYQAAA HHHHHHHCHHHHHHC	25.81	23312004
114	Phosphorylation	YINKISSTLYQAAAP HHHHHHCHHHHHHCC	2.49	23312004
116	Phosphorylation	NKISSTLYQAAAPVL HHHHCHHHHHHCCCC	22.59	29759185
124	Phosphorylation	QAAAPVLTPAKVTGK HHHCCCCCCCCCCCC	6.24	25159151
129	Phosphorylation	VLTPAKVTGKSKKRN CCCCCCCCCCCCCCC	4.65	23312004
150	Phosphorylation	--------------------- ---------------------	22.79	19413330
153	Ubiquitination	------------------------ ------------------------	41.34	-
157	Ubiquitination	---------------------------- ----------------------------	50.14	-

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

Oops, there are no upstream regulatory protein records of KTAP2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KTAP2_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 KTAP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OST48_HUMAN	DDOST	physical	22266900
A4_HUMAN	APP	physical	21832049
STT3A_HUMAN	STT3A	physical	22266900
STT3B_HUMAN	STT3B	physical	22266900

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

Phosphorylation

"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 THR-150, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-150, AND MASSSPECTROMETRY.
PubMed: 18669648