TAPT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TAPT1_HUMAN
• UniProt AC: Q6NXT6
• Protein Name: Transmembrane anterior posterior transformation protein 1 homolog
• Gene Name: TAPT1
• Organism: Homo sapiens (Human).
• Sequence Length: 567
• Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, cilium basal body . Membrane ; Multi-pass membrane protein .
• Protein Description: Plays a role in primary cilia formation. [PubMed: 26365339 May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity May be involved in cartilage and bone development (By similarity May play a role in the differentiation of cranial neural crest cells (By similarity; (Microbial infection) In case of infection, may act as a fusion receptor for cytomegalovirus (HCMV) strain AD169.]
• Protein Sequence: MAGVGDAAAPGEGGGGGVDGPQRDGRGEAEQPGGSGGQGPPPAPQLTETLGFYESDRRRERRRGRTELSLLRFLSAELTRGYFLEHNEAKYTERRERVYTCLRIPRELEKLMVFGIFLCLDAFLYVFTLLPLRVFLALFRLLTLPCYGLRDRRLLQPAQVCDILKGVILVICYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYVLLLIVCLRNMEQFSWNPDHLWVLFPDVCMVIASEIAVDIVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDYSDSVARRMGFIPLPLAVLLIRVVTSSIKVQGILSYACVILFYFGLISLKVLNSIVLLGKSCQYVKEAKMEEKLSNPPATCTPGKPSSKSQNKCKPSQGLSTEENLSASITKQPIHQKENIIPLLVTSNSDQFLTTPDGDEKDITQDNSELKHRSSKKDLLEIDRFTICGNRID

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
2	Acetylation	------MAGVGDAAA ------CCCCCCCCC	22.75	22814378
35	Phosphorylation	EAEQPGGSGGQGPPP CCCCCCCCCCCCCCC	45.74	22210691
47	Phosphorylation	PPPAPQLTETLGFYE CCCCCCHHHHHCCCH	22.98	22210691
53	Phosphorylation	LTETLGFYESDRRRE HHHHHCCCHHHHHHH	16.84	27642862
55	Phosphorylation	ETLGFYESDRRRERR HHHCCCHHHHHHHHH	25.66	22210691
66	Phosphorylation	RERRRGRTELSLLRF HHHHCCCHHHHHHHH	44.07	23312004
75	Phosphorylation	LSLLRFLSAELTRGY HHHHHHHHHHHHHCH	19.58	-
90	Malonylation	FLEHNEAKYTERRER HHHCCCCCCHHHHHH	46.67	26320211
90	Ubiquitination	FLEHNEAKYTERRER HHHCCCCCCHHHHHH	46.67	-
173	Phosphorylation	GVILVICYFMMHYVD HHHHHHHHHHHHHCC	5.38	26552605
178	Phosphorylation	ICYFMMHYVDYSMMY HHHHHHHHCCHHHHH	4.15	25693802
181	Phosphorylation	FMMHYVDYSMMYHLI HHHHHCCHHHHHHHH	6.60	25693802
182	Phosphorylation	MMHYVDYSMMYHLIR HHHHCCHHHHHHHHC	7.81	25693802
185	Phosphorylation	YVDYSMMYHLIRGQS HCCHHHHHHHHCCCH	5.71	25693802
280	Phosphorylation	SLLTIMMSNNFVEIK CCEEEEECCCCEEEE	15.96	29759185
303	Phosphorylation	KNNLFQMSNSDIKER HCCCEECCCHHHHHH	23.54	27174698
305	Phosphorylation	NLFQMSNSDIKERFT CCEECCCHHHHHHHH	33.15	27174698
377	Phosphorylation	VYSEYRASLAFDLVS HHHHHHHHHHHHHHC	15.95	-
384	Phosphorylation	SLAFDLVSSRQKNAY HHHHHHHCCCCCCCC	27.40	24719451
388	Ubiquitination	DLVSSRQKNAYTDYS HHHCCCCCCCCCCCC	42.30	21906983
441	Phosphorylation	LFYFGLISLKVLNSI HHHHHHHHHHHHHHH	27.47	24719451
459	Ubiquitination	GKSCQYVKEAKMEEK CHHCHHHHHHHHHHH	47.20	-
468	Phosphorylation	AKMEEKLSNPPATCT HHHHHHHCCCCCCCC	59.36	28102081
473	Phosphorylation	KLSNPPATCTPGKPS HHCCCCCCCCCCCCC	23.76	22199227
475	Phosphorylation	SNPPATCTPGKPSSK CCCCCCCCCCCCCCC	30.62	23403867
480	Phosphorylation	TCTPGKPSSKSQNKC CCCCCCCCCCCCCCC	54.61	27174698
481	Phosphorylation	CTPGKPSSKSQNKCK CCCCCCCCCCCCCCC	44.87	23403867
482	Ubiquitination	TPGKPSSKSQNKCKP CCCCCCCCCCCCCCC	61.47	-
483	Phosphorylation	PGKPSSKSQNKCKPS CCCCCCCCCCCCCCC	40.72	27174698
486	Ubiquitination	PSSKSQNKCKPSQGL CCCCCCCCCCCCCCC	35.68	-
500	Phosphorylation	LSTEENLSASITKQP CCCHHHHCCHHHCCC	31.39	26074081
502	Phosphorylation	TEENLSASITKQPIH CHHHHCCHHHCCCCC	27.67	25159151
504	Phosphorylation	ENLSASITKQPIHQK HHHCCHHHCCCCCCC	22.56	26074081
511	Ubiquitination	TKQPIHQKENIIPLL HCCCCCCCCCEEEEE	38.27	-
520	Phosphorylation	NIIPLLVTSNSDQFL CEEEEEEECCCCCCC	23.35	23898821
521	Phosphorylation	IIPLLVTSNSDQFLT EEEEEEECCCCCCCC	27.19	23898821
523	Phosphorylation	PLLVTSNSDQFLTTP EEEEECCCCCCCCCC	32.34	23898821
528	Phosphorylation	SNSDQFLTTPDGDEK CCCCCCCCCCCCCCC	37.26	23898821
529	Phosphorylation	NSDQFLTTPDGDEKD CCCCCCCCCCCCCCC	22.87	21712546
538	Phosphorylation	DGDEKDITQDNSELK CCCCCCCCCCCHHHC	39.75	18669648
542	Phosphorylation	KDITQDNSELKHRSS CCCCCCCHHHCCCCC	53.23	18669648
548	Phosphorylation	NSELKHRSSKKDLLE CHHHCCCCCHHHHHC	46.35	30108239
549	Phosphorylation	SELKHRSSKKDLLEI HHHCCCCCHHHHHCC	43.62	26657352
551	Ubiquitination	LKHRSSKKDLLEIDR HCCCCCHHHHHCCCC	56.40	-

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

Oops, there are no upstream regulatory protein records of TAPT1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TAPT1_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 TAPT1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TAPT1_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

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330