PK1L1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PK1L1_HUMAN
• UniProt AC: Q8TDX9
• Protein Name: Polycystic kidney disease protein 1-like 1
• Gene Name: PKD1L1
• Organism: Homo sapiens (Human).
• Sequence Length: 2849
• Subcellular Localization: Cell projection, cilium membrane ; Multi-pass membrane protein .
• Protein Description: Component of a ciliary calcium channel that controls calcium concentration within primary cilia without affecting cytoplasmic calcium concentration. Forms a heterodimer with PKD2L1 in primary cilia and forms a calcium-permeant ciliary channel that regulates sonic hedgehog/SHH signaling and GLI2 transcription. Does not constitute the pore-forming subunit. Also involved in left/right axis specification downstream of nodal flow: forms a complex with PKD2 in cilia to facilitate flow detection in left/right patterning..
• Protein Sequence: MAEEAAQNISDDQERCLQAACCLSFGGELSVSTDKSWGLHLCSCSPPGGGLWVEVYANHVLLMSDGKCGCPWCALNGKAEDRESQSPSSSASRQKNIWKTTSEAALSVVNEKTQAVVNEKTQAPLDCDNSADRIPHKPFIIIARAWSSGGPRFHHRRLCATGTADSTFSALLQLQGTTSAAAPCSLKMEASCCVLRLLCCAEDVATGLLPGTVTMETPTKVARPTQTSSQRVPLWPISHFPTSPRSSHGLPPGIPRTPSFTASQSGSEILYPPTQHPPVAILARNSDNFMNPVLNCSLEVEARAPPNLGFRVHMASGEALCLMMDFGDSSGVEMRLHNMSEAMAVTAYHQYSKGIFFHLLHFQLDMSTYKEAETQNTTLNVYLCQSENSCLEDSDPSNLGYELISAFVTKGVYMLKAVIYNEFHGTEVELGPYYVEIGHEAVSAFMNSSSVHEDEVLVFADSQVNQKSTVVIHHFPSIPSYNVSFISQTQVGDSQAWHSMTVWYKMQSVSVYTNGTVFATDTDITFTAVTKETIPLEFEWYFGEDPPVRTTSRSIKKRLSIPQWYRVMVKASNRMSSVVSEPHVIRVQKKIVANRLTSPSSALVNASVAFECWINFGTDVAYLWDFGDGTVSLGSSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIVCEPCQPPLVKNMGPGKVQIWRSQPVRLGVTFEAAVFCDISQGLSYTWNLMDSEGLPVSLPAAVDTHRQTLILPSHTLEYGNYTALAKVQIEGSVVYSNYCVGLEVRAQAPVSVISEGTHLFFSRTTSSPIVLRGTQSFDPDDPGATLRYHWECATAGSPAHPCFDSSTAHQLDAAAPTVSFEAQWLSDSYDQFLVMLRVSSGGRNSSETRVFLSPYPDSAFRFVHISWVSFKDTFVNWNDELSLQAMCEDCSEIPNLSYSWDLFLVNATEKNRIEVPFCRVVGLLGSLGLGAISESSQLNLLPTEPGTADPDATTTPFSREPSPVTLGQPATSAPRGTPTEPMTGVYWIPPAGDSAVLGEAPEEGSLDLEPGPQSKGSLMTGRSERSQPTHSPDPHLSDFEAYYSDIQEAIPSGGRQPAKDTSFPGSGPSLSAEESPGDGDNLVDPSLSAGRAEPVLMIDWPKALLGRAVFQGYSSSGITEQTVTIKPYSLSSGETYVLQVSVASKHGLLGKAQLYLTVNPAPRDMACQVQPHHGLEAHTVFSVFCMSGKPDFHYEFSYQIGNTSKHTLYHGRDTQYYFVLPAGEHLDNYKVMVSTEITDGKGSKVQPCTVVVTVLPRYHGNDCLGEDLYNSSLKNLSTLQLMGSYTEIRNYITVITRILSRLSKEDKTASCNQWSRIQDALISSVCRLAFVDQEEMIGSVLMLRDLVSFSNKLGFMSAVLILKYTRALLAQGQFSGPFVIDKGVRLELIGLISRVWEVSEQENSKEEVYRHEEGITVISDLLLGCLSLNHVSTGQMEFRTLLHYNLQSSVQSLGSVQVHLPGDLAGHSPAGAETQSPCYISQLILFKKNPYPGSQAPGQIGGVVGLNLYTCSSRRPINRQWLRKPVMVEFGEEDGLDNRRNKTTFVLLRDKVNLHQFTELSENPQESLQIEIEFSKPVTRAFPVMLLVRFSEKPTPSDFLVKQIYFWDESIVQIYIPAASQKDASVGYLSLLDADYDRKPPNRYLAKAVNYTVHFQWIRCLFWDKREWKSERFSPQPGTSPEKVNCSYHRLAAFALLRRKLKASFEVSDISKLQSHPENLLPSIFIMGSVILYGFLVAKSRQVDHHEKKKAGYIFLQEASLPGHQLYAVVIDTGFRAPARLTSKVYIVLCGDNGLSETKELSCPEKPLFERNSRHTFILSAPAQLGLLRKIRLWHDSRGPSPGWFISHVMVKELHTGQGWFFPAQCWLSAGRHDGRVERELTCLQGGLGFRKLFYCKFTEYLEDFHVWLSVYSRPSSSRYLHTPRLTVSFSLLCVYACLTALVAAGGQEQPHLDVSPTLGSFRVGLLCTLLASPGAQLLSLLFRLSKEAPGSARVEPHSPLRGGAQTEAPHGPNSWGRIPDAQEPRKQPASAILSGSGRAQRKAASDNGTACPAPKLQVHGADHSRTSLMGKSHCCPPHTQAPSSGLEGLMPQWSRALQPWWSSAVWAICGTASLACSLGTGFLAYRFGQEQCVQWLHLLSLSVVCCIFITQPLMVCLMALGFAWKRRADNHFFTESLCEATRDLDSELAERSWTRLPFSSSCSIPDCAGEVEKVLAARQQARHLRWAHPPSKAQLRGTRQRMRRESRTRAALRDISMDILMLLLLLCVIYGRFSQDEYSLNQAIRKEFTRNARNCLGGLRNIADWWDWSLTTLLDGLYPGGTPSARVPGAQPGALGGKCYLIGSSVIRQLKVFPRHLCKPPRPFSALIEDSIPTCSPEVGGPENPYLIDPENQNVTLNGPGGCGTREDCVLSLGRTRTEAHTALSRLRASMWIDRSTRAVSVHFTLYNPPTQLFTSVSLRVEILPTGSLVPSSLVESFSIFRSDSALQYHLMLPQLVFLALSLIHLCVQLYRMMDKGVLSYWRKPRNWLELSVVGVSLTYYAVSGHLVTLAGDVTNQFHRGLCRAFMDLTLMASWNQRARWLRGILLFLFTLKCVYLPGIQNTMASCSSMMRHSLPSIFVAGLVGALMLAALSHLHRFLLSMWVLPPGTFTDAFPGLLFHFPRRSQKDCLLGLSKSDQRAMACYFGILLIVSATLCFGMLRGFLMTLPQKRKSFQSKSFVRLKDVTAYMWEKVLTFLRLETPKLEEAEMVENHNYYLDEFANLLDELLMKINGLSDSLQLPLLEKTSNNTGEARTEESPLVDISSYQAAEPADIKDF

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
8	N-linked_Glycosylation	MAEEAAQNISDDQER CHHHHHHHCCHHHHH	30.88	UniProtKB CARBOHYD
84	Phosphorylation	GKAEDRESQSPSSSA CCCCCCCCCCCCCCH	36.53	25072903
86	Phosphorylation	AEDRESQSPSSSASR CCCCCCCCCCCCHHH	35.71	25072903
88	Phosphorylation	DRESQSPSSSASRQK CCCCCCCCCCHHHHH	42.02	25072903
89	Phosphorylation	RESQSPSSSASRQKN CCCCCCCCCHHHHHC	33.05	25072903
90	Phosphorylation	ESQSPSSSASRQKNI CCCCCCCCHHHHHCC	34.30	25072903
92	Phosphorylation	QSPSSSASRQKNIWK CCCCCCHHHHHCCCH	36.87	25072903
100	Phosphorylation	RQKNIWKTTSEAALS HHHCCCHHHHHHHHH	22.13	29052541
101	Phosphorylation	QKNIWKTTSEAALSV HHCCCHHHHHHHHHH	22.35	29052541
102	Phosphorylation	KNIWKTTSEAALSVV HCCCHHHHHHHHHHH	30.39	22468782
107	Phosphorylation	TTSEAALSVVNEKTQ HHHHHHHHHHCHHCH	21.20	29052541
263	Phosphorylation	RTPSFTASQSGSEIL CCCCEECCCCCCCCC	23.09	-
295	N-linked_Glycosylation	NFMNPVLNCSLEVEA CCCCCCCEEEEEEEE	17.36	UniProtKB CARBOHYD
338	N-linked_Glycosylation	GVEMRLHNMSEAMAV CCEEEEECHHHHHHH	40.02	UniProtKB CARBOHYD
369	Phosphorylation	FQLDMSTYKEAETQN EECCCCCCCCHHCCC	10.26	29759185
376	N-linked_Glycosylation	YKEAETQNTTLNVYL CCCHHCCCCEEEEEE	42.31	UniProtKB CARBOHYD
433	Phosphorylation	TEVELGPYYVEIGHE CEEEECCEEEEECHH	20.53	22468782
443	Phosphorylation	EIGHEAVSAFMNSSS EECHHHHHHHHCCCC	23.88	22468782
447	N-linked_Glycosylation	EAVSAFMNSSSVHED HHHHHHHCCCCCCCC	32.08	UniProtKB CARBOHYD
482	N-linked_Glycosylation	FPSIPSYNVSFISQT CCCCCCCCEEEEECC	27.56	UniProtKB CARBOHYD
514	N-linked_Glycosylation	QSVSVYTNGTVFATD CEEEEEECCEEEEEC	26.84	UniProtKB CARBOHYD
525	Phosphorylation	FATDTDITFTAVTKE EEECCCEEEEEECCC	20.10	-
530	Phosphorylation	DITFTAVTKETIPLE CEEEEEECCCEECEE	22.24	-
605	N-linked_Glycosylation	SPSSALVNASVAFEC CHHHHHHCHHHEEEE	27.61	UniProtKB CARBOHYD
657	N-linked_Glycosylation	VEVLAFNNVSASTLR EEEEEECCCCHHHHH	23.75	UniProtKB CARBOHYD
751	N-linked_Glycosylation	SHTLEYGNYTALAKV CCEEEECCEEEEEEE	30.04	UniProtKB CARBOHYD
797	Phosphorylation	LFFSRTTSSPIVLRG EEEECCCCCCEEEEC	33.24	-
875	N-linked_Glycosylation	RVSSGGRNSSETRVF EECCCCCCCCCEEEE	53.84	UniProtKB CARBOHYD
926	N-linked_Glycosylation	EDCSEIPNLSYSWDL CCHHHCCCCCCEEEE	47.48	UniProtKB CARBOHYD
937	N-linked_Glycosylation	SWDLFLVNATEKNRI EEEEEEEECCCCCCC	43.20	UniProtKB CARBOHYD
1097	Phosphorylation	KDTSFPGSGPSLSAE CCCCCCCCCCCCCCC	48.01	-
1100	Phosphorylation	SFPGSGPSLSAEESP CCCCCCCCCCCCCCC	38.18	-
1119	Phosphorylation	NLVDPSLSAGRAEPV CCCCCCCCCCCCCCE	32.77	30257219
1233	N-linked_Glycosylation	EFSYQIGNTSKHTLY EEEEEECCCCCCEEE	42.69	UniProtKB CARBOHYD
1301	N-linked_Glycosylation	CLGEDLYNSSLKNLS CCCHHHCCCCCCCCH	32.21	UniProtKB CARBOHYD
1306	N-linked_Glycosylation	LYNSSLKNLSTLQLM HCCCCCCCCHHHHHC	44.51	UniProtKB CARBOHYD
1308	Phosphorylation	NSSLKNLSTLQLMGS CCCCCCCHHHHHCCC	36.14	-
1316	Phosphorylation	TLQLMGSYTEIRNYI HHHHCCCHHHHHHHH	11.58	-
1324	Phosphorylation	TEIRNYITVITRILS HHHHHHHHHHHHHHH	8.76	23403867
1525	Phosphorylation	KKNPYPGSQAPGQIG ECCCCCCCCCCCCCC	20.75	-
1572	N-linked_Glycosylation	DGLDNRRNKTTFVLL CCCCCCCCCEEEEEE	42.67	UniProtKB CARBOHYD
1681	N-linked_Glycosylation	RYLAKAVNYTVHFQW HHHHHHCCEEEEEEE	31.45	UniProtKB CARBOHYD
1716	N-linked_Glycosylation	GTSPEKVNCSYHRLA CCCHHHCCCCHHHHH	21.78	UniProtKB CARBOHYD
1813	Phosphorylation	FRAPARLTSKVYIVL CCCCCCCCCCEEEEE	22.43	28509920
1814	Phosphorylation	RAPARLTSKVYIVLC CCCCCCCCCEEEEEE	25.39	28509920
1817	Phosphorylation	ARLTSKVYIVLCGDN CCCCCCEEEEEECCC	6.77	28509920
1833	Phosphorylation	LSETKELSCPEKPLF CCCCCCCCCCCCCCC	28.81	23403867
1992	Phosphorylation	DVSPTLGSFRVGLLC CCCCCCCHHHHHHHH	17.00	24719451
2030	Phosphorylation	SARVEPHSPLRGGAQ CCCCCCCCCCCCCCC	36.02	26091039
2038	Phosphorylation	PLRGGAQTEAPHGPN CCCCCCCCCCCCCCC	33.31	-
2046	Phosphorylation	EAPHGPNSWGRIPDA CCCCCCCCCCCCCCC	33.76	-
2058	Acetylation	PDAQEPRKQPASAIL CCCCCCCCCCCHHHH	71.93	19413330
2062	Phosphorylation	EPRKQPASAILSGSG CCCCCCCHHHHCCCH	23.64	19413330
2426	N-linked_Glycosylation	LIDPENQNVTLNGPG CCCCCCCEEEECCCC	40.08	UniProtKB CARBOHYD
2488	Phosphorylation	PPTQLFTSVSLRVEI CCCCEEEEEEEEEEE	11.45	24719451
2490	Phosphorylation	TQLFTSVSLRVEILP CCEEEEEEEEEEECC	15.38	24719451
2708	Phosphorylation	CLLGLSKSDQRAMAC CCCCCCHHHHHHHHH	35.28	28165663

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

Oops, there are no upstream regulatory protein records of PK1L1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PK1L1_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 PK1L1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PK1L1_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.