MCLN1_HUMAN - dbPTM
MCLN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCLN1_HUMAN
UniProt AC Q9GZU1
Protein Name Mucolipin-1 {ECO:0000303|PubMed:12459486}
Gene Name MCOLN1
Organism Homo sapiens (Human).
Sequence Length 580
Subcellular Localization Late endosome membrane
Multi-pass membrane protein . Lysosome membrane
Multi-pass membrane protein . Cytoplasmic vesicle membrane
Multi-pass membrane protein . Cell projection, phagocytic cup . Cytoplasmic vesicle, phagosome membrane
Multi-pass me
Protein Description Nonselective cation channel probably playing a role in the regulation of membrane trafficking events and of metal homeostasis. Proposed to play a major role in Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, which is important for many lysosome-dependent cellular events, including the fusion and trafficking of these organelles, exocytosis and autophagy. [PubMed: 11013137]
Protein Sequence MTAPAGPRGSETERLLTPNPGYGTQAGPSPAPPTPPEEEDLRRRLKYFFMSPCDKFRAKGRKPCKLMLQVVKILVVTVQLILFGLSNQLAVTFREENTIAFRHLFLLGYSDGADDTFAAYTREQLYQAIFHAVDQYLALPDVSLGRYAYVRGGGDPWTNGSGLALCQRYYHRGHVDPANDTFDIDPMVVTDCIQVDPPERPPPPPSDDLTLLESSSSYKNLTLKFHKLVNVTIHFRLKTINLQSLINNEIPDCYTFSVLITFDNKAHSGRIPISLETQAHIQECKHPSVFQHGDNSFRLLFDVVVILTCSLSFLLCARSLLRGFLLQNEFVGFMWRQRGRVISLWERLEFVNGWYILLVTSDVLTISGTIMKIGIEAKNLASYDVCSILLGTSTLLVWVGVIRYLTFFHNYNILIATLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQAQQGRSSLVWLFSQLYLYSFISLFIYMVLSLFIALITGAYDTIKHPGGAGAEESELQAYIAQCQDSPTSGKFRRGSGSACSLLCCCGRDPSEEHSLLVN
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 Orthologous
Protein Cluster
2Phosphorylation------MTAPAGPRG
------CCCCCCCCC		41.1520639409
10PhosphorylationAPAGPRGSETERLLT
CCCCCCCCCCCEECC		42.5029255136
12PhosphorylationAGPRGSETERLLTPN
CCCCCCCCCEECCCC		28.2720639409
17PhosphorylationSETERLLTPNPGYGT
CCCCEECCCCCCCCC		26.1326425664
22PhosphorylationLLTPNPGYGTQAGPS
ECCCCCCCCCCCCCC		20.46-
24PhosphorylationTPNPGYGTQAGPSPA
CCCCCCCCCCCCCCC		13.5325850435
29PhosphorylationYGTQAGPSPAPPTPP
CCCCCCCCCCCCCCC		32.5425850435
34PhosphorylationGPSPAPPTPPEEEDL
CCCCCCCCCCCHHHH		50.8725159151
46UbiquitinationEDLRRRLKYFFMSPC
HHHHHHHHHHHCCCH		37.8929967540
47PhosphorylationDLRRRLKYFFMSPCD
HHHHHHHHHHCCCHH		13.47-
51PhosphorylationRLKYFFMSPCDKFRA
HHHHHHCCCHHHHHC		19.7421815630
55UbiquitinationFFMSPCDKFRAKGRK
HHCCCHHHHHCCCCC		43.3932142685
230N-linked_GlycosylationLKFHKLVNVTIHFRL
EEEEHHHCEEEEEEE		35.3319159218
232PhosphorylationFHKLVNVTIHFRLKT
EEHHHCEEEEEEEEE		11.9722985185
244PhosphorylationLKTINLQSLINNEIP
EEECCHHHHHCCCCC		34.09-
355PhosphorylationLEFVNGWYILLVTSD
HHHHCCEEEEEEECC		5.3129759185
360PhosphorylationGWYILLVTSDVLTIS
CEEEEEEECCEEEEC		21.1229759185
365PhosphorylationLVTSDVLTISGTIMK
EEECCEEEECCEEEE		16.9729759185
369PhosphorylationDVLTISGTIMKIGIE
CEEEECCEEEECCEE		15.8829759185
547PhosphorylationYIAQCQDSPTSGKFR
HHHHCCCCCCCCCCC		12.2829255136
549PhosphorylationAQCQDSPTSGKFRRG
HHCCCCCCCCCCCCC		54.8023663014
550PhosphorylationQCQDSPTSGKFRRGS
HCCCCCCCCCCCCCC		43.2929255136
552UbiquitinationQDSPTSGKFRRGSGS
CCCCCCCCCCCCCCC		35.1533845483
557PhosphorylationSGKFRRGSGSACSLL
CCCCCCCCCCCCCCH		27.9725159151
559PhosphorylationKFRRGSGSACSLLCC
CCCCCCCCCCCCHHC		28.0022733759
562PhosphorylationRGSGSACSLLCCCGR
CCCCCCCCCHHCCCC		24.8830108239
565S-palmitoylationGSACSLLCCCGRDPS
CCCCCCHHCCCCCCC		1.8816497227
566S-palmitoylationSACSLLCCCGRDPSE
CCCCCHHCCCCCCCH		2.5116497227
567S-palmitoylationACSLLCCCGRDPSEE
CCCCHHCCCCCCCHH		4.9616497227
572PhosphorylationCCCGRDPSEEHSLLV
HCCCCCCCHHCCCCC		60.9627732954
576PhosphorylationRDPSEEHSLLVN---
CCCCHHCCCCCC---		27.0321815630
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
557SPhosphorylationKinasePRKACAP17612
GPS
557SPhosphorylationKinasePKA-FAMILY-GPS
557SPhosphorylationKinasePAK-Uniprot
559SPhosphorylationKinasePRKACAP17612
GPS
559SPhosphorylationKinasePKA-FAMILY-GPS
559SPhosphorylationKinasePAK-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCLN1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MCLN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI27_HUMANTRIM27physical
16169070
S35E1_HUMANSLC35E1physical
16169070
Drug and Disease Associations
Kegg Disease
H00144 Mucolipidosis IV
OMIM Disease
252650Mucolipidosis type IV (MLIV)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCLN1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-230, AND MASSSPECTROMETRY.

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