MKLN1_HUMAN - dbPTM
MKLN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MKLN1_HUMAN
UniProt AC Q9UL63
Protein Name Muskelin
Gene Name MKLN1
Organism Homo sapiens (Human).
Sequence Length 735
Subcellular Localization Cytoplasm . Cell projection, ruffle . Cytoplasm, cell cortex . Colocalizes with actin fibers in the cell cortex.
Protein Description Acts as a mediator of cell spreading and cytoskeletal responses to the extracellular matrix component THBS1..
Protein Sequence MAAGGAVAAAPECRLLPYALHKWSSFSSTYLPENILVDKPNDQSSRWSSESNYPPQYLILKLERPAIVQNITFGKYEKTHVCNLKKFKVFGGMNEENMTELLSSGLKNDYNKETFTLKHKIDEQMFPCRFIKIVPLLSWGPSFNFSIWYVELSGIDDPDIVQPCLNWYSKYREQEAIRLCLKHFRQHNYTEAFESLQKKTKIALEHPMLTDIHDKLVLKGDFDACEELIEKAVNDGLFNQYISQQEYKPRWSQIIPKSTKGDGEDNRPGMRGGHQMVIDVQTETVYLFGGWDGTQDLADFWAYSVKENQWTCISRDTEKENGPSARSCHKMCIDIQRRQIYTLGRYLDSSVRNSKSLKSDFYRYDIDTNTWMLLSEDTAADGGPKLVFDHQMCMDSEKHMIYTFGGRILTCNGSVDDSRASEPQFSGLFAFNCQCQTWKLLREDSCNAGPEDIQSRIGHCMLFHSKNRCLYVFGGQRSKTYLNDFFSYDVDSDHVDIISDGTKKDSGMVPMTGFTQRATIDPELNEIHVLSGLSKDKEKREENVRNSFWIYDIVRNSWSCVYKNDQAAKDNPTKSLQEEEPCPRFAHQLVYDELHKVHYLFGGNPGKSCSPKMRLDDFWSLKLCRPSKDYLLRHCKYLIRKHRFEEKAQVDPLSALKYLQNDLYITVDHSDPEETKEFQLLASALFKSGSDFTALGFSDVDHTYAQRTQLFDTLVNFFPDSMTPPKGNLVDLITL
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
2Acetylation------MAAGGAVAA
------CCCCCCCCC		18.1422223895
75AcetylationVQNITFGKYEKTHVC
EEEEECCCCCEEEEE		46.157825449
78UbiquitinationITFGKYEKTHVCNLK
EECCCCCEEEEECCE		40.62-
85AcetylationKTHVCNLKKFKVFGG
EEEEECCEEEEEECC		42.027825459
85UbiquitinationKTHVCNLKKFKVFGG
EEEEECCEEEEEECC		42.02-
104PhosphorylationNMTELLSSGLKNDYN
HHHHHHHHCCCCCCC		48.3830257219
112UbiquitinationGLKNDYNKETFTLKH
CCCCCCCCCEEEEEE		52.48-
195PhosphorylationNYTEAFESLQKKTKI
CHHHHHHHHHHHHHH		29.6425159151
198UbiquitinationEAFESLQKKTKIALE
HHHHHHHHHHHHHHC		68.64-
215UbiquitinationMLTDIHDKLVLKGDF
CCCCHHHHEECCCCH		26.74-
225 (in isoform 2)Ubiquitination-4.4921906983
231UbiquitinationACEELIEKAVNDGLF
HHHHHHHHHHHCCHH		51.12-
237 (in isoform 2)Ubiquitination-3.9821906983
248 (in isoform 1)Ubiquitination-27.6221906983
248UbiquitinationYISQQEYKPRWSQII
HCCCCCCCCCHHHCC		27.6221906983
257UbiquitinationRWSQIIPKSTKGDGE
CHHHCCCCCCCCCCC		61.42-
260 (in isoform 1)Ubiquitination-63.1921906983
260UbiquitinationQIIPKSTKGDGEDNR
HCCCCCCCCCCCCCC		63.192190698
341PhosphorylationDIQRRQIYTLGRYLD
HHHHHHHHHHHHHHC		6.3827642862
358UbiquitinationVRNSKSLKSDFYRYD
HHCCCCCCCCCEEEE		55.88-
414PhosphorylationRILTCNGSVDDSRAS
EEEEECCCCCCCCCC		14.3721815630
535UbiquitinationHVLSGLSKDKEKREE
HHHHCCCCCHHHHHH		77.26-
574UbiquitinationAAKDNPTKSLQEEEP
HHCCCCCCCCCCCCC		50.88-
607UbiquitinationLFGGNPGKSCSPKMR
HCCCCCCCCCCCCCC		49.93-
607AcetylationLFGGNPGKSCSPKMR
HCCCCCCCCCCCCCC		49.9325953088
647UbiquitinationRKHRFEEKAQVDPLS
HHCCCHHHHCCCHHH		36.60-
657UbiquitinationVDPLSALKYLQNDLY
CCHHHHHHHHHCCEE		43.56-
664PhosphorylationKYLQNDLYITVDHSD
HHHHCCEEEEECCCC		9.4527642862
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

Oops, there are no upstream regulatory protein records of MKLN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MKLN1_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 MKLN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MKLN1_HUMANMKLN1physical
17467196
MAEA_HUMANMAEAphysical
17467196
GID8_HUMANGID8physical
17467196
RMD5A_HUMANRMND5Aphysical
17467196
RANB9_HUMANRANBP9physical
17467196
RANB9_HUMANRANBP9physical
18710924
RANB9_HUMANRANBP9physical
27173435
ARMC8_HUMANARMC8physical
27173435
ZMY19_HUMANZMYND19physical
27173435
WDR26_HUMANWDR26physical
27173435
MMAD_HUMANMMADHCphysical
27173435
LONM_HUMANLONP1physical
27173435
R10B2_HUMANRSPH10Bphysical
27173435
R10B1_HUMANRSPH10Bphysical
27173435
YPEL5_HUMANYPEL5physical
27173435
RBP10_HUMANRANBP10physical
27173435
RAB8A_HUMANRAB8Aphysical
27173435
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.
Regulatory Network of MKLN1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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