MUP4_CAEEL - dbPTM
MUP4_CAEEL - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MUP4_CAEEL
UniProt AC Q21281
Protein Name Transmembrane matrix receptor MUP-4 {ECO:0000312|EMBL:AAK69172.1}
Gene Name mup-4 {ECO:0000312|EMBL:CCD63613.1, ECO:0000312|WormBase:K07D8.1}
Organism Caenorhabditis elegans.
Sequence Length 2104
Subcellular Localization Cell junction, hemidesmosome . Cytoplasm, cytoskeleton . Cell membrane
Single-pass membrane protein . Detected in intermediate filaments and hemidesmosomes.
Protein Description Required for junctional attachments between hypodermis and muscle, and between the apical epithelial surface and the cuticular matrix. Essential for enclosure of the embryo by the hypodermis, hypodermal integrity, embryo elongation, and maintenance of hypodermal morphology in fully elongated embryos..
Protein Sequence MRWVPLVLLPLIASAATTYQHRQTYSSLQCRVNDPLSCNQAKSEVCVFVNGQYRCECPVGVSRLADGRCLVVNECARPSLNACHKDAQCVDLAEGYTCRCNSGFADTSPDKVNKPGRQCQKTTNECGAKQTYGVDCDENAACVDTPEGFQCVCQPGYADVSTSISKLPGRKCVESVNECTNGEADCSNNADCFDRADGYECKCRPGFVDASPNVDKYPGRVCNKPKAPEYYGQQSRQPQCSEGSGCGPNEECRFNTAGEKVCQCRRGSVQQSNGVCKVFSQCEQANECDRNAFCSNTYDGPKCQCKDGFLDVSPDPVRLPGRKCQQVRNECADGSHDCSHQAACQDTPTGYICSCNSNCIDVSSRYNLPPGRKCSVAANQCSDKSLNSCDENADCVQLPDGYTCKCFAGYVDVSSNANLPPGRVCTLSTACPAQPTDLVFLIDGSGSIGSYVFQTEVLRFLAEFTELFDIAPQKTRVSVVQYSDQIRHEFGLDNYSDRKSLQNAIRNIEYLTGLTRTGAAIEHVANEAFSERRGARPVGQVSRVAIVITDGRSQDNVTRPSDNARRQDIQLFAVGVTNHVLDAELEEISGSKDRTFHVSGFEDLNTRLRSAIQRVACPHQNNEDTYNKGPCDPSNHNGCDRSLNQVCQQKNGKFVCACPAGFDIHPVTKVCGGDICNPEIATSCPDPEICEKTPFGNWRCTCPADLGWRDRLTGVCKIGEKPVQTSESNDECSPNDVHSCPANSKCEKGAGGEFICKCDAGFQRNGRTNKCEAPGTCDPRMPDSCDARKKEKCLPDGRGAFACMCDRHHKRHPVTDICLIDECAAGVADCDPNAKCTDTDESYICTCNEGFLDKSPEQNKKPGRVCSKQRNECLDGTHNCSMNADCIDLPDGFLCRCKEDFVDISPNPNAFGGIDCRALVNECLITGGHNCHEHAICIDTRDSYKCQCKEGYVDHDELRNPGRTCKKLNQICESGKHECDKNARCVEKGANDYECVCNAGFIDKSPLTHRPGRKCVEPICSDDSKHDCHSAAICEENDSVPEKYTCKCRDGYLDVGAVMGGGKSGRECKELVNECLSASLNSCDAAATCIDLDDGYTCKCPLGSKDESPVPKLPGRSCKGLVNECNIPHLNNCSHFATCIDLEEGYECKCKPEYHDQKPEQPGTECKFIINECLAENLNDCSPNAMCIDKIDGYDCKCKAPFQDEMPSNPGRICRFDECADPKDNDCDKHALCIDTDDSYTCQCKEGFFDEISDPKKPGRVCIGLVIEPQNQSEDPTTPDPNTIKCGNGLCHLDLGEVCVGGATCSCRPGESRDNEKEKCVPTTSIPLVVRVMEYDGEPIQYRTDYSKPDTQAHIEIVDAVKKSVGKIIGKTDVAPRFVTTDVNYITNPKVQNSEWDKGLLGNVSVHLAGKEEVDKCRFYEQFAEIVREMGGRVDRIKLSDDADLDPCKKEEEKKGIPCGNTFCSIELGEECIAGKICGCPKGQKRKDANSPCRAVESWNLPLYVIRDGHEKITYSPSLSNPLNDDHKDLVSRFESGVAQSYDKTPLKGAFVTAEVNEIENPESRKKSWDTGILYNFTSHFVKGSVAEPASVFTDLIDYIQKRNDFEVGKSKLFISPEQLNPFSNCYHSDCHPDAICKEVGKGYTCTCPDGFRDLNPSRPGRNCLSYRGVNECEKPELNECSPHARCIDLDYLYKCECIRPYVNSAVGDALPGSVCSIDYCQDVNYCPLNSTCVNVDEQARCDCKPGFVDLRKSGHLSEAGLGESICRRQSDIDECALGLHNCSAAAICIDKKIGYECQCQEGYEDGNPSQPGRICAASLCGLCNGHGDCIHDALSSNVTCACLDGYTGQFCETAPSNLPLILMTLLALLFLLLTLLCCLYMCARCRCFGARGRSEGSASGQEILGSDYYTIPRAKLARPLYGDEMGDDHAGALAAYLDDGASISSDGSIEEIERRVTTDVTTREVRTTTVRDDDGNIISQSQTISHGNPHETDTEQYGMISSDHYKTSASEAMDAAMSTSASGAAYNQSSGAMMSSASGHKSAYNQGYASDSEDSDAGHAVYDRTTRTNQSHDFEPGADPRTGTERSKREFVTTTKAEEVNYF
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
494N-linked_GlycosylationRHEFGLDNYSDRKSL
HHHHCCCCCCCHHHH
-
556N-linked_GlycosylationTDGRSQDNVTRPSDN
ECCCCCCCCCCCCCC
-
879N-linked_GlycosylationECLDGTHNCSMNADC
CCCCCCCCCCCCCCE
-
1037N-linked_GlycosylationSAAICEENDSVPEKY
CCEEECCCCCCCCCE
-
1132N-linked_GlycosylationCNIPHLNNCSHFATC
CCCCCCCCCCCEEEE
-
1271N-linked_GlycosylationGLVIEPQNQSEDPTT
EEEECCCCCCCCCCC
-
1403N-linked_GlycosylationWDKGLLGNVSVHLAG
CCCCCCCCEEEEECC
-
1576N-linked_GlycosylationWDTGILYNFTSHFVK
CCCCHHHHCCHHHCC
-
1730N-linked_GlycosylationDVNYCPLNSTCVNVD
CCCCCCCCCCEECCC
-
1782N-linked_GlycosylationECALGLHNCSAAAIC
HHHHHHCCCCCEEEE
-
1838N-linked_GlycosylationIHDALSSNVTCACLD
HHHHHHCCCEEEEEC
-
1895PhosphorylationCFGARGRSEGSASGQ
HHCCCCCCCCCCCCC
19060867
1898PhosphorylationARGRSEGSASGQEIL
CCCCCCCCCCCCCCC
19060867
1900PhosphorylationGRSEGSASGQEILGS
CCCCCCCCCCCCCCC
19060867
1909PhosphorylationQEILGSDYYTIPRAK
CCCCCCCCCCCCHHH
27067626
1958PhosphorylationEEIERRVTTDVTTRE
HHHHHHCCCCCCCCE
19530675
1959PhosphorylationEIERRVTTDVTTREV
HHHHHCCCCCCCCEE
19530675
1998PhosphorylationHETDTEQYGMISSDH
CCCCHHHHCCCCCCH
27067626
2049PhosphorylationKSAYNQGYASDSEDS
HHHCCCCCCCCCCCC
19530675
2051PhosphorylationAYNQGYASDSEDSDA
HCCCCCCCCCCCCCC
19060867
2053PhosphorylationNQGYASDSEDSDAGH
CCCCCCCCCCCCCCC
19060867
2056PhosphorylationYASDSEDSDAGHAVY
CCCCCCCCCCCCCEE
19060867

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 MUP4_CAEEL !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MUP4_CAEEL !!

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 MUP4_CAEEL !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MUP4_CAEEL !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MUP4_CAEEL

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Related Literatures of Post-Translational Modification

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