EPI1_CAEEL - dbPTM
EPI1_CAEEL - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPI1_CAEEL
UniProt AC Q21313
Protein Name Laminin-like protein epi-1
Gene Name epi-1
Organism Caenorhabditis elegans.
Sequence Length 3672
Subcellular Localization
Protein Description During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably downstream of the integrin complex formed by pat-2 and pat-3..
Protein Sequence MSPYDSSPWATKALFLIVTLLAQFTYSQVLTPSQITISHRKPITATSTCGEIQGQPVTEIYCSLTGSTQYTPLNSYSYQDDEQQKSWSQYENPMVRGGHGCGHCNAGNENSHPAANMVDGNNSWWMSPPLSRGLQHNEVNITIDLEQEFHVAYVWIQMANSPRPGSWVLERSTDHGKTYQPWFNFAENAAECMRRFGMESLSPISEDDSVTCRTDMASLQPLENAEMVIRILEHRPSSRQFATSEALQNFTRATNVRLRLLGTRTLQGHLMDMNEWRDPTVTRRYFYAIKEIMIGGRCVCNGHAVTCDILEPQRPKSLLCRCEHNTCGDMCERCCPGFVQKQWQAATAHNNFTCEACNCFGRSNECEYDAEVDLNKQSIDSQGNYEGGGVCKNCRENTEGVNCNKCSFGYFRPEGVTWNEPQPCKVCDCDPDKHTGACAEETGKCECLPRFVGEDCDQCASGYYDAPKCKPCECNVNGTIGDVCLPEDGQCPCKAGFGGTFCETCADGYTNVTAGCVECVCDATGSEHGNCSASTGQCECKPAYAGLSCDKCQVGYFGDDCKFCNCDPMGTEGGVCDQTTGQCLCKEGFAGDKCDRCDIAFYGYPNCKACACDGAGITSPECDATSGQCPCNGNFTGRTCDKCAAGFYNYPDCRGCECLLSGAKGQTCDSNGQCYCKGNFEGERCDRCKPNFYNFPICEECNCNPSGVTRDFQGCDKVSPGELCSCRKHVTGRICDQCKPTFWDLQYHHEDGCRSCDCNVNGTISGLNTCDLKTGQCMCKKNADGRRCDQCADGFYRLNSYNQMGCESCHCDIGGALRAECDITSGQCKCRPRVTGLRCDQPIENHYFPTLWHNQYEAEDAHTEDQKPVRFAVDPEQFADFSWRGYAVFSPIQDKILIDVDITKATVYRLLFRYRNPTSVPVTATVTINPRFTHTHDVEQTGKATFAPGDLPAMKEITVDGKPFVLNPGKWSLAISTKQRLFLDYVVVLPAEYYEGTVLRQRAPQPCLSHSTKNTTCVDLIYPPIPSVSRQFVDMDKVPFNYINEDGTTTALEHVPVEILLSEITGPAAFVRADENPRVVEAKLDVPETGEYVIVLEYHNREETDGNIGVGISQNDKEVLNGNAVIHHCPYATFCRELVSSEGTIPYIPLEKGEATVRLNIKPNHEFGLAGVQLIKKSDFSSEYLQQVPVCIKKDARCVQQSYPPAADSVTTEAESGSNMDKSILGDKLPFPVSNSKEMRVVPLDDAQATVEISGVVPTRGHYMFMVHYFNPDNTPINIDVLIQNEHYFQGDSCNSFACSSVPLAFCPSISGCRALIRDKERPEVIQFYMDDKYTATFYHNSSQKGPIYIDSITAVPYNSYKDKLMEPLALDLSNEFLKECSEDNLKNHPESVSDFCKQKIFSLTTDFNAAALSCDCVAQGSESFQCEQYGGQCKCKPGVIGRRCERCAPGYYNFPECIKCQCNAGQQCDERTGQCFCPPHVEGQTCDRCVSNAFGYDPLIGCQKCGCHPQGSEGGNLVCDPESGQCLCRESMGGRQCDRCLAGFYGFPHCYGCSCNRAGTTEEICDATNAQCKCKENVYGGRCEACKAGTFDLSAENPLGCVNCFCFGVTDSCRSSMYPVTIMSVDMSSFLTTDDNGMVDNKDDTVIYTSEETSPNSVYFNVPIEKKDYTTSYGLKLTFKLSTVPRGGRKSMNADADVRLTGANMTIEYWASEQPTNPEEQFTVKCKLVPENFLTAEGKTVTREELMKVLHSLQNITLKASYFDHPKTSTLYEFGLEISEPNGVDSVIKASSVEQCQCPAPYTGPSCQLCASGYHRVQSGSFLGACVPCECNGHSATCDPDTGICTDCEHNTNGDHCEFCNEGHYGNATNGSPYDCMACACPFAPTNNFAKSCDVSEEGQLLQCNCKPGYTGDRCDRCASGFFGHPQISGESCSPCQCNGNNNLTDSRSCHPNSGDCYLCEQNTDGRHCESCAAWFYGDAVTAKNCSSCECSQCGSQYCDNKSGGCECKINVEGDSCDRCKPDHWGFSKCQGCQGCHCGTAAFNTQCNVENGQCTCRPGATGMRCEHCEHGYWNYGEHGCDKCDCEADLSMGTVCDVRTGQCHCQEGATGSRCDQCLPSYLRIPTYGCRRCDECVHHLIGDVDNLELEIDVLGTAIANISSATIVGARLARNKKEFNDINEITKMLNDEENSFGNVFGDAQDILTNSTQIQNKLVRTKTHSQNSVSSAKNITLNGTEFLQEVMKRAQRARQSVRSLAEIALAIGSSSKAVNVDPRLLKEAEETLMTLEAASADQYPEKAQTVPGKLEEIQKKIQEETEKLDKQKETFEAQKKRAEELAAYLNSAQQLLKESKSKADKSNNIAKMLQLTKVENLVAAITDDLERVEAAKGEFQKLNVAIGNITENLKDKREEMTHAVTTLNETRNDVAEALEAAKKRVRRDEKSVDMQLVNAKAHELHLQATTLRQTFDNNKDNTDQAVEAANAFSNLTDTLKNAKAQIDNAYEALSAEPAFAESVQNARDKPFPDETKEKIDALSKTVSQDLKETEKLKKQLEQLTELSEKLRKRKEAVKAGIPKYSKNTLDSIDEKVQEVEKLKAEIDANIEETRAKISEIAGKAEEITEKANSAMEGIRLARRNSVQLNKLAPVIVSKFEELKKLSSARSAKVDSVSDKVSQIKEMIAVARDAANRIKLGAHFEKGSSLDLNIPQRVTRSAAHADISFYFRTEQEHGIPLFFGNEETAVGSRAVPTADYVAAEIEYGRPKITVDLGDAPAVVKLDTPVNDGLWRRLNIERIGKTVSVTLSKPNSVETAETKSSVAGGNKSVLNLNQQISRLFVGGVPTSARISKDLYNRDFVGDIESLKLHGEPIGLWNSREKGNTNVNGAQKKPKITDNADELVVSLDGEGYTSYKPSHWNPRKATKISLSFLTFSPHGLLFFVGKDKDFMALELSDGGVKLSVDLGSGVGQWITESSNYNDGKWHTVSIVREEKHVKIMIDGETEVLEGDVPGKDSEMSVTEFLYIGGTPSGLSVRTTIVPLRGCIKSVKLGSDNVDLESSHASKGVRSGCPLHSVRTVSFLSDRTTASFNNATEFSEDVSVTFKFKTRSIRQPSSLFTVNDDEDSVLSVSINEDGILTVTSGEDIATLELAASPDEKWHYVSIRKTKYIIRIDADDSFSNEVARKHADDSNPDASFLSAFFGKSGETPSFVGCIGDVTLNGKLLDFANSEIKEISLNGCSLSDDENISTTTTAAPKPTDDSDVAVLPIDEEEESTTTTTTTTTEEPTEEPAEARPDGHCSLPEDPMVQFEDAEGFNFGSQQYSRIEYDILPEAIDKSGEFTFKIRPTSDNGIIFIATNKRTDHIAVMLEHGRVVFTYDTGSGQVIIKSDKSIIDGRWHTIKVSRRGKSAHLIVDDNSYESEGAANQNEDLIETQPPFYVGGVPADLAGFARNLVVGVRSQFSGCIKDFKLNGKSLDNGKEFGTEQCSQFSEPGMYFGKDGGYAIVQKDYEVGLTFGLEVEMRPRMKNGILFSVGVLEYITVEFVNGSIKTTVESGSGGEELWHHPDIENQYCDGQWQSFKISKKRNLLTVAVNGKAHLKILKKAKTDVLTKDPLYFGGLPEGVTNKGIKTNKPFVGCIRFVSFGLKKDRKIRRKKQVDTERFDVFGDVHRNACPAI
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
121N-linked_GlycosylationAANMVDGNNSWWMSP
CCCCCCCCCCCCCCC		34.5917761667
140N-linked_GlycosylationGLQHNEVNITIDLEQ
CCCCCEEEEEEECHH		21.36-
249N-linked_GlycosylationATSEALQNFTRATNV
CCHHHHHHHHHHHHH		40.9017761667
351N-linked_GlycosylationQAATAHNNFTCEACN
HHHHHCCCCEEECCC		24.6017761667
477N-linked_GlycosylationKPCECNVNGTIGDVC
CCCCCCCCCCCCCEE		28.0917761667
511N-linked_GlycosylationTCADGYTNVTAGCVE
CCCCCCCCCCCCCEE		22.21-
530N-linked_GlycosylationATGSEHGNCSASTGQ
CCCCCCCCCCCCCCC		20.62-
634N-linked_GlycosylationGQCPCNGNFTGRTCD
CCCCCCCCCCCCCCC		19.8117761667
761N-linked_GlycosylationRSCDCNVNGTISGLN
CCCCCCCCCCCCCCC		28.0917761667
1014N-linked_GlycosylationCLSHSTKNTTCVDLI
CCCCCCCCCEEEEEE		40.4817761667
1341N-linked_GlycosylationYTATFYHNSSQKGPI
CEEEEEECCCCCCCE		31.7917761667
1705N-linked_GlycosylationDVRLTGANMTIEYWA
CEEECCCCEEEEEEC		29.4917761667
1756N-linked_GlycosylationKVLHSLQNITLKASY
HHHHHHHCCEEEEHH		34.2117761667
1868N-linked_GlycosylationCNEGHYGNATNGSPY
CCCCCCCCCCCCCCC		36.10-
1944N-linked_GlycosylationCQCNGNNNLTDSRSC
CCCCCCCCCCCCCCC		48.6017761667
1986N-linked_GlycosylationGDAVTAKNCSSCECS
CCEEECCCCCCCCCC		28.56-
2002N-linked_GlycosylationCGSQYCDNKSGGCEC
CCCCCCCCCCCCEEE		36.51-
2159N-linked_GlycosylationVLGTAIANISSATIV
EHHHHHHHCCHHHHH		28.67-
2207N-linked_GlycosylationDAQDILTNSTQIQNK
CHHHHHCCCHHHHHH		39.3517761667
2231N-linked_GlycosylationNSVSSAKNITLNGTE
CCCCCCEEEEECHHH		31.9917761667
2235N-linked_GlycosylationSAKNITLNGTEFLQE
CCEEEEECHHHHHHH		46.8417761667
2401N-linked_GlycosylationKLNVAIGNITENLKD
HHHEEECCCCHHHHH		31.7117761667
2421N-linked_GlycosylationTHAVTTLNETRNDVA
HHHHHHHHHHHHHHH		46.64-
2487N-linked_GlycosylationEAANAFSNLTDTLKN
HHHHHHHCHHHHHHH		40.2717761667
2638PhosphorylationIRLARRNSVQLNKLA
HHHHHHCCCCHHHHH		14.9321082442
2821N-linked_GlycosylationKSSVAGGNKSVLNLN
CCCCCCCCHHHHCHH		32.29-
3087N-linked_GlycosylationRTTASFNNATEFSED
CCCCCCCCCCCCCCC		46.35-
3242N-linked_GlycosylationCSLSDDENISTTTTA
CCCCCCCCCCCCCCC		40.27-
3541N-linked_GlycosylationYITVEFVNGSIKTTV
EEEEEEECCEEEEEE		43.76-
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 EPI1_CAEEL !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPI1_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 EPI1_CAEEL !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EPI1_CAEEL !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPI1_CAEEL

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditiselegans and suggests an atypical translocation mechanism for integralmembrane proteins.";
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,Taoka M., Takahashi N., Isobe T.;
Mol. Cell. Proteomics 6:2100-2109(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-249; ASN-351;ASN-477; ASN-634; ASN-761; ASN-1014; ASN-1341; ASN-1705; ASN-1756;ASN-1944; ASN-2207; ASN-2231; ASN-2235; ASN-2401 AND ASN-2487, ANDMASS SPECTROMETRY.
"Identification of the hydrophobic glycoproteins of Caenorhabditiselegans.";
Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H.,Mahuran D.J.;
Glycobiology 15:952-964(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249; ASN-351; ASN-761;ASN-1014; ASN-1341; ASN-1756; ASN-2231; ASN-2235; ASN-2401 ANDASN-2487, AND MASS SPECTROMETRY.
"Lectin affinity capture, isotope-coded tagging and mass spectrometryto identify N-linked glycoproteins.";
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,Kasai K., Takahashi N., Isobe T.;
Nat. Biotechnol. 21:667-672(2003).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, AND MASSSPECTROMETRY.

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