ROL3_CAEEL - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ROL3_CAEEL
• UniProt AC: Q8I7I5
• Protein Name: Protein roller-3
• Gene Name: rol-3
• Organism: Caenorhabditis elegans.
• Sequence Length: 2481
• Subcellular Localization: Membrane ; Single-pass type I membrane protein .
• Protein Description: Thought to have a role in developmental establishment of posterior morphology..
• Protein Sequence: MLSLHLRSLAILFLLFFLLHDVVKSATVFSSSLKTCQSQCEERNLAYPLDSGEVHWTGLAEYNYSSRISSCRHGCEDVDERESKCDVKCSEEGIVSNACKQGCRAVLVSFLAQAQALLIQVHVNMEVLETSMKLKWEFPETLAEELKEIANADIFWFSQTKPLNGILGWRWTSLPQNSFRNSSLSSEVHVPFEHGEHVEVRLALSYRNQVLVSRTTTYHLPLSKSGTTLEVIGQLQLSDDRVAVCYRTNQPTPKFKLTIMTLNDNTINTEESIARCHLFSNLPRDNCCKASISAIDEHGATTAFVEIKLDFYVNQVEIELVSVASSRLIFSNGTHLLESEIDQYALGDSATVIPFPLPTDDTITAIAGISDTTIAIGSSKGSLWTYQMSANQTDEDQPSSVIQLKTVGEMDTKINQIEIDHIQRTLYAVQHDKGIIRCKLRTMEAEESPNCVLIVNNDALNAPKEITLDSVNGHVYTLNADNKVYRTEMVAFNATGIETVASLQYLQDMSPSNGIFFDVSKFLLYSALQNGSMMTLNPVTDHVHIFKDVGYADIQHFRIKNDLIYWMKKKCGETDADENCIFAENLQRSEEDIPNKFTYSSSLMSFGVLEEILLKPRITAVSTIAMLTSDKTARVSWDESNTLPFQAQGSSWRNFTYFLKVTAPDITDFSPIEIYTSNTEMKIDVTPGNIYNAQVQVCSDDFCSIPTSTSNTALPDLGDVVPFVFTKRQADDIISVDILGNIIPADDSVKIVEKLQYPHVLDNTTKTVYLAGDHSMGIFKKYLDDTAGLPKPFKDGLFVEMMSIMPARSIILIASSYKITSYRLPTTFDFEYFSCEEPLEACSEVMGISSDDTTGMVHFLTQARNGTITLWESDPENRTPRDIASVPSIVPFRRFLILHDKMILVTKNNHIVQTDKKLKVVNVATELERVDHILPLRYATISHKIEFSDEIKFIDGSKTNLQWTLSPPLEAGTVLFKVSIFREKMGGQDPPIITIQSETNFTIPSEVLEAWSSAQRFDVSVQAMTPWATAVLNRTGLTAPVKPPTSPTQLRIFATQQKTVDGPRALISFFWGPPSEWNGTPYQYIVNCTKDDGSWIGGPVTTSQSHYSFAVKSGKVSCQAAAANEPTNIGSFSELITIDSSELKPLVKLFAIDSTNSLISINDLAHEEPRRETRQVAQPVKLEYQAMAFIGEDLYAVRKEGESAQPVLVQIDTNHIDNTVHKVSIGGDVTRIDAMTSDWVGNRLIFVAGTNVYQLSLEPFLSTSLLNPHKLIQLTSATDAKQLAYDPFMNTAYLLTKNGSLFALDMNKNTEANLALTVSCLASQTVTWMMTEFAWNRASSPKIYALTWNGLIYVDLTEDSQCNEVRIDWTKFGDKGLKDISSFAIADKLFAFVTSSEMLIYGKDTVTPITIANPPLKQILAVSQSSQPYPERSCFELPSSKGIVFSIVNEGKTGSFLEVTKSSSSSSCQEVSMPQTQYEIYFTRKNTDKVKHVRSFSDRIHVENGILDKETDYDVTVTWLNRYSPASGVSASKSFRTGFGYPSAPRDPHAIPVTPDTVYLYWNLPETLNAPISEIKYKISQQAAGISVPTSIAVIALSETVSSNISSDTTSCLINPCRVKIANLRPSNEYKFWVTATHISHLDAATILKDDDAVSSEAVARTLDVPGTLRPDNVTGSSLLLRWNGLEPEHRPSSIAVQYRESGGANNEWQFPMNVSFEPDVTTELVPITNLLSATSYDYRFVATYTGTYTIDGKVLAFKEDYLQLPQQARTKAGVPTAPQFVEAKQDEEGWIVTWKEPMSDGGSPITSYAVETRINKTAEWEIAERGLDGWKTWWRPGKSDTTSSTSTSSTEVSEFRIRAANIEGFGAYAYTEDKKEEKEEEPSSVLPYLLLLSIIFLLAAMILVACFWLKSRRRQQQKKREAEDERNCIRLDVVANMNFSSSHQSLPPEYESEMRNLPVVNYSTVTFNDYIDTCAYGIVHSGTAEEVPMSWEKDVRVAIKKLKPNHSFQEKMMFMKEAILLNNLDHPNIVKELGVCITPGQELILLEYMEGGNLLKFLQKSTPNEYQSSELSPRDLLSISVDIARGMNYLERLPHVHKNLSARKCLLAGRPGVTKLEMGMSKELSNGQVNRSDLENMEIVRWMAPEVLKDFQFSSKSDVWAYGVLLYEVFSFGEVPYGDKDNRRIMTDVRNGSVLPIPSYCPSKRIYKVIKQCLTSDSTKRANFATILKIFETFRDDQKCQDDKPIQFNDGTDNTNFSASQDSTSSREPPSPSHRMRDFIDTRDLEPPSPSHLNQSFGGFEHPYEGERPATMWNGSGARNSAKNSIGRSMKKEKLRNPIHSMDDLVARNQRPLSIHSEDTESTDYGASSSMYSPGSSNRISSQVDPPIGRLSSAPGIGIVNDAFESSNPSLNLSRSWAGLSREVNQNPAGAGSSGTLPQHTNSAGHLRLPGVQVGAGGGRVYRNASGGGGPSNRGRISQV

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
63	N-linked_Glycosylation	WTGLAEYNYSSRISS EEEEEECCCCCCCCC	23.01	-
181	N-linked_Glycosylation	LPQNSFRNSSLSSEV CCCCCCCCCCCCEEE	33.66	-
332	N-linked_Glycosylation	SSRLIFSNGTHLLES CCEEEECCCCCCHHH	48.94	-
391	N-linked_Glycosylation	WTYQMSANQTDEDQP EEEEEECCCCCCCCC	37.67	-
493	N-linked_Glycosylation	RTEMVAFNATGIETV EEEEEEEECCCCHHH	27.19	-
530	N-linked_Glycosylation	LLYSALQNGSMMTLN HHHHHHHCCCCCCCC	45.41	-
654	N-linked_Glycosylation	AQGSSWRNFTYFLKV CCCCCCCCEEEEEEE	27.61	-
763	N-linked_Glycosylation	QYPHVLDNTTKTVYL CCCEECCCCCCEEEE	45.55	-
865	N-linked_Glycosylation	HFLTQARNGTITLWE EEHEECCCCEEEEEE	55.78	-
1000	N-linked_Glycosylation	ITIQSETNFTIPSEV EEEECCCCCCCCHHH	28.19	-
1033	N-linked_Glycosylation	PWATAVLNRTGLTAP HHHHHHHCCCCCCCC	32.63	-
1087	N-linked_Glycosylation	TPYQYIVNCTKDDGS CCEEEEEEEECCCCC	20.41	-
1298	N-linked_Glycosylation	TAYLLTKNGSLFALD HHHHCCCCCCEEEEE	39.80	-
1604	N-linked_Glycosylation	LSETVSSNISSDTTS EECHHHCCCCCCCCC	30.56	-
1673	N-linked_Glycosylation	PGTLRPDNVTGSSLL CCCCCCCCCCCCEEE	35.61	17761667
1714	N-linked_Glycosylation	NEWQFPMNVSFEPDV CCEECCCEEEECCCC	26.90	-
1816	N-linked_Glycosylation	YAVETRINKTAEWEI EEEEEECCCCCCHHH	32.13	-
2342	Phosphorylation	KLRNPIHSMDDLVAR HHCCCCCCHHHHHHC	25.32	28854356
2393	Phosphorylation	DPPIGRLSSAPGIGI CCCCCCCCCCCCEEE	24.08	28854356
2394	Phosphorylation	PPIGRLSSAPGIGIV CCCCCCCCCCCEEEC	42.97	28854356
2442	Phosphorylation	SGTLPQHTNSAGHLR CCCCCCCCCCCCCEE	26.14	28854356
2444	Phosphorylation	TLPQHTNSAGHLRLP CCCCCCCCCCCEECC	36.46	28854356

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

Oops, there are no upstream regulatory protein records of ROL3_CAEEL !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ROL3_CAEEL !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ROL3_CAEEL !!

Protein-Protein Interaction

Oops, there are no PPI records of ROL3_CAEEL !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-1673, AND MASSSPECTROMETRY.
PubMed: 17761667