UniProt ID | LRP_CAEEL | |
---|---|---|
UniProt AC | Q04833 | |
Protein Name | Low-density lipoprotein receptor-related protein | |
Gene Name | lrp-1 | |
Organism | Caenorhabditis elegans. | |
Sequence Length | 4753 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein. Membrane, coated pit. |
|
Protein Description | May act as a receptor for the endocytosis of extracellular ligands such as chylomicron remnants, protease-inhibitor complexes and vitellogenin.. | |
Protein Sequence | MILRLLIFTALAVTTANSSTRQQSTFHSIQVDSPPSVRSRIISASVNTASSVCNENDFRCNDGKCIRTEWKCDGSGDCSDGEDEKDCPHPGCKSDQWQCDTYTWHSVSCIAEYQRCDNITDCADGSDEKDCPASTVDCSSQNVFMCADGRQCFDVSKKCDGKYDCRDLSDEKDSCSRNHTACFQYQFRCADKTQCIQKSWVCDGSKDCADGSDEPDTCEFKKCTANEFQCKNKRCQPRKFRCDYYDDCGDNSDEDECGEYRCPPGKWNCPGTGHCIDQLKLCDGSKDCADGADEQQCSQNLCPSLGCQAGCHPSPHGGECTCPSGYKLDDRFHRTCSDINECAEFGYCDQLCANHRPGFTCSCLGDCFTLQMEHGPGKDNLTMRGYCVSNNADKMKLFVARREGLYRLNPKNPDEEVKKLASGEFIYGIDFDYGDRKIFWTDRLAHSAFSADVDDEGEISQIKKLSLKSLVYPRCLAVDWITNTLYIIESGSRRIDVSSYDGERRTVLLADGLTLPLDIALDPLRGEMFFTNQLKLEAAAMDGTNRRTLVNTHTHQVSGIVVDITAKRVYWVDPKVDRLESIDYQGNDRRIVAQGMNVVPHPFGLALFDQYLYWTDWTRLGVIQVEKFGSDTKLLWSNTENNVFPMGISAYHPMAQPGPGQSECLAMKIENPCTNADCEGMCILSKDNGGFGVGYKCACPIGQKLVNGKRCIDSIDYLLFSSNKIVRGIFPEINEKALAEAVLPISPISQRRIGMYFEVECDVHGNSFFYADIMDNTIYRIRPDGEGAAPVLVTHNDGLFSMSFDWISKQLYYVDNIRNSLEVVKIGETGLVHPDELVRRQLITELRDPVSVVVHPWKGLLFYAEAMRPAAIYRCHIDGQNCQVIRNTTLGRPSEMAIDFAENRLCWGDTLLKTISCMDFDGKNVVKLDIDNPIPVAITIMNEYIYYVHQRPYSIRRVHKKNGGGSKIVREFGADERSIFSLKACSHQNQPIPDDSREHPCRASQCTQLCFATPSESHPNELEAKCACRQGFMINKENNHSCQKDPAEKIEQLCSSNSTQFQCKNGRCIPKEWKCDGENDCLDESDEIDEKGDKCFHETECAENTIKCRNTKKCIPAQYGCDGDNDCGDYSDEDVKYCKDGQKPVCAAKKFQCDNHRCIPEQWKCDSDNDCGDGSDEKLEMCGNATCAANQFSCANGRCIPIYWLCDGDNDCYDGTDEDKERCPPVQCSALQFRCANGRQCVPLRNHCDGQSDCEDGSDEDSCAVTAESCTPDQFKCVSSGLCIPASWKCDGQQDCDDGSDEPKFGCTSGRQCSSDQFKCGNGRCILNNWLCDGENDCGDGSDESSERGCKTSMNARKCPFEHVACENDQETCIPLHQLCDGKTHCPGGTDEGGRCARDLCSADRAGCSFKCHNSPNGPICSCPFGEQLVNKTKCEPENECLDSSSCSQRCKDEKHGFTCSCDEGYELDVDKRTCKVADNVKDTRIYVSNRNRIYYSDHKLDNWHTFGAIVENAIALAWDSLTDRIYWSDIREKKILSANRNGTNATVFIADGLDITEGIALDWVGRNLYWVDSSLNTIEVANLEDPKQRTLLVHQNVSQPRGIAVDPRKGVMFWTDWGQNPCIERASMDGTDRQIIVKTKIYWPNTIALDYTTDRVYFADSKLDFIDFVNYDGSGRTQVLASSKFVQHPHALAIFEDMMYYSDRRLQKLQVYPKYPNGTTSEYPSHTFSKALGVVAVHPVLQPVIKNNPCSTNPCSHLCLLNNKNTFTCKCPMGEKLDASGKKCIDDAKPFLVIIQKTNVFGIEMNSASEKETPVLAGMVPLSGLGNAFDAAYDALSEEMFILEHTNHAKTLAQITTDSAIYRSTVNGGNKTKMFSSAVPDDAYCLGFDWNGRNLVVGNKITQTIEIIRTQGKQYRSVILSNDQSPTAVVTPVAIAVDADKGYVFWLDRGGGAADAKVARAGLDGSNPLVIASNDLAELDHIAIDTTNTRVYFSEAKAGRISSVTYDGQDRHYVLSDGGRQPNGLAFYGDRLFYADSAFDSIEVATINGDSQPPQWTHFKKDVENLANIKALQPRASSSGHPCHINNGNCDHICIPLMFAQRTCTCANGYVKDGQTSCKLFDESFVIVATKTKVIGYPIDETQSKGVAMEPIGGLSITGVDYDYESKTIYVAEASGINKGITAYTIGESSPRAVIRDSIGSLTIKSLAIDWINYNMYFINHDAERTNIEVSKLDGTYRKILLTTKTETPSSIAVDPVSRYLYWADQGQKPTIQRSFLDGSRREVIVSSGIAEPTDLVVDVASKMIYWSDAKMDGIYRVRSTGGTPELVRSDIASAAGVALHGQNMYWTDNRLEKLFRATSKPNQTSLLLSPTTVAASLKDIGDVAVFSSNNQPRASSPCQITDNLRKSPCTQLCFATPGTQTPTCSCARGVLKGRTCEEPDTYIMFSDGDKIIDVAIEPDVKASRPLKDPFPEISNLQTFDVDVNLRRVYFVVESPVGVNISWFSMNNAENPRLVFGASKQPHAKEIRHISDMKLDWLTQKIYFTTGRGGKVMAIDTAGEHLSTIASGDWTYALAIDPCSGLLFWSDSGYKTSGGLYEPRIERSNLAGGSRKVIVSESISLPAAIAVDFRNQKIYWADVNRLNIEVADYDGQNRKVIASGYRAKSLDIWDRWLYMSDPLSNGVFRIDKESGSGLENVVSDRRIPGALRVFASESDVRTRNQVCNALTSQLCKTDNGGCDQLCTVVADDIGLAASKVQCSCNDTYELVQEPGKDYPTQCVLRGSNSEPAKECLPPYNFQCGDGSCILLGATCDSKPDCADASDENPNYCNTRSCPEDYNLCTNRRCIDSAKKCNHIDDCGDGSDELDCPSAVACAEGTFPCSNGHCINQTKVCDGHNDCHDEQVSDESLATCPGLPIDCRGVKVRCPNTNICIQPADLCDGYDDCGDKADENQLFCMNQQCAQHYVRCPSGRCIPETWQCDGDNDCSDGWDETHTNCTDTAGKKICVGDYLFQCDNLKCISRAFICDGEDDCGDGSDEHSRHGCGNRTCTDQEFHCTSNAKLAQPKYECIPRAWLCDGDVTCAGGEDESTELCKTEKKECNKGEFRCSNQHCIHSTWECDGDNDCLDGSDEHANCTYSSCQPDFFQCANHKCVPNSWKCDGNDDCEDGSDEKDCPKNSASAQKASKCSNGQFQCTSGECIDDAKVCDRNFDCTDRSDESSLCFIDECSLAEKPLCEQKCMDMKIGYKCDCFEGFAIDISDQKSCHNVNECYEGISGCSQKCDDKIGSYKCGCVDGYQLSSDDHSCKRTEMEPEPFFLLANKHYIRKISIDGNKYELAAQGFDNVVSLDIDLTEKKAYLIDQGKLRLLRVDLDEMDSPLSSYETVLRHNVYGTEGIAVDWVGRKLYMLNRQERSIRVCELDGRFCKTLIRDRIQQPKAIVVHPGKGYLFFTEWSLQPYIGRIALDGSPELQDPIFKLAEHDLGWPNAIAIDYFSDRLFWGDAHLNEIGFMDFDGNGRRHIPAQRTSHVSSMVVFDDYLYWADWNLREVLRCDKWTGKNETILKKTVQLPNDLRIVHPMRQPAYPNPCGDNNGGCSHLCLIGAGGNGYTCSCPDQFVLLSDQKTCEPNCTERQFACGGDDAKCIPKLWYCDGEPDCRDGSDEPGESICGQRICPVGEFQCTNHNCTRPFQICDGNDDCGDSSDEQNCDKACDPWMFKCAATGRCIPRRFTCDGDDDCGDRSDEADTLCMSAERNCTAEEFRCNNNKCIAKAWRCDNDDDCGDGSDETPECAQIECKKGWTRCSSSYRCIPNWAFCNGQDDCRDNSDEDKQRCPTCDDVGEFRCATSGKCIPRRWMCDTENDCGDNSDELDASCGGTTRPCSESEFRCNDGKCIPGSKVCDGTIQCSDGLDESQCTLRRCLPGHRQCDDGTCIAEHKWCDRKKDCPNAADELHCEDVSRRTCSPFEFECANSVCIPRKFMCDGDNDCGDNSDETSSECRSAQCDPPLRFRCAHSRLCLNILQLCNGFNDCGPNDFSDEHLSMCSSFSEYGDCSSDQFKCANGKCVNGTVACDRKDDCGDASDEIGCSKHGGKTSCEAFGNNGGCKHICTDVRDGFYCHCRDGFRPDPQSPKECIDIDECAGNNTCTQLCLNTKGSYLCRCHEDYENNVVVGSMTGKDCRAKGDAANVMIGADDSLVQLSLHGSGTNRHAAAKANDDDNDIIGIAFDPRKELMYWIDGSERTIYRSAIANGNQSHEGQKLDVDFAAMGVVPTAIAVDYTTGNLFIAAVSENIENGLVTARKKRMSEPIDNQNTGFIFVCLPDGRYLKKIVAGHLQQPTALITAPSAGRICYSDAGLHAKIECADMDGTHRQIIVKDLVFSPTSMAIDEGKGNRIYWVDPKYRRVDAVNIDGSERTTVVHDRHIPYAVDVFENHIYWLSRESKTLYVQDKFGRGRVSVLASDLEDGHTVRVSQKYAKDTQRTVSGCERAQCSHLCVSLPSTGFACLCPDGIVPQLDGSCATQHVEALTMPKQCKCTNGGKCRLDGSCECTSDFEGDQCEKESSVSRKIIGTLSENFITVLLYILAFLFAFGLIGFCALNLYKRRQLLFKKNEAADGSVSFHGNVISFSNPVLENKQDAPGSEFNMQQMTSMHDDSTTFTNPVYELEDVDMSSPPPSNDQPSTSASAMSPNRPSTSAASSFVPPTFDQDEIELKTADEIIVPKAEISKPPIPARPKKEKADPLRVDNPLYDPDSEVSDV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
17 | N-linked_Glycosylation | ALAVTTANSSTRQQS HHHHHCCCCCCCCCE | 34.11 | - | |
118 | N-linked_Glycosylation | AEYQRCDNITDCADG HHHCCCCCCCCCCCC | 42.56 | 17761667 | |
178 | N-linked_Glycosylation | EKDSCSRNHTACFQY CCCCCCCCCCCEEEE | 22.14 | 17761667 | |
380 | N-linked_Glycosylation | EHGPGKDNLTMRGYC CCCCCCCCEEEEEEE | 40.68 | - | |
544 | Phosphorylation | EAAAMDGTNRRTLVN HEECCCCCCCCEEEE | 22.68 | 19530675 | |
887 | N-linked_Glycosylation | QNCQVIRNTTLGRPS CCCEEEECCCCCCCH | 26.70 | - | |
1039 | N-linked_Glycosylation | FMINKENNHSCQKDP EEEECCCCCCCCCCH | 29.55 | - | |
1057 | N-linked_Glycosylation | IEQLCSSNSTQFQCK HHHHHCCCCCCEECC | 32.55 | 15888633 | |
1184 | N-linked_Glycosylation | EKLEMCGNATCAANQ HHHHCCCCCCHHHHH | 27.44 | - | |
1431 | N-linked_Glycosylation | PFGEQLVNKTKCEPE CCHHHHCCCCCCCCC | 55.67 | 17761667 | |
1542 | N-linked_Glycosylation | KILSANRNGTNATVF EEEECCCCCCCEEEE | 62.54 | 17761667 | |
1545 | N-linked_Glycosylation | SANRNGTNATVFIAD ECCCCCCCEEEEECC | 34.70 | 17761667 | |
1597 | N-linked_Glycosylation | RTLLVHQNVSQPRGI CEEEEECCCCCCCCE | 22.11 | 17761667 | |
1718 | N-linked_Glycosylation | QVYPKYPNGTTSEYP EEECCCCCCCCCCCC | 58.30 | 17761667 | |
1871 | N-linked_Glycosylation | RSTVNGGNKTKMFSS HEECCCCCCEEEECC | 50.66 | - | |
2364 | N-linked_Glycosylation | FRATSKPNQTSLLLS HHCCCCCCCCCEEEC | 62.59 | 17761667 | |
2501 | N-linked_Glycosylation | VESPVGVNISWFSMN EECCCCCEEEEEECC | 19.35 | - | |
2762 | N-linked_Glycosylation | SKVQCSCNDTYELVQ CEEECCCCCCHHHCC | 28.50 | 17761667 | |
2888 | N-linked_Glycosylation | CSNGHCINQTKVCDG CCCCEEECCEEECCC | 49.19 | - | |
2996 | N-linked_Glycosylation | GWDETHTNCTDTAGK CCCCCCCCCCCCCCC | 21.06 | - | |
3046 | N-linked_Glycosylation | HSRHGCGNRTCTDQE CCCCCCCCCCCCCCE | 39.92 | - | |
3134 | N-linked_Glycosylation | DGSDEHANCTYSSCQ CCCHHCCCCCCCCCC | 22.14 | - | |
3557 | N-linked_Glycosylation | CDKWTGKNETILKKT CCCCCCCCCCHHHHE | 53.65 | 17761667 | |
3626 | N-linked_Glycosylation | DQKTCEPNCTERQFA CCCCCCCCCCCCCCC | 24.05 | - | |
3682 | N-linked_Glycosylation | EFQCTNHNCTRPFQI EEEECCCCCCCCEEE | 30.81 | - | |
3752 | N-linked_Glycosylation | LCMSAERNCTAEEFR HHHHCCCCCCHHHHC | 20.99 | 17761667 | |
4063 | N-linked_Glycosylation | CANGKCVNGTVACDR ECCCEEECCEEEECC | 50.30 | 17761667 | |
4139 | N-linked_Glycosylation | DIDECAGNNTCTQLC CHHHHCCCCCHHHHH | 23.32 | - | |
4248 | N-linked_Glycosylation | RSAIANGNQSHEGQK EEHHHCCCCCCCCCC | 39.73 | 15888633 | |
4744 | Phosphorylation | LRVDNPLYDPDSEVS CCCCCCCCCCCCCCC | 27.04 | 30078680 | |
4748 | Phosphorylation | NPLYDPDSEVSDV-- CCCCCCCCCCCCC-- | 45.33 | 30078680 | |
4751 | Phosphorylation | YDPDSEVSDV----- CCCCCCCCCC----- | 28.71 | 30078680 |
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 LRP_CAEEL !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LRP_CAEEL !! |
* 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 LRP_CAEEL !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of LRP_CAEEL !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"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-118; ASN-178; ASN-1431;ASN-1542; ASN-1545; ASN-1597; ASN-1718; ASN-2364; ASN-2762; ASN-3557;ASN-3752 AND ASN-4063, AND MASS 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-1057; ASN-1597; ASN-1718AND ASN-4248, 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-118, AND MASSSPECTROMETRY. |