HMR1_CAEEL - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HMR1_CAEEL
• UniProt AC: Q967F4
• Protein Name: Cadherin-related hmr-1
• Gene Name: hmr-1
• Organism: Caenorhabditis elegans.
• Sequence Length: 2920
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cell junction, adherens junction . Cell junction . The basal to apical translocation from the cell membrane to adherens junctions is determined by the coupled sumoylation and desumoylation state o
• Protein Description: Cadherins are calcium-dependent cell adhesion proteins. [PubMed: 25938815]
• Protein Sequence: MSWNILLILLISNLDEVLAKTLLKLPSNAPPGWLISDLQFQNLIGDSEIATLQPSIFSTNFEVEDGYRIITNTTVTQFHGELFELFLNVKEQNFQRLVTLHVYVDPRGTSQQPATFLSTVYHATVYTSQQPGSTVVFSKPITVRNRKNFVISPISKIDKISKYSSPFSVMTRGKSVDIVMMKQKLEEDDITRHVIFLGAFTEKTGEMIAQTKVIIDVIDSGDVHFLLKSKKSIAKFASAIPANSTVFDVEKRNLSEPLLFHLEEPSRFFKIDQFSGRVSTVLPVGYGTYHIHVVARNQKKQRSDAWLEISVKKEQKLEPMTSSRSRRHLDDIVFRIPENTTMEDIEKKDMKIPLFAGETIGEINVAKEWLKIDDDGKIHLLKPLNYEKTSSIIATVPINGLQSTRTQTIRIHVADIDEPPSFVNSPLPMLAVVPLNPTIGRIVYQFVARDEHGDGDSNVLYKTIDVIPAGSFIVDPKSGVVRTGWSKYERGDTYRISAQAMDLSPSDNTTSQLSEVAILEILADERPPQFAKQEYEVTVSEDNLVDYSVVDVKAQSFRSFEDGRSKGPITYSLEGDTPEDETKWFRIDPSTGIIHLTRLLDFDDPALPKLHKLKVTAREDNRESHVDLTIRIDDVNDNVPTFTRPLYTAQVREDIPLNQTILKVTAVDKDTGDNSRITYSVDNHNFSINSNGEISAKVRLDADQLNERHFVYRFNVTARDHGEPVSLSSSAMIHIRTENTNDESAVFLPTSQYTAFVAEDAQGGTPVIQIQARDADRDEVTYSFMDKNGRSTQKMNLFSIDEHTGLVKLRHGVSAADLAEAENPINLTVIVQDDGSCCVYPSKTHTSYATLLIGIEDVNNNKPEFPDCAKYSDIAKIMEGTYKTDPPTIVKVEATDDDSSANGDIVYSLYYTQSESRKAFVIDRQTGVLTPSPHVVFDRETRPREDVTVKATDRGDRPLIGFCQFSVEVVDINDNSPQFERPSYETSVSRFEAVGTSVITVFAFDNDAAHNAEITYSLEIDTTAGEEHQNDLDFFELVNRRSGEITLIKPIPMKTQKFIFNVIADDNGIPEALQSSAQVTLNVLDKQQKAPKWQTSPDCKPGITVDENVELNKVILRCRAVSSGDSRNSDVIYKLTASGGPGNKAESKFRQFNKFENGNEWVEVVIMEGLDYEQVNNYTLTLTATDMTSRVASTKTFVVEVRDVNDVVPQFTVDLFTGTIDEEMTPNEHLEKTNGKPIVTVKAIDTDSDGPQNEVHYRIVGEANGEETKHFRIDELTGEIFPNEKFDREKIDMYILTVEASDRSVSALPGANGPNKDNVKVQIVINDVNDNAPSFEEQKYIGRVKESEGEGHDVITIKAHDLDKHSNLRYHLIGAGGGRIPFGVRTDSGTIFVKEPLDFEASDQYHLVLIASDGRHNATTNVYIHIEDVNDNAPQFEQQKYATTVIEEDVDIPKVLFNVHATDADQDEKSSRIVYRLEGQGADEVFRIGKYSGTIELVKALDRDPPAGVPSWNFVVQAIDDDGNGLVGYADVQVNVRDINDNSPIFPERLFGYIEENREPIHSDGVYFMDVQARDFDDPTTENANIEYGIVRNKLINGESVFRIDQNTGKIFAMRSLDREISSEREFIIEVRANDRGVPSREGFANVTIKVTDMNDNAPFFEKTRYEGSVEETAPIGAAVMSFSAFDADEEAKDNVFTYQLSEESDYFYVTTDKDSKQSSVGVLRVKQPLDYEDVTQRDGFHLGIRVSDGRHDAEAAVHVALVDRNDHAPHIHGATEHRVREDVPRGTSIGRYTATDRDAGDTARFRINRQSDPKRQFTIDQDGTLRVAHTLDREDIAVYNLIIEAYDNSNNIGRQMVAVYLQDVNDNGPEPYTVPRPCIFRENTPVNQLGTCEIRATDRDTAEFGPPFTMEVSPSFKYSQYLNVIFNANGDGGNGSMTITPLQEFDREAPVPGKILEIPLILADRAGRRNEASVHVIIGDLNDNTMHDGRMTIHVNSYLGRLKETVIGRVYVDDADDWDLGDKTFSWKDSRPGFELSDKGSITMAGEMAAGTYTMSANVHDNARDEDAVGYVTVIVNAVPQIAFDNQGSVQLLIAEETPLQLPDDFIRADSNGQSLMDTFKQEMTAYMGGDVTVDVFSVQVGIATLQTRDVPVLNVRFNARGSTYRDTAQLNGLIAAHRADLQRKLNVEIVGVGIDMCKFTQCDAGCQTLNSADYDGIVVSANSTVIVGVNATSRDDCTCPVWRAPPACQHSLCHNDGVCHNTNPGFFCECRNDGLKGARCQGTTRSFGGNGFAWYKPMPACTSLNISFSFMTTQSDALLFYNGPLETLRNDTHIEYSDYIFIQLRGGRISLEVSMNGQSRSSLEVASTALNDGTWHDISVNQEGKRVELVVDNCRFLGAGADDSSCRAELYTPDDDERLNIVTPVQIGGLAPLSGQDYPQTIPRAGLNGCVRNLNVNGDQYDLATPAFEQNSEKGCRLWGATCDSNSVDSLNHCIHGDCFADVQGSGAMVAKCVCDPGWGGARCERRMEWIQFAQGAFIEYSPRIAFPEQVSDIELLFISGKVNGAPAELSFGTDSQQSYVSTNLESGQNGVTAAGKFDIGTGGRRARQELRVSEVLLKENASYWLQFTRNPTRASLSIDNAYTVSTQLDKGEPFSLQVNQITLGTQGQNKGFQGCIGTYRWSKQNLPLKRGGAMDENEESIVSISNMAGVQDGCDLRITCADLPAGYCGGSFVCVDFWKGPFCTCNDGANAILGDDGQVVGCGETLAVSKLGISSPAIILILVSLALLILLVMMMVVYTRRSPGAFENVRPEEMNRDNLRQYGVEGGGEADNDQYSMAGLRKPVMPLDTGMGPAIGGHPPHYPPRGMAPPKDDHELNSKIKDLETDQNAAPYDELRIYDDERDNISVVTLESIESAQ

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
72	N-linked_Glycosylation	DGYRIITNTTVTQFH CCEEEEECCEEEEEC	24.28	-
243	N-linked_Glycosylation	FASAIPANSTVFDVE HHHCCCCCCEEEEHH	32.62	-
253	N-linked_Glycosylation	VFDVEKRNLSEPLLF EEEHHHCCCCCCEEE	60.01	-
339	N-linked_Glycosylation	IVFRIPENTTMEDIE CEEECCCCCCHHHHH	35.18	-
508	N-linked_Glycosylation	MDLSPSDNTTSQLSE ECCCCCCCCCCHHHH	49.98	-
658	N-linked_Glycosylation	VREDIPLNQTILKVT CCCCCCCCCEEEEEE	31.43	-
685	N-linked_Glycosylation	TYSVDNHNFSINSNG EEEEECCEEEECCCC	38.32	-
715	N-linked_Glycosylation	RHFVYRFNVTARDHG CEEEEEEECEECCCC	22.64	-
826	N-linked_Glycosylation	AEAENPINLTVIVQD HHCCCCCCEEEEEEC	30.80	-
1177	N-linked_Glycosylation	LDYEQVNNYTLTLTA CCHHHCCCEEEEEEE	32.10	-
1417	N-linked_Glycosylation	IASDGRHNATTNVYI EECCCCCCCEEEEEE	37.31	-
1491	Phosphorylation	EVFRIGKYSGTIELV CEEEEEECCCHHHHH	13.71	19530675
1492	Phosphorylation	VFRIGKYSGTIELVK EEEEEECCCHHHHHH	32.71	19530675
1494	Phosphorylation	RIGKYSGTIELVKAL EEEECCCHHHHHHHH	12.82	19530675
1646	N-linked_Glycosylation	PSREGFANVTIKVTD CCCCCCCEEEEEEEC	29.24	-
1935	N-linked_Glycosylation	NANGDGGNGSMTITP ECCCCCCCCCEEECC	44.91	-
2224	N-linked_Glycosylation	DGIVVSANSTVIVGV CCEEEECCCEEEEEC	30.61	-
2232	N-linked_Glycosylation	STVIVGVNATSRDDC CEEEEECCCCCCCCC	31.41	-
2307	N-linked_Glycosylation	MPACTSLNISFSFMT CCCCCEEEEEEEEEE	27.85	-
2332	N-linked_Glycosylation	GPLETLRNDTHIEYS CCHHHHCCCCCCCCC	62.74	-
2623	N-linked_Glycosylation	SEVLLKENASYWLQF EEHHHHCCCEEEEEE	32.38	12754521
2838	Phosphorylation	GEADNDQYSMAGLRK CCCCCCCCCCCCCCC	11.86	30078680
2839	Phosphorylation	EADNDQYSMAGLRKP CCCCCCCCCCCCCCC	9.12	30078680
2909	Phosphorylation	DDERDNISVVTLESI ECCCCCEEEEEHHHH	19.45	25850673
2912	Phosphorylation	RDNISVVTLESIESA CCCEEEEEHHHHHCC	23.74	25850673
2915	Phosphorylation	ISVVTLESIESAQ-- EEEEEHHHHHCCC--	34.47	25850673
2918	Phosphorylation	VTLESIESAQ----- EEHHHHHCCC-----	30.24	26412237

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

Oops, there are no upstream regulatory protein records of HMR1_CAEEL !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HMR1_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 HMR1_CAEEL !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JAC1_CAEEL	jac-1	physical	12847081
HMP2_CAEEL	hmp-2	physical	12847081

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-2623, AND MASSSPECTROMETRY.
PubMed: 15888633

"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-2623, AND MASSSPECTROMETRY.
PubMed: 12754521