dbPTM

UNC52_CAEEL - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UNC52_CAEEL
UniProt AC	Q06561
Protein Name	Basement membrane proteoglycan {ECO:0000303\|PubMed:8393416}
Gene Name	unc-52 {ECO:0000312\|WormBase:ZC101.2e}
Organism	Caenorhabditis elegans.
Sequence Length	3375
Subcellular Localization	Secreted, extracellular space, extracellular matrix, basement membrane . Cytoplasm, myofibril, sarcomere, M line . In body wall muscles, colocalizes to dense bodies and M lines with beta-integrin pat-3 (PubMed:10512861). In myoepithelial sheath cells
Protein Description	Component of an integrin containing attachment complex, which is required for muscle development and maintenance. [PubMed: 22253611 Probable structural role in myofilament assembly and/or attachment of the myofilament lattice to the cell membrane]
Protein Sequence	MKRSSTVLAALLALLLVATNDAARHRKYRQTYQDIDSDDDDTSDVQITVFPSEKEVRDGRDVSFECRARTSDNSVYPTVRWARVGGPLPSSAHDSGGRLTINPVQLSDAGTYICVSDYNGNTVEARATLSVVSYGPQEVSNGLRQAGQCMADEKACGNNECVKNDYVCDGEPDCRDRSDEANCPAISRTCEPNEFKCNNNKCVQKMWLCDGDDDCGDNSDELNCNAKPSSSDCKPTEFQCHDRRQCVPSSFHCDGTNDCHDGSDEVGCVQPTVVDPPQTNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKGRVLATPDCIVRVVDDPRPQPPQPPTAPPQRASCDTRGAVTPYPNNYGTCECKSQVTGPNCDQCKPGAFHLSEKSPEGCLKCFCFGVSNDCRSSGHYRTKDRLMFAGDAEGVTISDIEERTIDRNTPFSFFKTGYLTFDGTTDGVAKYWRLPQRFLGDKVTAYGGKMEFEIEFSGSGHHSSEPMVVLKGNQNILVHRVRNQEHVLRSDSPVRITVETYETNYEQLNGAAATREDLLMVLADLDAFLIRATHVAHQTSTSLGDVSWEIAVDRYTPDGLALEVEQCVCPPGYLGTSCEDCAPGYERSGYGPYLGTCVPIQPRHQQCGPGAVAPTAPAQGQCQCKASVIGPNCDRCAPNSFGLAPTNPQGCIPCFCSGVTQQCSASSYRRTSVSIDYARGDRDQLELTTSDSRQPYSPQTRAELSGQAIEFRSFEEARGQTLYWKLPEKFLGDKVTSYGGTLEYTFKFSGNGNSDQSADVILRGNDIALQYKHREPFYADRENKVQIKIIETSWQRVDGQQATREHLLMTLADLDTLLIKSTYNDDCTDSQLLSANLEFAEPYGQGLTAAEVEQCICPPGYVGTSCEDCAPGYSRTGGGLYLGLCEKCECNGHASQCDKEYGYCLDCQHNTEGDQCERCKPGFVGDARRGTPNDCQPEATRAPCHCNNHSPRGCDSFGRCLLCEHNTEGTHCERCKKGYYGDATKGSPYDCTPCPCPGASDCYLDNEGQVACRICPAGLQGRLCNECAPGYTRSNKPAGRVCEPIGQVTNEDITFVQKPHEVLRVRIMEPKRQIALPGDRVHWICQVTGYTTEKIHVEWTKVGEMSLPPNAKAYDGYLVLKGVEAENAGQYRCTATTITQYATDDALLTISKRISGRPPQPVIDPPHLVVNEGEPAAFRCWVPGIPDCQITWHREQLGGPLPHGVYQTGNALKIPQSQLHHAGRYICSAANQYGTGQSPPAVLEVKKPVIPPKVDPIRQTVDRDQPARFKCWVPGNSNVQLRWSRPGGAPLPSGVQEQQGILHIPRASDQEVGQYVCTATDPSDNTPLQSEPVQLNIRDPAPPQRGAAPQIDPPNQTVNVNDPAQFRCWVPGQPRAQLKWSRKDGRPLPNGILERDGFLRIDKSQLHDAGEYECTSTEPDGSTQLSPPARLNVNQPQAIQPQVDPPVQTVNEGEPSRIRCWVPGHPNIQLQFVKRGRRPLPAHARFSQGNLEIPRTLKSDEDEYICIATDPTTNRPVESNPARVIVKSPIRPIIDPAEQTVPEGSPFKIRCYVPGHPSVQLTFRRVSGQLNEDADENNGLLAVQRAELTDEGDYICTARDPDTGAPIDSTPATVHVTNAAAPPQVEARPPQHPVITPQTQTIPEGDPARIQCTVPGNPSAAQHLSFERVDGKGLPFGSSDDRGVLTIPSTQLQDAGEYVCLYSPENSPPVKTNPSTLNVTPEGTPPRPVATPPLLSVAPGSPARFNCVAHSDTPARIRWGFREENGPLPEHVNQDGDDIVISEAGDRNVGEYVCSATNDFGTGVADPVRLEVTEDQEPPTAVVEPRTWNGKPGERHQFRCITTGSPTPKITWTGPNGSPLPHDVTPLEPNILDFSNGRSELNGDYTCTASNPIGEASDHGNVNIGPSLTVKTNPPGPKLIVTVGEPLQVKCEAFGAPGDPEPEVEWLHDPGPERGDLPDDFKPVTISEQFIRHPNVGLGNAGVYTCKGSSAHATATKNIYIEVVEPSRIATVSILGGSSQWFDQGEKGELICTATGSSLVDRLEWEKVDDQLPTDVEEHNEPGLLHFPSFKNSYAGEYRCNGYRNNEIIASAAVHVHSSANADDEPKVEIEPPRVRVVSQGDNIVLKCSVQGAENGEHFKWALLRGGSLVRQLGTEPTLEITKADPSNDFGVYRCNVEDNNGLVIGSAFTAVSVGQQDKSHAQIVKFDDKSDASFTCPIYSVPGSKVDWTYENGDLPSKAVPNGNKIEIKEFDDASAGTYVCKVSFDGNVVEGFVTAQMFVPDTIIQVLLEVSSESPQIGDRAWFDCKVTGDPSAVISWTKEGNDDLPPNAQVTGGRLLFTDLKEDNAGVYRCVAKTKAGPLQTRTVLNVGSGKQDQVTFTVADSLPVVYTVGQPAYLSCIGKTETKPNQSVVWTKEEGDLPSGSRVEQGVLMLPSVHRDDEGSYTCEIVKEENPVFSTVDLQIDDFIPVIDGEPIELPPLSDEEIVNLDIEITLNTANPKGIIFETKRINSGDLLATPYDTIHHEAKITDYGTVLYEFDIGNGRQIVETTNPINPNEWNVIKIKNDKNQVTIQLNDESATIRQHTNPLPSLSTGVNRPVFIGGRHEPTNEANDFRGIISQVVLSGHNVGLGDARIPSSVVKYDACASTNLCLNGANCRNANNHHGFSCECAEEFHGEYCQWRSNSCHDESCNTGICLDNEESWQCVCPLGTTGLRCEEKTEIPQPLGFTSDTSFLAVKRPVKFESIKMKLRPQADSDEHILMYFASDYGSNTKQYTSLSLIANQVVLTVRRPDKEVQKIRSETLEAGELIDVAVRQAGNALVMTVDGNQVSTIETDTLKPGTEIFIGGLPPGLNSPDDVVEQSFQGCVYEILINSQDVDLQNLSSSGDISSCEESQFPVEEDDTTTTTTTEEPEAVIEEPTTEEPTTTEEPITEEPTEEPTTTEEPTTTEEPTTTTEEPTTTTTEEPYHIYETSRDDDPEIIIPVETTTTSTTTTSTTEEPEAEPALVLPTDPVEENDVSDEEEEISTISTVSPDNGLDSDSDYSEGTLPPDSSSEEIVVGDVYSTQEPNNICANSTCGMNGQCVPRNMTHYTCECKLYYDGPTCSLFKPIEHAARFDGDAFIELSSDEFPHLTSEKDEIVAFKFKTEQQNGVLLWQGQRPTVQQMEDYISVGIVNGHLHFSYELGGGAAHLISEERVDDGKEHSVRFERKGREGQMRIDNYREVDGRSTGILAMLNVDGNIFVGGVPDISKATGGLFSNNFVGCIADVELNGVKLDLMATAIDGKNVKPCDEWMHRKRWLYRRRVR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
780	Phosphorylation	GQAIEFRSFEEARGQ CCEEEEEEHHHHCCC	42.18	19530675
1140 (in isoform 3)	Phosphorylation	-	31.28	19530675
1141 (in isoform 3)	Phosphorylation	-	5.02	19530675
1422	N-linked_Glycosylation	APQIDPPNQTVNVND CCCCCCCCCCCCCCC	56.39	17761667
2476	N-linked_Glycosylation	GKTETKPNQSVVWTK ECCCCCCCCEEEEEC	48.60	17761667
2950	N-linked_Glycosylation	SQDVDLQNLSSSGDI CCCCCCCCCCCCCCC	49.54	-
3143	N-linked_Glycosylation	EPNNICANSTCGMNG CCCCCCCCCCCCCCC	33.18	-
3156	N-linked_Glycosylation	NGQCVPRNMTHYTCE CCEEECCCCCEEEEE	33.37	-

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 UNC52_CAEEL !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UNC52_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 UNC52_CAEEL !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of UNC52_CAEEL !!

Drug and Disease Associations

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

Regulatory Network of UNC52_CAEEL

Related Literatures of Post-Translational Modification

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-1422, AND MASSSPECTROMETRY.	17761667 [Abstract]
"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-1422, AND MASSSPECTROMETRY.	12754521 [Abstract]