dbPTM

PAT3_CAEEL - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAT3_CAEEL
UniProt AC	Q27874
Protein Name	Integrin beta pat-3
Gene Name	pat-3 {ECO:0000312\|WormBase:ZK1058.2}
Organism	Caenorhabditis elegans.
Sequence Length	809
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Lateral cell membrane Single-pass type I membrane protein . Basal cell membrane Single-pass type I membrane protein . Cytoplasm, myofibril, sarcomere, M line . In body wall muscle cells locali
Protein Description	Integrin alpha ina-1/beta pat-3 is a receptor for laminin. Integrin alpha pat-2/beta pat-3 recognizes the sequence R-G-D in its ligands (Probable). Plays a role in cell migration, morphogenesis and probably in cell-cell interactions. [PubMed: 19023419]
Protein Sequence	MPPSTSLLLLAALLPFALPASDWKTGEVTGKVVEKSEFPCYSLSRDNYTCSACIQYHESCAWCGAPMFDEKKPYARCDSRAKLMEHGCPNSYIEDPATKLDITEDSKLSDQGQVESEEEAVQIKPQEMYVEIRPKSRVRFNVTYRQAVDYPVDLYYLMDLSYSMKDDKQKLSELGDLLAERMRTVTKNFRLGFGSFIDKKLMPFIDPRIEKQLSPCPTPCAEPYGFKHQMSLTTNTAKFKAEVDKAEISGNLDAPEGGFDAVVQALACNKTIGWRERARKMIVFSTDAGFHFAGDGRLAGVVEPNDGTCHLDREGYYTETLNQDYPSIALLHQMIKDRKANVIFAVTKNNQDLYTQLSNALPDVSSSVGVLANDSRNIVDLIEKEYLKISEKIIMVDNANASEGLKLTYRSMCLDGTTLKDTNVCEGIRVGDEVQFEVTLENTHCIDKRDFVLRIGPSGLDETLIVNVKVLCDCDCERQDRIVTNSADCNGGDMVCGVCRCKGGNVGKYCECNRPGMSTAALNEKCKRTNESAICEGRGVCNCGRCECNPRANPEEQISGEFCECDNFNCPRHDRKICAEHGECNCGKCICAPGWTGRACECPISTDSCLSANGKICNGKGECICGRCRCFDSPDGNRYSGAKCEICPTCPTKCVEYKNCVMCQQWQTGPLNETACDQCEFKVIPVEELPNLNETTPCQFVDPADDCTFYYLYYYDEATDNATVWVRKHKDCPPPVPVLAIVLGVIAGIVILGILLLLLWKLLTVLHDRSEYATFNNERLMAKWDTNENPIYKQATTTFKNPVYAGKAN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	N-linked_Glycosylation	CYSLSRDNYTCSACI CEECCCCCEEEHHHH	32.66	-
141	N-linked_Glycosylation	PKSRVRFNVTYRQAV CCCCEEEEEEECCCC	18.04	17761667
269	N-linked_Glycosylation	VVQALACNKTIGWRE HHHHHHCCCCCCHHH	38.61	17761667
373	N-linked_Glycosylation	SSVGVLANDSRNIVD HHHHHHCCCCCCHHH	43.56	-
400	N-linked_Glycosylation	IIMVDNANASEGLKL EEEECCCCCCCCCCC	50.70	17761667
530	N-linked_Glycosylation	NEKCKRTNESAICEG HHHHHCCCCCCCCCC	45.30	17761667
672	N-linked_Glycosylation	QWQTGPLNETACDQC CCCCCCCCCCCCCCC	47.94	17761667
693	N-linked_Glycosylation	VEELPNLNETTPCQF HHHCCCCCCCCCCEE	51.73	-
721	N-linked_Glycosylation	YYDEATDNATVWVRK EEECCCCCEEEEEEE	32.91	-
772	Phosphorylation	VLHDRSEYATFNNER HHCCCHHHCCCCCHH	16.52	27067626
792	Phosphorylation	DTNENPIYKQATTTF CCCCCCCCCCCCCEE	9.78	17761667
804	Phosphorylation	TTFKNPVYAGKAN-- CEECCCCCCCCCC--	15.76	27067626

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 PAT3_CAEEL !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PAT3_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 PAT3_CAEEL !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PAT3_CAEEL !!

Drug and Disease Associations

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

Regulatory Network of PAT3_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-141; ASN-269; ASN-400;ASN-530 AND ASN-672, AND MASS SPECTROMETRY.	17761667 [Abstract]
"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-141 AND ASN-269, AND MASSSPECTROMETRY.	15888633 [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-400, AND MASSSPECTROMETRY.	12754521 [Abstract]