PAT2_CAEEL - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PAT2_CAEEL
• UniProt AC: P34446
• Protein Name: Integrin alpha pat-2
• Gene Name: pat-2 {ECO:0000312|WormBase:F54F2.1}
• Organism: Caenorhabditis elegans.
• Sequence Length: 1226
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Required for muscle development probably through the regulation of the actin-myosin cytoskeleton. [PubMed: 8106547]
• Protein Sequence: MREGSFPRRIGLLLGLLGLLAGVATFNIDTKNVVVHHMAGNYFGYSLDFYHEQKGMPVLVVGAPEAESNNPNLAGIRRPGAVYACSVNRATCREVHVDKMKGNLKKLNGSHLVPIEEKSHQFFGATVRSNDKHDKIVVCAPKYTYFYSKFEVIEPVGTCFYAENGFDNAEEFSSCKQEPARHGRHRLGYGQCGFSAAVPGKKNQNRVFIGAPGVWYWQGAMFSQNIKNQTDRPNTEYGSKEYDHDMMGYSTATGDFDGDGIDDIVAGVPRGNDLHGKLVLYTSKLKMMINLTDEVSTQHGQYCGGSVAVADVNKDGRDDIIMGCPFYTDYGSVKDAKTQERKPQYDVGKVIVMLQTAPGVFGKQIAVVGDDQWGRFGHAVAAAGDLNLDGYNDVIVGAPYAGKNKQGAVYVIHGSKDGVRELPTQKIEGANIGHGNIKSFGFSLTGNEDVDGNGMPDIAVGAWKSGNAAVLLTKPVVTVTGQTEPESALISVEDKNCDVDGKLGKQACKHINTCFKYEGKGDTPNDLEFDLRFNLDDHSPEPRAYFLQKDVKSDRSIKVAQGSKTRDHPSSIEQRVRLEKGRQKCFRHRFFASSTMKDKLSPIHWSVNYTYVESKTGKLRGDKLEPAIDTTVPLSFQNKINIANNCGKDDLCVPDLKVTAVADREKFLLGTQDNTMLINVTVQNGGEDSYETKLYFDVPQGFEYGGIESVGGDGSKSAPACSPTSDEPDSDGKWTFACDLGNPLPANKVVSSVVRVTASSDKPPLAPISINAHVNSSNDEEAHTVADNKVTFTIPVDFKNQLSLNGRSNPEQVDFSMTNKTRVDAFDDNEIGPVVSHLYQISNRGPSEVDSATLDIFWPSFSTEGGHLLYIITEPVVNPPNKGRCRVKQLQNVNPLNLRITNEHVPTEPPVAKTPNEYSREEDDESYEDETTTQSQSTRHQSTQHQTHHQSGPVHVYEKDEEKIRQNTGNWQYVEDKKKKGDYEYIPDDQEYDGDDFEEEDDEDFDRAGSKRVKRNPTPKKKKKGGEHRGEPRSDKARFSDLREAVKLSKEAGGVVDYKGPLSRASVDCNSLRCTHIECDIYDLKEDEFVLVEIFSRLYTNTLVDEKNPGGDISSLALARVTSTKYNLPHKPTLITAVSTNMNAIASEEGRDLPWWLYLLAILIGLAILILLILLLWRCGFFKRNRPPTEHAELRADRQPNAQYADSQSRYTSQDQYNQGRHGQML

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
108	N-linked_Glycosylation	KGNLKKLNGSHLVPI CCCHHHCCCCCEEEC	59.82	17761667
228	N-linked_Glycosylation	MFSQNIKNQTDRPNT HHCHHCCCCCCCCCC	46.30	17761667
290	N-linked_Glycosylation	SKLKMMINLTDEVST CCCEEEEECCCHHHH	20.99	15888633
608	N-linked_Glycosylation	SPIHWSVNYTYVESK CCCEEEEEEEEEECC	20.22	17761667
679	N-linked_Glycosylation	QDNTMLINVTVQNGG CCCEEEEEEEEECCC	21.32	17761667
775	N-linked_Glycosylation	ISINAHVNSSNDEEA EEEEEEECCCCCCCC	29.83	-
819	N-linked_Glycosylation	QVDFSMTNKTRVDAF HCCCCCCCCCCCCCC	34.75	17761667
1204	Phosphorylation	DRQPNAQYADSQSRY CCCCCHHCCCCCCCC	15.23	27067626
1211	Phosphorylation	YADSQSRYTSQDQYN CCCCCCCCCCHHHCC	18.91	27067626

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

Oops, there are no upstream regulatory protein records of PAT2_CAEEL !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PAT2_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 PAT2_CAEEL !!

Protein-Protein Interaction

Oops, there are no PPI records of PAT2_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-108; ASN-228; ASN-608;ASN-679 AND ASN-819, AND MASS SPECTROMETRY.
PubMed: 17761667

"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-108; ASN-228; ASN-290;ASN-608 AND ASN-819, AND MASS SPECTROMETRY.
PubMed: 15888633