CRUM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CRUM2_HUMAN
• UniProt AC: Q5IJ48
• Protein Name: Protein crumbs homolog 2 {ECO:0000305}
• Gene Name: CRB2 {ECO:0000312|HGNC:HGNC:18688}
• Organism: Homo sapiens (Human).
• Sequence Length: 1285
• Subcellular Localization: Isoform 1: Apical cell membrane ; Single-pass type I membrane protein . O-glucosylation is required for localization at the apical plasma membrane.; Isoform 2: Secreted .
• Protein Description: Apical polarity protein that plays a central role during the epithelial-to-mesenchymal transition (EMT) at gastrulation, when newly specified mesodermal cells move inside the embryo. Acts by promoting cell ingression, the process by which cells leave the epithelial epiblast and move inside the embryo to form a new tissue layer. The anisotropic distribution of CRB2 and MYH10/myosin-IIB at cell edges define which cells will ingress: cells with high apical CRB2 are probably extruded from the epiblast by neighboring cells with high levels of apical MYH10/myosin-IIB. Also required for maintenance of the apical polarity complex during development of the cortex..
• Protein Sequence: MALARPGTPDPQALASVLLLLLWAPALSLLAGTVPSEPPSACASDPCAPGTECQATESGGYTCGPMEPRGCATQPCHHGALCVPQGPDPTGFRCYCVPGFQGPRCELDIDECASRPCHHGATCRNLADRYECHCPLGYAGVTCEMEVDECASAPCLHGGSCLDGVGSFRCVCAPGYGGTRCQLDLDECQSQPCAHGGTCHDLVNGFRCDCAGTGYEGTHCEREVLECASAPCEHNASCLEGLGSFRCLCWPGYSGELCEVDEDECASSPCQHGGRCLQRSDPALYGGVQAAFPGAFSFRHAAGFLCHCPPGFEGADCGVEVDECASRPCLNGGHCQDLPNGFQCHCPDGYAGPTCEEDVDECLSDPCLHGGTCSDTVAGYICRCPETWGGRDCSVQLTGCQGHTCPLAATCIPIFESGVHSYVCHCPPGTHGPFCGQNTTFSVMAGSPIQASVPAGGPLGLALRFRTTLPAGTLATRNDTKESLELALVAATLQATLWSYSTTVLVLRLPDLALNDGHWHQVEVVLHLATLELRLWHEGCPARLCVASGPVALASTASATPLPAGISSAQLGDATFAGCLQDVRVDGHLLLPEDLGENVLLGCERREQCRPLPCVHGGSCVDLWTHFRCDCARPHRGPTCADEIPAATFGLGGAPSSASFLLQELPGPNLTVSFLLRTRESAGLLLQFANDSAAGLTVFLSEGRIRAEVPGSPAVVLPGRWDDGLRHLVMLSFGPDQLQDLGQHVHVGGRLLAADSQPWGGPFRGCLQDLRLDGCHLPFFPLPLDNSSQPSELGGRQSWNLTAGCVSEDMCSPDPCFNGGTCLVTWNDFHCTCPANFTGPTCAQQLWCPGQPCLPPATCEEVPDGFVCVAEATFREGPPAAFSGHNASSGRLLGGLSLAFRTRDSEAWLLRAAAGALEGVWLAVRNGSLAGGVRGGHGLPGAVLPIPGPRVADGAWHRVRLAMERPAATTSRWLLWLDGAATPVALRGLASDLGFLQGPGAVRILLAENFTGCLGRVALGGLPLPLARPRPGAAPGAREHFASWPGTPAPILGCRGAPVCAPSPCLHDGACRDLFDAFACACGPGWEGPRCEAHVDPCHSAPCARGRCHTHPDGRFECRCPPGFGGPRCRLPVPSKECSLNVTCLDGSPCEGGSPAANCSCLEGLAGQRCQVPTLPCEANPCLNGGTCRAAGGVSECICNARFSGQFCEVAKGLPLPLPFPLLEVAVPAACACLLLLLLGLLSGILAARKRRQSEGTYSPSQQEVAGARLEMDSVLKVPPEERLI

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
235	N-linked_Glycosylation	ASAPCEHNASCLEGL HCCCCCCCCHHHHCC	15.97	UniProtKB CARBOHYD
244	Phosphorylation	SCLEGLGSFRCLCWP HHHHCCCCEEEEECC	17.98	24719451
267	O-linked_Glycosylation	VDEDECASSPCQHGG ECCHHHCCCCCCCCC	46.61	-
297	Phosphorylation	AAFPGAFSFRHAAGF CCCCCCEEHHHCCCE	22.34	24719451
438	N-linked_Glycosylation	HGPFCGQNTTFSVMA CCCCCCCCCEEEEEC	26.77	UniProtKB CARBOHYD
476	Phosphorylation	LPAGTLATRNDTKES CCCCCEECCCCHHHH	32.87	-
478	N-linked_Glycosylation	AGTLATRNDTKESLE CCCEECCCCHHHHHH	57.88	UniProtKB CARBOHYD
480	Phosphorylation	TLATRNDTKESLELA CEECCCCHHHHHHHH	40.02	-
560	O-linked_Glycosylation	LASTASATPLPAGIS EEECCCCCCCCCCCC	23.90	OGP
669	N-linked_Glycosylation	LQELPGPNLTVSFLL HHHCCCCCEEEEEEE	55.01	UniProtKB CARBOHYD
673	Phosphorylation	PGPNLTVSFLLRTRE CCCCEEEEEEEECHH	12.63	24719451
690	N-linked_Glycosylation	GLLLQFANDSAAGLT CCEEEECCCCCCCEE	45.09	UniProtKB CARBOHYD
786	N-linked_Glycosylation	FFPLPLDNSSQPSEL CCCCCCCCCCCCHHH	51.77	UniProtKB CARBOHYD
800	N-linked_Glycosylation	LGGRQSWNLTAGCVS HCCCCCEECCCCCCC	32.53	UniProtKB CARBOHYD
836	N-linked_Glycosylation	FHCTCPANFTGPTCA EEEECCCCCCCCCCH	21.83	UniProtKB CARBOHYD
886	N-linked_Glycosylation	PAAFSGHNASSGRLL CCCCCCCCCCCCCCC	45.07	UniProtKB CARBOHYD
926	N-linked_Glycosylation	GVWLAVRNGSLAGGV CEEEEEECCCCCCCC	37.49	UniProtKB CARBOHYD
970	Phosphorylation	MERPAATTSRWLLWL HCCCCCCCCCCHHHH	16.15	-
971	Phosphorylation	ERPAATTSRWLLWLD CCCCCCCCCCHHHHC	19.66	-
1009	N-linked_Glycosylation	VRILLAENFTGCLGR HHEEEECCCCCCCHH	33.89	UniProtKB CARBOHYD
1141	N-linked_Glycosylation	PSKECSLNVTCLDGS CCCCEEEEEEEECCC	15.68	UniProtKB CARBOHYD
1158	N-linked_Glycosylation	EGGSPAANCSCLEGL CCCCCCCCCCCCCCC	21.97	UniProtKB CARBOHYD
1261	Phosphorylation	SEGTYSPSQQEVAGA CCCCCCHHHHHHCCC	38.26	28857561
1274	Phosphorylation	GARLEMDSVLKVPPE CCEEECCCCCCCCHH	28.21	19664994

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

Oops, there are no upstream regulatory protein records of CRUM2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CRUM2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CRUM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 616220: Focal segmental glomerulosclerosis 9 (FSGS9)
• 219730: Ventriculomegaly with cystic kidney disease (VMCKD)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.