FCRL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FCRL2_HUMAN
• UniProt AC: Q96LA5
• Protein Name: Fc receptor-like protein 2
• Gene Name: FCRL2
• Organism: Homo sapiens (Human).
• Sequence Length: 508
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Description: May have an regulatory role in normal and neoplastic B cell development..
• Protein Sequence: MLLWSLLVIFDAVTEQADSLTLVAPSSVFEGDSIVLKCQGEQNWKIQKMAYHKDNKELSVFKKFSDFLIQSAVLSDSGNYFCSTKGQLFLWDKTSNIVKIKVQELFQRPVLTASSFQPIEGGPVSLKCETRLSPQRLDVQLQFCFFRENQVLGSGWSSSPELQISAVWSEDTGSYWCKAETVTHRIRKQSLQSQIHVQRIPISNVSLEIRAPGGQVTEGQKLILLCSVAGGTGNVTFSWYREATGTSMGKKTQRSLSAELEIPAVKESDAGKYYCRADNGHVPIQSKVVNIPVRIPVSRPVLTLRSPGAQAAVGDLLELHCEALRGSPPILYQFYHEDVTLGNSSAPSGGGASFNLSLTAEHSGNYSCEANNGLGAQCSEAVPVSISGPDGYRRDLMTAGVLWGLFGVLGFTGVALLLYALFHKISGESSATNEPRGASRPNPQEFTYSSPTPDMEELQPVYVNVGSVDVDVVYSQVWSMQQPESSANIRTLLENKDSQVIYSSVKKS

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
32 (in isoform 4)	Phosphorylation	-	28.17	25852190
32 (in isoform 3)	Phosphorylation	-	28.17	25852190
32 (in isoform 2)	Phosphorylation	-	28.17	25852190
41 (in isoform 4)	Phosphorylation	-	18.18	25852190
41 (in isoform 3)	Phosphorylation	-	18.18	25852190
41 (in isoform 2)	Phosphorylation	-	18.18	25852190
45 (in isoform 4)	Phosphorylation	-	42.69	25852190
45 (in isoform 3)	Phosphorylation	-	42.69	25852190
45 (in isoform 2)	Phosphorylation	-	42.69	25852190
133	Phosphorylation	LKCETRLSPQRLDVQ EEEEECCCCCHHEEE	18.72	24719451
204	N-linked_Glycosylation	VQRIPISNVSLEIRA EEECCCCEEEEEEEC	28.28	UniProtKB CARBOHYD
206	Phosphorylation	RIPISNVSLEIRAPG ECCCCEEEEEEECCC	25.24	24719451
232	Phosphorylation	LCSVAGGTGNVTFSW EEEECCCCCCEEEEE	25.35	22964224
234	N-linked_Glycosylation	SVAGGTGNVTFSWYR EECCCCCCEEEEEEE	29.50	UniProtKB CARBOHYD
236	Phosphorylation	AGGTGNVTFSWYREA CCCCCCEEEEEEEEC	18.89	22964224
238	Phosphorylation	GTGNVTFSWYREATG CCCCEEEEEEEECCC	17.52	22964224
343	N-linked_Glycosylation	HEDVTLGNSSAPSGG ECCCEECCCCCCCCC	35.58	UniProtKB CARBOHYD
355	N-linked_Glycosylation	SGGGASFNLSLTAEH CCCCCEEEEEEEEEE	26.65	UniProtKB CARBOHYD
365	N-linked_Glycosylation	LTAEHSGNYSCEANN EEEEECCCEEEECCC	28.67	UniProtKB CARBOHYD
426	Phosphorylation	YALFHKISGESSATN HHHHHHHCCCCCCCC	41.11	-
429	Phosphorylation	FHKISGESSATNEPR HHHHCCCCCCCCCCC	28.88	-
430	Phosphorylation	HKISGESSATNEPRG HHHCCCCCCCCCCCC	34.51	-
432	Phosphorylation	ISGESSATNEPRGAS HCCCCCCCCCCCCCC	41.90	-
491	Phosphorylation	ESSANIRTLLENKDS CCCCCHHHHHHCCCC	31.71	29083192
496	Ubiquitination	IRTLLENKDSQVIYS HHHHHHCCCCCEEEE	49.75	-
498	Phosphorylation	TLLENKDSQVIYSSV HHHHCCCCCEEEEEC	28.14	29083192
502	Phosphorylation	NKDSQVIYSSVKKS- CCCCCEEEEECCCC-	8.95	29083192
503	Phosphorylation	KDSQVIYSSVKKS-- CCCCEEEEECCCC--	19.96	29083192
504	Phosphorylation	DSQVIYSSVKKS--- CCCEEEEECCCC---	22.45	29083192
506	Ubiquitination	QVIYSSVKKS----- CEEEEECCCC-----	49.61	-
507	Ubiquitination	VIYSSVKKS------ EEEEECCCC------	60.28	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF9	Q86YJ5	PMID:19457934

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FCRL2_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 FCRL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAP2_HUMAN	METAP2	physical	28514442

Drug and Disease Associations

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