dbPTM

LRC32_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LRC32_HUMAN
UniProt AC	Q14392
Protein Name	Leucine-rich repeat-containing protein 32
Gene Name	LRRC32
Organism	Homo sapiens (Human).
Sequence Length	662
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description
Protein Sequence	MRPQILLLLALLTLGLAAQHQDKVPCKMVDKKVSCQVLGLLQVPSVLPPDTETLDLSGNQLRSILASPLGFYTALRHLDLSTNEISFLQPGAFQALTHLEHLSLAHNRLAMATALSAGGLGPLPRVTSLDLSGNSLYSGLLERLLGEAPSLHTLSLAENSLTRLTRHTFRDMPALEQLDLHSNVLMDIEDGAFEGLPRLTHLNLSRNSLTCISDFSLQQLRVLDLSCNSIEAFQTASQPQAEFQLTWLDLRENKLLHFPDLAALPRLIYLNLSNNLIRLPTGPPQDSKGIHAPSEGWSALPLSAPSGNASGRPLSQLLNLDLSYNEIELIPDSFLEHLTSLCFLNLSRNCLRTFEARRLGSLPCLMLLDLSHNALETLELGARALGSLRTLLLQGNALRDLPPYTFANLASLQRLNLQGNRVSPCGGPDEPGPSGCVAFSGITSLRSLSLVDNEIELLRAGAFLHTPLTELDLSSNPGLEVATGALGGLEASLEVLALQGNGLMVLQVDLPCFICLKRLNLAENRLSHLPAWTQAVSLEVLDLRNNSFSLLPGSAMGGLETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFSSQEEVSLSHVRPEDCEKGGLKNINLIIILTFILVSAILLTTLAACCCVRRQKFNQQYKA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
63	Phosphorylation	LSGNQLRSILASPLG CCHHHHHHHHHHHHH	30.46	24719451
72	Phosphorylation	LASPLGFYTALRHLD HHHHHHHHHHHHCCC	6.84	24719451
203	N-linked_Glycosylation	LPRLTHLNLSRNSLT CCCCEEEECCCCCEE	28.50	UniProtKB CARBOHYD
269	Phosphorylation	AALPRLIYLNLSNNL HHHCCEEEEECCCCE	8.30	-
271	N-linked_Glycosylation	LPRLIYLNLSNNLIR HCCEEEEECCCCEEE	25.18	UniProtKB CARBOHYD
287	Phosphorylation	PTGPPQDSKGIHAPS CCCCCCCCCCCCCCC	27.77	-
308	N-linked_Glycosylation	PLSAPSGNASGRPLS CCCCCCCCCCCCCHH	34.96	19159218
345	N-linked_Glycosylation	LTSLCFLNLSRNCLR HHHHHHHHCCHHHHH	18.73	UniProtKB CARBOHYD
387	Phosphorylation	LGARALGSLRTLLLQ HHHHHHHHHHHHHHC	18.61	24719451
404	Phosphorylation	ALRDLPPYTFANLAS CCCCCCCCCHHCHHH	16.73	-
405	Phosphorylation	LRDLPPYTFANLASL CCCCCCCCHHCHHHH	23.26	-
423	Phosphorylation	NLQGNRVSPCGGPDE CCCCCEECCCCCCCC	15.96	-
434	Phosphorylation	GPDEPGPSGCVAFSG CCCCCCCCCCEEECC	51.22	-
440	Phosphorylation	PSGCVAFSGITSLRS CCCCEEECCCCCCCC	21.39	-
444	Phosphorylation	VAFSGITSLRSLSLV EEECCCCCCCCCCCC	21.62	-
545	N-linked_Glycosylation	LEVLDLRNNSFSLLP EEEEECCCCCCCCCC	56.65	UniProtKB CARBOHYD
549	Phosphorylation	DLRNNSFSLLPGSAM ECCCCCCCCCCCCHH	28.90	-
561	Phosphorylation	SAMGGLETSLRRLYL CHHCCHHHHHHHHHH	37.80	26270265
562	Phosphorylation	AMGGLETSLRRLYLQ HHCCHHHHHHHHHHC	15.54	26270265

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 LRC32_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LRC32_HUMAN !!

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 LRC32_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZDHC6_HUMAN	ZDHHC6	physical	28514442
TGFB1_HUMAN	TGFB1	physical	28514442
STAT3_HUMAN	STAT3	physical	28514442
DCP2_HUMAN	DCP2	physical	28514442
NSMA_HUMAN	SMPD2	physical	28514442
MOT10_HUMAN	SLC16A10	physical	28514442
TMM11_HUMAN	TMEM11	physical	28514442
S11IP_HUMAN	STK11IP	physical	28514442
GRP78_HUMAN	HSPA5	physical	28514442
MAN1_HUMAN	LEMD3	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.

Regulatory Network of LRC32_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308, AND MASSSPECTROMETRY.	19159218 [Abstract]