dbPTM

VNN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VNN2_HUMAN
UniProt AC	O95498
Protein Name	Vascular non-inflammatory molecule 2
Gene Name	VNN2
Organism	Homo sapiens (Human).
Sequence Length	520
Subcellular Localization	Cell membrane Lipid-anchor, GPI-anchor .
Protein Description	Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. Involved in the thymus homing of bone marrow cells. May regulate beta-2 integrin-mediated cell adhesion, migration and motility of neutrophil..
Protein Sequence	MVTSSFPISVAVFALITLQVGTQDSFIAAVYEHAVILPNKTETPVSQEDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVNWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSEPQFNVPEKPELVTFNTAFGRFGIFTCFDIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLVANTHHVSLNMTGSGIYAPNGPKVYHYDMKTELGKLLLSEVDSHPLSSLAYPTAVNWNAYATTIKPFPVQKNTFRGFISRDGFNFTELFENAGNLTVCQKELCCHLSYRMLQKEENEVYVLGAFTGLHGRRRREYWQVCTLLKCKTTNLTTCGRPVETASTRFEMFSLSGTFGTEYVFPEVLLTEIHLSPGKFEVLKDGRLVNKNGSSGPILTVSLFGRWYTKDSLYSSCGTSNSAITYLLIFILLMIIALQNIVML

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
39	N-linked_Glycosylation	EHAVILPNKTETPVS CCEEECCCCCCCCCC	61.51	UniProtKB CARBOHYD
119	Phosphorylation	DPHRFGHTPVQARLS CCHHCCCCCHHHHHH	26.07	-
158	Phosphorylation	STCPPNGYFQYNTNV CCCCCCCEEEECCEE	8.31	22817900
161	Phosphorylation	PPNGYFQYNTNVVYN CCCCEEEECCEEEEC	17.66	22817900
273	N-linked_Glycosylation	NTHHVSLNMTGSGIY ECCEEEEECCCCCEE	20.61	UniProtKB CARBOHYD
347	N-linked_Glycosylation	FISRDGFNFTELFEN EECCCCCCHHHHHHH	48.75	UniProtKB CARBOHYD
357	N-linked_Glycosylation	ELFENAGNLTVCQKE HHHHHCCCCEEEHHH	30.08	UniProtKB CARBOHYD
361	S-palmitoylation	NAGNLTVCQKELCCH HCCCCEEEHHHHHHH	3.94	29575903
366	S-palmitoylation	TVCQKELCCHLSYRM EEEHHHHHHHHHHHH	1.12	29575903
367	S-palmitoylation	VCQKELCCHLSYRML EEHHHHHHHHHHHHH	5.90	29575903
411	N-linked_Glycosylation	LLKCKTTNLTTCGRP EEEECCCCCCCCCCC	40.39	16335952
452	Phosphorylation	LLTEIHLSPGKFEVL EEEEEECCCCCEEEE	19.90	24719451
468	N-linked_Glycosylation	DGRLVNKNGSSGPIL CCCEECCCCCCCCEE	50.83	UniProtKB CARBOHYD
493	GPI-anchor	KDSLYSSCGTSNSAI CCHHHHCCCCCHHHH	5.91	-

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 VNN2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VNN2_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 VNN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACADV_HUMAN	ACADVL	physical	28514442
FKB14_HUMAN	FKBP14	physical	28514442
COX18_HUMAN	COX18	physical	28514442
FZD3_HUMAN	FZD3	physical	28514442
S1PR5_HUMAN	S1PR5	physical	28514442
CLDN1_HUMAN	CLDND1	physical	28514442
KLK7_HUMAN	KLK7	physical	28514442
AT2A1_HUMAN	ATP2A1	physical	28514442
FZD6_HUMAN	FZD6	physical	28514442
FZD7_HUMAN	FZD7	physical	28514442
CATL2_HUMAN	CTSV	physical	28514442
PIGU_HUMAN	PIGU	physical	28514442
D19L4_HUMAN	DPY19L4	physical	28514442
ECEL1_HUMAN	ECEL1	physical	28514442
ZNT9_HUMAN	SLC30A9	physical	28514442
TSN6_HUMAN	TSPAN6	physical	28514442
WASC5_HUMAN	KIAA0196	physical	28514442
FKRP_HUMAN	FKRP	physical	28514442
ALG8_HUMAN	ALG8	physical	28514442
GPAA1_HUMAN	GPAA1	physical	28514442
TGO1_HUMAN	MIA3	physical	28514442
GP1BB_HUMAN	GP1BB	physical	28514442
APOD_HUMAN	APOD	physical	28514442
GPM6A_HUMAN	GPM6A	physical	28514442
LMF2_HUMAN	LMF2	physical	28514442
CYTM_HUMAN	CST6	physical	28514442
SAP3_HUMAN	GM2A	physical	28514442
PIGS_HUMAN	PIGS	physical	28514442
SPCS2_HUMAN	SPCS2	physical	28514442
LMBR1_HUMAN	LMBR1	physical	28514442
AGRL1_HUMAN	LPHN1	physical	28514442
FACR2_HUMAN	FAR2	physical	28514442
SOAT1_HUMAN	SOAT1	physical	28514442
POMT1_HUMAN	POMT1	physical	28514442
GRM1A_HUMAN	GRAMD1A	physical	28514442
NAT14_HUMAN	NAT14	physical	28514442
TIM14_HUMAN	DNAJC19	physical	28514442
TNFL9_HUMAN	TNFSF9	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 VNN2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND MASSSPECTROMETRY.	16335952 [Abstract]