HAVR2_HUMAN - dbPTM
HAVR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAVR2_HUMAN
UniProt AC Q8TDQ0
Protein Name Hepatitis A virus cellular receptor 2
Gene Name HAVCR2
Organism Homo sapiens (Human).
Sequence Length 301
Subcellular Localization Membrane
Single-pass type I membrane protein . Cell junction . Localizes to the immunological synapse between CD8+ T-cells and target cells.
Protein Description Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand. [PubMed: 24825777 Regulates macrophage activation]
Protein Sequence MFSHLPFDCVLLLLLLLLTRSSEVEYRAEVGQNAYLPCFYTPAAPGNLVPVCWGKGACPVFECGNVVLRTDERDVNYWTSRYWLNGDFRKGDVSLTIENVTLADSGIYCCRIQIPGIMNDEKFNLKLVIKPAKVTPAPTRQRDFTAAFPRMLTTRGHGPAETQTLGSLPDINLTQISTLANELRDSRLANDLRDSGATIRIGIYIGAGICAGLALALIFGALIFKWYSHSKEKIQNLSLISLANLPPSGLANAVAEGIRSEENIYTIEENVYEVEEPNEYYCYVSSRQQPSQPLGCRFAMP
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 Orthologous
Protein Cluster
105PhosphorylationENVTLADSGIYCCRI
ECEEECCCCEEEEEE
22.8330377224
108PhosphorylationTLADSGIYCCRIQIP
EECCCCEEEEEEECC
6.7730377224
126AcetylationNDEKFNLKLVIKPAK
CCCCCCEEEEEECCC
41.647370233
145O-linked_GlycosylationPTRQRDFTAAFPRML
CCCCCCHHHHHCCHH
22.7422171320
153PhosphorylationAAFPRMLTTRGHGPA
HHHCCHHHCCCCCCC
12.71-
154PhosphorylationAFPRMLTTRGHGPAE
HHCCHHHCCCCCCCC
30.60-
172N-linked_GlycosylationLGSLPDINLTQISTL
CCCCCCCCHHHHHHH
44.40UniProtKB CARBOHYD
174O-linked_GlycosylationSLPDINLTQISTLAN
CCCCCCHHHHHHHHH
21.26OGP
178O-linked_GlycosylationINLTQISTLANELRD
CCHHHHHHHHHHHHH
31.36OGP
238PhosphorylationKEKIQNLSLISLANL
HHHHHCEEEEECCCC
31.0728857561
241PhosphorylationIQNLSLISLANLPPS
HHCEEEEECCCCCCC
27.0728857561
265PhosphorylationIRSEENIYTIEENVY
CCCCCCEEEEECCEE
17.1617069754
272PhosphorylationYTIEENVYEVEEPNE
EEEECCEEECCCCCC
26.32-

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
265YPhosphorylationKinaseITKQ08881
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAVR2_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 HAVR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
LCK_HUMANLCKphysical
22863785
PHLP1_HUMANPHLPP1physical
28514442
ZDHC5_HUMANZDHHC5physical
28514442
M3K21_HUMANKIAA1804physical
28514442
DIP2B_HUMANDIP2Bphysical
28514442
DEN6A_HUMANDENND6Aphysical
28514442
CLDN1_HUMANCLDND1physical
28514442
CBPC5_HUMANAGBL5physical
28514442
GOGA7_HUMANGOLGA7physical
28514442
TSN7_HUMANTSPAN7physical
28514442
DIP2A_HUMANDIP2Aphysical
28514442
PKN3_HUMANPKN3physical
28514442
KDM1B_HUMANKDM1Bphysical
28514442
TCAF2_HUMANFAM115Cphysical
28514442
MTMR5_HUMANSBF1physical
28514442
CNKR3_HUMANCNKSR3physical
28514442
DGKQ_HUMANDGKQphysical
28514442
P4K2B_HUMANPI4K2Bphysical
28514442
IL1AP_HUMANIL1RAPphysical
28514442
CISD3_HUMANCISD3physical
28514442
PK3CA_HUMANPIK3CAphysical
28514442
AVR2A_HUMANACVR2Aphysical
28514442
PK3CB_HUMANPIK3CBphysical
28514442
PKP2_HUMANPKP2physical
28514442
RHBT3_HUMANRHOBTB3physical
28514442
S22AI_HUMANSLC22A18physical
28514442
CERK1_HUMANCERKphysical
28514442
MYADM_HUMANMYADMphysical
28514442
S20A2_HUMANSLC20A2physical
28514442
AT132_HUMANATP13A2physical
28514442
TTF2_HUMANTTF2physical
28514442
CNTP1_HUMANCNTNAP1physical
28514442
TIGD5_HUMANTIGD5physical
28514442
MTMR1_HUMANMTMR1physical
28514442
NISCH_HUMANNISCHphysical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
WDR36_HUMANWDR36physical
28514442
P55G_HUMANPIK3R3physical
28514442
PLPL6_HUMANPNPLA6physical
28514442
P85B_HUMANPIK3R2physical
28514442
ZMYM6_HUMANZMYM6physical
28514442
PKHH3_HUMANPLEKHH3physical
28514442
MYO1D_HUMANMYO1Dphysical
28514442
PKP4_HUMANPKP4physical
28514442
PLCA_HUMANAGPAT1physical
28514442
MELK_HUMANMELKphysical
28514442
SNX17_HUMANSNX17physical
28514442
PIGA_HUMANPIGAphysical
28514442
UTP18_HUMANUTP18physical
28514442
PKN2_HUMANPKN2physical
28514442
PLD2_HUMANPLD2physical
28514442
LGR4_HUMANLGR4physical
28514442
JAK1_HUMANJAK1physical
28514442
UTP4_HUMANCIRH1Aphysical
28514442
P3C2A_HUMANPIK3C2Aphysical
28514442
TYK2_HUMANTYK2physical
28514442
ERBB2_HUMANERBB2physical
28514442
P85A_HUMANPIK3R1physical
28514442
PIGM_HUMANPIGMphysical
28514442
LPCT4_HUMANLPCAT4physical
28514442
NOCT_HUMANCCRN4Lphysical
28514442
WDR44_HUMANWDR44physical
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 HAVR2_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-145, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.

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