HAVR1_HUMAN - dbPTM
HAVR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAVR1_HUMAN
UniProt AC Q96D42
Protein Name Hepatitis A virus cellular receptor 1
Gene Name HAVCR1
Organism Homo sapiens (Human).
Sequence Length 359
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description May play a role in T-helper cell development and the regulation of asthma and allergic diseases. Receptor for TIMD4 (By similarity). May play a role in kidney injury and repair.; (Microbial infection) Acts as a receptor for Hepatitis A virus.; (Microbial infection) Acts as a receptor for Ebolavirus and Marburg virus by binding exposed phosphatidyl-serine at the surface of virion membrane.; (Microbial infection) Acts as a receptor for Dengue virus by binding exposed phosphatidyl-serine at the surface of virion membrane..
Protein Sequence MHPQVVILSLILHLADSVAGSVKVGGEAGPSVTLPCHYSGAVTSMCWNRGSCSLFTCQNGIVWTNGTHVTYRKDTRYKLLGDLSRRDVSLTIENTAVSDSGVYCCRVEHRGWFNDMKITVSLEIVPPKVTTTPIVTTVPTVTTVRTSTTVPTTTTVPTTTVPTTMSIPTTTTVLTTMTVSTTTSVPTTTSIPTTTSVPVTTTVSTFVPPMPLPRQNHEPVATSPSSPQPAETHPTTLQGAIRREPTSSPLYSYTTDGNDTVTESSDGLWNNNQTQLFLEHSLLTANTTKGIYAGVCISVLVLLALLGVIIAKKYFFKKEVQQLSVSFSSLQIKALQNAVEKEVQAEDNIYIENSLYATD
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
65N-linked_GlycosylationQNGIVWTNGTHVTYR
CCCEEEECCCEEEEE
37.34UniProtKB CARBOHYD
65N-linked_GlycosylationQNGIVWTNGTHVTYR
CCCEEEECCCEEEEE
37.349557657
103PhosphorylationAVSDSGVYCCRVEHR
CCCCCCEEEEEEEEC
6.86-
210O-linked_GlycosylationVSTFVPPMPLPRQNH
EEECCCCCCCCCCCC
4.33OGP
222PhosphorylationQNHEPVATSPSSPQP
CCCCCCCCCCCCCCC
41.2124043423
223PhosphorylationNHEPVATSPSSPQPA
CCCCCCCCCCCCCCC
17.0418669648
225PhosphorylationEPVATSPSSPQPAET
CCCCCCCCCCCCCCC
55.1824043423
226PhosphorylationPVATSPSSPQPAETH
CCCCCCCCCCCCCCC
30.8224043423
228PhosphorylationATSPSSPQPAETHPT
CCCCCCCCCCCCCCC
52.3518669648
232PhosphorylationSSPQPAETHPTTLQG
CCCCCCCCCCCCHHH
34.9524043423
235PhosphorylationQPAETHPTTLQGAIR
CCCCCCCCCHHHHCC
32.3124043423
236PhosphorylationPAETHPTTLQGAIRR
CCCCCCCCHHHHCCC
22.8724043423
240O-linked_GlycosylationHPTTLQGAIRREPTS
CCCCHHHHCCCCCCC
4.52OGP
258N-linked_GlycosylationYSYTTDGNDTVTESS
EEEECCCCCEEEECC
44.59UniProtKB CARBOHYD
263N-linked_GlycosylationDGNDTVTESSDGLWN
CCCCEEEECCCCCCC
43.86-
272N-linked_GlycosylationSDGLWNNNQTQLFLE
CCCCCCCCCHHHHHH
42.96UniProtKB CARBOHYD
277N-linked_GlycosylationNNNQTQLFLEHSLLT
CCCCHHHHHHEECHH
5.60-
286N-linked_GlycosylationEHSLLTANTTKGIYA
HEECHHCCCCCCHHH
42.94UniProtKB CARBOHYD
291N-linked_GlycosylationTANTTKGIYAGVCIS
HCCCCCCHHHHHHHH
1.96-
324PhosphorylationKKEVQQLSVSFSSLQ
HHHHHHHEEEHHHHH
16.0428857561
326PhosphorylationEVQQLSVSFSSLQIK
HHHHHEEEHHHHHHH
18.9428857561
328PhosphorylationQQLSVSFSSLQIKAL
HHHEEEHHHHHHHHH
23.7228857561
329PhosphorylationQLSVSFSSLQIKALQ
HHEEEHHHHHHHHHH
23.4528857561
341UbiquitinationALQNAVEKEVQAEDN
HHHHHHHHHHHHCCC
57.49-
350PhosphorylationVQAEDNIYIENSLYA
HHHCCCEEEECCEEE
14.40-

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 HAVR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAVR1_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 HAVR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HAVR1_HUMAN !!

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HAVR1_HUMAN

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Related Literatures of Post-Translational Modification

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