SCAR3_HUMAN - dbPTM
SCAR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCAR3_HUMAN
UniProt AC Q6AZY7
Protein Name Scavenger receptor class A member 3
Gene Name SCARA3
Organism Homo sapiens (Human).
Sequence Length 606
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein . Golgi apparatus membrane
Single-pass type II membrane protein . Endoplasmic reticulum and/or Golgi.
Protein Description Seems to protect cells by scavenging oxidative molecules or harmful products of oxidation..
Protein Sequence MKVRSAGGDGDALCVTEEDLAGDDEDMPTFPCTQKGRPGPRCSRCQKNLSLHTSVRILYLFLALLLVAVAVLASLVFRKVDSLSEDISLTQSIYDKKLVLMQKNLQGLDPKALNNCSFCHEAGQLGPEIRKLQEELEGIQKLLLAQEVQLDQTLQAQEVLSTTSRQISQEMGSCSFSIHQVNQSLGLFLAQVRGWQATTAGLDLSLKDLTQECYDVKAAVHQINFTVGQTSEWIHGIQRKTDEETLTLQKIVTDWQNYTRLFSGLRTTSTKTGEAVKNIQATLGASSQRISQNSESMHDLVLQVMGLQLQLDNISSFLDDHEENMHDLQYHTHYAQNRTVERFESLEGRMASHEIEIGTIFTNINATDNHVHSMLKYLDDVRLSCTLGFHTHAEELYYLNKSVSIMLGTTDLLRERFSLLSARLDLNVRNLSMIVEEMKAVDTQHGEILRNVTILRGAPGPPGPRGFKGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQPGPKGDIGPPGPEGPPGSPGPSGPQGKPGIAGKTGSPGQRGAMGPKGEPGIQGPPGLPGPPGPPGSQSFY
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
50PhosphorylationSRCQKNLSLHTSVRI
CHHHHCCCHHHHHHH
27.7424043423
53PhosphorylationQKNLSLHTSVRILYL
HHCCCHHHHHHHHHH
33.9224043423
54PhosphorylationKNLSLHTSVRILYLF
HCCCHHHHHHHHHHH
9.9224043423
59PhosphorylationHTSVRILYLFLALLL
HHHHHHHHHHHHHHH
7.9524043423
74PhosphorylationVAVAVLASLVFRKVD
HHHHHHHHHHHHCCC
22.3924043423
84PhosphorylationFRKVDSLSEDISLTQ
HHCCCCCCCCCCCCH
36.8627050516
97UbiquitinationTQSIYDKKLVLMQKN
CHHHHHHHHHHHHHH
40.7129967540
103UbiquitinationKKLVLMQKNLQGLDP
HHHHHHHHHCCCCCH
45.7329967540
115N-linked_GlycosylationLDPKALNNCSFCHEA
CCHHHHCCCHHHHHH
24.53UniProtKB CARBOHYD
131UbiquitinationQLGPEIRKLQEELEG
HCCHHHHHHHHHHHH
61.2529967540
182N-linked_GlycosylationSFSIHQVNQSLGLFL
CEEHHHHHHHHHHHH
21.10UniProtKB CARBOHYD
224N-linked_GlycosylationKAAVHQINFTVGQTS
HHHHHCCCEECCCCH
21.70UniProtKB CARBOHYD
240UbiquitinationWIHGIQRKTDEETLT
HHHCCCCCCCCCCCH
43.9129967540
257N-linked_GlycosylationKIVTDWQNYTRLFSG
HHHHCHHHHHHHHCC
35.57UniProtKB CARBOHYD
277UbiquitinationTKTGEAVKNIQATLG
CCHHHHHHHHHHHHC
56.2121987572
277 (in isoform 1)Ubiquitination-56.2121906983
277 (in isoform 2)Ubiquitination-56.2121906983
286PhosphorylationIQATLGASSQRISQN
HHHHHCCCHHHHHCC
25.79-
313N-linked_GlycosylationGLQLQLDNISSFLDD
CHHHHHHCHHHHHHH
44.63UniProtKB CARBOHYD
337N-linked_GlycosylationYHTHYAQNRTVERFE
HHHHHHCCCHHHHHH
33.16UniProtKB CARBOHYD
365N-linked_GlycosylationGTIFTNINATDNHVH
EEEEECCCCCCCHHH
38.57UniProtKB CARBOHYD
400N-linked_GlycosylationAEELYYLNKSVSIML
HHHHHHHCCCHHHHH
20.59UniProtKB CARBOHYD
421PhosphorylationRERFSLLSARLDLNV
HHHHHHHHHHHCCCC
19.3524719451
430N-linked_GlycosylationRLDLNVRNLSMIVEE
HHCCCCCCHHHHHHH
31.98UniProtKB CARBOHYD
451N-linked_GlycosylationQHGEILRNVTILRGA
CCCHHHHHEEEECCC
31.66UniProtKB CARBOHYD
459 (in isoform 2)Phosphorylation-59.66-
462 (in isoform 2)Phosphorylation-71.92-

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 SCAR3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCAR3_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 SCAR3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XIAP_HUMANXIAPphysical
22683311
COL12_HUMANCOLEC12physical
26186194
XPO7_HUMANXPO7physical
26186194
COCH_HUMANCOCHphysical
26186194
1A02_HUMANHLA-Aphysical
26186194
1A03_HUMANHLA-Aphysical
26186194
1A01_HUMANHLA-Aphysical
26186194
1A26_HUMANHLA-Aphysical
26186194
PXDN_HUMANPXDNphysical
26186194
ABHEA_HUMANABHD14Aphysical
26186194
ATR_HUMANATRphysical
26186194
HEAT3_HUMANHEATR3physical
26186194
SENP1_HUMANSENP1physical
26186194
IQCB1_HUMANIQCB1physical
26186194
CLC4K_HUMANCD207physical
26186194
LRIG1_HUMANLRIG1physical
26186194
DNJB9_HUMANDNAJB9physical
26186194
INT6_HUMANINTS6physical
26186194
PBIP1_HUMANPBXIP1physical
26186194
S39A6_HUMANSLC39A6physical
26186194
TXD11_HUMANTXNDC11physical
26186194
F207A_HUMANFAM207Aphysical
26186194
AT2B2_HUMANATP2B2physical
26186194
S39A1_HUMANSLC39A1physical
26186194
SETD2_HUMANSETD2physical
26186194
TNPO3_HUMANTNPO3physical
26186194
MA1A2_HUMANMAN1A2physical
26186194
EXOC2_HUMANEXOC2physical
26186194
EXTL3_HUMANEXTL3physical
26186194
SUN1_HUMANSUN1physical
26186194
GPC6_HUMANGPC6physical
26186194
SDCG8_HUMANSDCCAG8physical
26186194
SAAL1_HUMANSAAL1physical
26186194
DEGS1_HUMANDEGS1physical
26186194
SUN2_HUMANSUN2physical
26186194
MD1L1_HUMANMAD1L1physical
26186194
EMIL3_HUMANEMILIN3physical
26186194
GRM1C_HUMANGRAMD1Cphysical
26186194
NDEL1_HUMANNDEL1physical
26186194
IKIP_HUMANIKBIPphysical
26186194
CKLF6_HUMANCMTM6physical
26186194
CS025_HUMANC19orf25physical
26186194
SNG2_HUMANSYNGR2physical
21516116
COL12_HUMANCOLEC12physical
28514442
SDCG8_HUMANSDCCAG8physical
28514442
INT6_HUMANINTS6physical
28514442
ATR_HUMANATRphysical
28514442
COCH_HUMANCOCHphysical
28514442
EXTL3_HUMANEXTL3physical
28514442
PBIP1_HUMANPBXIP1physical
28514442
TNPO3_HUMANTNPO3physical
28514442
SUN1_HUMANSUN1physical
28514442
GRM1C_HUMANGRAMD1Cphysical
28514442
S39A1_HUMANSLC39A1physical
28514442
HEAT3_HUMANHEATR3physical
28514442
SETD2_HUMANSETD2physical
28514442
XPO7_HUMANXPO7physical
28514442
ABHEA_HUMANABHD14Aphysical
28514442
MA1A2_HUMANMAN1A2physical
28514442
LRIG1_HUMANLRIG1physical
28514442
IQCB1_HUMANIQCB1physical
28514442
DEGS1_HUMANDEGS1physical
28514442
DNJB9_HUMANDNAJB9physical
28514442
SAAL1_HUMANSAAL1physical
28514442
SUN2_HUMANSUN2physical
28514442
AT2B2_HUMANATP2B2physical
28514442
IKIP_HUMANIKBIPphysical
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 SCAR3_HUMAN

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Related Literatures of Post-Translational Modification

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