SCRB1_HUMAN - dbPTM
SCRB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCRB1_HUMAN
UniProt AC Q8WTV0
Protein Name Scavenger receptor class B member 1
Gene Name SCARB1
Organism Homo sapiens (Human).
Sequence Length 552
Subcellular Localization Cell membrane
Multi-pass membrane protein. Membrane, caveola
Multi-pass membrane protein. Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae.
Protein Description Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. [PubMed: 12016218]
Protein Sequence MGCSAKARWAAGALGVAGLLCAVLGAVMIVMVPSLIKQQVLKNVRIDPSSLSFNMWKEIPIPFYLSVYFFDVMNPSEILKGEKPQVRERGPYVYREFRHKSNITFNNNDTVSFLEYRTFQFQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFMNRTVGEIMWGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGLSKVDFWHSDQCNMINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKESGVFEGIPTYRFVAPKTLFANGSIYPPNEGFCPCLESGIQNVSTCRFSAPLFLSHPHFLNADPVLAEAVTGLHPNQEAHSLFLDIHPVTGIPMNCSVKLQLSLYMKSVAGIGQTGKIEPVVLPLLWFAESGAMEGETLHTFYTQLVLMPKVMHYAQYVLLALGCVLLLVPVICQIRSQVGAGQRAARADSHSLACWGKGASDRTLWPTAAWSPPPAAVLRLCRSGSGHCWGLRSTLASFACRVATTLPVLEGLGPSLGGGTGS
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
3S-palmitoylation-----MGCSAKARWA
-----CCCHHHHHHH		3.2729575903
34PhosphorylationVMIVMVPSLIKQQVL
HHHHHCHHHHHHHHH		31.1724719451
64PhosphorylationKEIPIPFYLSVYFFD
CCCCCCEEEEEEEEE		7.8529083192
66PhosphorylationIPIPFYLSVYFFDVM
CCCCEEEEEEEEECC		11.9129083192
68PhosphorylationIPFYLSVYFFDVMNP
CCEEEEEEEEECCCH		8.6429083192
84 (in isoform 3)Ubiquitination-33.3321890473
92PhosphorylationQVRERGPYVYREFRH
CHHHCCCCCEEEEEC		16.97-
102N-linked_GlycosylationREFRHKSNITFNNND
EEEECCCCEEECCCC		41.9719159218
108N-linked_GlycosylationSNITFNNNDTVSFLE
CCEEECCCCEEEEEE		47.65UniProtKB CARBOHYD
149 (in isoform 4)Ubiquitination-43.9621890473
154PhosphorylationMMENKPMTLKLIMTL
HHCCCCCHHHHHHHH		29.3024719451
160PhosphorylationMTLKLIMTLAFTTLG
CHHHHHHHHHHHHHH		14.1322210691
164PhosphorylationLIMTLAFTTLGERAF
HHHHHHHHHHHHHHH		18.5922210691
165PhosphorylationIMTLAFTTLGERAFM
HHHHHHHHHHHHHHH		26.7222210691
173N-linked_GlycosylationLGERAFMNRTVGEIM
HHHHHHHCCCHHHHH		29.98UniProtKB CARBOHYD
175PhosphorylationERAFMNRTVGEIMWG
HHHHHCCCHHHHHHC		28.0522210691
184 (in isoform 2)Ubiquitination-49.2721890473
184UbiquitinationGEIMWGYKDPLVNLI
HHHHHCCCCHHHHHH		49.27-
184 (in isoform 1)Ubiquitination-49.2721906983
188 (in isoform 3)Ubiquitination-7.1521890473
212N-linked_GlycosylationFGLFAELNNSDSGLF
CCCEEEECCCCCCCE		37.15UniProtKB CARBOHYD
227N-linked_GlycosylationTVFTGVQNISRIHLV
EEEECCCCCCEEEEE		31.62UniProtKB CARBOHYD
253 (in isoform 4)Ubiquitination-3.1121890473
255N-linked_GlycosylationSDQCNMINGTSGQMW
HHHCCCCCCCCCCCC		36.60UniProtKB CARBOHYD
267O-linked_GlycosylationQMWPPFMTPESSLEF
CCCCCCCCCHHHCEE		25.04OGP
288UbiquitinationRSMKLMYKESGVFEG
HHCCEEHHHCCCCCC		31.29-
288 (in isoform 1)Ubiquitination-31.2921906983
288 (in isoform 2)Ubiquitination-31.2921890473
290PhosphorylationMKLMYKESGVFEGIP
CCEEHHHCCCCCCCC		35.7822210691
298PhosphorylationGVFEGIPTYRFVAPK
CCCCCCCEEEEECCC		25.9622210691
310N-linked_GlycosylationAPKTLFANGSIYPPN
CCCEEEECCCCCCCC		37.09UniProtKB CARBOHYD
330N-linked_GlycosylationCLESGIQNVSTCRFS
HHHHHCCCCCCCCCC		27.9919159218
375 (in isoform 3)Phosphorylation-15.5030108239
376 (in isoform 3)Phosphorylation-26.2130108239
377 (in isoform 3)Phosphorylation-4.7822617229
378PhosphorylationFLDIHPVTGIPMNCS
EEEEECCCCCCCCCE		33.57-
383N-linked_GlycosylationPVTGIPMNCSVKLQL
CCCCCCCCCEEEEEH		15.01UniProtKB CARBOHYD
384 (in isoform 3)Ubiquitination-3.9321890473
385PhosphorylationTGIPMNCSVKLQLSL
CCCCCCCEEEEEHHH		19.79-
390 (in isoform 3)Phosphorylation-5.7325159151
391 (in isoform 3)Phosphorylation-12.4220166139
391PhosphorylationCSVKLQLSLYMKSVA
CEEEEEHHHHHHCCC		12.4226852163
393PhosphorylationVKLQLSLYMKSVAGI
EEEEHHHHHHCCCCC		10.1026852163
393 (in isoform 3)Phosphorylation-10.1025159151
396 (in isoform 3)Phosphorylation-10.7320166139
397 (in isoform 3)Phosphorylation-4.7630108239
400 (in isoform 3)Ubiquitination-2.3921890473
402 (in isoform 3)Phosphorylation-45.2030108239
403PhosphorylationSVAGIGQTGKIEPVV
CCCCCCCCCCCCCCE		34.9220068231
408 (in isoform 3)Ubiquitination-25.6221890473
440 (in isoform 4)Phosphorylation-2.0530108239
441 (in isoform 4)Phosphorylation-2.2030108239
442 (in isoform 4)Phosphorylation-20.1222617229
446PhosphorylationKVMHYAQYVLLALGC
HHHHHHHHHHHHHHH		5.7222817900
449 (in isoform 4)Ubiquitination-2.3621890473
455 (in isoform 4)Phosphorylation-3.3925159151
456 (in isoform 4)Phosphorylation-1.9520166139
458 (in isoform 4)Phosphorylation-3.4325159151
461 (in isoform 4)Phosphorylation-0.8720166139
462S-palmitoylationLLLVPVICQIRSQVG
HHHHHHHHHHHHHCC		2.5429575903
462 (in isoform 4)Phosphorylation-2.5430108239
465 (in isoform 4)Ubiquitination-8.6521890473
466 (in isoform 5)Phosphorylation-30.7430177828
467 (in isoform 4)Phosphorylation-28.0230108239
472 (in isoform 5)Phosphorylation-31.1630177828
473 (in isoform 4)Ubiquitination-29.3321890473
474 (in isoform 5)Phosphorylation-8.0730177828
475 (in isoform 2)Phosphorylation-14.9130108239
476 (in isoform 2)Phosphorylation-37.6330108239
477 (in isoform 2)Phosphorylation-20.2422617229
481PhosphorylationAARADSHSLACWGKG
HHHCCCCCCCCCCCC		22.9320068231
484 (in isoform 2)Ubiquitination-6.2921890473
484UbiquitinationADSHSLACWGKGASD
CCCCCCCCCCCCCCC		6.2921890473
487 (in isoform 5)Phosphorylation-27.1424275569
489 (in isoform 5)Phosphorylation-16.2530177828
490 (in isoform 2)Phosphorylation-35.9725159151
490PhosphorylationACWGKGASDRTLWPT
CCCCCCCCCCCCCCC		35.9719901323
490 (in isoform 5)Phosphorylation-35.9730177828
491 (in isoform 2)Phosphorylation-47.2320166139
491PhosphorylationCWGKGASDRTLWPTA
CCCCCCCCCCCCCCC		47.2320166139
493PhosphorylationGKGASDRTLWPTAAW
CCCCCCCCCCCCCCC		37.8620166139
493 (in isoform 2)Phosphorylation-37.8625159151
496PhosphorylationASDRTLWPTAAWSPP
CCCCCCCCCCCCCCC		18.4420166139
496 (in isoform 5)Phosphorylation-18.4430177828
496 (in isoform 2)Phosphorylation-18.4420166139
497 (in isoform 2)Phosphorylation-19.8930108239
498 (in isoform 5)Phosphorylation-11.6730177828
500 (in isoform 2)Ubiquitination-14.6521890473
502 (in isoform 2)Phosphorylation-28.3530108239
503 (in isoform 5)Phosphorylation-26.1630177828
505 (in isoform 5)Phosphorylation-18.9030177828
508 (in isoform 2)Ubiquitination-2.7221890473
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 SCRB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCRB1_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 SCRB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APOA1_HUMANAPOA1physical
10764676
APOA2_HUMANAPOA2physical
10764676
KRA59_HUMANKRTAP5-9physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
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 SCRB1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-102 AND ASN-330, AND MASSSPECTROMETRY.

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