SREC2_HUMAN - dbPTM
SREC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SREC2_HUMAN
UniProt AC Q96GP6
Protein Name Scavenger receptor class F member 2
Gene Name SCARF2
Organism Homo sapiens (Human).
Sequence Length 870
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Probable adhesion protein, which mediates homophilic and heterophilic interactions. In contrast to SCARF1, it poorly mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL) (By similarity)..
Protein Sequence MEGAGPRGAGPARRRGAGGPPSPLLPSLLLLLLLWMLPDTVAPQELNPRGRNVCRAPGSQVPTCCAGWRQQGDECGIAVCEGNSTCSENEVCVRPGECRCRHGYFGANCDTKCPRQFWGPDCKELCSCHPHGQCEDVTGQCTCHARRWGARCEHACQCQHGTCHPRSGACRCEPGWWGAQCASACYCSATSRCDPQTGACLCHAGWWGRSCNNQCACNSSPCEQQSGRCQCRERTFGARCDRYCQCFRGRCHPVDGTCACEPGYRGKYCREPCPAGFYGLGCRRRCGQCKGQQPCTVAEGRCLTCEPGWNGTKCDQPCATGFYGEGCSHRCPPCRDGHACNHVTGKCTRCNAGWIGDRCETKCSNGTYGEDCAFVCADCGSGHCDFQSGRCLCSPGVHGPHCNVTCPPGLHGADCAQACSCHEDTCDPVTGACHLETNQRKGVMGAGALLVLLVCLLLSLLGCCCACRGKDPTRRPRPRRELSLGRKKAPHRLCGRFSRISMKLPRIPLRRQKLPKVVVAHHDLDNTLNCSFLEPPSGLEQPSPSWSSRASFSSFDTTDEGPVYCVPHEEAPAESRDPEVPTVPAEAPAPSPVPLTTPASAEEAIPLPASSDSERSASSVEGPGGALYARVARREARPARARGEIGGLSLSPSPERRKPPPPDPATKPKVSWIHGKHSAAAAGRAPSPPPPGSEAAPSPSKRKRTPSDKSAHTVEHGSPRTRDPTPRPPGLPEEATALAAPSPPRARARAAPRPLGAHGRRRSPAKRAEAASMLAADVRGKTRSLGRAEVALGAQGPREKPAPPQKAKRSVPPASPARAPPATETPGPEKAATDLPAPETPRKKTPIQKPPRKKSREAAGELGRAGAPTL
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
83N-linked_GlycosylationGIAVCEGNSTCSENE
EEEEECCCCCCCCCC
16.32UniProtKB CARBOHYD
104PhosphorylationECRCRHGYFGANCDT
CEECCCCEECCCCCC
7.85-
111PhosphorylationYFGANCDTKCPRQFW
EECCCCCCCCCHHHC
36.42-
127PhosphorylationPDCKELCSCHPHGQC
CCHHHHHCCCCCCCC
28.25-
138PhosphorylationHGQCEDVTGQCTCHA
CCCCCCCCCEEEEEC
33.58-
142PhosphorylationEDVTGQCTCHARRWG
CCCCCEEEEECCCCC
10.23-
210PhosphorylationHAGWWGRSCNNQCAC
ECCCCCCCCCCCCCC
19.7724114839
219PhosphorylationNNQCACNSSPCEQQS
CCCCCCCCCHHHCCC
35.2324114839
220PhosphorylationNQCACNSSPCEQQSG
CCCCCCCCHHHCCCC
21.4124114839
226PhosphorylationSSPCEQQSGRCQCRE
CCHHHCCCCCCCCCC
28.0924114839
310N-linked_GlycosylationLTCEPGWNGTKCDQP
EECCCCCCCCCCCCC
54.92UniProtKB CARBOHYD
365N-linked_GlycosylationRCETKCSNGTYGEDC
CCCCCCCCCCCCCCC
57.19UniProtKB CARBOHYD
367PhosphorylationETKCSNGTYGEDCAF
CCCCCCCCCCCCCEE
32.38-
388PhosphorylationSGHCDFQSGRCLCSP
CCCCCCCCCCEEECC
28.35-
403N-linked_GlycosylationGVHGPHCNVTCPPGL
CCCCCCCCCCCCCCC
29.15UniProtKB CARBOHYD
474MethylationCRGKDPTRRPRPRRE
HCCCCCCCCCCCCCH
52.5830892187
478 (in isoform 2)Phosphorylation-42.2228842319
479MethylationPTRRPRPRRELSLGR
CCCCCCCCCHHHCCC
46.0846518869
483PhosphorylationPRPRRELSLGRKKAP
CCCCCHHHCCCCCCC
24.8324670416
498UbiquitinationHRLCGRFSRISMKLP
HHHCCHHHHHHCCCC
27.6123000965
498PhosphorylationHRLCGRFSRISMKLP
HHHCCHHHHHHCCCC
27.6129449344
501PhosphorylationCGRFSRISMKLPRIP
CCHHHHHHCCCCCCC
14.5724719451
503UbiquitinationRFSRISMKLPRIPLR
HHHHHHCCCCCCCCC
48.8523000965
527PhosphorylationAHHDLDNTLNCSFLE
EECCCCCCCCCCCCC
21.0028857561
531PhosphorylationLDNTLNCSFLEPPSG
CCCCCCCCCCCCCCC
31.6228857561
537PhosphorylationCSFLEPPSGLEQPSP
CCCCCCCCCCCCCCC
67.7227251275
543PhosphorylationPSGLEQPSPSWSSRA
CCCCCCCCCCHHCCC
31.1229978859
545PhosphorylationGLEQPSPSWSSRASF
CCCCCCCCHHCCCCC
43.8827251275
547PhosphorylationEQPSPSWSSRASFSS
CCCCCCHHCCCCCCC
17.8127251275
548PhosphorylationQPSPSWSSRASFSSF
CCCCCHHCCCCCCCC
26.1327251275
551PhosphorylationPSWSSRASFSSFDTT
CCHHCCCCCCCCCCC
25.2626657352
553PhosphorylationWSSRASFSSFDTTDE
HHCCCCCCCCCCCCC
27.8326657352
554PhosphorylationSSRASFSSFDTTDEG
HCCCCCCCCCCCCCC
25.7328192239
557PhosphorylationASFSSFDTTDEGPVY
CCCCCCCCCCCCCEE
33.8526657352
558PhosphorylationSFSSFDTTDEGPVYC
CCCCCCCCCCCCEEE
33.6227732954
564PhosphorylationTTDEGPVYCVPHEEA
CCCCCCEEEEECCCC
7.2925884760
575PhosphorylationHEEAPAESRDPEVPT
CCCCCHHHCCCCCCC
44.0523312004
582PhosphorylationSRDPEVPTVPAEAPA
HCCCCCCCCCCCCCC
44.2725850435
591PhosphorylationPAEAPAPSPVPLTTP
CCCCCCCCCCCCCCC
40.4125850435
596PhosphorylationAPSPVPLTTPASAEE
CCCCCCCCCCCCHHH
25.3525850435
597PhosphorylationPSPVPLTTPASAEEA
CCCCCCCCCCCHHHC
25.2525850435
600PhosphorylationVPLTTPASAEEAIPL
CCCCCCCCHHHCCCC
37.1025850435
610PhosphorylationEAIPLPASSDSERSA
HCCCCCCCCCCCCCC
32.5124275569
611PhosphorylationAIPLPASSDSERSAS
CCCCCCCCCCCCCCC
47.4624275569
613PhosphorylationPLPASSDSERSASSV
CCCCCCCCCCCCCCC
36.5424275569
616PhosphorylationASSDSERSASSVEGP
CCCCCCCCCCCCCCC
28.5726356563
618PhosphorylationSDSERSASSVEGPGG
CCCCCCCCCCCCCHH
35.8426356563
619PhosphorylationDSERSASSVEGPGGA
CCCCCCCCCCCCHHH
24.7326356563
628PhosphorylationEGPGGALYARVARRE
CCCHHHHHHHHHHHH
7.5725884760
646PhosphorylationARARGEIGGLSLSPS
CHHCCCCCCCCCCCC
27.0432142685
648PhosphorylationARGEIGGLSLSPSPE
HCCCCCCCCCCCCCC
3.8232142685
649PhosphorylationRGEIGGLSLSPSPER
CCCCCCCCCCCCCCC
30.0329255136
651PhosphorylationEIGGLSLSPSPERRK
CCCCCCCCCCCCCCC
21.6930266825
653PhosphorylationGGLSLSPSPERRKPP
CCCCCCCCCCCCCCC
35.7030266825
667AcetylationPPPDPATKPKVSWIH
CCCCCCCCCCEEEEC
44.9724847299
682PhosphorylationGKHSAAAAGRAPSPP
CCCCHHHCCCCCCCC
11.8632142685
687PhosphorylationAAAGRAPSPPPPGSE
HHCCCCCCCCCCCCC
49.4030266825
693PhosphorylationPSPPPPGSEAAPSPS
CCCCCCCCCCCCCCC
29.8125219547
695PhosphorylationPPPPGSEAAPSPSKR
CCCCCCCCCCCCCCC
26.7732142685
698PhosphorylationPGSEAAPSPSKRKRT
CCCCCCCCCCCCCCC
36.7630266825
700PhosphorylationSEAAPSPSKRKRTPS
CCCCCCCCCCCCCCC
49.8030266825
705PhosphorylationSPSKRKRTPSDKSAH
CCCCCCCCCCCHHCC
30.1327732954
707PhosphorylationSKRKRTPSDKSAHTV
CCCCCCCCCHHCCCC
57.9928857561
710PhosphorylationKRTPSDKSAHTVEHG
CCCCCCHHCCCCCCC
30.2120363803
713PhosphorylationPSDKSAHTVEHGSPR
CCCHHCCCCCCCCCC
27.5726699800
718PhosphorylationAHTVEHGSPRTRDPT
CCCCCCCCCCCCCCC
17.0830266825
721PhosphorylationVEHGSPRTRDPTPRP
CCCCCCCCCCCCCCC
42.6926437602
725PhosphorylationSPRTRDPTPRPPGLP
CCCCCCCCCCCCCCC
35.9021902226
736PhosphorylationPGLPEEATALAAPSP
CCCCHHHHHHCCCCC
26.0321902226
737PhosphorylationGLPEEATALAAPSPP
CCCHHHHHHCCCCCH
11.4032142685
742PhosphorylationATALAAPSPPRARAR
HHHHCCCCCHHHHHH
42.6930266825
784PhosphorylationDVRGKTRSLGRAEVA
HHCCCCCCCCCHHHH
40.1724719451
785PhosphorylationVRGKTRSLGRAEVAL
HCCCCCCCCCHHHHC
4.9227251275
815PhosphorylationKRSVPPASPARAPPA
CCCCCCCCCCCCCCC
25.5122985185
823PhosphorylationPARAPPATETPGPEK
CCCCCCCCCCCCCCC
46.28-
825PhosphorylationRAPPATETPGPEKAA
CCCCCCCCCCCCCCC
29.23-
833PhosphorylationPGPEKAATDLPAPET
CCCCCCCCCCCCCCC
42.82-
840PhosphorylationTDLPAPETPRKKTPI
CCCCCCCCCCCCCCC
27.6019664994
841PhosphorylationDLPAPETPRKKTPIQ
CCCCCCCCCCCCCCC
44.4227251275
855PhosphorylationQKPPRKKSREAAGEL
CCCCCHHHHHHHHHH
38.0920363803
856PhosphorylationKPPRKKSREAAGELG
CCCCHHHHHHHHHHH
46.5927251275
869PhosphorylationLGRAGAPTL------
HHHCCCCCC------
44.5624670416

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 SREC2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SREC2_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 SREC2_HUMAN !!

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

Oops, there are no PPI records of SREC2_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600920Van den Ende-Gupta syndrome (VDEGS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SREC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; SER-653; SER-687AND SER-698, AND MASS SPECTROMETRY.

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