STAB2_HUMAN - dbPTM
STAB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAB2_HUMAN
UniProt AC Q8WWQ8
Protein Name Stabilin-2
Gene Name STAB2 {ECO:0000312|EMBL:CAC82105.1}
Organism Homo sapiens (Human).
Sequence Length 2551
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cytoplasm . Only a small amount appears to be present at the cell surface (PubMed:17145755).
Protein Description Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalisation as well as HA and CS..
Protein Sequence MMLQHLVIFCLGLVVQNFCSPAETTGQARRCDRKSLLTIRTECRSCALNLGVKCPDGYTMITSGSVGVRDCRYTFEVRTYSLSLPGCRHICRKDYLQPRCCPGRWGPDCIECPGGAGSPCNGRGSCAEGMEGNGTCSCQEGFGGTACETCADDNLFGPSCSSVCNCVHGVCNSGLDGDGTCECYSAYTGPKCDKPIPECAALLCPENSRCSPSTEDENKLECKCLPNYRGDGKYCDPINPCLRKICHPHAHCTYLGPNRHSCTCQEGYRGDGQVCLPVDPCQINFGNCPTKSTVCKYDGPGQSHCECKEHYQNFVPGVGCSMTDICKSDNPCHRNANCTTVAPGRTECICQKGYVGDGLTCYGNIMERLRELNTEPRGKWQGRLTSFISLLDKAYAWPLSKLGPFTVLLPTDKGLKGFNVNELLVDNKAAQYFVKLHIIAGQMNIEYMNNTDMFYTLTGKSGEIFNSDKDNQIKLKLHGGKKKVKIIQGDIIASNGLLHILDRAMDKLEPTFESNNEQTIMTMLQPRYSKFRSLLEETNLGHALDEDGVGGPYTIFVPNNEALNNMKDGTLDYLLSPEGSRKLLELVRYHIVPFTQLEVATLISTPHIRSMANQLIQFNTTDNGQILANDVAMEEIEITAKNGRIYTLTGVLIPPSIVPILPHRCDETKREMKLGTCVSCSLVYWSRCPANSEPTALFTHRCVYSGRFGSLKSGCARYCNATVKIPKCCKGFYGPDCNQCPGGFSNPCSGNGQCADSLGGNGTCICEEGFQGSQCQFCSDPNKYGPRCNKKCLCVHGTCNNRIDSDGACLTGTCRDGSAGRLCDKQTSACGPYVQFCHIHATCEYSNGTASCICKAGYEGDGTLCSEMDPCTGLTPGGCSRNAECIKTGTGTHTCVCQQGWTGNGRDCSEINNCLLPSAGGCHDNASCLYVGPGQNECECKKGFRGNGIDCEPITSCLEQTGKCHPLASCQSTSSGVWSCVCQEGYEGDGFLCYGNAAVELSFLSEAAIFNRWINNASLQPTLSATSNLTVLVPSQQATEDMDQDEKSFWLSQSNIPALIKYHMLLGTYRVADLQTLSSSDMLATSLQGNFLHLAKVDGNITIEGASIVDGDNAATNGVIHIINKVLVPQRRLTGSLPNLLMRLEQMPDYSIFRGYIIQYNLANAIEAADAYTVFAPNNNAIENYIREKKVLSLEEDVLRYHVVLEEKLLKNDLHNGMHRETMLGFSYFLSFFLHNDQLYVNEAPINYTNVATDKGVIHGLGKVLEIQKNRCDNNDTTIIRGRCRTCSSELTCPFGTKSLGNEKRRCIYTSYFMGRRTLFIGCQPKCVRTVITRECCAGFFGPQCQPCPGNAQNVCFGNGICLDGVNGTGVCECGEGFSGTACETCTEGKYGIHCDQACSCVHGRCNQGPLGDGSCDCDVGWRGVHCDNATTEDNCNGTCHTSANCLTNSDGTASCKCAAGFQGNGTICTAINACEISNGGCSAKADCKRTTPGRRVCTCKAGYTGDGIVCLEINPCLENHGGCDKNAECTQTGPNQAACNCLPAYTGDGKVCTLINVCLTKNGGCSEFAICNHTGQVERTCTCKPNYIGDGFTCRGSIYQELPKNPKTSQYFFQLQEHFVKDLVGPGPFTVFAPLSAAFDEEARVKDWDKYGLMPQVLRYHVVACHQLLLENLKLISNATSLQGEPIVISVSQSTVYINNKAKIISSDIISTNGIVHIIDKLLSPKNLLITPKDNSGRILQNLTTLATNNGYIKFSNLIQDSGLLSVITDPIHTPVTLFWPTDQALHALPAEQQDFLFNQDNKDKLKEYLKFHVIRDAKVLAVDLPTSTAWKTLQGSELSVKCGAGRDIGDLFLNGQTCRIVQRELLFDLGVAYGIDCLLIDPTLGGRCDTFTTFDASGECGSCVNTPSCPRWSKPKGVKQKCLYNLPFKRNLEGCRERCSLVIQIPRCCKGYFGRDCQACPGGPDAPCNNRGVCLDQYSATGECKCNTGFNGTACEMCWPGRFGPDCLPCGCSDHGQCDDGITGSGQCLCETGWTGPSCDTQAVLPAVCTPPCSAHATCKENNTCECNLDYEGDGITCTVVDFCKQDNGGCAKVARCSQKGTKVSCSCQKGYKGDGHSCTEIDPCADGLNGGCHEHATCKMTGPGKHKCECKSHYVGDGLNCEPEQLPIDRCLQDNGQCHADAKCVDLHFQDTTVGVFHLRSPLGQYKLTFDKAREACANEAATMATYNQLSYAQKAKYHLCSAGWLETGRVAYPTAFASQNCGSGVVGIVDYGPRPNKSEMWDVFCYRMKDVNCTCKVGYVGDGFSCSGNLLQVLMSFPSLTNFLTEVLAYSNSSARGRAFLEHLTDLSIRGTLFVPQNSGLGENETLSGRDIEHHLANVSMFFYNDLVNGTTLQTRLGSKLLITASQDPLQPTETRFVDGRAILQWDIFASNGIIHVISRPLKAPPAPVTLTHTGLGAGIFFAIILVTGAVALAAYSYFRINRRTIGFQHFESEEDINVAALGKQQPENISNPLYESTTSAPPEPSYDPFTDSEERQLEGNDPLRTL
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
20PhosphorylationLVVQNFCSPAETTGQ
HHHHHCCCHHHCCCC		24.0224043423
24PhosphorylationNFCSPAETTGQARRC
HCCCHHHCCCCCCCC		38.0324043423
25PhosphorylationFCSPAETTGQARRCD
CCCHHHCCCCCCCCC		20.8524043423
35O-linked_GlycosylationARRCDRKSLLTIRTE
CCCCCCCCCEEEEHH		29.5231492838
38O-linked_GlycosylationCDRKSLLTIRTECRS
CCCCCCEEEEHHHHH		17.4431492838
45PhosphorylationTIRTECRSCALNLGV
EEEHHHHHHHHHCCC		18.52-
58PhosphorylationGVKCPDGYTMITSGS
CCCCCCCCEEEECCC		10.66-
133N-linked_GlycosylationCAEGMEGNGTCSCQE
CCCCCCCCCCCCCCC		29.33UniProtKB CARBOHYD
337N-linked_GlycosylationNPCHRNANCTTVAPG
CCCCCCCCCCEECCC		27.50UniProtKB CARBOHYD
374PhosphorylationERLRELNTEPRGKWQ
HHHHHHCCCCCCCCC		61.0525690035
385PhosphorylationGKWQGRLTSFISLLD
CCCCCHHHHHHHHHH		21.89-
386PhosphorylationKWQGRLTSFISLLDK
CCCCHHHHHHHHHHH		25.77-
389PhosphorylationGRLTSFISLLDKAYA
CHHHHHHHHHHHHHC		22.3729457462
395PhosphorylationISLLDKAYAWPLSKL
HHHHHHHHCCCHHHH		18.2322817900
449N-linked_GlycosylationQMNIEYMNNTDMFYT
CCCEEECCCCCEEEE		47.55UniProtKB CARBOHYD
619N-linked_GlycosylationANQLIQFNTTDNGQI
HHHHEEEECCCCCCE		26.20UniProtKB CARBOHYD
720N-linked_GlycosylationSGCARYCNATVKIPK
HCCHHHCCCEEECCC		29.70UniProtKB CARBOHYD
761N-linked_GlycosylationCADSLGGNGTCICEE
CCHHCCCCCEEEECC		40.58UniProtKB CARBOHYD
847N-linked_GlycosylationHATCEYSNGTASCIC
EEEEECCCCCEEEEE		51.43UniProtKB CARBOHYD
925N-linked_GlycosylationSAGGCHDNASCLYVG
CCCCCCCCCCEEEEC		15.30UniProtKB CARBOHYD
1016N-linked_GlycosylationIFNRWINNASLQPTL
HHHHHHHCCCCCCCE		23.05UniProtKB CARBOHYD
1026PhosphorylationLQPTLSATSNLTVLV
CCCCEECCCCEEEEE		18.1225332170
1028N-linked_GlycosylationPTLSATSNLTVLVPS
CCEECCCCEEEEECC		35.06UniProtKB CARBOHYD
1061AcetylationSNIPALIKYHMLLGT
CCHHHHHHHHHHHCC		29.927429713
1062PhosphorylationNIPALIKYHMLLGTY
CHHHHHHHHHHHCCE		5.8624114839
1068PhosphorylationKYHMLLGTYRVADLQ
HHHHHHCCEEEECCC		14.23-
1069PhosphorylationYHMLLGTYRVADLQT
HHHHHCCEEEECCCC		10.99-
1100N-linked_GlycosylationHLAKVDGNITIEGAS
EEEEECCCEEEECCE		24.62UniProtKB CARBOHYD
1102PhosphorylationAKVDGNITIEGASIV
EEECCCEEEECCEEE		19.58-
1107PhosphorylationNITIEGASIVDGDNA
CEEEECCEEECCCCC		33.72-
1116PhosphorylationVDGDNAATNGVIHII
ECCCCCCCCCCEEEE		30.05-
1136PhosphorylationPQRRLTGSLPNLLMR
CCHHHCCCHHHHHHH		35.10-
1247N-linked_GlycosylationYVNEAPINYTNVATD
EECCCCCCCEEECCC		36.20UniProtKB CARBOHYD
1275N-linked_GlycosylationQKNRCDNNDTTIIRG
HHCCCCCCCCEEEEC		34.45UniProtKB CARBOHYD
1286PhosphorylationIIRGRCRTCSSELTC
EEECCCCCCCCCEEC		21.9925907765
1288PhosphorylationRGRCRTCSSELTCPF
ECCCCCCCCCEECCC		26.6625907765
1289PhosphorylationGRCRTCSSELTCPFG
CCCCCCCCCEECCCC		38.4825907765
1292PhosphorylationRTCSSELTCPFGTKS
CCCCCCEECCCCCCC		17.6825907765
1297PhosphorylationELTCPFGTKSLGNEK
CEECCCCCCCCCCCC		20.1725907765
1299PhosphorylationTCPFGTKSLGNEKRR
ECCCCCCCCCCCCCE		41.1525907765
1309PhosphorylationNEKRRCIYTSYFMGR
CCCCEEEEEEEECCC		8.0224043423
1310PhosphorylationEKRRCIYTSYFMGRR
CCCEEEEEEEECCCC		9.3124043423
1311PhosphorylationKRRCIYTSYFMGRRT
CCEEEEEEEECCCCE		10.2124043423
1312PhosphorylationRRCIYTSYFMGRRTL
CEEEEEEEECCCCEE		6.9824043423
1367N-linked_GlycosylationGICLDGVNGTGVCEC
CEEECCCCCCCEECC		48.08UniProtKB CARBOHYD
1429N-linked_GlycosylationWRGVHCDNATTEDNC
CCEEECCCCCCCCCC		44.58UniProtKB CARBOHYD
1437N-linked_GlycosylationATTEDNCNGTCHTSA
CCCCCCCCCEEECCC		55.87UniProtKB CARBOHYD
1465N-linked_GlycosylationCAAGFQGNGTICTAI
CCCCCCCCCEEEEEE		33.38UniProtKB CARBOHYD
1504PhosphorylationVCTCKAGYTGDGIVC
EEEEECCCCCCCEEE		16.6527642862
1573N-linked_GlycosylationCSEFAICNHTGQVER
CCCEEEECCCCCEEE		29.64UniProtKB CARBOHYD
1588PhosphorylationTCTCKPNYIGDGFTC
EEECCCCEECCCEEE		18.14-
1679N-linked_GlycosylationENLKLISNATSLQGE
HHHHHHHCCHHCCCC		40.00UniProtKB CARBOHYD
1707PhosphorylationNNKAKIISSDIISTN
CCCCEEEECCCCCCC		25.98-
1725PhosphorylationHIIDKLLSPKNLLIT
HHHHHHCCCCCEEEE		44.2424719451
1732PhosphorylationSPKNLLITPKDNSGR
CCCCEEEECCCCCCC		25.02-
1743N-linked_GlycosylationNSGRILQNLTTLATN
CCCCHHHHHHEECCC		35.5919159218
1993N-linked_GlycosylationCKCNTGFNGTACEMC
CCCCCCCCCCCCCEE		48.53UniProtKB CARBOHYD
2064N-linked_GlycosylationAHATCKENNTCECNL
CCCCCCCCCEEEECC		34.31UniProtKB CARBOHYD
2104PhosphorylationARCSQKGTKVSCSCQ
EEECCCCCEEEEECC		35.00-
2107PhosphorylationSQKGTKVSCSCQKGY
CCCCCEEEEECCCCC		11.23-
2109PhosphorylationKGTKVSCSCQKGYKG
CCCEEEEECCCCCCC		16.45-
2256PhosphorylationLETGRVAYPTAFASQ
HCCCCCCCCCHHHCC		9.7723403867
2258PhosphorylationTGRVAYPTAFASQNC
CCCCCCCCHHHCCCC		23.0223403867
2262PhosphorylationAYPTAFASQNCGSGV
CCCCHHHCCCCCCCE		18.5723403867
2280N-linked_GlycosylationVDYGPRPNKSEMWDV
EECCCCCCHHHCCEE		62.86UniProtKB CARBOHYD
2282PhosphorylationYGPRPNKSEMWDVFC
CCCCCCHHHCCEEEE		39.0523403867
2296N-linked_GlycosylationCYRMKDVNCTCKVGY
EEEECCCCCEEEEEE		26.05UniProtKB CARBOHYD
2336N-linked_GlycosylationTEVLAYSNSSARGRA
HHHHHHCCCCHHHHH		27.57UniProtKB CARBOHYD
2352PhosphorylationLEHLTDLSIRGTLFV
HHHHHHCEECCEEEE		17.0424719451
2368N-linked_GlycosylationQNSGLGENETLSGRD
CCCCCCCCCCCCCHH		45.84UniProtKB CARBOHYD
2382N-linked_GlycosylationDIEHHLANVSMFFYN
HHHHHHHHCCEEEEC		32.53UniProtKB CARBOHYD
2393N-linked_GlycosylationFFYNDLVNGTTLQTR
EEECCCCCCCCEEEE		49.76UniProtKB CARBOHYD
2403PhosphorylationTLQTRLGSKLLITAS
CEEEECCCEEEEEEC		25.4024043423
2408PhosphorylationLGSKLLITASQDPLQ
CCCEEEEEECCCCCC		21.8924043423
2410PhosphorylationSKLLITASQDPLQPT
CEEEEEECCCCCCCC		26.8524043423
2419PhosphorylationDPLQPTETRFVDGRA
CCCCCCCEEEECCEE		31.7024043423
2435PhosphorylationLQWDIFASNGIIHVI
EEEEEEECCCEEEEE		25.4922210691
2443PhosphorylationNGIIHVISRPLKAPP
CCEEEEEECCCCCCC		27.1022210691
2489PhosphorylationYFRINRRTIGFQHFE
HHHCCCCCCCCCCCC		23.4020166139
2497PhosphorylationIGFQHFESEEDINVA
CCCCCCCCHHHCCHH		45.3920166139
2537PhosphorylationSYDPFTDSEERQLEG
CCCCCCCHHHHHHCC		38.0024275569
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 STAB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAB2_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 STAB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK03_HUMANMAPK3physical
18387958
MK01_HUMANMAPK1physical
18387958
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 STAB2_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-1743, AND MASSSPECTROMETRY.

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