STAB1_HUMAN - dbPTM
STAB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAB1_HUMAN
UniProt AC Q9NY15
Protein Name Stabilin-1
Gene Name STAB1
Organism Homo sapiens (Human).
Sequence Length 2570
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Acts as a scavenger receptor for acetylated low density lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. When inhibited in endothelial tube formation assays, there is a marked decrease in cell-cell interactions, suggesting a role in angiogenesis. Involved in the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic compartment to the endosomal/lysosomal system..
Protein Sequence MAGPRGLLPLCLLAFCLAGFSFVRGQVLFKGCDVKTTFVTHVPCTSCAAIKKQTCPSGWLRELPDQITQDCRYEVQLGGSMVSMSGCRRKCRKQVVQKACCPGYWGSRCHECPGGAETPCNGHGTCLDGMDRNGTCVCQENFRGSACQECQDPNRFGPDCQSVCSCVHGVCNHGPRGDGSCLCFAGYTGPHCDQELPVCQELRCPQNTQCSAEAPSCRCLPGYTQQGSECRAPNPCWPSPCSLLAQCSVSPKGQAQCHCPENYHGDGMVCLPKDPCTDNLGGCPSNSTLCVYQKPGQAFCTCRPGLVSINSNASAGCFAFCSPFSCDRSATCQVTADGKTSCVCRESEVGDGRACYGHLLHEVQKATQTGRVFLQLRVAVAMMDQGCREILTTAGPFTVLVPSVSSFSSRTMNASLAQQLCRQHIIAGQHILEDTRTQQTRRWWTLAGQEITVTFNQFTKYSYKYKDQPQQTFNIYKANNIAANGVFHVVTGLRWQAPSGTPGDPKRTIGQILASTEAFSRFETILENCGLPSILDGPGPFTVFAPSNEAVDSLRDGRLIYLFTAGLSKLQELVRYHIYNHGQLTVEKLISKGRILTMANQVLAVNISEEGRILLGPEGVPLQRVDVMAANGVIHMLDGILLPPTILPILPKHCSEEQHKIVAGSCVDCQALNTSTCPPNSVKLDIFPKECVYIHDPTGLNVLKKGCASYCNQTIMEQGCCKGFFGPDCTQCPGGFSNPCYGKGNCSDGIQGNGACLCFPDYKGIACHICSNPNKHGEQCQEDCGCVHGLCDNRPGSGGVCQQGTCAPGFSGRFCNESMGDCGPTGLAQHCHLHARCVSQEGVARCRCLDGFEGDGFSCTPSNPCSHPDRGGCSENAECVPGSLGTHHCTCHKGWSGDGRVCVAIDECELDMRGGCHTDALCSYVGPGQSRCTCKLGFAGDGYQCSPIDPCRAGNGGCHGLATCRAVGGGQRVCTCPPGFGGDGFSCYGDIFRELEANAHFSIFYQWLKSAGITLPADRRVTALVPSEAAVRQLSPEDRAFWLQPRTLPNLVRAHFLQGALFEEELARLGGQEVATLNPTTRWEIRNISGRVWVQNASVDVADLLATNGVLHILSQVLLPPRGDVPGGQGLLQQLDLVPAFSLFRELLQHHGLVPQIEAATAYTIFVPTNRSLEAQGNSSHLDADTVRHHVVLGEALSMETLRKGGHRNSLLGPAHWIVFYNHSGQPEVNHVPLEGPMLEAPGRSLIGLSGVLTVGSSRCLHSHAEALREKCVNCTRRFRCTQGFQLQDTPRKSCVYRSGFSFSRGCSYTCAKKIQVPDCCPGFFGTLCEPCPGGLGGVCSGHGQCQDRFLGSGECHCHEGFHGTACEVCELGRYGPNCTGVCDCAHGLCQEGLQGDGSCVCNVGWQGLRCDQKITSPQCPRKCDPNANCVQDSAGASTCACAAGYSGNGIFCSEVDPCAHGHGGCSPHANCTKVAPGQRTCTCQDGYMGDGELCQEINSCLIHHGGCHIHAECIPTGPQQVSCSCREGYSGDGIRTCELLDPCSKNNGGCSPYATCKSTGDGQRTCTCDTAHTVGDGLTCRARVGLELLRDKHASFFSLRLLEYKELKGDGPFTIFVPHADLMSNLSQDELARIRAHRQLVFRYHVVGCRRLRSEDLLEQGYATALSGHPLRFSEREGSIYLNDFARVVSSDHEAVNGILHFIDRVLLPPEALHWEPDDAPIPRRNVTAAAQGFGYKIFSGLLKVAGLLPLLREASHRPFTMLWPTDAAFRALPPDRQAWLYHEDHRDKLAAILRGHMIRNVEALASDLPNLGPLRTMHGTPISFSCSRTRAGELMVGEDDARIVQRHLPFEGGLAYGIDQLLEPPGLGARCDHFETRPLRLNTCSICGLEPPCPEGSQEQGSPEACWRFYPKFWTSPPLHSLGLRSVWVHPSLWGRPQGLGRGCHRNCVTTTWKPSCCPGHYGSECQACPGGPSSPCSDRGVCMDGMSGSGQCLCRSGFAGTACELCAPGAFGPHCQACRCTVHGRCDEGLGGSGSCFCDEGWTGPRCEVQLELQPVCTPPCAPEAVCRAGNSCECSLGYEGDGRVCTVADLCQDGHGGCSEHANCSQVGTMVTCTCLPDYEGDGWSCRARNPCTDGHRGGCSEHANCLSTGLNTRRCECHAGYVGDGLQCLEESEPPVDRCLGQPPPCHSDAMCTDLHFQEKRAGVFHLQATSGPYGLNFSEAEAACEAQGAVLASFPQLSAAQQLGFHLCLMGWLANGSTAHPVVFPVADCGNGRVGIVSLGARKNLSERWDAYCFRVQDVACRCRNGFVGDGISTCNGKLLDVLAATANFSTFYGMLLGYANATQRGLDFLDFLDDELTYKTLFVPVNEGFVDNMTLSGPDLELHASNATLLSANASQGKLLPAHSGLSLIISDAGPDNSSWAPVAPGTVVVSRIIVWDIMAFNGIIHALASPLLAPPQPQAVLAPEAPPVAAGVGAVLAAGALLGLVAGALYLRARGKPMGFGFSAFQAEDDADDDFSPWQEGTNPTLVSVPNPVFGSDTFCEPFDDSLLEEDFPDTQRILTVK
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
133N-linked_GlycosylationCLDGMDRNGTCVCQE
CCCCCCCCCCEEECC		45.95UniProtKB CARBOHYD
286N-linked_GlycosylationNLGGCPSNSTLCVYQ
CCCCCCCCCEEEEEE		24.93UniProtKB CARBOHYD
312N-linked_GlycosylationGLVSINSNASAGCFA
CEEEECCCCCCCCEE		33.17UniProtKB CARBOHYD
413N-linked_GlycosylationSFSSRTMNASLAQQL
HCCHHHCCHHHHHHH		26.26UniProtKB CARBOHYD
461PhosphorylationTFNQFTKYSYKYKDQ
EEEHHCCCEEECCCC		17.7422817900
463PhosphorylationNQFTKYSYKYKDQPQ
EHHCCCEEECCCCCC		18.4222817900
465PhosphorylationFTKYSYKYKDQPQQT
HCCCEEECCCCCCCE		16.1522817900
476PhosphorylationPQQTFNIYKANNIAA
CCCEEEEEEECCEEC		12.7322817900
501PhosphorylationRWQAPSGTPGDPKRT
CEECCCCCCCCCCCC		28.56-
547PhosphorylationPFTVFAPSNEAVDSL
CEEEEECCCHHHHHC		43.82-
553PhosphorylationPSNEAVDSLRDGRLI
CCCHHHHHCCCCCEE		20.78-
606N-linked_GlycosylationANQVLAVNISEEGRI
CCCEEEEECCCCCCE		26.85UniProtKB CARBOHYD
673N-linked_GlycosylationCVDCQALNTSTCPPN
CEECCCCCCCCCCCC		34.69UniProtKB CARBOHYD
712N-linked_GlycosylationKGCASYCNQTIMEQG
HCHHHHHCHHHHHCC		33.52UniProtKB CARBOHYD
730 (in isoform 2)Phosphorylation-40.3522210691
737 (in isoform 2)Phosphorylation-43.0422210691
745N-linked_GlycosylationNPCYGKGNCSDGIQG
CCCCCCCCCCCCCCC		26.13UniProtKB CARBOHYD
758 (in isoform 2)Phosphorylation-4.7122210691
816N-linked_GlycosylationGFSGRFCNESMGDCG
CCCCCCCCCCCCCCC		41.48UniProtKB CARBOHYD
847MethylationQEGVARCRCLDGFEG
CCCCCEEEECCCCCC		20.62115388969
896PhosphorylationCTCHKGWSGDGRVCV
CEECCCCCCCCCEEE		35.36-
1002PhosphorylationLEANAHFSIFYQWLK
HHHCCEEHHHHHHHH		11.2622167270
1005PhosphorylationNAHFSIFYQWLKSAG
CCEEHHHHHHHHHCC		9.3422167270
1022PhosphorylationLPADRRVTALVPSEA
CCCCCCEEEEECCHH		16.68-
1027PhosphorylationRVTALVPSEAAVRQL
CEEEEECCHHHHHHC		32.18-
1047PhosphorylationAFWLQPRTLPNLVRA
HHHCCCCCHHHHHHH		53.93-
1076PhosphorylationLGGQEVATLNPTTRW
CCCEEEEECCCCCCE		32.0423312004
1080PhosphorylationEVATLNPTTRWEIRN
EEEECCCCCCEEEEE		28.1123312004
1081PhosphorylationVATLNPTTRWEIRNI
EEECCCCCCEEEEEC		34.7323312004
1087N-linked_GlycosylationTTRWEIRNISGRVWV
CCCEEEEECCCCEEE		38.14UniProtKB CARBOHYD
1096N-linked_GlycosylationSGRVWVQNASVDVAD
CCCEEEEECCCCHHH		25.2719159218
1115PhosphorylationNGVLHILSQVLLPPR
CCHHHHHHHCCCCCC		20.0324505115
1170N-linked_GlycosylationYTIFVPTNRSLEAQG
EEEEEECCCCHHHCC		26.02UniProtKB CARBOHYD
1178N-linked_GlycosylationRSLEAQGNSSHLDAD
CCHHHCCCCCCCCHH		28.41UniProtKB CARBOHYD
1198PhosphorylationVVLGEALSMETLRKG
HHHHHHCCHHHHHHC		22.9424719451
1201PhosphorylationGEALSMETLRKGGHR
HHHCCHHHHHHCCCC		24.1824719451
1222N-linked_GlycosylationAHWIVFYNHSGQPEV
EEEEEEECCCCCCCC		16.04UniProtKB CARBOHYD
1257PhosphorylationSGVLTVGSSRCLHSH
CCEEEECCCHHHHHH		15.4122817900
1258PhosphorylationGVLTVGSSRCLHSHA
CEEEECCCHHHHHHH		22.5322817900
1274N-linked_GlycosylationALREKCVNCTRRFRC
HHHHHHCCCCCCCCC		30.80UniProtKB CARBOHYD
1378N-linked_GlycosylationELGRYGPNCTGVCDC
CCCCCCCCCCCCCCC		31.45UniProtKB CARBOHYD
1471N-linked_GlycosylationGGCSPHANCTKVAPG
CCCCCCCCCCEECCC		30.84UniProtKB CARBOHYD
1626N-linked_GlycosylationPHADLMSNLSQDELA
EHHHHHHCCCHHHHH		29.7319159218
1727N-linked_GlycosylationDAPIPRRNVTAAAQG
CCCCCCCCHHHHHCC		36.4519159218
1829PhosphorylationTPISFSCSRTRAGEL
CCCEEEECCCCCCEE		35.17-
2107N-linked_GlycosylationGGCSEHANCSQVGTM
CCCCCCCCCCCCCCE		28.07UniProtKB CARBOHYD
2222N-linked_GlycosylationTSGPYGLNFSEAEAA
CCCCCCCCHHHHHHH		33.75UniProtKB CARBOHYD
2261N-linked_GlycosylationCLMGWLANGSTAHPV
HHHHHHHCCCCCCCE		42.66UniProtKB CARBOHYD
2290N-linked_GlycosylationVSLGARKNLSERWDA
EEECCCCCHHHHCHH		43.15UniProtKB CARBOHYD
2334N-linked_GlycosylationDVLAATANFSTFYGM
HHHHHHCCHHHHHHH		27.35UniProtKB CARBOHYD
2347N-linked_GlycosylationGMLLGYANATQRGLD
HHHHHHHHHHHCCCC		34.7319159218
2379N-linked_GlycosylationVNEGFVDNMTLSGPD
CCCCCCCCCEEECCC		21.75UniProtKB CARBOHYD
2393N-linked_GlycosylationDLELHASNATLLSAN
CCEEECCCCEEEECC		37.41UniProtKB CARBOHYD
2400N-linked_GlycosylationNATLLSANASQGKLL
CCEEEECCCCCCCCE		36.43UniProtKB CARBOHYD
2424N-linked_GlycosylationISDAGPDNSSWAPVA
EECCCCCCCCCCCCC		40.8719159218
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 STAB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAB1_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 STAB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GGA1_HUMANGGA1physical
15345724
GGA2_HUMANGGA2physical
15345724
GGA3_HUMANGGA3physical
15345724
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 STAB1_HUMAN

loading...

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-1096; ASN-1626; ASN-1727;ASN-2347 AND ASN-2424, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1257 AND SER-1258, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory