CD68_HUMAN - dbPTM
CD68_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD68_HUMAN
UniProt AC P34810
Protein Name Macrosialin
Gene Name CD68
Organism Homo sapiens (Human).
Sequence Length 354
Subcellular Localization Isoform Short: Cell membrane
Single-pass type I membrane protein.
Isoform Long: Endosome membrane
Single-pass type I membrane protein. Lysosome membrane
Single-pass type I membrane protein.
Protein Description Could play a role in phagocytic activities of tissue macrophages, both in intracellular lysosomal metabolism and extracellular cell-cell and cell-pathogen interactions. Binds to tissue- and organ-specific lectins or selectins, allowing homing of macrophage subsets to particular sites. Rapid recirculation of CD68 from endosomes and lysosomes to the plasma membrane may allow macrophages to crawl over selectin-bearing substrates or other cells..
Protein Sequence MRLAVLFSGALLGLLAAQGTGNDCPHKKSATLLPSFTVTPTVTESTGTTSHRTTKSHKTTTHRTTTTGTTSHGPTTATHNPTTTSHGNVTVHPTSNSTATSQGPSTATHSPATTSHGNATVHPTSNSTATSPGFTSSAHPEPPPPSPSPSPTSKETIGDYTWTNGSQPCVHLQAQIQIRVMYTTQGGGEAWGISVLNPNKTKVQGSCEGAHPHLLLSFPYGHLSFGFMQDLQQKVVYLSYMAVEYNVSFPHAAQWTFSAQNASLRDLQAPLGQSFSCSNSSIILSPAVHLDLLSLRLQAAQLPHTGVFGQSFSCPSDRSILLPLIIGLILLGLLALVLIAFCIIRRRPSAYQAL
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
8PhosphorylationMRLAVLFSGALLGLL
CCEEHHHHHHHHHHH		20.99-
59PhosphorylationRTTKSHKTTTHRTTT
EEECCCCEEEEEEEC		31.35-
88N-linked_GlycosylationPTTTSHGNVTVHPTS
CCCCCCCCEEEECCC		22.36UniProtKB CARBOHYD
96N-linked_GlycosylationVTVHPTSNSTATSQG
EEEECCCCCCCCCCC		45.95UniProtKB CARBOHYD
118N-linked_GlycosylationPATTSHGNATVHPTS
CCCCCCCCCEECCCC		27.32UniProtKB CARBOHYD
126N-linked_GlycosylationATVHPTSNSTATSPG
CEECCCCCCCCCCCC		45.95UniProtKB CARBOHYD
135O-linked_GlycosylationTATSPGFTSSAHPEP
CCCCCCCCCCCCCCC		27.90OGP
137O-linked_GlycosylationTSPGFTSSAHPEPPP
CCCCCCCCCCCCCCC		27.78OGP
164N-linked_GlycosylationIGDYTWTNGSQPCVH
CCCCEECCCCCCEEE		39.41UniProtKB CARBOHYD
182PhosphorylationQIQIRVMYTTQGGGE
EEEEEEEEEECCCCC		12.0929978859
183PhosphorylationIQIRVMYTTQGGGEA
EEEEEEEEECCCCCE		8.4429978859
184PhosphorylationQIRVMYTTQGGGEAW
EEEEEEEECCCCCEE		14.0229978859
194PhosphorylationGGEAWGISVLNPNKT
CCCEEEEEEECCCCC		19.3329978859
199N-linked_GlycosylationGISVLNPNKTKVQGS
EEEEECCCCCEEECC		64.6517660510
246N-linked_GlycosylationSYMAVEYNVSFPHAA
HEEEEEECCCCCCHH		14.95UniProtKB CARBOHYD
261N-linked_GlycosylationQWTFSAQNASLRDLQ
HEEEECCCCCHHHCC		31.0816263699
279N-linked_GlycosylationGQSFSCSNSSIILSP
CCCCCCCCCCEEECC		44.0719159218
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 CD68_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD68_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 CD68_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNDS_HUMANRALGDSphysical
21988832
SYRC_HUMANRARSphysical
26186194
BZW2_HUMANBZW2physical
26186194
KIF14_HUMANKIF14physical
26186194
TNPO2_HUMANTNPO2physical
26186194
SAAL1_HUMANSAAL1physical
26186194
TTI1_HUMANTTI1physical
26186194
COG6_HUMANCOG6physical
26186194
GRN_HUMANGRNphysical
26186194
LEG1_HUMANLGALS1physical
26186194
EI2BE_HUMANEIF2B5physical
26186194
LEG3_HUMANLGALS3physical
26186194
GCP4_HUMANTUBGCP4physical
26186194
MTX3_HUMANMTX3physical
26186194
GRN_HUMANGRNphysical
28514442
KIF14_HUMANKIF14physical
28514442
LEG1_HUMANLGALS1physical
28514442
MTX3_HUMANMTX3physical
28514442
SYRC_HUMANRARSphysical
28514442
TNPO2_HUMANTNPO2physical
28514442
SAAL1_HUMANSAAL1physical
28514442
BZW2_HUMANBZW2physical
28514442
TTI1_HUMANTTI1physical
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 CD68_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-199; ASN-261 AND ASN-279,AND MASS SPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261, AND MASSSPECTROMETRY.

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