GDPD5_HUMAN - dbPTM
GDPD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDPD5_HUMAN
UniProt AC Q8WTR4
Protein Name Glycerophosphodiester phosphodiesterase domain-containing protein 5
Gene Name GDPD5
Organism Homo sapiens (Human).
Sequence Length 605
Subcellular Localization Endomembrane system
Multi-pass membrane protein . Cytoplasm, perinuclear region . Cell projection, growth cone . In a punctate perinuclear pattern.
Protein Description Promotes neurite formation. Cooperates with PRDX1 to drive postmitotic motor neuron differentiation. The glycerophosphodiester phosphodiesterase activity may be required for its role in neuronal differentiation. May contribute to the osmotic regulation of cellular glycerophosphocholine..
Protein Sequence MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLTFTFGLTLTWLYFWWEVHNDYDEFNWYLYNRMGYWSDWPVPILVTTAAAFAYIAGLLVLALCHIAVGQQMNLHWLHKIGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGTAPFLHVGAVAAVTMLSWIVAGQFARAERTSSQVTILCTFFTVVFALYLAPLTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADITISLDGVPFLMHDTTLRRTTNVEEEFPELARRPASMLNWTTLQRLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELAKGNATLLLNLRDPPREHPYRSSFINVTLEAVLHSGFPQHQVMWLPSRQRPLVRKVAPGFQQTSGSKEAVASLRRGHIQRLNLRYTQVSRQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHALSQVPSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISDGVEVSDVLSVCSDNSYDTYANSTATPVGPRGGGSHTKTLIERSGR
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
30PhosphorylationYGCRWKRYQRSHDDT
HHCCCHHCCCCCCCC		12.45-
190PhosphorylationFARAERTSSQVTILC
HHHHCCCCCHHHHHH		25.6222210691
201PhosphorylationTILCTFFTVVFALYL
HHHHHHHHHHHHHHH		16.1522210691
207PhosphorylationFTVVFALYLAPLTIS
HHHHHHHHHHHHCCC		9.4422210691
247PhosphorylationAPEHTLMSFRKALEQ
CCHHHHHHHHHHHHH		25.6324719451
301N-linked_GlycosylationRRPASMLNWTTLQRL
HCCHHHCCCHHHHHH		25.96UniProtKB CARBOHYD
317PhosphorylationAGQWFLKTDPFWTAS
CCCCEEECCCCCCHH		51.5622210691
322PhosphorylationLKTDPFWTASSLSPS
EECCCCCCHHHCCHH		19.6222210691
327PhosphorylationFWTASSLSPSDHREA
CCCHHHCCHHHHHHH		25.0622210691
329PhosphorylationTASSLSPSDHREAQN
CHHHCCHHHHHHHHH		42.5522210691
336N-linked_GlycosylationSDHREAQNQSICSLA
HHHHHHHHHHHHHHH		44.61UniProtKB CARBOHYD
352UbiquitinationLLELAKGNATLLLNL
HHHHHCCCEEEEEEC		29.1029901268
352N-linked_GlycosylationLLELAKGNATLLLNL
HHHHHCCCEEEEEEC		29.10UniProtKB CARBOHYD
374N-linked_GlycosylationPYRSSFINVTLEAVL
CCCHHCCHHHHHHHH		20.79UniProtKB CARBOHYD
433PhosphorylationIQRLNLRYTQVSRQE
HHHHHCEEEEECHHH		12.51-
437PhosphorylationNLRYTQVSRQELRDY
HCEEEEECHHHHHHH		20.59-
448N-linked_GlycosylationLRDYASWNLSVNLYT
HHHHHHCCCEEEEEE		21.68UniProtKB CARBOHYD
459UbiquitinationNLYTVNAPWLFSLLW
EEEEECHHHHHHHHH		24.0929901268
542PhosphorylationLSAAVRRTSRDVSIM
HHHHHHHHHCCHHHH		19.9724719451
543PhosphorylationSAAVRRTSRDVSIMK
HHHHHHHHCCHHHHH		25.3623403867
547PhosphorylationRRTSRDVSIMKEKLI
HHHHCCHHHHHHHHH		22.66-
579PhosphorylationSDNSYDTYANSTATP
CCCCCCCCCCCCCCC		10.82-
597UbiquitinationRGGGSHTKTLIERSG
CCCCHHHHHHHHCCC		35.5929901268
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 GDPD5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDPD5_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 GDPD5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR261_HUMANKRTAP26-1physical
25416956
ROBO1_HUMANROBO1physical
28514442
GPDM_HUMANGPD2physical
28514442
PIGQ_HUMANPIGQphysical
28514442
SELT_HUMANSELTphysical
28514442
PP4P2_HUMANTMEM55Aphysical
28514442
IGSF8_HUMANIGSF8physical
28514442
LEMD2_HUMANLEMD2physical
28514442
SCAM4_HUMANSCAMP4physical
28514442
FACE1_HUMANZMPSTE24physical
28514442
VTI1B_HUMANVTI1Bphysical
28514442
NDUS4_HUMANNDUFS4physical
28514442
KCJ11_HUMANKCNJ11physical
28514442
ZDHC9_HUMANZDHHC9physical
28514442
TYW1_HUMANTYW1physical
28514442
CA043_HUMANC1orf43physical
28514442
STX7_HUMANSTX7physical
28514442
NDUAC_HUMANNDUFA12physical
28514442
STX8_HUMANSTX8physical
28514442
CHSS3_HUMANCHSY3physical
28514442
EDA_HUMANEDAphysical
28514442
RETST_HUMANRETSATphysical
28514442
ADCY6_HUMANADCY6physical
28514442
NDUS6_HUMANNDUFS6physical
28514442
ZDH18_HUMANZDHHC18physical
28514442
GPHRA_HUMANGPR89Bphysical
28514442
GPHRB_HUMANGPR89Bphysical
28514442
TX264_HUMANTEX264physical
28514442
TM205_HUMANTMEM205physical
28514442
GPC5C_HUMANGPRC5Cphysical
28514442
MARC1_HUMANMARC1physical
28514442
GOLI4_HUMANGOLIM4physical
28514442
THEM6_HUMANTHEM6physical
28514442
SGPP1_HUMANSGPP1physical
28514442
F213A_HUMANFAM213Aphysical
28514442
NDC1_HUMANNDC1physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GDPD5_HUMAN

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Related Literatures of Post-Translational Modification

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