P3H1_HUMAN - dbPTM
P3H1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P3H1_HUMAN
UniProt AC Q32P28
Protein Name Prolyl 3-hydroxylase 1 {ECO:0000312|HGNC:HGNC:19316}
Gene Name P3H1 {ECO:0000312|HGNC:HGNC:19316}
Organism Homo sapiens (Human).
Sequence Length 736
Subcellular Localization Isoform 1: Endoplasmic reticulum.
Secreted, extracellular space, extracellular matrix. Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG).
Protein Description Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts..
Protein Sequence MAVRALKLLTTLLAVVAAASQAEVESEAGWGMVTPDLLFAEGTAAYARGDWPGVVLSMERALRSRAALRALRLRCRTQCAADFPWELDPDWSPSPAQASGAAALRDLSFFGGLLRRAACLRRCLGPPAAHSLSEEMELEFRKRSPYNYLQVAYFKINKLEKAVAAAHTFFVGNPEHMEMQQNLDYYQTMSGVKEADFKDLETQPHMQEFRLGVRLYSEEQPQEAVPHLEAALQEYFVAYEECRALCEGPYDYDGYNYLEYNADLFQAITDHYIQVLNCKQNCVTELASHPSREKPFEDFLPSHYNYLQFAYYNIGNYTQAVECAKTYLLFFPNDEVMNQNLAYYAAMLGEEHTRSIGPRESAKEYRQRSLLEKELLFFAYDVFGIPFVDPDSWTPEEVIPKRLQEKQKSERETAVRISQEIGNLMKEIETLVEEKTKESLDVSRLTREGGPLLYEGISLTMNSKLLNGSQRVVMDGVISDHECQELQRLTNVAATSGDGYRGQTSPHTPNEKFYGVTVFKALKLGQEGKVPLQSAHLYYNVTEKVRRIMESYFRLDTPLYFSYSHLVCRTAIEEVQAERKDDSHPVHVDNCILNAETLVCVKEPPAYTFRDYSAILYLNGDFDGGNFYFTELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKAVTRGQRCAIALWFTLDPRHSERDRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEPAQESLSGSESKPKDEL
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
20PhosphorylationLAVVAAASQAEVESE
HHHHHHHHHCHHHHH		25.79-
34O-linked_GlycosylationEAGWGMVTPDLLFAE
HCCCCCCCHHHHEEE		11.37OGP
92O-linked_GlycosylationWELDPDWSPSPAQAS
CCCCCCCCCCHHHHH		23.92OGP
108PhosphorylationAAALRDLSFFGGLLR
HHHHHHHHHHHHHHH		23.8721712546
144PhosphorylationELEFRKRSPYNYLQV
HHHHHHCCCCCEEHH		34.4720068231
146PhosphorylationEFRKRSPYNYLQVAY
HHHHCCCCCEEHHEE		20.0720068231
148PhosphorylationRKRSPYNYLQVAYFK
HHCCCCCEEHHEEEE		7.8320068231
153PhosphorylationYNYLQVAYFKINKLE
CCEEHHEEEEHHHHH		13.4220068231
176UbiquitinationFFVGNPEHMEMQQNL
CCCCCHHHHHHHHHH		20.8221890473
186UbiquitinationMQQNLDYYQTMSGVK
HHHHHHHHHHHCCCC		9.3621890473
187UbiquitinationQQNLDYYQTMSGVKE
HHHHHHHHHHCCCCC		25.2121890473
316N-linked_GlycosylationFAYYNIGNYTQAVEC
EEEEECCCHHHHHHH		32.64UniProtKB CARBOHYD
369PhosphorylationAKEYRQRSLLEKELL
HHHHHHHHHHHHHHH		29.0324719451
413PhosphorylationKQKSERETAVRISQE
HHHHHHHHHHHHHHH		36.3527703031
418 (in isoform 3)Phosphorylation-15.9327251275
418PhosphorylationRETAVRISQEIGNLM
HHHHHHHHHHHHHHH		15.9327732954
425SulfoxidationSQEIGNLMKEIETLV
HHHHHHHHHHHHHHH		4.2021406390
426UbiquitinationQEIGNLMKEIETLVE
HHHHHHHHHHHHHHH		59.7229967540
435UbiquitinationIETLVEEKTKESLDV
HHHHHHHHHHHHCCH		51.9329967540
437UbiquitinationTLVEEKTKESLDVSR
HHHHHHHHHHCCHHH		57.2729967540
439PhosphorylationVEEKTKESLDVSRLT
HHHHHHHHCCHHHHH		31.2729507054
467N-linked_GlycosylationTMNSKLLNGSQRVVM
EECCHHCCCCCEEEE		59.51UniProtKB CARBOHYD
474SulfoxidationNGSQRVVMDGVISDH
CCCCEEEECCCCCHH		3.2130846556
483GlutathionylationGVISDHECQELQRLT
CCCCHHHHHHHHHHH		3.2322555962
490PhosphorylationCQELQRLTNVAATSG
HHHHHHHHCCCCCCC		29.8120068231
495PhosphorylationRLTNVAATSGDGYRG
HHHCCCCCCCCCCCC		24.4120068231
496PhosphorylationLTNVAATSGDGYRGQ
HHCCCCCCCCCCCCC		30.1120068231
500PhosphorylationAATSGDGYRGQTSPH
CCCCCCCCCCCCCCC		19.1320068231
505PhosphorylationDGYRGQTSPHTPNEK
CCCCCCCCCCCCCCC		13.5425159151
512 (in isoform 1)Ubiquitination-50.9921890473
512UbiquitinationSPHTPNEKFYGVTVF
CCCCCCCCCCEEEHE		50.9922817900
512 (in isoform 3)Ubiquitination-50.9921890473
520 (in isoform 3)Ubiquitination-48.77-
523UbiquitinationVTVFKALKLGQEGKV
EEHEEHHHCCCCCCC		56.2729967540
540N-linked_GlycosylationQSAHLYYNVTEKVRR
CHHEEEECHHHHHHH		22.2219159218
551PhosphorylationKVRRIMESYFRLDTP
HHHHHHHHHHCCCCC		16.5223663014
552PhosphorylationVRRIMESYFRLDTPL
HHHHHHHHHCCCCCC		4.5723663014
557PhosphorylationESYFRLDTPLYFSYS
HHHHCCCCCCEEEHH		21.5623663014
560PhosphorylationFRLDTPLYFSYSHLV
HCCCCCCEEEHHHHH		7.5323663014
562PhosphorylationLDTPLYFSYSHLVCR
CCCCCEEEHHHHHHH		16.5123663014
563PhosphorylationDTPLYFSYSHLVCRT
CCCCEEEHHHHHHHH		7.1023663014
564PhosphorylationTPLYFSYSHLVCRTA
CCCEEEHHHHHHHHH		14.7823663014
607PhosphorylationCVKEPPAYTFRDYSA
EECCCCCEECCCCEE		16.5121406692
608PhosphorylationVKEPPAYTFRDYSAI
ECCCCCEECCCCEEE		17.8221406692
645GlutathionylationTAEVQPQCGRAVGFS
EEEECCCCCCCCCCC		5.1822555962
652PhosphorylationCGRAVGFSSGTENPH
CCCCCCCCCCCCCCC		23.1720068231
653PhosphorylationGRAVGFSSGTENPHG
CCCCCCCCCCCCCCH		47.6922210691
655O-linked_GlycosylationAVGFSSGTENPHGVK
CCCCCCCCCCCCHHE		34.24OGP
662 (in isoform 3)Ubiquitination-41.55-
662UbiquitinationTENPHGVKAVTRGQR
CCCCCHHEEECCCCC		41.55-
699PhosphorylationDLVKMLFSPEEMDLS
HHHHHHCCHHHCCCC		27.6924043423
706PhosphorylationSPEEMDLSQEQPLDA
CHHHCCCCCCCCCCC		27.6629507054
724PhosphorylationPPEPAQESLSGSESK
CCCCCHHHCCCCCCC		18.7627251275
726PhosphorylationEPAQESLSGSESKPK
CCCHHHCCCCCCCCC		49.9427251275
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 P3H1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P3H1_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 P3H1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARP2_HUMANACTR2physical
22863883
AGFG1_HUMANAGFG1physical
22863883
HEM2_HUMANALADphysical
22863883
ARI1_HUMANARIH1physical
22863883
GON7_HUMANC14orf142physical
22863883
SZRD1_HUMANSZRD1physical
22863883
DDX17_HUMANDDX17physical
22863883
DPP8_HUMANDPP8physical
22863883
ERO1A_HUMANERO1Lphysical
22863883
GPN1_HUMANGPN1physical
22863883
HPBP1_HUMANHSPBP1physical
22863883
LRSM1_HUMANLRSAM1physical
22863883
LSM1_HUMANLSM1physical
22863883
MAT2B_HUMANMAT2Bphysical
22863883
NRDC_HUMANNRD1physical
22863883
OGT1_HUMANOGTphysical
22863883
OSGEP_HUMANOSGEPphysical
22863883
PDIA1_HUMANP4HBphysical
22863883
PDIA6_HUMANPDIA6physical
22863883
PFD1_HUMANPFDN1physical
22863883
PPME1_HUMANPPME1physical
22863883
TRUA_HUMANPUS1physical
22863883
SHLB1_HUMANSH3GLB1physical
22863883
SRP14_HUMANSRP14physical
22863883
SRP09_HUMANSRP9physical
22863883
SURF2_HUMANSURF2physical
22863883
TM1L1_HUMANTOM1L1physical
22863883
TPRKB_HUMANTPRKBphysical
22863883
TSN_HUMANTSNphysical
22863883
UBE3A_HUMANUBE3Aphysical
22863883
WDR4_HUMANWDR4physical
22863883
ZPR1_HUMANZPR1physical
22863883
CRTAP_HUMANCRTAPphysical
26344197
RENBP_HUMANRENBPphysical
28514442
KRBA1_HUMANKRBA1physical
28514442
TIGD5_HUMANTIGD5physical
28514442
UQCC1_HUMANUQCC1physical
28514442
CRTAP_HUMANCRTAPphysical
28514442
HOOK2_HUMANHOOK2physical
28514442
ZN446_HUMANZNF446physical
28514442
UQCC2_HUMANUQCC2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610915Osteogenesis imperfecta 8 (OI8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00172L-Proline
DB00139Succinic acid
DB00126Vitamin C
Regulatory Network of P3H1_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-540, AND MASSSPECTROMETRY.

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