P3H2_HUMAN - dbPTM
P3H2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P3H2_HUMAN
UniProt AC Q8IVL5
Protein Name Prolyl 3-hydroxylase 2 {ECO:0000312|HGNC:HGNC:19317}
Gene Name P3H2 {ECO:0000312|HGNC:HGNC:19317}
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Endoplasmic reticulum . Sarcoplasmic reticulum . Golgi apparatus .
Protein Description Prolyl 3-hydroxylase that catalyzes the post-translational formation of 3-hydroxyproline on collagens. [PubMed: 18487197 Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons, the eye sclera and in the eye lens capsule (By similarity Has high activity with the type IV collagen COL4A1, and lower activity with COL1A1]
Protein Sequence MRERIWAPPLLLLLPLLLPPPLWGGPPDSPRRELELEPGPLQPFDLLYASGAAAYYSGDYERAVRDLEAALRSHRRLREIRTRCARHCAARHPLPPPPPGEGPGAELPLFRSLLGRARCYRSCETQRLGGPASRHRVSEDVRSDFQRRVPYNYLQRAYIKLNQLEKAVEAAHTFFVANPEHMEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREYFVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSPIENFLPLHYDYLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSIDPASIEAREDLTMFVKRHKLESELIKSAAEGLGFSYTEPNYWIRYGGRQDENRVPSGVNVEGAEVHGFSMGKKLSPKIDRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELHSVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKSGYEGRVPLKSARLFYDISEKARRIVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAYTFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTKGKRCAVALWFTLDPLYRELERIQADEVIAILDQEQQGKHELNINPKDEL
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
27UbiquitinationPPLWGGPPDSPRREL
CCCCCCCCCCCCCCC
58.9729967540
112PhosphorylationAELPLFRSLLGRARC
CCCHHHHHHHCCHHH
22.1727251275
143UbiquitinationRVSEDVRSDFQRRVP
CCCHHHHHHHHHHCC
42.5021963094
143UbiquitinationRVSEDVRSDFQRRVP
CCCHHHHHHHHHHCC
42.50-
160UbiquitinationYLQRAYIKLNQLEKA
HHHHHHHHHHHHHHH
28.8021963094
166UbiquitinationIKLNQLEKAVEAAHT
HHHHHHHHHHHHHHH
67.3429967540
191PhosphorylationMQQNIENYRATAGVE
HHHHHHHHHHHHHHH
6.7123663014
192UbiquitinationQQNIENYRATAGVEA
HHHHHHHHHHHHHHH
36.7222817900
195UbiquitinationIENYRATAGVEALQL
HHHHHHHHHHHHHHH
21.03-
195UbiquitinationIENYRATAGVEALQL
HHHHHHHHHHHHHHH
21.0321963094
202UbiquitinationAGVEALQLVDREAKP
HHHHHHHHHCCCCCC
4.5021963094
202UbiquitinationAGVEALQLVDREAKP
HHHHHHHHHCCCCCC
4.50-
208UbiquitinationQLVDREAKPHMESYN
HHHCCCCCCCHHHCC
30.6129967540
248UbiquitinationFVEDTECRTLCEGPQ
HCCCCCCHHCCCCCC
25.2229967540
253UbiquitinationECRTLCEGPQRFEEY
CCHHCCCCCCHHHHH
23.7329967540
315UbiquitinationHYDYLQFAYYRVGEY
CCHHHHHHHHHHHHH
6.3629967540
324UbiquitinationYRVGEYVKALECAKA
HHHHHHHHHHHHHHH
46.4821963094
324UbiquitinationYRVGEYVKALECAKA
HHHHHHHHHHHHHHH
46.48-
332UbiquitinationALECAKAYLLCHPDD
HHHHHHHHHHCCCCC
10.25-
332UbiquitinationALECAKAYLLCHPDD
HHHHHHHHHHCCCCC
10.2521963094
335UbiquitinationCAKAYLLCHPDDEDV
HHHHHHHCCCCCCCH
3.95-
335UbiquitinationCAKAYLLCHPDDEDV
HHHHHHHCCCCCCCH
3.9521963094
373UbiquitinationEDLTMFVKRHKLESE
HHHHHHHHHHHHHHH
37.2022817900
376UbiquitinationTMFVKRHKLESELIK
HHHHHHHHHHHHHHH
58.9621963094
383UbiquitinationKLESELIKSAAEGLG
HHHHHHHHHHHHHCC
46.8221963094
414UbiquitinationDENRVPSGVNVEGAE
CCCCCCCCCCCCCCE
14.6721963094
414UbiquitinationDENRVPSGVNVEGAE
CCCCCCCCCCCCCCE
14.67-
429UbiquitinationVHGFSMGKKLSPKID
EEEECCCCCCCCCCC
41.7329967540
434UbiquitinationMGKKLSPKIDRDLRE
CCCCCCCCCCHHHHC
54.5929967540
449N-linked_GlycosylationGGPLLYENITFVYNS
CCCEEEEEEEEEEEH
25.66UniProtKB CARBOHYD
454UbiquitinationYENITFVYNSEQLNG
EEEEEEEEEHHHCCC
14.5829967540
456UbiquitinationNITFVYNSEQLNGTQ
EEEEEEEHHHCCCCE
14.7229967540
474UbiquitinationLDNVLSEEQCRELHS
HHHCCCHHHHHHHHH
52.1621963094
474UbiquitinationLDNVLSEEQCRELHS
HHHCCCHHHHHHHHH
52.16-
478UbiquitinationLSEEQCRELHSVASG
CCHHHHHHHHHHHCE
59.4622817900
496UbiquitinationVGDGYRGKTSPHTPN
ECCCCCCCCCCCCCC
36.5129967540
505UbiquitinationSPHTPNEKFEGATVL
CCCCCCCCCCHHHHH
56.1921963094
513UbiquitinationFEGATVLKALKSGYE
CCHHHHHHHHHCCCC
47.5421963094
516UbiquitinationATVLKALKSGYEGRV
HHHHHHHHCCCCCCC
46.85-
516UbiquitinationATVLKALKSGYEGRV
HHHHHHHHCCCCCCC
46.8521963094
524UbiquitinationSGYEGRVPLKSARLF
CCCCCCCCCCHHEEE
32.4829967540
532PhosphorylationLKSARLFYDISEKAR
CCHHEEEEEHHHHHH
19.5724732914
535PhosphorylationARLFYDISEKARRIV
HEEEEEHHHHHHHHH
30.1024732914
549N-linked_GlycosylationVESYFMLNSTLYFSY
HHHHHCHHCEEEEEH
22.59UniProtKB CARBOHYD
595UbiquitinationPEANECWKEPPAYTF
CCHHHHCCCCCCEEC
72.5021963094
600PhosphorylationCWKEPPAYTFRDYSA
HCCCCCCEECCCCEE
16.5121406692
601PhosphorylationWKEPPAYTFRDYSAL
CCCCCCEECCCCEEE
17.8221406692
635UbiquitinationKTVTASIKPKCGRMI
CEEEEECCCCCCCEE
35.6129967540
637UbiquitinationVTASIKPKCGRMISF
EEEECCCCCCCEEEE
44.3029967540
655UbiquitinationGENPHGVKAVTKGKR
CCCCCCCEECCCCCC
41.5521963094
659UbiquitinationHGVKAVTKGKRCAVA
CCCEECCCCCCEEEE
56.7022817900
697UbiquitinationLDQEQQGKHELNINP
ECHHHCCCCCCCCCC
29.5721963094
705UbiquitinationHELNINPKDEL----
CCCCCCCCCCC----
60.3929967540
705"N6,N6-dimethyllysine"HELNINPKDEL----
CCCCCCCCCCC----
60.39-
705MethylationHELNINPKDEL----
CCCCCCCCCCC----
60.39-

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 P3H2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P3H2_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 P3H2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of P3H2_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P3H2_HUMAN

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Related Literatures of Post-Translational Modification

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