P4HA2_HUMAN - dbPTM
P4HA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P4HA2_HUMAN
UniProt AC O15460
Protein Name Prolyl 4-hydroxylase subunit alpha-2
Gene Name P4HA2
Organism Homo sapiens (Human).
Sequence Length 535
Subcellular Localization Endoplasmic reticulum lumen.
Protein Description Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins..
Protein Sequence MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSHERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVKLTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPKLARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVANYGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKKGTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD
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
31PhosphorylationFTSIGHMTDLIYAEK
HHHHHHHHHHHHHHH
23.2122617229
35PhosphorylationGHMTDLIYAEKELVQ
HHHHHHHHHHHHHHH
18.9222617229
43PhosphorylationAEKELVQSLKEYILV
HHHHHHHHHHHHHHH
33.6522617229
45UbiquitinationKELVQSLKEYILVEE
HHHHHHHHHHHHHHH
54.4321906983
45 (in isoform 2)Ubiquitination-54.4321890473
45 (in isoform 1)Ubiquitination-54.4321890473
54UbiquitinationYILVEEAKLSKIKSW
HHHHHHHHHHHHHHH
57.48-
59UbiquitinationEAKLSKIKSWANKME
HHHHHHHHHHHHHHH
43.62-
64UbiquitinationKIKSWANKMEALTSK
HHHHHHHHHHHHHCC
30.3021906983
64 (in isoform 1)Ubiquitination-30.3021890473
64 (in isoform 2)Ubiquitination-30.3021890473
71 (in isoform 2)Ubiquitination-38.59-
71UbiquitinationKMEALTSKSAADAEG
HHHHHHCCCHHHHCC
38.59-
79PhosphorylationSAADAEGYLAHPVNA
CHHHHCCCCCCHHHH
7.69-
88UbiquitinationAHPVNAYKLVKRLNT
CCHHHHHHHHHHHCC
44.38-
115N-linked_GlycosylationSAAGFIANLSVQRQF
CCCHHEEEHHHHHCC
28.21UniProtKB CARBOHYD
134 (in isoform 1)Ubiquitination-41.3321890473
134UbiquitinationEDEIGAAKALMRLQD
HHHHHHHHHHHHHHC
41.3321890473
134 (in isoform 2)Ubiquitination-41.3321890473
194UbiquitinationLWMEQVLKQLDAGEE
HHHHHHHHHCCCCCC
50.38-
206 (in isoform 2)Ubiquitination-36.4821890473
206 (in isoform 1)Ubiquitination-36.4821890473
206UbiquitinationGEEATTTKSQVLDYL
CCCCCCCHHHHHHHH
36.4821906983
235PhosphorylationELTRRLLSLDPSHER
HHHHHHHCCCCCCCC
35.0129507054
239PhosphorylationRLLSLDPSHERAGGN
HHHCCCCCCCCCCCC
37.3326503514
264N-linked_GlycosylationEREKTLTNQTEAELA
HHHHHCCCHHHHHHC
50.30UniProtKB CARBOHYD
272O-linked_GlycosylationQTEAELATPEGIYER
HHHHHHCCCCCCCCC
34.20OGP
300UbiquitinationLCRGEGVKLTPRRQK
HHCCCCCCCCHHHHH
58.4621906983
300 (in isoform 1)Ubiquitination-58.4621890473
300 (in isoform 2)Ubiquitination-58.4621890473
328 (in isoform 1)Ubiquitination-60.1721890473
328 (in isoform 2)Ubiquitination-60.1721890473
328SumoylationQLLIAPFKEEDEWDS
EEEEECCCCCCCCCC
60.17-
328SumoylationQLLIAPFKEEDEWDS
EEEEECCCCCCCCCC
60.17-
328UbiquitinationQLLIAPFKEEDEWDS
EEEEECCCCCCCCCC
60.1721906983
345SulfoxidationIVRYYDVMSDEEIER
CHHHEECCCHHHHHH
3.6930846556
346PhosphorylationVRYYDVMSDEEIERI
HHHEECCCHHHHHHH
41.5426434776
383 (in isoform 2)Ubiquitination-45.7321890473
383 (in isoform 1)Ubiquitination-45.7321890473
383UbiquitinationVASYRVSKSSWLEED
EEEEEEECCHHCCCC
45.732190698
421PhosphorylationELLQVANYGVGGQYE
HHHHHHCCCCCCCCC
11.94-
441PhosphorylationSRNDERDTFKHLGTG
CCCCCCCHHHHCCCC
40.58-
443 (in isoform 2)Ubiquitination-39.7621890473
443UbiquitinationNDERDTFKHLGTGNR
CCCCCHHHHCCCCCH
39.76-
447PhosphorylationDTFKHLGTGNRVATF
CHHHHCCCCCHHHHH
37.33-
480SuccinylationGAAIWPKKGTAVFWY
CCEECCCCCCEEEHH
58.37-
480SuccinylationGAAIWPKKGTAVFWY
CCEECCCCCCEEEHH
58.37-
482PhosphorylationAIWPKKGTAVFWYNL
EECCCCCCEEEHHHH
28.64-
487PhosphorylationKGTAVFWYNLLRSGE
CCCEEEHHHHHHCCC
5.62-

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 P4HA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P4HA2_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 P4HA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PEPL_HUMANPPLphysical
26344197
KIF7_HUMANKIF7physical
28514442
TTC28_HUMANTTC28physical
28514442
WDR33_HUMANWDR33physical
28514442
TSYL4_HUMANTSPYL4physical
28514442
K1671_HUMANKIAA1671physical
28514442
FOXF2_HUMANFOXF2physical
28514442
CO1A1_HUMANCOL1A1physical
28514442
CTF18_HUMANCHTF18physical
28514442
CO039_HUMANC15orf39physical
28514442
KI18B_HUMANKIF18Bphysical
28514442
UBP54_HUMANUSP54physical
28514442
ATG4D_HUMANATG4Dphysical
28514442
ZN195_HUMANZNF195physical
28514442
IQEC1_HUMANIQSEC1physical
28514442
TCPB_HUMANCCT2physical
28514442
UT14A_HUMANUTP14Aphysical
28514442
FP100_HUMANC17orf70physical
28514442
IFFO1_HUMANIFFO1physical
28514442
DISC1_HUMANDISC1physical
28514442
TRM44_HUMANTRMT44physical
28514442
DCC1_HUMANDSCC1physical
28514442
BAG3_HUMANBAG3physical
28514442
GTSE1_HUMANGTSE1physical
28514442
NEK7_HUMANNEK7physical
28514442
MA7D1_HUMANMAP7D1physical
28514442
PKN3_HUMANPKN3physical
28514442
SAV1_HUMANSAV1physical
28514442
ATX2_HUMANATXN2physical
28514442
SMG8_HUMANSMG8physical
28514442
IF4E2_HUMANEIF4E2physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
DNJB5_HUMANDNAJB5physical
28514442
RPC2_HUMANPOLR3Bphysical
28514442
RAVR1_HUMANRAVER1physical
28514442
CTU1_HUMANCTU1physical
28514442
CHIP_HUMANSTUB1physical
28514442
TCPH_HUMANCCT7physical
28514442
MELK_HUMANMELKphysical
28514442
TSR3_HUMANTSR3physical
28514442
TCPG_HUMANCCT3physical
28514442
WDR62_HUMANWDR62physical
28514442
TAF1C_HUMANTAF1Cphysical
28514442
SHKB1_HUMANSHKBP1physical
28514442
CC85C_HUMANCCDC85Cphysical
28514442
PK3CB_HUMANPIK3CBphysical
28514442
MYO9A_HUMANMYO9Aphysical
28514442
TNG6_HUMANTANGO6physical
28514442
ARVC_HUMANARVCFphysical
28514442
RECQ4_HUMANRECQL4physical
28514442
MA7D2_HUMANMAP7D2physical
28514442
ERF_HUMANERFphysical
28514442
RICTR_HUMANRICTORphysical
28514442
MYO5C_HUMANMYO5Cphysical
28514442
TRI32_HUMANTRIM32physical
28514442
TRI65_HUMANTRIM65physical
28514442
ARAF_HUMANARAFphysical
28514442
MCM8_HUMANMCM8physical
28514442
FA83H_HUMANFAM83Hphysical
28514442
TRM1_HUMANTRMT1physical
28514442
TSC2_HUMANTSC2physical
28514442
NEK7_HUMANNEK7physical
27173435
PDIA1_HUMANP4HBphysical
27173435

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
DB00172L-Proline
DB00139Succinic acid
Regulatory Network of P4HA2_HUMAN

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Related Literatures of Post-Translational Modification

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