P4HA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: P4HA1_HUMAN
• UniProt AC: P13674
• Protein Name: Prolyl 4-hydroxylase subunit alpha-1
• Gene Name: P4HA1
• Organism: Homo sapiens (Human).
• Sequence Length: 534
• 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: MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE

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
4	Phosphorylation	----MIWYILIIGIL ----CHHHHHHHHHH	3.79	24043423
15	Phosphorylation	IGILLPQSLAHPGFF HHHHCCHHHCCCCCC	26.11	24043423
23	Phosphorylation	LAHPGFFTSIGQMTD HCCCCCCCCHHHHHH	19.71	24043423
24	Phosphorylation	AHPGFFTSIGQMTDL CCCCCCCCHHHHHHH	21.40	24043423
29	Phosphorylation	FTSIGQMTDLIHTEK CCCHHHHHHHCCCCH	21.55	24043423
34	Phosphorylation	QMTDLIHTEKDLVTS HHHHHCCCCHHHHHH	37.42	24043423
40	Phosphorylation	HTEKDLVTSLKDYIK CCCHHHHHHHHHHHH	35.32	21406692
41	Phosphorylation	TEKDLVTSLKDYIKA CCHHHHHHHHHHHHH	26.41	21406692
43	Ubiquitination	KDLVTSLKDYIKAEE HHHHHHHHHHHHHHH	48.53	-
45	Phosphorylation	LVTSLKDYIKAEEDK HHHHHHHHHHHHHHH	11.61	21406692
47	Ubiquitination	TSLKDYIKAEEDKLE HHHHHHHHHHHHHHH	43.44	-
52	2-Hydroxyisobutyrylation	YIKAEEDKLEQIKKW HHHHHHHHHHHHHHH	58.15	-
57	2-Hydroxyisobutyrylation	EDKLEQIKKWAEKLD HHHHHHHHHHHHHHH	41.79	-
62	Ubiquitination	QIKKWAEKLDRLTST HHHHHHHHHHHHHHC	48.19	-
71	O-linked_Glycosylation	DRLTSTATKDPEGFV HHHHHCCCCCCCCCC	35.75	OGP
72	Ubiquitination	RLTSTATKDPEGFVG HHHHCCCCCCCCCCC	69.67	-
113	N-linked_Glycosylation	MSDGFISNLTIQRQY CCCCCCCCEEEEECC	36.07	19159218
132	Ubiquitination	EDQVGAAKALLRLQD HHHHHHHHHHHHHHH	38.75	-
150	Ubiquitination	LDTDTISKGNLPGVK CCCCCCCCCCCCCCC	48.22	-
187	Sulfoxidation	YYHTELWMEQALRQL HHHHHHHHHHHHHHC	4.23	30846556
229	2-Hydroxyisobutyrylation	DKALLLTKKLLELDP HHHHHHHHHHHHCCH	41.20	-
230	Ubiquitination	KALLLTKKLLELDPE HHHHHHHHHHHCCHH	53.74	-
259	N-linked_Glycosylation	MAKEKDVNKSASDDQ EEHHCCCCCCCCCCC	42.57	UniProtKB CARBOHYD
271	Phosphorylation	DDQSDQKTTPKKKGV CCCCCCCCCCCCCCC	42.57	29396449
272	Phosphorylation	DQSDQKTTPKKKGVA CCCCCCCCCCCCCCC	39.90	28985074
282	Phosphorylation	KKGVAVDYLPERQKY CCCCCCCCCCHHHHH	19.98	-
288	Acetylation	DYLPERQKYEMLCRG CCCCHHHHHHHHHCC	49.77	27452117
288	Ubiquitination	DYLPERQKYEMLCRG CCCCHHHHHHHHHCC	49.77	-
299	Ubiquitination	LCRGEGIKMTPRRQK HHCCCCCCCCCHHCC	47.80	-
327	Ubiquitination	KFILAPAKQEDEWDK CEEEEECCCCCCCCC	53.84	-
345	Phosphorylation	IRFHDIISDAEIEIV EEHHHHCCHHHHHHH	30.97	28450419
353	Ubiquitination	DAEIEIVKDLAKPRL HHHHHHHHHHCCHHC	53.32	-
364	Phosphorylation	KPRLRRATISNPITG CHHCCCCEECCCCCC	24.11	28450419
366	Phosphorylation	RLRRATISNPITGDL HCCCCEECCCCCCCC	32.00	28450419
370	Phosphorylation	ATISNPITGDLETVH CEECCCCCCCCEEEE	26.37	23312004
378 (in isoform 2)	Phosphorylation	-	12.81	-
378 (in isoform 3)	Phosphorylation	-	12.81	-
382	Acetylation	TVHYRISKSAWLSGY EEEEEECHHHHHCCC	41.65	23236377
382	Ubiquitination	TVHYRISKSAWLSGY EEEEEECHHHHHCCC	41.65	-
382 (in isoform 2)	Ubiquitination	-	41.65	-
387	Phosphorylation	ISKSAWLSGYENPVV ECHHHHHCCCCCCHH	28.73	-
442	Ubiquitination	KDEPDAFKELGTGNR CCCCCHHHHCCCCCH	54.47	-
491	Phosphorylation	FWYNLFASGEGDYST EEEEEECCCCCCHHH	30.00	28851738
497	Phosphorylation	ASGEGDYSTRHAACP CCCCCCHHHCCCCCC	24.57	28851738
498	Phosphorylation	SGEGDYSTRHAACPV CCCCCHHHCCCCCCE	21.90	28851738
510	Ubiquitination	CPVLVGNKWVSNKWL CCEEECCCCCCCHHH	42.94	-
515	Ubiquitination	GNKWVSNKWLHERGQ CCCCCCCHHHHHHHH	43.56	-
529	Phosphorylation	QEFRRPCTLSELE-- HHHCCCCCHHHCC--	35.68	28450419
531	Phosphorylation	FRRPCTLSELE---- HCCCCCHHHCC----	23.21	28450419

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of P4HA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of P4HA1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of P4HA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EVPL_HUMAN	EVPL	physical	26344197

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
• DB01275: Hydralazine
• DB00172: L-Proline
• DB00139: Succinic acid
• DB00126: Vitamin C

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-113, AND MASSSPECTROMETRY.
PubMed: 19159218