dbPTM

HIF3A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HIF3A_HUMAN
UniProt AC	Q9Y2N7
Protein Name	Hypoxia-inducible factor 3-alpha {ECO:0000303\|PubMed:11573933}
Gene Name	HIF3A {ECO:0000312\|HGNC:HGNC:15825}
Organism	Homo sapiens (Human).
Sequence Length	669
Subcellular Localization	Nucleus . Cytoplasm . Nucleus speckle . Mitochondrion . In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes. Shuttles between the nucleus and the cytoplasm in a CRM1-
Protein Description	Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression. [PubMed: 11573933]
Protein Sequence	MALGLQRARSTTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVGAGGEPLDACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALTPQQTLSRRKVEAPTERCFSLRMKSTLTSRGRTLNLKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHFLISQVEETGVVLSLEQTEQHSRRPIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRRLLGPILDGASVAATPSTPLATRHPQSPLSADLPDELPVGTENVHRLFTSGKDTEAVETDLDIAQDADALDLEMLAPYISMDDDFQLNASEQLPRAYHRPLGAVPRPRARSFHGLSPPALEPSLLPRWGSDPRLSCSSPSRGDPSASSPMAGARKRTLAQSSEDEDEGVELLGVRPPKRSPSPEHENFLLFPLSLSFLLTGGPAPGSLQDPSTPLLNLNEPLGLGPSLLSPYSDEDTTQPGGPFQPRAGSAQAD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7 (in isoform 5)	Phosphorylation	-	36.69	27762562
11	Phosphorylation	GLQRARSTTELRKEK HHHHHHCHHHHHHHH	20.80	22210691
27 (in isoform 7)	Phosphorylation	-	43.89	26657352
27 (in isoform 6)	Phosphorylation	-	43.89	26657352
28	Phosphorylation	DAARSRRSQETEVLY HHHHHHHHHHHHHHH	31.12	24719451
35	Phosphorylation	SQETEVLYQLAHTLP HHHHHHHHHHHHHHH	13.47	24719451
55	Phosphorylation	SAHLDKASIMRLTIS HHHCCHHHHHHHHHH	23.74	24719451
60	Phosphorylation	KASIMRLTISYLRMH HHHHHHHHHHHHHHH	9.49	24719451
63	Phosphorylation	IMRLTISYLRMHRLC HHHHHHHHHHHHHHH	8.42	24719451
170	Phosphorylation	CFSLRMKSTLTSRGR HHHHHHHHHHHCCCC	21.21	26437602
173	Phosphorylation	LRMKSTLTSRGRTLN HHHHHHHHCCCCEEE	19.23	26437602
246	Phosphorylation	GAFLSRHSLDMKFTY CCCCCCCCCCCEEEE	25.59	24719451
295	Phosphorylation	KSIHTLLSKGQAVTG HHHHHHHHCCCCCCC	37.54	24719451
396	Phosphorylation	LAFLHPPSLSEAALA EEECCCCCCCHHHHH	49.32	-
398	Phosphorylation	FLHPPSLSEAALAAD ECCCCCCCHHHHHCC	29.53	-
398	Ubiquitination	FLHPPSLSEAALAAD ECCCCCCCHHHHHCC	29.53	12538644
411	Phosphorylation	ADPRRFCSPDLRRLL CCHHHHCCHHHHHHH	20.80	24719451
430	Phosphorylation	DGASVAATPSTPLAT CCCCEECCCCCCCCC	14.18	24719451
433	Phosphorylation	SVAATPSTPLATRHP CEECCCCCCCCCCCC	24.43	24719451
467	Ubiquitination	HRLFTSGKDTEAVET HHHHHCCCCCCHHCC	62.33	12538644
492	Hydroxylation	LDLEMLAPYISMDDD CCHHHHHCCCCCCCH	24.03	12538644
501	Ubiquitination	ISMDDDFQLNASEQL CCCCCHHCCCHHHCC	40.58	12538644
526	Phosphorylation	VPRPRARSFHGLSPP CCCCCCCCCCCCCCC	22.17	28348404
531	Phosphorylation	ARSFHGLSPPALEPS CCCCCCCCCCCCCCC	33.17	28348404
555	Phosphorylation	RLSCSSPSRGDPSAS CCCCCCCCCCCCCCC	51.33	22210691
570	Ubiquitination	SPMAGARKRTLAQSS CCCCHHHHHHCCCCC	49.56	12538644

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
-	K	Ubiquitination	E3 ubiquitin ligase	VHL	P40337	PMID:10353251

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
492	P	Hydroxylation		12538644
In normoxia, hydroxylated on Pro-492 in the oxygen-dependent degradation domain (ODD) by prolyl hydroxylase(s) (PHD).

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 HIF3A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
VHL_HUMAN	VHL	physical	12538644
EPAS1_HUMAN	EPAS1	physical	17998805

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
There are no disease associations of PTM sites.

Regulatory Network of HIF3A_HUMAN

Related Literatures of Post-Translational Modification

Hydroxylation
Reference	PubMed
"Multiple splice variants of the human HIF-3 alpha locus are targetsof the von Hippel-Lindau E3 ubiquitin ligase complex."; Maynard M.A., Qi H., Chung J., Lee E.H., Kondo Y., Hara S.,Conaway R.C., Conaway J.W., Ohh M.; J. Biol. Chem. 278:11032-11040(2003). Cited for: ALTERNATIVE SPLICING, INTERACTION WITH VHL, UBIQUITINATION AT LYS-467AND LYS-570, HYDROXYLATION AT PRO-492, AND MUTAGENESIS OF LYS-467;PRO-492 AND LYS-570.	12538644 [Abstract]
Ubiquitylation
Reference	PubMed
"Multiple splice variants of the human HIF-3 alpha locus are targetsof the von Hippel-Lindau E3 ubiquitin ligase complex."; Maynard M.A., Qi H., Chung J., Lee E.H., Kondo Y., Hara S.,Conaway R.C., Conaway J.W., Ohh M.; J. Biol. Chem. 278:11032-11040(2003). Cited for: ALTERNATIVE SPLICING, INTERACTION WITH VHL, UBIQUITINATION AT LYS-467AND LYS-570, HYDROXYLATION AT PRO-492, AND MUTAGENESIS OF LYS-467;PRO-492 AND LYS-570.	12538644 [Abstract]

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