dbPTM

HIF1N_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HIF1N_HUMAN
UniProt AC	Q9NWT6
Protein Name	Hypoxia-inducible factor 1-alpha inhibitor
Gene Name	HIF1AN
Organism	Homo sapiens (Human).
Sequence Length	349
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mainly cytoplasmic localization, but interaction with NOTCH1 results in nuclear localization and interaction with ABPA3 results in perinuclear localization in macrophages.
Protein Description	Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation..
Protein Sequence	MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAATAAEAV ------CCCHHHHHH	17.33	22223895
8	Ubiquitination	MAATAAEAVASGSGE CCCHHHHHHHCCCCC	9.46	21890473
24	Ubiquitination	REEAGALGPAWDESQ HHHHCCCCCCCCHHH	14.89	21890473
35	Phosphorylation	DESQLRSYSFPTRPI CHHHHHHCCCCCCCC	14.11	27642862
48	Phosphorylation	PIPRLSQSDPRAEEL CCCCCCCCCCCHHHH	46.32	26270265
102	Phosphorylation	ASTHKFLYYDEKKMA CCCCEEEEECHHHHH	16.41	-
106	Ubiquitination	KFLYYDEKKMANFQN EEEEECHHHHHCCCC	44.97	27667366
115	Ubiquitination	MANFQNFKPRSNREE HHCCCCCCCCCCHHH	47.25	23000965
126	Ubiquitination	NREEMKFHEFVEKLQ CHHHHHHHHHHHHHH	23.28	27667366
131	Ubiquitination	KFHEFVEKLQDIQQR HHHHHHHHHHHHHHC	46.26	21906983
135	Ubiquitination	FVEKLQDIQQRGGEE HHHHHHHHHHCCCHH	2.13	21890473
138	Methylation	KLQDIQQRGGEERLY HHHHHHHCCCHHHEH	38.41	115478491
151	Ubiquitination	LYLQQTLNDTVGRKI EHHHHHHHHHCCHHH	46.42	21890473
204	Ubiquitination	PAHYDEQQNFFAQIK CCCCCCCCCHHHHHC	46.80	27667366
311	Ubiquitination	KRIEYPLKAHQKVAI CEECCCCHHHHHHHH	39.04	27667366
315	Ubiquitination	YPLKAHQKVAIMRNI CCCHHHHHHHHHHCH	24.62	29967540
331	Ubiquitination	KMLGEALGNPQEVGP HHHHHHHCCHHHHHH	51.31	27667366
345	Ubiquitination	PLLNTMIKGRYN--- HHHHHHHCCCCC---	26.89	21890473

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	SIAH1	Q8IUQ4	PMID:17188242
-	K	Ubiquitination	E3 ubiquitin ligase	VHL	P40337	PMID:17132228

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HIF1N_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 HIF1N_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASB9_HUMAN	ASB9	physical	16189514
FBF1_HUMAN	FBF1	physical	16189514
ASB13_HUMAN	ASB13	physical	16189514
HIF1A_HUMAN	HIF1A	physical	11641274
VHL_HUMAN	VHL	physical	11641274
HIF1N_HUMAN	HIF1AN	physical	12482756
HIF1A_HUMAN	HIF1A	physical	19696166
NFKB1_HUMAN	NFKB1	physical	17003112
FEM1B_HUMAN	FEM1B	physical	17003112
UACA_HUMAN	UACA	physical	17003112
HIF1A_HUMAN	HIF1A	physical	12042299
APBA3_HUMAN	APBA3	physical	28514442
IKBB_HUMAN	NFKBIB	physical	28514442
CSKI1_HUMAN	CASKIN1	physical	28514442
OTU7B_HUMAN	OTUD7B	physical	28514442
UBE3A_HUMAN	UBE3A	physical	28514442
TNKS2_HUMAN	TNKS2	physical	28514442
ANR27_HUMAN	ANKRD27	physical	28514442
FYCO1_HUMAN	FYCO1	physical	28514442
NOTC3_HUMAN	NOTCH3	physical	28514442
ANR52_HUMAN	ANKRD52	physical	28514442
RN5A_HUMAN	RNASEL	physical	28514442
FBF1_HUMAN	FBF1	physical	28514442
ANS1A_HUMAN	ANKS1A	physical	28514442
TNKS1_HUMAN	TNKS	physical	28514442
UBP24_HUMAN	USP24	physical	28514442
RPRD2_HUMAN	RPRD2	physical	28514442
TXLNG_HUMAN	TXLNG	physical	28514442
PI42B_HUMAN	PIP4K2B	physical	28514442
REL_HUMAN	REL	physical	28514442
ANK3_HUMAN	ANK3	physical	28514442
OSBL1_HUMAN	OSBPL1A	physical	28514442
PI42C_HUMAN	PIP4K2C	physical	28514442
WDCP_HUMAN	C2orf44	physical	28514442
ANFY1_HUMAN	ANKFY1	physical	28514442
OTUB1_HUMAN	OTUB1	physical	28514442
GMDS_HUMAN	GMDS	physical	28514442
TXLNA_HUMAN	TXLNA	physical	28514442
AFAD_HUMAN	MLLT4	physical	28514442
NFKB2_HUMAN	NFKB2	physical	28514442
4ET_HUMAN	EIF4ENIF1	physical	28514442
ANK2_HUMAN	ANK2	physical	28514442
TISD_HUMAN	ZFP36L2	physical	28514442
M3K21_HUMAN	KIAA1804	physical	28514442
OSBL3_HUMAN	OSBPL3	physical	28514442
TBK1_HUMAN	TBK1	physical	28514442
HECD1_HUMAN	HECTD1	physical	28514442
INVS_HUMAN	INVS	physical	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
There are no disease associations of PTM sites.

Regulatory Network of HIF1N_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]