Q61221

PTMD Annotation Information

※ Protein Information

Tag Content
UniProt Accession HIF1A_MOUSE; Q61221;
Entrez ID 15251
GenBank Protein ID NM_001313919.1; NM_001313920.1; NM_010431.2; XM_017314961.1;
GenBank Nucleotide ID NP_001300848.1; NP_001300849.1; NP_034561.2; XP_017170450.1;
Protein Name Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein)
Gene Name Hif1a
Organism Mus musculus
NCBI Taxa ID 10090
Functional DescriptionFunctions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (By similarity).
Sequence
(Fasta)		MEGAGGENEK KKMSSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM 60
RLTISYLRVR KLLDAGGLDS EDEMKAQMDC FYLKALDGFV MVLTDDGDMV YISDNVNKYM 120
GLTQFELTGH SVFDFTHPCD HEEMREMLTH RNGPVRKGKE LNTQRSFFLR MKCTLTSRGR 180
TMNIKSATWK VLHCTGHIHV YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK 240
TFLSRHSLDM KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV 300
TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL IFSLQQTESV 360
LKPVESSDMK MTQLFTKVES EDTSCLFDKL KKEPDALTLL APAAGDTIIS LDFGSDDTET 420
EDQQLEDVPL YNDVMFPSSN EKLNINLAMS PLPSSETPKP LRSSADPALN QEVALKLESS 480
PESLGLSFTM PQIQDQPASP SDGSTRQSSP ERLLQENVNT PNFSQPNSPS EYCFDVDSDM 540
VNVFKLELVE KLFAEDTEAK NPFSTQDTDL DLEMLAPYIP MDDDFQLRSF DQLSPLESNS 600
PSPPSMSTVT GFQQTQLQKP TITATATTTA TTDESKTETK DNKEDIKILI ASPSSTQVPQ 660
ETTTAKASAY SGTHSRTASP DRAGKRVIEQ TDKAHPRSLN LSATLNQRNT VPEEELNPKT 720
IASQNAQRKR KMEHDGSLFQ AAGIGTLLQQ PGDCAPTMSL SWKRVKGFIS SEQNGTEQKT 780
IILIPSDLAC RLLGQSMDES GLPQLTSYDC EVNAPIQGSR NLLQGEELLR ALDQVN 837

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1UbiquitinationRenal cell carcinomaA14595381
[Reference]: The von Hippel-Lindau tumor suppressor protein (pVHL) suppresses tumor formation by binding the alpha subunits of hypoxia-inducible factors (HIFs) responsible for stimulating tumor angiogenesis and glycolysis, targeting them for ubiquitination and proteasomal destruction.
2UbiquitinationProstate cancer/carcinoma/adenocarcinomaD11359907
[Reference]: Increased phosphatidylinositol 3-kinase (PI3K) and AKT or decreased PTEN activity in prostate cancer cells also increases HIF-1alpha expression by an undefined mechanism.

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 30)
(view all)		MESH:D000708 ; Anaplasia
MESH:D001254 ; Astrocytoma
MESH:D002545 ; Brain Ischemia
MESH:D001943 ; Breast Neoplasms
MESH:D002277 ; Carcinoma
MESH:D044584 ; Carcinoma, Ductal

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 7)
(view all)		 357       LIFSLQQTESVLKPV     dbPAF
366       SVLKPVESSDMKMTQ     dbPAF
450       LNINLAMSPLPSSET     dbPAF
654       KILIASPSSTQVPQE     dbPAF
656       LIASPSSTQVPQETT     dbPAF
679       GTHSRTASPDRAGKR     dbPAF

※ Protein-Protein Interaction

NetworkInteraction
ABSource