CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029526
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Hypoxia-inducible factor 1, alpha subunit (Basic helix-loop-helix transcription factor), isoform CRA_a 
Protein Synonyms/Alias
 Hypoxia-inducible factor 1-alpha 
Gene Name
 HIF1A 
Gene Synonyms/Alias
 hCG_21199 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11AGGANDKKNRISSERubiquitination[1]
33AARSRRSKESEVFYEubiquitination[1, 2, 3, 4]
57NVSSHLDKASVMRLTubiquitination[3, 4]
72ISYLRVRKLLDAGDLubiquitination[1, 2, 3, 4]
86LDIEDDMKAQMNCFYubiquitination[3]
173RSFFLRMKCTLTSRGubiquitination[1]
186RGRTMNIKSATWKVLubiquitination[1, 2, 3, 4]
215QPQCGYKKPPMTCLVubiquitination[3]
241IEIPLDSKTFLSRHSubiquitination[3]
252SRHSLDMKFSYCDERubiquitination[1, 3, 4, 5]
290LDSDHLTKTHHDMFTubiquitination[1, 2, 3, 4]
298THHDMFTKGQVTTGQubiquitination[1, 2, 3, 4]
378KMTQLFTKVESEDTSubiquitination[1, 2, 3, 4]
390DTSSLFDKLKKEPDAubiquitination[1, 2, 3, 4]
392SSLFDKLKKEPDALTubiquitination[2]
393SLFDKLKKEPDALTLubiquitination[1]
478LNQEVALKLEPNPESubiquitination[2, 3, 4]
539FKLELVEKLFAEDTEubiquitination[2, 3, 4, 6, 7]
675ASPNRAGKGVIEQTEubiquitination[2]
710PEEELNPKILALQNAacetylation[8]
710PEEELNPKILALQNAubiquitination[1, 2, 4]
770EQNGMEQKTIILIPSubiquitination[1, 3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; DNA-binding; Nucleus; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 827 AA 
Protein Sequence
MEGAGGANDK KNRISSERRK EKSRDAARSR RSKESEVFYE LAHQLPLPHN VSSHLDKASV 60
MRLTISYLRV RKLLDAGDLD IEDDMKAQMN CFYLKALDGF VMVLTDDGDM IYISDNVNKY 120
MGLTQFELTG HSVFDFTHPC DHEEMREMLT HRNGLVKKGK EQNTQRSFFL RMKCTLTSRG 180
RTMNIKSATW KVLHCTGHIH VYDTNSNQPQ CGYKKPPMTC LVLICEPIPH PSNIEIPLDS 240
KTFLSRHSLD MKFSYCDERI TELMGYEPEE LLGRSIYEYY HALDSDHLTK THHDMFTKGQ 300
VTTGQYRMLA KRGGYVWVET QATVIYNTKN SQPQCIVCVN YVVSGIIQHD LIFSLQQTEC 360
VLKPVESSDM KMTQLFTKVE SEDTSSLFDK LKKEPDALTL LAPAAGDTII SLDFGSNDTE 420
TDDQQLEEVP LYNDVMLPSP NEKLQNINLA MSPLPTAETP KPLRSSADPA LNQEVALKLE 480
PNPESLELSF TMPQIQDQTP SPSDGSTRQS SPEPNSPSEY CFYVDSDMVN EFKLELVEKL 540
FAEDTEAKNP FSTQDTDLDL EMLAPYIPMD DDFQLRSFDQ LSPLESSSAS PESASPQSTV 600
TVFQQTQIQE PTANATTTTA TTDELKTVTK DRMEDIKILI ASPSPTHIHK ETTSATSSPY 660
RDTQSRTASP NRAGKGVIEQ TEKSHPRSPN VLSVALSQRT TVPEEELNPK ILALQNAQRK 720
RKMEHDGSLF QAVGIGTLLQ QPDDHAATTS LSWKRVKGCK SSEQNGMEQK TIILIPSDLA 780
CRLLGQSMDE SGLPQLTSYD CEVNAPIQGS RNLLQGEELL RALDQVN 827 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
 GO:0004871; F:signal transducer activity; IEA:InterPro.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011598; bHLH_dom.
 IPR001321; HIF-1_alpha.
 IPR014887; HIF-1_TAD_C.
 IPR021537; HIF_alpha_subunit.
 IPR001610; PAC.
 IPR000014; PAS.
 IPR013767; PAS_fold.
 IPR013655; PAS_fold_3. 
Pfam
 PF11413; HIF-1
 PF08778; HIF-1a_CTAD
 PF00989; PAS
 PF08447; PAS_3 
SMART
 SM00353; HLH
 SM00086; PAC
 SM00091; PAS 
PROSITE
 PS50888; BHLH
 PS50112; PAS 
PRINTS
 PR01080; HYPOXIAIF1A.