CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017609
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Holliday junction recognition protein 
Protein Synonyms/Alias
 14-3-3-associated AKT substrate; Fetal liver-expressing gene 1 protein; Up-regulated in lung cancer 9 
Gene Name
 HJURP 
Gene Synonyms/Alias
 FAKTS; FLEG1; URLC9 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21EDDQLLQKLRASRRRubiquitination[1, 2]
39RMQRLIEKYNQPFEDubiquitination[1]
85EIQDSSMKPADRTDGubiquitination[1, 2]
207KSPGDPAKPASSPREubiquitination[2]
278MSRLLSTKPSSIISTubiquitination[1, 2, 3, 4, 5]
286PSSIISTKTFIMQNWubiquitination[2]
321RRSQRSSKENFIPCSubiquitination[2]
332IPCSEPVKGTGALRDubiquitination[2]
341TGALRDCKNVLDVSCubiquitination[2]
354SCRKTGLKLEKAFLEubiquitination[2]
369VNRPQIHKLDPSWKEubiquitination[2]
375HKLDPSWKERKVTPSubiquitination[2]
408ENRFRTLKWLISPVKubiquitination[2, 3, 5, 6]
415KWLISPVKIVSRPTIubiquitination[2]
493SLPSSKAKAKSLSEAubiquitination[2]
495PSSKAKAKSLSEAFEubiquitination[2]
506EAFENLGKRSLEAGRubiquitination[2]
517EAGRCLPKSDSSSSLubiquitination[2]
567KTLSVPDKEVPGHGRubiquitination[2]
594LHQKYCLKSPGQMTVubiquitination[2]
611CIGVSTDKASMEVRYubiquitination[2]
626QTEGFLGKLNPDPHFubiquitination[2]
638PHFQGFQKLPSSPLGubiquitination[2]
648SSPLGCRKSLLGSTAubiquitination[2, 7]
681RDHQFPAKRPRLSEPubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerization and prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds Holliday junctions. 
Sequence Annotation
 MOD_RES 123 123 Phosphoserine.
 MOD_RES 140 140 Phosphoserine.
 MOD_RES 185 185 Phosphoserine.
 MOD_RES 448 448 Phosphoserine.
 MOD_RES 473 473 Phosphoserine.
 MOD_RES 486 486 Phosphoserine; by PKB/AKT1.
 MOD_RES 595 595 Phosphoserine.
 MOD_RES 642 642 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Centromere; Chaperone; Chromosome; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 748 AA 
Protein Sequence
MLGTLRAMEG EDVEDDQLLQ KLRASRRRFQ RRMQRLIEKY NQPFEDTPVV QMATLTYETP 60
QGLRIWGGRL IKERNEGEIQ DSSMKPADRT DGSVQAAAWG PELPSHRTVL GADSKSGEVD 120
ATSDQEESVA WALAPAVPQS PLKNELRRKY LTQVDILLQG AEYFECAGNR AGRDVRVTPL 180
PSLASPAVPA PGYCSRISRK SPGDPAKPAS SPREWDPLHP SSTDMALVPR NDSLSLQETS 240
SSSFLSSQPF EDDDICNVTI SDLYAGMLHS MSRLLSTKPS SIISTKTFIM QNWNSRRRHR 300
YKSRMNKTYC KGARRSQRSS KENFIPCSEP VKGTGALRDC KNVLDVSCRK TGLKLEKAFL 360
EVNRPQIHKL DPSWKERKVT PSKYSSLIYF DSSATYNLDE ENRFRTLKWL ISPVKIVSRP 420
TIRQGHGENR QREIEIRFDQ LHREYCLSPR NQPRRMCLPD SWAMNMYRGG PASPGGLQGL 480
ETRRLSLPSS KAKAKSLSEA FENLGKRSLE AGRCLPKSDS SSSLPKTNPT HSATRPQQTS 540
DLHVQGNSSG IFRKSVSPSK TLSVPDKEVP GHGRNRYDEI KEEFDKLHQK YCLKSPGQMT 600
VPLCIGVSTD KASMEVRYQT EGFLGKLNPD PHFQGFQKLP SSPLGCRKSL LGSTAIEAPS 660
STCVARAITR DGTRDHQFPA KRPRLSEPQG SGRQGNSLGA SDGVDNTVRP GDQGSSSQPN 720
SEERGENTSY RMEEKSDFML EKLETKSV 748 
Gene Ontology
 GO:0000777; C:condensed chromosome kinetochore; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0034080; P:CENP-A containing nucleosome assembly at centromere; IMP:UniProtKB.
 GO:0007059; P:chromosome segregation; IMP:UniProtKB.
 GO:0051101; P:regulation of DNA binding; IDA:UniProtKB.
 GO:0043254; P:regulation of protein complex assembly; IDA:UniProtKB. 
Interpro
 IPR018465; Centromere_Scm3_N.
 IPR021052; HJURP.
 IPR022102; HJURP_C. 
Pfam
 PF12347; HJURP_C
 PF12346; HJURP_mid
 PF10384; Scm3 
SMART
  
PROSITE
  
PRINTS