HJURP_HUMAN - dbPTM
HJURP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HJURP_HUMAN
UniProt AC Q8NCD3
Protein Name Holliday junction recognition protein
Gene Name HJURP
Organism Homo sapiens (Human).
Sequence Length 748
Subcellular Localization Nucleus, nucleolus. Chromosome, centromere. Localizes in centromeres during late telophase and early G1, when CENPA nucleosomes are assembled. Localizes to nucleolus during S phase, nucleolus site being often related to storage.
Protein 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..
Protein Sequence MLGTLRAMEGEDVEDDQLLQKLRASRRRFQRRMQRLIEKYNQPFEDTPVVQMATLTYETPQGLRIWGGRLIKERNEGEIQDSSMKPADRTDGSVQAAAWGPELPSHRTVLGADSKSGEVDATSDQEESVAWALAPAVPQSPLKNELRRKYLTQVDILLQGAEYFECAGNRAGRDVRVTPLPSLASPAVPAPGYCSRISRKSPGDPAKPASSPREWDPLHPSSTDMALVPRNDSLSLQETSSSSFLSSQPFEDDDICNVTISDLYAGMLHSMSRLLSTKPSSIISTKTFIMQNWNSRRRHRYKSRMNKTYCKGARRSQRSSKENFIPCSEPVKGTGALRDCKNVLDVSCRKTGLKLEKAFLEVNRPQIHKLDPSWKERKVTPSKYSSLIYFDSSATYNLDEENRFRTLKWLISPVKIVSRPTIRQGHGENRQREIEIRFDQLHREYCLSPRNQPRRMCLPDSWAMNMYRGGPASPGGLQGLETRRLSLPSSKAKAKSLSEAFENLGKRSLEAGRCLPKSDSSSSLPKTNPTHSATRPQQTSDLHVQGNSSGIFRKSVSPSKTLSVPDKEVPGHGRNRYDEIKEEFDKLHQKYCLKSPGQMTVPLCIGVSTDKASMEVRYQTEGFLGKLNPDPHFQGFQKLPSSPLGCRKSLLGSTAIEAPSSTCVARAITRDGTRDHQFPAKRPRLSEPQGSGRQGNSLGASDGVDNTVRPGDQGSSSQPNSEERGENTSYRMEEKSDFMLEKLETKSV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
8SulfoxidationMLGTLRAMEGEDVED
CCCCCCCCCCCCCCC
5.7021406390
21UbiquitinationEDDQLLQKLRASRRR
CCHHHHHHHHHHHHH
39.6521906983
21 (in isoform 1)Ubiquitination-39.6521890473
21 (in isoform 2)Ubiquitination-39.6521890473
21 (in isoform 3)Ubiquitination-39.6521890473
25PhosphorylationLLQKLRASRRRFQRR
HHHHHHHHHHHHHHH
21.64-
39UbiquitinationRMQRLIEKYNQPFED
HHHHHHHHHCCCCCC
42.3722817900
39 (in isoform 1)Ubiquitination-42.3721890473
39 (in isoform 2)Ubiquitination-42.3721890473
39 (in isoform 3)Ubiquitination-42.3721890473
82PhosphorylationNEGEIQDSSMKPADR
CCCCCCCCCCCCCCC
18.89-
83PhosphorylationEGEIQDSSMKPADRT
CCCCCCCCCCCCCCC
38.83-
85UbiquitinationEIQDSSMKPADRTDG
CCCCCCCCCCCCCCC
38.7121906983
85 (in isoform 1)Ubiquitination-38.7121890473
116PhosphorylationVLGADSKSGEVDATS
EECCCCCCCCCCCCC
44.1028102081
122PhosphorylationKSGEVDATSDQEESV
CCCCCCCCCCCHHHH
28.5122617229
122UbiquitinationKSGEVDATSDQEESV
CCCCCCCCCCCHHHH
28.5129967540
123PhosphorylationSGEVDATSDQEESVA
CCCCCCCCCCHHHHH
38.7322617229
128PhosphorylationATSDQEESVAWALAP
CCCCCHHHHHHHHCC
19.1822617229
140PhosphorylationLAPAVPQSPLKNELR
HCCCCCCCCCCHHHH
26.5726055452
153UbiquitinationLRRKYLTQVDILLQG
HHHHHHHHHHHHHHC
28.4329967540
163PhosphorylationILLQGAEYFECAGNR
HHHHCHHHEECCCCC
12.25-
166UbiquitinationQGAEYFECAGNRAGR
HCHHHEECCCCCCCC
4.1621890473
178PhosphorylationAGRDVRVTPLPSLAS
CCCCCEECCCCCCCC
14.4525159151
182PhosphorylationVRVTPLPSLASPAVP
CEECCCCCCCCCCCC
44.2225159151
185PhosphorylationTPLPSLASPAVPAPG
CCCCCCCCCCCCCCC
20.7725159151
193PhosphorylationPAVPAPGYCSRISRK
CCCCCCCCCCCCCCC
6.0329396449
193UbiquitinationPAVPAPGYCSRISRK
CCCCCCCCCCCCCCC
6.0327667366
193 (in isoform 3)Ubiquitination-6.0321890473
195PhosphorylationVPAPGYCSRISRKSP
CCCCCCCCCCCCCCC
24.9426552605
198PhosphorylationPGYCSRISRKSPGDP
CCCCCCCCCCCCCCC
32.3324719451
201PhosphorylationCSRISRKSPGDPAKP
CCCCCCCCCCCCCCC
32.7630266825
207UbiquitinationKSPGDPAKPASSPRE
CCCCCCCCCCCCCCC
46.6429967540
210PhosphorylationGDPAKPASSPREWDP
CCCCCCCCCCCCCCC
49.7730266825
211PhosphorylationDPAKPASSPREWDPL
CCCCCCCCCCCCCCC
30.0430266825
221PhosphorylationEWDPLHPSSTDMALV
CCCCCCCCCCCEEEE
34.8122199227
222PhosphorylationWDPLHPSSTDMALVP
CCCCCCCCCCEEEEE
32.6422199227
223PhosphorylationDPLHPSSTDMALVPR
CCCCCCCCCEEEEEC
33.8522199227
224UbiquitinationPLHPSSTDMALVPRN
CCCCCCCCEEEEECC
23.4727667366
224 (in isoform 2)Ubiquitination-23.4721890473
236UbiquitinationPRNDSLSLQETSSSS
ECCCCCCCEECCCCC
6.9133845483
247UbiquitinationSSSSFLSSQPFEDDD
CCCCCCCCCCCCCCC
43.9833845483
256UbiquitinationPFEDDDICNVTISDL
CCCCCCCCCEEHHHH
4.2733845483
267UbiquitinationISDLYAGMLHSMSRL
HHHHHHHHHHHHHHH
2.0133845483
269UbiquitinationDLYAGMLHSMSRLLS
HHHHHHHHHHHHHHC
16.7429967540
272UbiquitinationAGMLHSMSRLLSTKP
HHHHHHHHHHHCCCC
23.8529967540
276PhosphorylationHSMSRLLSTKPSSII
HHHHHHHCCCCHHCE
38.6924719451
278UbiquitinationMSRLLSTKPSSIIST
HHHHHCCCCHHCEEE
39.2627667366
278 (in isoform 1)Ubiquitination-39.2621890473
280PhosphorylationRLLSTKPSSIISTKT
HHHCCCCHHCEEEHH
35.4127732954
281PhosphorylationLLSTKPSSIISTKTF
HHCCCCHHCEEEHHH
32.2527732954
284PhosphorylationTKPSSIISTKTFIMQ
CCCHHCEEEHHHHHH
23.3727732954
284UbiquitinationTKPSSIISTKTFIMQ
CCCHHCEEEHHHHHH
23.3729967540
285PhosphorylationKPSSIISTKTFIMQN
CCHHCEEEHHHHHHC
24.5627732954
286UbiquitinationPSSIISTKTFIMQNW
CHHCEEEHHHHHHCC
34.35-
287UbiquitinationSSIISTKTFIMQNWN
HHCEEEHHHHHHCCH
20.6233845483
290UbiquitinationISTKTFIMQNWNSRR
EEEHHHHHHCCHHHH
1.8933845483
296UbiquitinationIMQNWNSRRRHRYKS
HHHCCHHHHHHHHHH
36.1221890473
300UbiquitinationWNSRRRHRYKSRMNK
CHHHHHHHHHHHCCH
38.4729967540
303PhosphorylationRRRHRYKSRMNKTYC
HHHHHHHHHCCHHHH
28.0318452278
303UbiquitinationRRRHRYKSRMNKTYC
HHHHHHHHHCCHHHH
28.0329967540
315UbiquitinationTYCKGARRSQRSSKE
HHHHHHHHHHCCCCC
36.2929967540
321UbiquitinationRRSQRSSKENFIPCS
HHHHCCCCCCCCCCC
58.9033845483
323UbiquitinationSQRSSKENFIPCSEP
HHCCCCCCCCCCCCC
43.8321890473
323 (in isoform 3)Ubiquitination-43.8321890473
328PhosphorylationKENFIPCSEPVKGTG
CCCCCCCCCCCCCCC
39.3121815630
332UbiquitinationIPCSEPVKGTGALRD
CCCCCCCCCCCHHHH
62.5633845483
341AcetylationTGALRDCKNVLDVSC
CCHHHHCCCCCCHHH
55.1425953088
341UbiquitinationTGALRDCKNVLDVSC
CCHHHHCCCCCCHHH
55.1433845483
347PhosphorylationCKNVLDVSCRKTGLK
CCCCCCHHHHHHCCC
14.1021815630
354SumoylationSCRKTGLKLEKAFLE
HHHHHCCCHHHHHHH
56.8128112733
354UbiquitinationSCRKTGLKLEKAFLE
HHHHHCCCHHHHHHH
56.8123000965
354 (in isoform 2)Ubiquitination-56.8121890473
357UbiquitinationKTGLKLEKAFLEVNR
HHCCCHHHHHHHCCC
55.6729967540
369UbiquitinationVNRPQIHKLDPSWKE
CCCHHHHCCCCCHHH
57.1029967540
375UbiquitinationHKLDPSWKERKVTPS
HCCCCCHHHCCCCHH
52.5633845483
380O-linked_GlycosylationSWKERKVTPSKYSSL
CHHHCCCCHHHCCEE
25.5330379171
380PhosphorylationSWKERKVTPSKYSSL
CHHHCCCCHHHCCEE
25.5324719451
382PhosphorylationKERKVTPSKYSSLIY
HHCCCCHHHCCEEEE
34.56-
401PhosphorylationATYNLDEENRFRTLK
CCCCCCCHHCHHHHH
54.0632142685
408SumoylationENRFRTLKWLISPVK
HHCHHHHHHHHCCCE
39.06-
408SumoylationENRFRTLKWLISPVK
HHCHHHHHHHHCCCE
39.06-
408UbiquitinationENRFRTLKWLISPVK
HHCHHHHHHHHCCCE
39.0623000965
408 (in isoform 1)Ubiquitination-39.0621890473
410UbiquitinationRFRTLKWLISPVKIV
CHHHHHHHHCCCEEE
2.3829967540
412PhosphorylationRTLKWLISPVKIVSR
HHHHHHHCCCEEECC
22.8219664994
415UbiquitinationKWLISPVKIVSRPTI
HHHHCCCEEECCCCC
40.55-
418PhosphorylationISPVKIVSRPTIRQG
HCCCEEECCCCCCCC
35.7022468782
421PhosphorylationVKIVSRPTIRQGHGE
CEEECCCCCCCCCCC
27.9023312004
421UbiquitinationVKIVSRPTIRQGHGE
CEEECCCCCCCCCCC
27.9029967540
432PhosphorylationGHGENRQREIEIRFD
CCCCCCCEEEEEEHH
43.5632142685
432UbiquitinationGHGENRQREIEIRFD
CCCCCCCEEEEEEHH
43.5629967540
441UbiquitinationIEIRFDQLHREYCLS
EEEEHHHHHHHHHCC
4.4129967540
445PhosphorylationFDQLHREYCLSPRNQ
HHHHHHHHHCCCCCC
9.9229396449
448PhosphorylationLHREYCLSPRNQPRR
HHHHHHCCCCCCCCC
20.4619664994
452UbiquitinationYCLSPRNQPRRMCLP
HHCCCCCCCCCCCCC
33.8729967540
461PhosphorylationRRMCLPDSWAMNMYR
CCCCCCCHHHHHCCC
18.1324043423
463UbiquitinationMCLPDSWAMNMYRGG
CCCCCHHHHHCCCCC
5.3929967540
467PhosphorylationDSWAMNMYRGGPASP
CHHHHHCCCCCCCCC
10.9124043423
472PhosphorylationNMYRGGPASPGGLQG
HCCCCCCCCCCCCCC
31.4732645325
472UbiquitinationNMYRGGPASPGGLQG
HCCCCCCCCCCCCCC
31.4729967540
473PhosphorylationMYRGGPASPGGLQGL
CCCCCCCCCCCCCCH
27.4919664994
482PhosphorylationGGLQGLETRRLSLPS
CCCCCHHHCCCCCCC
26.5723927012
482UbiquitinationGGLQGLETRRLSLPS
CCCCCHHHCCCCCCC
26.5729967540
486PhosphorylationGLETRRLSLPSSKAK
CHHHCCCCCCCHHHH
36.1023401153
489PhosphorylationTRRLSLPSSKAKAKS
HCCCCCCCHHHHHHH
50.1722617229
490PhosphorylationRRLSLPSSKAKAKSL
CCCCCCCHHHHHHHH
34.3925159151
493UbiquitinationSLPSSKAKAKSLSEA
CCCCHHHHHHHHHHH
61.15-
495SumoylationPSSKAKAKSLSEAFE
CCHHHHHHHHHHHHH
51.74-
495MethylationPSSKAKAKSLSEAFE
CCHHHHHHHHHHHHH
51.7482974403
495SumoylationPSSKAKAKSLSEAFE
CCHHHHHHHHHHHHH
51.74-
495UbiquitinationPSSKAKAKSLSEAFE
CCHHHHHHHHHHHHH
51.7429967540
496PhosphorylationSSKAKAKSLSEAFEN
CHHHHHHHHHHHHHH
41.8225159151
496UbiquitinationSSKAKAKSLSEAFEN
CHHHHHHHHHHHHHH
41.8229967540
498PhosphorylationKAKAKSLSEAFENLG
HHHHHHHHHHHHHHH
33.6927050516
501UbiquitinationAKSLSEAFENLGKRS
HHHHHHHHHHHHHHH
5.8529967540
503PhosphorylationSLSEAFENLGKRSLE
HHHHHHHHHHHHHHH
47.8732645325
505UbiquitinationSEAFENLGKRSLEAG
HHHHHHHHHHHHHHC
34.6129967540
506AcetylationEAFENLGKRSLEAGR
HHHHHHHHHHHHHCC
41.8125953088
506MethylationEAFENLGKRSLEAGR
HHHHHHHHHHHHHCC
41.81115970695
506UbiquitinationEAFENLGKRSLEAGR
HHHHHHHHHHHHHCC
41.8129967540
508PhosphorylationFENLGKRSLEAGRCL
HHHHHHHHHHHCCCC
33.76-
509UbiquitinationENLGKRSLEAGRCLP
HHHHHHHHHHCCCCC
6.4129967540
513UbiquitinationKRSLEAGRCLPKSDS
HHHHHHCCCCCCCCC
26.3329967540
517SumoylationEAGRCLPKSDSSSSL
HHCCCCCCCCCCCCC
54.68-
517SumoylationEAGRCLPKSDSSSSL
HHCCCCCCCCCCCCC
54.68-
517UbiquitinationEAGRCLPKSDSSSSL
HHCCCCCCCCCCCCC
54.6829967540
518PhosphorylationAGRCLPKSDSSSSLP
HCCCCCCCCCCCCCC
40.5626852163
520PhosphorylationRCLPKSDSSSSLPKT
CCCCCCCCCCCCCCC
38.9321815630
521PhosphorylationCLPKSDSSSSLPKTN
CCCCCCCCCCCCCCC
29.0129396449
522PhosphorylationLPKSDSSSSLPKTNP
CCCCCCCCCCCCCCC
39.5929396449
523PhosphorylationPKSDSSSSLPKTNPT
CCCCCCCCCCCCCCC
51.1129396449
526UbiquitinationDSSSSLPKTNPTHSA
CCCCCCCCCCCCCCC
67.2529967540
527UbiquitinationSSSSLPKTNPTHSAT
CCCCCCCCCCCCCCC
44.4829967540
532PhosphorylationPKTNPTHSATRPQQT
CCCCCCCCCCCCCCC
33.5425627689
532UbiquitinationPKTNPTHSATRPQQT
CCCCCCCCCCCCCCC
33.5429967540
534PhosphorylationTNPTHSATRPQQTSD
CCCCCCCCCCCCCCE
45.9928555341
536UbiquitinationPTHSATRPQQTSDLH
CCCCCCCCCCCCEEE
26.6929967540
539PhosphorylationSATRPQQTSDLHVQG
CCCCCCCCCEEEECC
20.9728555341
540UbiquitinationATRPQQTSDLHVQGN
CCCCCCCCEEEECCC
33.5629967540
541UbiquitinationTRPQQTSDLHVQGNS
CCCCCCCEEEECCCC
44.1529967540
549PhosphorylationLHVQGNSSGIFRKSV
EEECCCCCCCEECCC
39.6528555341
553UbiquitinationGNSSGIFRKSVSPSK
CCCCCCEECCCCCCC
28.5529967540
555PhosphorylationSSGIFRKSVSPSKTL
CCCCEECCCCCCCCC
24.4623927012
557PhosphorylationGIFRKSVSPSKTLSV
CCEECCCCCCCCCCC
30.4623401153
559PhosphorylationFRKSVSPSKTLSVPD
EECCCCCCCCCCCCC
30.6628464451
561PhosphorylationKSVSPSKTLSVPDKE
CCCCCCCCCCCCCCC
28.7128464451
563PhosphorylationVSPSKTLSVPDKEVP
CCCCCCCCCCCCCCC
36.5128464451
563UbiquitinationVSPSKTLSVPDKEVP
CCCCCCCCCCCCCCC
36.5129967540
567AcetylationKTLSVPDKEVPGHGR
CCCCCCCCCCCCCCC
55.3225953088
567UbiquitinationKTLSVPDKEVPGHGR
CCCCCCCCCCCCCCC
55.3229967540
572UbiquitinationPDKEVPGHGRNRYDE
CCCCCCCCCCCCHHH
26.4329967540
581SumoylationRNRYDEIKEEFDKLH
CCCHHHHHHHHHHHH
49.49-
581SumoylationRNRYDEIKEEFDKLH
CCCHHHHHHHHHHHH
49.4928112733
581UbiquitinationRNRYDEIKEEFDKLH
CCCHHHHHHHHHHHH
49.4929967540
584UbiquitinationYDEIKEEFDKLHQKY
HHHHHHHHHHHHHHH
12.0029967540
586SumoylationEIKEEFDKLHQKYCL
HHHHHHHHHHHHHCC
53.8728112733
586UbiquitinationEIKEEFDKLHQKYCL
HHHHHHHHHHHHHCC
53.8729967540
590UbiquitinationEFDKLHQKYCLKSPG
HHHHHHHHHCCCCCC
27.4729967540
591PhosphorylationFDKLHQKYCLKSPGQ
HHHHHHHHCCCCCCC
9.1029083192
594UbiquitinationLHQKYCLKSPGQMTV
HHHHHCCCCCCCCEE
51.5529967540
595PhosphorylationHQKYCLKSPGQMTVP
HHHHCCCCCCCCEEE
22.7029255136
596UbiquitinationQKYCLKSPGQMTVPL
HHHCCCCCCCCEEEE
35.1329967540
600PhosphorylationLKSPGQMTVPLCIGV
CCCCCCCEEEEEEEE
15.8729255136
608PhosphorylationVPLCIGVSTDKASME
EEEEEEEECCCCCCE
26.1922199227
609PhosphorylationPLCIGVSTDKASMEV
EEEEEEECCCCCCEE
38.8322199227
611UbiquitinationCIGVSTDKASMEVRY
EEEEECCCCCCEEEE
42.31-
626AcetylationQTEGFLGKLNPDPHF
CCCCCHHCCCCCCCC
47.4325953088
626UbiquitinationQTEGFLGKLNPDPHF
CCCCCHHCCCCCCCC
47.4329967540
627UbiquitinationTEGFLGKLNPDPHFQ
CCCCHHCCCCCCCCC
12.1929967540
638UbiquitinationPHFQGFQKLPSSPLG
CCCCCCCCCCCCCCC
61.1729967540
641PhosphorylationQGFQKLPSSPLGCRK
CCCCCCCCCCCCCCH
55.8330266825
642PhosphorylationGFQKLPSSPLGCRKS
CCCCCCCCCCCCCHH
23.3929255136
648SumoylationSSPLGCRKSLLGSTA
CCCCCCCHHHHCCCC
49.92-
648SumoylationSSPLGCRKSLLGSTA
CCCCCCCHHHHCCCC
49.92-
648UbiquitinationSSPLGCRKSLLGSTA
CCCCCCCHHHHCCCC
49.9229967540
649PhosphorylationSPLGCRKSLLGSTAI
CCCCCCHHHHCCCCE
14.9622199227
653PhosphorylationCRKSLLGSTAIEAPS
CCHHHHCCCCEECCC
18.0330576142
654PhosphorylationRKSLLGSTAIEAPSS
CHHHHCCCCEECCCC
29.8330576142
660PhosphorylationSTAIEAPSSTCVARA
CCCEECCCCCEEEEE
45.3829396449
661PhosphorylationTAIEAPSSTCVARAI
CCEECCCCCEEEEEH
25.4328555341
662PhosphorylationAIEAPSSTCVARAIT
CEECCCCCEEEEEHH
18.4829396449
681UbiquitinationRDHQFPAKRPRLSEP
CCCCCCCCCCCCCCC
64.2729967540
686PhosphorylationPAKRPRLSEPQGSGR
CCCCCCCCCCCCCCC
48.8121815630
691PhosphorylationRLSEPQGSGRQGNSL
CCCCCCCCCCCCCCC
26.0923532336
707PhosphorylationASDGVDNTVRPGDQG
CCCCCCCCCCCCCCC
17.2728985074
735SumoylationTSYRMEEKSDFMLEK
CCCCHHHHCHHHHHH
41.86-
735SumoylationTSYRMEEKSDFMLEK
CCCCHHHHCHHHHHH
41.86-
736PhosphorylationSYRMEEKSDFMLEKL
CCCHHHHCHHHHHHH
39.08-
739SulfoxidationMEEKSDFMLEKLETK
HHHHCHHHHHHHHCC
5.9221406390
742SumoylationKSDFMLEKLETKSV-
HCHHHHHHHHCCCC-
47.89-
742SumoylationKSDFMLEKLETKSV-
HCHHHHHHHHCCCC-
47.89-
745PhosphorylationFMLEKLETKSV----
HHHHHHHCCCC----
38.7723312004
747PhosphorylationLEKLETKSV------
HHHHHCCCC------
40.2421712546

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
412SPhosphorylationKinaseCDK1P06493
PSP
448SPhosphorylationKinaseCDK1P06493
PSP
473SPhosphorylationKinaseCDK1P06493
PSP
486SPhosphorylationKinaseAKT1P31749
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HJURP_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 HJURP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIC60_HUMANIMMTphysical
16169070
CENPA_YEASTCSE4genetic
21980305
CENPA_HUMANCENPAgenetic
21980305
CENPA_HUMANCENPAphysical
19410545
CENPA_HUMANCENPAphysical
19410544
CENPA_HUMANCENPAphysical
21478274
CENPA_HUMANCENPAphysical
20080577
RUVB1_HUMANRUVBL1physical
20080577
RUVB2_HUMANRUVBL2physical
20080577
RBBP7_HUMANRBBP7physical
20080577
RBBP4_HUMANRBBP4physical
20080577
NPM_HUMANNPM1physical
20080577
CENPA_XENLAcenpaphysical
21321101
CENPA_HUMANCENPAphysical
22406139
TBA3C_HUMANTUBA3Cphysical
26186194
MS18A_HUMANMIS18Aphysical
26186194
DUS1L_HUMANDUS1Lphysical
26186194
CENPA_HUMANCENPAphysical
25727006
DUS1L_HUMANDUS1Lphysical
28514442
TBA3C_HUMANTUBA3Cphysical
28514442
MS18A_HUMANMIS18Aphysical
28514442

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 HJURP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-473 ANDSER-642, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-140; SER-412;SER-448; SER-473 AND SER-642, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-486 ANDSER-642, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-642, ANDMASS SPECTROMETRY.
"Identification of FAKTS as a novel 14-3-3-associated nuclearprotein.";
Luhn P., Wang H., Marcus A.I., Fu H.;
Proteins 67:479-489(2007).
Cited for: INTERACTION WITH 14-3-3 PROTEINS, SUBCELLULAR LOCATION, TISSUESPECIFICITY, PHOSPHORYLATION AT SER-486, AND MUTAGENESIS OF SER-486.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-473, ANDMASS SPECTROMETRY.

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