ACINU_HUMAN - dbPTM
ACINU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACINU_HUMAN
UniProt AC Q9UKV3
Protein Name Apoptotic chromatin condensation inducer in the nucleus
Gene Name ACIN1
Organism Homo sapiens (Human).
Sequence Length 1341
Subcellular Localization Nucleus. Nucleus speckle. Nucleus, nucleoplasm. Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm.
Protein Description Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells..
Protein Sequence MWRRKHPRTSGGTRGVLSGNRGVEYGSGRGHLGTFEGRWRKLPKMPEAVGTDPSTSRKMAELEEVTLDGKPLQALRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAAELEEASAESEDEMIHPEGVASLLPPDFQSSLERPELELSRHSPRKSSSISEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSPSPPRLTEDRKKASLVALPEQTASEEETPPPLLTKEASSPPPHPQLHSEEEIEPMEGPAPAVLIQLSPPNTDADTRELLVSQHTVQLVGGLSPLSSPSDTKAESPAEKVPEESVLPLVQKSTLADYSAQKDLEPESDRSAQPLPLKIEELALAKGITEECLKQPSLEQKEGRRASHTLLPSHRLKQSADSSSSRSSSSSSSSSRSRSRSPDSSGSRSHSPLRSKQRDVAQARTHANPRGRPKMGSRSTSESRSRSRSRSRSASSNSRKSLSPGVSRDSSTSYTETKDPSSGQEVATPPVPQLQVCEPKERTSTSSSSVQARRLSQPESAEKHVTQRLQPERGSPKKCEAEEAEPPAATQPQTSETQTSHLPESERIHHTVEEKEEVTMDTSENRPENDVPEPPMPIADQVSNDDRPEGSVEDEEKKESSLPKSFKRKISVVSATKGVPAGNSDTEGGQPGRKRRWGASTATTQKKPSISITTESLKSLIPDIKPLAGQEAVVDLHADDSRISEDETERNGDDGTHDKGLKICRTVTQVVPAEGQENGQREEEEEEKEPEAEPPVPPQVSVEVALPPPAEHEVKKVTLGDTLTRRSISQQKSGVSITIDDPVRTAQVPSPPRGKISNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQDELDYHRGLLVDRPSETKTEEQGIPRPLHPPPPPPVQPPQHPRAEQREQERAVREQWAEREREMERRERTRSEREWDRDKVREGPRSRSRSRDRRRKERAKSKEKKSEKKEKAQEEPPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQKEAERAERAKEREKRRKEQEEEEQKEREKEAERERNRQLEREKRREHSRERDRERERERERDRGDRDRDRERDRERGRERDRRDTKRHSRSRSRSTPVRDRGGRR
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
5Ubiquitination---MWRRKHPRTSGG
---CCCCCCCCCCCC
49.7617370265
8DimethylationMWRRKHPRTSGGTRG
CCCCCCCCCCCCCCC
41.04-
8MethylationMWRRKHPRTSGGTRG
CCCCCCCCCCCCCCC
41.04-
9PhosphorylationWRRKHPRTSGGTRGV
CCCCCCCCCCCCCCC
35.8530108239
10PhosphorylationRRKHPRTSGGTRGVL
CCCCCCCCCCCCCCC
36.1830108239
13PhosphorylationHPRTSGGTRGVLSGN
CCCCCCCCCCCCCCC
27.9830108239
14DimethylationPRTSGGTRGVLSGNR
CCCCCCCCCCCCCCC
36.18-
14MethylationPRTSGGTRGVLSGNR
CCCCCCCCCCCCCCC
36.18-
15 (in isoform 3)Phosphorylation-25.2628787133
18PhosphorylationGGTRGVLSGNRGVEY
CCCCCCCCCCCCCEE
31.4523312004
18 (in isoform 3)Phosphorylation-31.4528787133
29DimethylationGVEYGSGRGHLGTFE
CCEECCCCCCCCCCC
30.93-
29MethylationGVEYGSGRGHLGTFE
CCEECCCCCCCCCCC
30.93-
65 (in isoform 3)Ubiquitination-4.7421890473
66PhosphorylationMAELEEVTLDGKPLQ
HEEEEEEECCCCCCE
23.5528122231
73 (in isoform 3)Ubiquitination-47.0521890473
81MalonylationALRVTDLKAALEQRG
EEEHHHHHHHHHHCC
34.1326320211
81MethylationALRVTDLKAALEQRG
EEEHHHHHHHHHHCC
34.13-
81UbiquitinationALRVTDLKAALEQRG
EEEHHHHHHHHHHCC
34.13-
87MethylationLKAALEQRGLAKSGQ
HHHHHHHCCCCCCCC
32.49-
96PhosphorylationLAKSGQKSALVKRLK
CCCCCCHHHHHHHHH
20.9622817900
96 (in isoform 2)Ubiquitination-20.9621890473
103UbiquitinationSALVKRLKGALMLEN
HHHHHHHHHHHHHHH
46.2821890473
103MethylationSALVKRLKGALMLEN
HHHHHHHHHHHHHHH
46.28-
103UbiquitinationSALVKRLKGALMLEN
HHHHHHHHHHHHHHH
46.2821890473
103 (in isoform 1)Ubiquitination-46.2821890473
103 (in isoform 3)Ubiquitination-46.2821890473
104 (in isoform 2)Ubiquitination-28.6521890473
107SulfoxidationKRLKGALMLENLQKH
HHHHHHHHHHHHHHC
4.3521406390
113TrimethylationLMLENLQKHSTPHAA
HHHHHHHHCCCCCHH
42.56-
113MethylationLMLENLQKHSTPHAA
HHHHHHHHCCCCCHH
42.56-
115PhosphorylationLENLQKHSTPHAAFQ
HHHHHHCCCCCHHCC
51.1523401153
116PhosphorylationENLQKHSTPHAAFQP
HHHHHCCCCCHHCCC
20.8625159151
125PhosphorylationHAAFQPNSQIGEEMS
CHHCCCCCHHCHHHH
29.8323401153
132PhosphorylationSQIGEEMSQNSFIKQ
CHHCHHHHCHHHHHH
29.5023401153
134 (in isoform 2)Ubiquitination-31.4221890473
135PhosphorylationGEEMSQNSFIKQYLE
CHHHHCHHHHHHHHH
22.2523401153
138UbiquitinationMSQNSFIKQYLEKQQ
HHCHHHHHHHHHHHH
30.77-
143UbiquitinationFIKQYLEKQQELLRQ
HHHHHHHHHHHHHHH
55.4721890473
143TrimethylationFIKQYLEKQQELLRQ
HHHHHHHHHHHHHHH
55.47-
143AcetylationFIKQYLEKQQELLRQ
HHHHHHHHHHHHHHH
55.4726051181
143MethylationFIKQYLEKQQELLRQ
HHHHHHHHHHHHHHH
55.47-
143UbiquitinationFIKQYLEKQQELLRQ
HHHHHHHHHHHHHHH
55.4721890473
143 (in isoform 1)Ubiquitination-55.4721890473
166PhosphorylationAAELEEASAESEDEM
HHHHHHHHCCCCCCC
35.5320164059
169PhosphorylationLEEASAESEDEMIHP
HHHHHCCCCCCCCCC
50.4920164059
176PhosphorylationSEDEMIHPEGVASLL
CCCCCCCCCHHHHHC
29.1624719451
181PhosphorylationIHPEGVASLLPPDFQ
CCCCHHHHHCCCCHH
28.2129496963
189PhosphorylationLLPPDFQSSLERPEL
HCCCCHHHHHCCCHH
36.5623909892
190PhosphorylationLPPDFQSSLERPELE
CCCCHHHHHCCCHHH
24.3823909892
199PhosphorylationERPELELSRHSPRKS
CCCHHHHHCCCCCCC
20.6923909892
202PhosphorylationELELSRHSPRKSSSI
HHHHHCCCCCCCCCC
25.8626074081
206PhosphorylationSRHSPRKSSSISEEK
HCCCCCCCCCCCCCC
30.5123927012
207PhosphorylationRHSPRKSSSISEEKG
CCCCCCCCCCCCCCC
34.4223927012
208PhosphorylationHSPRKSSSISEEKGD
CCCCCCCCCCCCCCC
36.9123927012
210PhosphorylationPRKSSSISEEKGDSD
CCCCCCCCCCCCCCC
41.4723927012
216PhosphorylationISEEKGDSDDEKPRK
CCCCCCCCCCCCCCC
56.4829255136
228PhosphorylationPRKGERRSSRVRQAR
CCCCCCHHHHHHHHH
28.8122817900
229PhosphorylationRKGERRSSRVRQARA
CCCCCHHHHHHHHHH
32.7422817900
238AcetylationVRQARAAKLSEGSQP
HHHHHHHHHCCCCCC
52.1123954790
240PhosphorylationQARAAKLSEGSQPAE
HHHHHHHCCCCCCCC
38.9229255136
243PhosphorylationAAKLSEGSQPAEEEE
HHHHCCCCCCCCHHC
29.0129255136
254PhosphorylationEEEEDQETPSRNLRV
CHHCCCCCCCHHHHH
22.4129255136
256PhosphorylationEEDQETPSRNLRVRA
HCCCCCCCHHHHHHH
41.0229255136
268AcetylationVRADRNLKTEEEEEE
HHHHHCCCCHHHHHH
58.3926051181
268SumoylationVRADRNLKTEEEEEE
HHHHHCCCCHHHHHH
58.3925114211
269PhosphorylationRADRNLKTEEEEEEE
HHHHCCCCHHHHHHH
52.3621712546
295PhosphorylationGDDEGQKSREAPILK
CCCHHHHHHCCHHHH
27.7125159151
302UbiquitinationSREAPILKEFKEEGE
HHCCHHHHHHHHCCC
62.9221890473
302UbiquitinationSREAPILKEFKEEGE
HHCCHHHHHHHHCCC
62.9221890473
302 (in isoform 1)Ubiquitination-62.9221890473
305SumoylationAPILKEFKEEGEEIP
CHHHHHHHHCCCCCC
56.8228112733
315SumoylationGEEIPRVKPEEMMDE
CCCCCCCCHHHHCCC
48.25-
315AcetylationGEEIPRVKPEEMMDE
CCCCCCCCHHHHCCC
48.2526051181
315SumoylationGEEIPRVKPEEMMDE
CCCCCCCCHHHHCCC
48.2528112733
326PhosphorylationMMDERPKTRSQEQEV
HCCCCCCCHHHHHHH
37.9325159151
328PhosphorylationDERPKTRSQEQEVLE
CCCCCCHHHHHHHHH
43.2122167270
336MethylationQEQEVLERGGRFTRS
HHHHHHHHCCCCCCC
49.02-
341PhosphorylationLERGGRFTRSQEEAR
HHHCCCCCCCHHHHH
28.2226853621
343PhosphorylationRGGRFTRSQEEARKS
HCCCCCCCHHHHHHH
38.6023403867
350PhosphorylationSQEEARKSHLARQQQ
CHHHHHHHHHHHHHH
20.4129214152
359AcetylationLARQQQEKEMKTTSP
HHHHHHHHHHCCCCC
59.7923749302
363PhosphorylationQQEKEMKTTSPLEEE
HHHHHHCCCCCHHHH
31.0623401153
364PhosphorylationQEKEMKTTSPLEEEE
HHHHHCCCCCHHHHH
23.8729255136
365PhosphorylationEKEMKTTSPLEEEER
HHHHCCCCCHHHHHH
32.4919664994
375SumoylationEEEEREIKSSQGLKE
HHHHHHHHHHHCHHH
39.0228112733
376PhosphorylationEEEREIKSSQGLKEK
HHHHHHHHHHCHHHH
33.2923898821
377PhosphorylationEEREIKSSQGLKEKS
HHHHHHHHHCHHHHC
24.2223403867
384PhosphorylationSQGLKEKSKSPSPPR
HHCHHHHCCCCCCCC
39.1823927012
386PhosphorylationGLKEKSKSPSPPRLT
CHHHHCCCCCCCCCC
37.3923927012
388PhosphorylationKEKSKSPSPPRLTED
HHHCCCCCCCCCCCH
55.4123927012
393PhosphorylationSPSPPRLTEDRKKAS
CCCCCCCCCHHHHHE
36.8025159151
400PhosphorylationTEDRKKASLVALPEQ
CCHHHHHEEEECCCC
32.0529255136
408PhosphorylationLVALPEQTASEEETP
EEECCCCCCCCCCCC
30.4129255136
410PhosphorylationALPEQTASEEETPPP
ECCCCCCCCCCCCCC
49.2629255136
414PhosphorylationQTASEEETPPPLLTK
CCCCCCCCCCCCCCC
44.3629255136
420PhosphorylationETPPPLLTKEASSPP
CCCCCCCCCCCCCCC
34.2229255136
424PhosphorylationPLLTKEASSPPPHPQ
CCCCCCCCCCCCCCC
44.4622496350
425PhosphorylationLLTKEASSPPPHPQL
CCCCCCCCCCCCCCC
48.7717287340
434PhosphorylationPPHPQLHSEEEIEPM
CCCCCCCCHHHCCCC
56.1218669648
453PhosphorylationPAVLIQLSPPNTDAD
CEEEEECCCCCCCCC
23.1820363803
453 (in isoform 2)Phosphorylation-23.18-
457PhosphorylationIQLSPPNTDADTREL
EECCCCCCCCCHHHH
38.0426074081
461PhosphorylationPPNTDADTRELLVSQ
CCCCCCCHHHHHHHH
27.9735585803
467PhosphorylationDTRELLVSQHTVQLV
CHHHHHHHHHHHHCC
19.0623927012
470PhosphorylationELLVSQHTVQLVGGL
HHHHHHHHHHCCCCC
11.4330278072
478PhosphorylationVQLVGGLSPLSSPSD
HHCCCCCCCCCCCCC
27.3729255136
481PhosphorylationVGGLSPLSSPSDTKA
CCCCCCCCCCCCCCC
43.5223927012
482PhosphorylationGGLSPLSSPSDTKAE
CCCCCCCCCCCCCCC
35.7923927012
484PhosphorylationLSPLSSPSDTKAESP
CCCCCCCCCCCCCCC
60.9230266825
486PhosphorylationPLSSPSDTKAESPAE
CCCCCCCCCCCCCCH
36.1730266825
490PhosphorylationPSDTKAESPAEKVPE
CCCCCCCCCCHHCCH
33.9829255136
499PhosphorylationAEKVPEESVLPLVQK
CHHCCHHHHHHHHHH
27.5630278072
506UbiquitinationSVLPLVQKSTLADYS
HHHHHHHHHHHHCHH
37.62-
507PhosphorylationVLPLVQKSTLADYSA
HHHHHHHHHHHCHHC
16.1526074081
508PhosphorylationLPLVQKSTLADYSAQ
HHHHHHHHHHCHHCC
32.7626074081
512PhosphorylationQKSTLADYSAQKDLE
HHHHHHCHHCCCCCC
10.5718669648
513PhosphorylationKSTLADYSAQKDLEP
HHHHHCHHCCCCCCC
25.4425159151
516AcetylationLADYSAQKDLEPESD
HHCHHCCCCCCCCCC
65.0925953088
516UbiquitinationLADYSAQKDLEPESD
HHCHHCCCCCCCCCC
65.09-
522PhosphorylationQKDLEPESDRSAQPL
CCCCCCCCCCCCCCC
49.3830576142
524MethylationDLEPESDRSAQPLPL
CCCCCCCCCCCCCCC
43.07-
525PhosphorylationLEPESDRSAQPLPLK
CCCCCCCCCCCCCCC
35.9263708635
532SumoylationSAQPLPLKIEELALA
CCCCCCCCHHHHHHH
46.24-
532AcetylationSAQPLPLKIEELALA
CCCCCCCCHHHHHHH
46.2425953088
532SumoylationSAQPLPLKIEELALA
CCCCCCCCHHHHHHH
46.2428112733
540AcetylationIEELALAKGITEECL
HHHHHHHCCCCHHHH
52.2626051181
540UbiquitinationIEELALAKGITEECL
HHHHHHHCCCCHHHH
52.26-
546GlutathionylationAKGITEECLKQPSLE
HCCCCHHHHHCCCCC
4.7222555962
548AcetylationGITEECLKQPSLEQK
CCCHHHHHCCCCCCC
72.3526051181
548UbiquitinationGITEECLKQPSLEQK
CCCHHHHHCCCCCCC
72.35-
551PhosphorylationEECLKQPSLEQKEGR
HHHHHCCCCCCCCCC
41.8823401153
555AcetylationKQPSLEQKEGRRASH
HCCCCCCCCCCCCHH
53.4026051181
561PhosphorylationQKEGRRASHTLLPSH
CCCCCCCHHCCCCHH
18.3929255136
563PhosphorylationEGRRASHTLLPSHRL
CCCCCHHCCCCHHHH
27.7425463755
567PhosphorylationASHTLLPSHRLKQSA
CHHCCCCHHHHHCCC
22.6224732914
581PhosphorylationADSSSSRSSSSSSSS
CCCCCCCCCCCCCCC
36.2026552605
582PhosphorylationDSSSSRSSSSSSSSS
CCCCCCCCCCCCCCC
32.8826552605
583PhosphorylationSSSSRSSSSSSSSSR
CCCCCCCCCCCCCCC
35.1726552605
584PhosphorylationSSSRSSSSSSSSSRS
CCCCCCCCCCCCCCC
35.8730576142
585PhosphorylationSSRSSSSSSSSSRSR
CCCCCCCCCCCCCCC
35.8726552605
586PhosphorylationSRSSSSSSSSSRSRS
CCCCCCCCCCCCCCC
35.8730576142
587PhosphorylationRSSSSSSSSSRSRSR
CCCCCCCCCCCCCCC
33.9924260401
588PhosphorylationSSSSSSSSSRSRSRS
CCCCCCCCCCCCCCC
31.5530576142
589PhosphorylationSSSSSSSSRSRSRSP
CCCCCCCCCCCCCCC
35.9030576142
593PhosphorylationSSSSRSRSRSPDSSG
CCCCCCCCCCCCCCC
38.0521406692
595PhosphorylationSSRSRSRSPDSSGSR
CCCCCCCCCCCCCCC
34.0130242111
598PhosphorylationSRSRSPDSSGSRSHS
CCCCCCCCCCCCCCC
39.7320363803
599PhosphorylationRSRSPDSSGSRSHSP
CCCCCCCCCCCCCCC
48.4420363803
601PhosphorylationRSPDSSGSRSHSPLR
CCCCCCCCCCCCCCH
32.3420363803
603PhosphorylationPDSSGSRSHSPLRSK
CCCCCCCCCCCCHHH
29.9820363803
604 (in isoform 2)Phosphorylation-32.12-
605PhosphorylationSSGSRSHSPLRSKQR
CCCCCCCCCCHHHHH
27.2023927012
609PhosphorylationRSHSPLRSKQRDVAQ
CCCCCCHHHHHHHHH
40.6021406692
631PhosphorylationRGRPKMGSRSTSESR
CCCCCCCCCCCCHHH
21.4020860994
633PhosphorylationRPKMGSRSTSESRSR
CCCCCCCCCCHHHHH
37.6728102081
634PhosphorylationPKMGSRSTSESRSRS
CCCCCCCCCHHHHHH
35.0920860994
635PhosphorylationKMGSRSTSESRSRSR
CCCCCCCCHHHHHHH
34.5268721451
637PhosphorylationGSRSTSESRSRSRSR
CCCCCCHHHHHHHHH
35.0168721453
643PhosphorylationESRSRSRSRSRSASS
HHHHHHHHHCCCCCC
35.5423312004
645PhosphorylationRSRSRSRSRSASSNS
HHHHHHHCCCCCCCC
31.6523312004
647PhosphorylationRSRSRSRSASSNSRK
HHHHHCCCCCCCCCC
33.4823663014
649PhosphorylationRSRSRSASSNSRKSL
HHHCCCCCCCCCCCC
31.1623663014
650PhosphorylationSRSRSASSNSRKSLS
HHCCCCCCCCCCCCC
38.2423663014
652PhosphorylationSRSASSNSRKSLSPG
CCCCCCCCCCCCCCC
42.9323663014
654"N6,N6,N6-trimethyllysine"SASSNSRKSLSPGVS
CCCCCCCCCCCCCCC
56.41-
654MethylationSASSNSRKSLSPGVS
CCCCCCCCCCCCCCC
56.4118438403
655PhosphorylationASSNSRKSLSPGVSR
CCCCCCCCCCCCCCC
32.7329255136
657O-linked_GlycosylationSNSRKSLSPGVSRDS
CCCCCCCCCCCCCCC
27.0523301498
657PhosphorylationSNSRKSLSPGVSRDS
CCCCCCCCCCCCCCC
27.0529255136
661O-linked_GlycosylationKSLSPGVSRDSSTSY
CCCCCCCCCCCCCCC
35.9623301498
661PhosphorylationKSLSPGVSRDSSTSY
CCCCCCCCCCCCCCC
35.9630266825
664PhosphorylationSPGVSRDSSTSYTET
CCCCCCCCCCCCEEC
34.1125159151
665PhosphorylationPGVSRDSSTSYTETK
CCCCCCCCCCCEECC
26.1725159151
666PhosphorylationGVSRDSSTSYTETKD
CCCCCCCCCCEECCC
29.7025159151
667PhosphorylationVSRDSSTSYTETKDP
CCCCCCCCCEECCCC
31.8225159151
668PhosphorylationSRDSSTSYTETKDPS
CCCCCCCCEECCCCC
14.5321712546
669PhosphorylationRDSSTSYTETKDPSS
CCCCCCCEECCCCCC
36.6221712546
671PhosphorylationSSTSYTETKDPSSGQ
CCCCCEECCCCCCCC
32.7128102081
672AcetylationSTSYTETKDPSSGQE
CCCCEECCCCCCCCE
62.5026051181
675PhosphorylationYTETKDPSSGQEVAT
CEECCCCCCCCEECC
58.1829255136
676PhosphorylationTETKDPSSGQEVATP
EECCCCCCCCEECCC
50.3029255136
682PhosphorylationSSGQEVATPPVPQLQ
CCCCEECCCCCCCCE
33.0529255136
697PhosphorylationVCEPKERTSTSSSSV
ECCCCCCCCCCCHHH
37.1325159151
698PhosphorylationCEPKERTSTSSSSVQ
CCCCCCCCCCCHHHH
32.2925159151
699PhosphorylationEPKERTSTSSSSVQA
CCCCCCCCCCHHHHH
31.8327794612
700PhosphorylationPKERTSTSSSSVQAR
CCCCCCCCCHHHHHH
28.1728450419
701PhosphorylationKERTSTSSSSVQARR
CCCCCCCCHHHHHHH
27.0728450419
702PhosphorylationERTSTSSSSVQARRL
CCCCCCCHHHHHHHH
34.0029978859
703PhosphorylationRTSTSSSSVQARRLS
CCCCCCHHHHHHHHC
21.8729978859
710PhosphorylationSVQARRLSQPESAEK
HHHHHHHCCCHHHHH
41.7129255136
714PhosphorylationRRLSQPESAEKHVTQ
HHHCCCHHHHHHHHH
48.7029255136
717AcetylationSQPESAEKHVTQRLQ
CCCHHHHHHHHHHCC
42.9919608861
720PhosphorylationESAEKHVTQRLQPER
HHHHHHHHHHCCCCC
14.0023927012
729PhosphorylationRLQPERGSPKKCEAE
HCCCCCCCCCCCCCC
39.5022167270
732SumoylationPERGSPKKCEAEEAE
CCCCCCCCCCCCCCC
40.4628112733
733GlutathionylationERGSPKKCEAEEAEP
CCCCCCCCCCCCCCC
8.1722555962
744PhosphorylationEAEPPAATQPQTSET
CCCCCCCCCCCCCCC
42.7724732914
748PhosphorylationPAATQPQTSETQTSH
CCCCCCCCCCCCCCC
34.9024732914
749PhosphorylationAATQPQTSETQTSHL
CCCCCCCCCCCCCCC
33.1424732914
751PhosphorylationTQPQTSETQTSHLPE
CCCCCCCCCCCCCCH
36.5924732914
753PhosphorylationPQTSETQTSHLPESE
CCCCCCCCCCCCHHH
26.0724732914
754PhosphorylationQTSETQTSHLPESER
CCCCCCCCCCCHHHH
17.1424732914
759PhosphorylationQTSHLPESERIHHTV
CCCCCCHHHHCCCCC
30.1824732914
776PhosphorylationKEEVTMDTSENRPEN
CCCEECCCCCCCCCC
27.4128555341
797PhosphorylationMPIADQVSNDDRPEG
CCHHHHCCCCCCCCC
28.9828348404
805PhosphorylationNDDRPEGSVEDEEKK
CCCCCCCCCCHHHHH
22.2228348404
814PhosphorylationEDEEKKESSLPKSFK
CHHHHHHHCCCHHHH
46.1620068231
815PhosphorylationDEEKKESSLPKSFKR
HHHHHHHCCCHHHHH
50.1917287340
815 (in isoform 5)Phosphorylation-50.1925849741
818UbiquitinationKKESSLPKSFKRKIS
HHHHCCCHHHHHCEE
74.04-
819PhosphorylationKESSLPKSFKRKISV
HHHCCCHHHHHCEEE
33.7823401153
823UbiquitinationLPKSFKRKISVVSAT
CCHHHHHCEEEEEEC
39.6721890473
823 (in isoform 1)Ubiquitination-39.6721890473
825PhosphorylationKSFKRKISVVSATKG
HHHHHCEEEEEECCC
21.3623927012
825 (in isoform 5)Phosphorylation-21.3630266825
828PhosphorylationKRKISVVSATKGVPA
HHCEEEEEECCCCCC
28.2330266825
828 (in isoform 5)Phosphorylation-28.2330266825
829 (in isoform 5)Phosphorylation-11.1723927012
830UbiquitinationKISVVSATKGVPAGN
CEEEEEECCCCCCCC
22.3321890473
830PhosphorylationKISVVSATKGVPAGN
CEEEEEECCCCCCCC
22.3330266825
831AcetylationISVVSATKGVPAGNS
EEEEEECCCCCCCCC
58.5926051181
831UbiquitinationISVVSATKGVPAGNS
EEEEEECCCCCCCCC
58.5921890473
831 (in isoform 1)Ubiquitination-58.5921890473
837PhosphorylationTKGVPAGNSDTEGGQ
CCCCCCCCCCCCCCC
38.5324719451
837 (in isoform 5)Phosphorylation-38.5325849741
838PhosphorylationKGVPAGNSDTEGGQP
CCCCCCCCCCCCCCC
45.0229255136
839 (in isoform 5)Phosphorylation-53.4229507054
840PhosphorylationVPAGNSDTEGGQPGR
CCCCCCCCCCCCCCC
36.0322167270
854PhosphorylationRKRRWGASTATTQKK
CCCCCCCCCCCCCCC
18.0323312004
855PhosphorylationKRRWGASTATTQKKP
CCCCCCCCCCCCCCC
27.7323312004
857PhosphorylationRWGASTATTQKKPSI
CCCCCCCCCCCCCCE
29.8223312004
858PhosphorylationWGASTATTQKKPSIS
CCCCCCCCCCCCCEE
35.6123312004
860UbiquitinationASTATTQKKPSISIT
CCCCCCCCCCCEEEE
65.6421890473
860AcetylationASTATTQKKPSISIT
CCCCCCCCCCCEEEE
65.6425953088
860UbiquitinationASTATTQKKPSISIT
CCCCCCCCCCCEEEE
65.64-
861AcetylationSTATTQKKPSISITT
CCCCCCCCCCEEEEH
33.8926051181
861SumoylationSTATTQKKPSISITT
CCCCCCCCCCEEEEH
33.8928112733
861UbiquitinationSTATTQKKPSISITT
CCCCCCCCCCEEEEH
33.8921890473
861 (in isoform 1)Ubiquitination-33.8921890473
862 (in isoform 5)Phosphorylation-43.8829116813
863PhosphorylationATTQKKPSISITTES
CCCCCCCCEEEEHHH
37.5425159151
864PhosphorylationTTQKKPSISITTESL
CCCCCCCEEEEHHHH
4.7224719451
864 (in isoform 5)Phosphorylation-4.7225627689
865PhosphorylationTQKKPSISITTESLK
CCCCCCEEEEHHHHH
20.4430266825
867PhosphorylationKKPSISITTESLKSL
CCCCEEEEHHHHHHH
20.0930266825
868PhosphorylationKPSISITTESLKSLI
CCCEEEEHHHHHHHC
23.1629691806
869 (in isoform 5)Phosphorylation-45.4825627689
870O-linked_GlycosylationSISITTESLKSLIPD
CEEEEHHHHHHHCCC
38.7223301498
870PhosphorylationSISITTESLKSLIPD
CEEEEHHHHHHHCCC
38.7220873877
873PhosphorylationITTESLKSLIPDIKP
EEHHHHHHHCCCCHH
36.5023403867
879SumoylationKSLIPDIKPLAGQEA
HHHCCCCHHHCCCEE
41.1628112733
882PhosphorylationIPDIKPLAGQEAVVD
CCCCHHHCCCEEEEE
26.5927251275
882 (in isoform 5)Phosphorylation-26.5925849741
885PhosphorylationIKPLAGQEAVVDLHA
CHHHCCCEEEEECCC
42.3824719451
885 (in isoform 5)Phosphorylation-42.3825849741
889PhosphorylationAGQEAVVDLHADDSR
CCCEEEEECCCCCCC
26.5827251275
895PhosphorylationVDLHADDSRISEDET
EECCCCCCCCCCCHH
31.8722167270
898PhosphorylationHADDSRISEDETERN
CCCCCCCCCCHHHHC
37.5729255136
902PhosphorylationSRISEDETERNGDDG
CCCCCCHHHHCCCCC
53.2030266825
910PhosphorylationERNGDDGTHDKGLKI
HHCCCCCCCCHHHHE
33.6230576142
913AcetylationGDDGTHDKGLKICRT
CCCCCCCHHHHEEEE
59.5525953088
963PhosphorylationVEVALPPPAEHEVKK
EEEECCCCCCCCCEE
48.6324719451
968PhosphorylationPPPAEHEVKKVTLGD
CCCCCCCCEEEECCC
8.6324719451
970PhosphorylationPAEHEVKKVTLGDTL
CCCCCCEEEECCCHH
45.7024719451
970SumoylationPAEHEVKKVTLGDTL
CCCCCCEEEECCCHH
45.7028112733
972PhosphorylationEHEVKKVTLGDTLTR
CCCCEEEECCCHHHH
33.6223403867
974PhosphorylationEVKKVTLGDTLTRRS
CCEEEECCCHHHHCC
19.2524719451
976PhosphorylationKKVTLGDTLTRRSIS
EEEECCCHHHHCCHH
28.3823401153
977PhosphorylationKVTLGDTLTRRSISQ
EEECCCHHHHCCHHC
4.1124719451
978PhosphorylationVTLGDTLTRRSISQQ
EECCCHHHHCCHHCC
26.5725159151
981PhosphorylationGDTLTRRSISQQKSG
CCHHHHCCHHCCCCC
24.2525159151
983PhosphorylationTLTRRSISQQKSGVS
HHHHCCHHCCCCCCE
28.0123401153
986UbiquitinationRRSISQQKSGVSITI
HCCHHCCCCCCEEEE
41.35-
987PhosphorylationRSISQQKSGVSITID
CCHHCCCCCCEEEEC
39.8430266825
990PhosphorylationSQQKSGVSITIDDPV
HCCCCCCEEEECCCC
19.9623401153
991PhosphorylationQQKSGVSITIDDPVR
CCCCCCEEEECCCCE
3.4824719451
992PhosphorylationQKSGVSITIDDPVRT
CCCCCEEEECCCCEE
15.7330183078
999PhosphorylationTIDDPVRTAQVPSPP
EECCCCEECCCCCCC
22.9823927012
1004PhosphorylationVRTAQVPSPPRGKIS
CEECCCCCCCCCCCC
48.9919664994
1009AcetylationVPSPPRGKISNIVHI
CCCCCCCCCCCEEEH
44.2125953088
1029UbiquitinationPFTLGQLKELLGRTG
CCCHHHHHHHHCCCC
38.13-
1047AcetylationEEAFWIDKIKSHCFV
HHHHHHHHHHHCEEE
42.7926051181
1047SumoylationEEAFWIDKIKSHCFV
HHHHHHHHHHHCEEE
42.7928112733
1047UbiquitinationEEAFWIDKIKSHCFV
HHHHHHHHHHHCEEE
42.79-
10492-HydroxyisobutyrylationAFWIDKIKSHCFVTY
HHHHHHHHHCEEEEE
39.63-
1049MalonylationAFWIDKIKSHCFVTY
HHHHHHHHHCEEEEE
39.6326320211
1052GlutathionylationIDKIKSHCFVTYSTV
HHHHHHCEEEEECHH
3.6622555962
1073AcetylationRTALHGVKWPQSNPK
HHHHCCCCCCCCCCC
58.7226051181
1080AcetylationKWPQSNPKFLCADYA
CCCCCCCCEEECCHH
56.0426051181
1083GlutathionylationQSNPKFLCADYAEQD
CCCCCEEECCHHHHC
2.8122555962
1094PhosphorylationAEQDELDYHRGLLVD
HHHCCCCCCCCCCCC
13.1726074081
1104PhosphorylationGLLVDRPSETKTEEQ
CCCCCCCCCCCCCCC
59.8130266825
1106PhosphorylationLVDRPSETKTEEQGI
CCCCCCCCCCCCCCC
47.8330266825
1107SumoylationVDRPSETKTEEQGIP
CCCCCCCCCCCCCCC
50.3028112733
1108PhosphorylationDRPSETKTEEQGIPR
CCCCCCCCCCCCCCC
52.7728122231
1159PhosphorylationEMERRERTRSEREWD
HHHHHHHHHHHHHHH
33.5223186163
1161PhosphorylationERRERTRSEREWDRD
HHHHHHHHHHHHHHH
40.1523401153
1176PhosphorylationKVREGPRSRSRSRDR
HHHCCCCCCHHHHHH
37.4326074081
1178PhosphorylationREGPRSRSRSRDRRR
HCCCCCCHHHHHHHH
35.5420068231
1180PhosphorylationGPRSRSRSRDRRRKE
CCCCCHHHHHHHHHH
39.5225218447
1209UbiquitinationAQEEPPAKLLDDLFR
HHHCCCHHHHHHHHH
56.192063986
1219AcetylationDDLFRKTKAAPCIYW
HHHHHHHCCCCEEEE
45.6626051181
1219PhosphorylationDDLFRKTKAAPCIYW
HHHHHHHCCCCEEEE
45.6624719451
1219UbiquitinationDDLFRKTKAAPCIYW
HHHHHHHCCCCEEEE
45.66-
1223GlutathionylationRKTKAAPCIYWLPLT
HHHCCCCEEEEEECC
2.9822555962
1225PhosphorylationTKAAPCIYWLPLTDS
HCCCCEEEEEECCHH
13.9628796482
1230PhosphorylationCIYWLPLTDSQIVQK
EEEEEECCHHHHHHH
31.5063772419
1232PhosphorylationYWLPLTDSQIVQKEA
EEEECCHHHHHHHHH
19.3046157711
1237AcetylationTDSQIVQKEAERAER
CHHHHHHHHHHHHHH
48.2526051181
1237UbiquitinationTDSQIVQKEAERAER
CHHHHHHHHHHHHHH
48.25-
1253MethylationKEREKRRKEQEEEEQ
HHHHHHHHHHHHHHH
68.71-
1284PhosphorylationREKRREHSRERDRER
HHHHHHHHHHHHHHH
30.9620068231
1314PhosphorylationERDRERGRERDRRDT
HHHHHHHHHHHHHHH
41.8324719451
1316PhosphorylationDRERGRERDRRDTKR
HHHHHHHHHHHHHHH
41.1824719451
1318PhosphorylationERGRERDRRDTKRHS
HHHHHHHHHHHHHHH
44.5924719451
1325PhosphorylationRRDTKRHSRSRSRST
HHHHHHHHHHCCCCC
35.6620068231
1327PhosphorylationDTKRHSRSRSRSTPV
HHHHHHHHCCCCCCC
37.3120068231
1329PhosphorylationKRHSRSRSRSTPVRD
HHHHHHCCCCCCCCC
31.6526055452
1331PhosphorylationHSRSRSRSTPVRDRG
HHHHCCCCCCCCCCC
38.0126055452
1332PhosphorylationSRSRSRSTPVRDRGG
HHHCCCCCCCCCCCC
25.3726055452

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
1180SPhosphorylationKinaseAKT1P31749
Uniprot
1180SPhosphorylationKinaseSRPK2P78362
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1180SPhosphorylation

18559500

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 ACINU_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RNPS1_HUMANRNPS1physical
22388736
SAP18_HUMANSAP18physical
22388736
SAP18_HUMANSAP18physical
22939629
SPF27_HUMANBCAS2physical
22939629
SMU1_HUMANSMU1physical
22939629
DHX9_HUMANDHX9physical
22939629
DHX15_HUMANDHX15physical
22939629
DDX17_HUMANDDX17physical
22939629
PRP6_HUMANPRPF6physical
22939629
SF3A1_HUMANSF3A1physical
22939629
PYM1_HUMANWIBGphysical
22939629
CGAT1_HUMANCSGALNACT1physical
22939629
SEPT7_HUMANSEPT7physical
22939629
SRP14_HUMANSRP14physical
22939629
MIRO2_HUMANRHOT2physical
22939629
BET1_HUMANBET1physical
22939629
FUT8_HUMANFUT8physical
22939629
DRS7B_HUMANDHRS7Bphysical
22939629
TR112_HUMANTRMT112physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
ATP7A_HUMANATP7Aphysical
22939629
SEPT2_HUMANSEPT2physical
22939629
AP180_HUMANSNAP91physical
22939629
ARMX3_HUMANARMCX3physical
22939629
CAV1_HUMANCAV1physical
22939629
EVPL_HUMANEVPLphysical
22939629
S10A9_HUMANS100A9physical
22939629
KPCA_HUMANPRKCAphysical
22939629
SMC1A_HUMANSMC1Aphysical
22939629
BOP1_HUMANBOP1physical
22939629
PTCD3_HUMANPTCD3physical
22939629
TR150_HUMANTHRAP3physical
22939629
LGMN_HUMANLGMNphysical
22939629
NFIA_HUMANNFIAphysical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
RCC1_HUMANRCC1physical
22939629
SAFB1_HUMANSAFBphysical
22939629
SON_HUMANSONphysical
22939629
RRS1_HUMANRRS1physical
22939629
NDUF4_HUMANNDUFAF4physical
22939629
RNPS1_HUMANRNPS1physical
22365833
SRPK2_HUMANSRPK2physical
22365833
RNPS1_HUMANRNPS1physical
26344197
RL7_HUMANRPL7physical
26344197
RS13_HUMANRPS13physical
26344197
SAFB1_HUMANSAFBphysical
26344197
SAP18_HUMANSAP18physical
26344197
4F2_HUMANSLC3A2physical
26344197
SRRM2_HUMANSRRM2physical
26344197
SSRP1_HUMANSSRP1physical
26344197
TCP4_HUMANSUB1physical
26344197
ZCH18_HUMANZC3H18physical
26344197

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 ACINU_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-717, AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"Protein lysine methyltransferase G9a acts on non-histone targets.";
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
Nat. Chem. Biol. 4:344-346(2008).
Cited for: METHYLATION AT LYS-654, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243; THR-254;THR-269; SER-328; SER-365; SER-400; THR-408; SER-410; THR-414;SER-478; SER-490; SER-838; SER-987; SER-990 AND SER-1004, 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 THR-254; THR-408; SER-410;THR-414; SER-655; SER-657; SER-664; SER-675; SER-676; THR-682;SER-825; SER-838; THR-840 AND SER-1004, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"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 SER-166; SER-169; SER-216;SER-240; SER-243; THR-254; THR-269; SER-295; SER-328; SER-365;SER-384; SER-386; SER-388; THR-393; SER-410; THR-414; SER-425;SER-434; SER-453; SER-490; TYR-512; SER-561; SER-655; SER-657;THR-682; SER-710; SER-714; THR-720; SER-838 AND SER-1004, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, AND MASSSPECTROMETRY.
"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-424; SER-425; SER-434;SER-453; SER-895; SER-898 AND SER-1004, AND MASS SPECTROMETRY.
"Serine/arginine protein-specific kinase 2 promotes leukemia cellproliferation by phosphorylating acinus and regulating cyclin A1.";
Jang S.W., Yang S.J., Ehlen A., Dong S., Khoury H., Chen J.,Persson J.L., Ye K.;
Cancer Res. 68:4559-4570(2008).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-1180 BY SRPK2, INTERACTION WITHSRPK2, AND SUBCELLULAR LOCATION.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-365; SER-657AND SER-661, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-216; SER-228;SER-229; THR-254; SER-256; SER-384; SER-386; SER-388; SER-425;SER-561; SER-710; SER-729; SER-814; SER-815; THR-830; SER-838;THR-976; THR-978; SER-981; SER-983; SER-1176; SER-1178 AND SER-1180,AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710; SER-714; SER-729AND SER-1004, AND MASS SPECTROMETRY.
"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 THR-254; THR-682 ANDSER-1004, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-240; SER-243;SER-328; SER-365; SER-384; SER-386; THR-393; THR-408; SER-410;SER-490; SER-655; SER-657; SER-710; SER-729; SER-1004; SER-1176;SER-1178 AND SER-1284, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-388 ANDSER-710, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243; SER-365;SER-386; SER-388; THR-414; SER-657; SER-661; SER-676; THR-682 ANDSER-1004, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-5, AND MASS SPECTROMETRY.

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