UN45A_HUMAN - dbPTM
UN45A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UN45A_HUMAN
UniProt AC Q9H3U1
Protein Name Protein unc-45 homolog A
Gene Name UNC45A
Organism Homo sapiens (Human).
Sequence Length 944
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Nucleus . Predominant in the perinuclear region. Little protein in the nucleus.
Protein Description Acts as co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity)..
Protein Sequence MTVSGPGTPEPRPATPGASSVEQLRKEGNELFKCGDYGGALAAYTQALGLDATPQDQAVLHRNRAACHLKLEDYDKAETEASKAIEKDGGDVKALYRRSQALEKLGRLDQAVLDLQRCVSLEPKNKVFQEALRNIGGQIQEKVRYMSSTDAKVEQMFQILLDPEEKGTEKKQKASQNLVVLAREDAGAEKIFRSNGVQLLQRLLDMGETDLMLAALRTLVGICSEHQSRTVATLSILGTRRVVSILGVESQAVSLAACHLLQVMFDALKEGVKKGFRGKEGAIIVDPARELKVLISNLLDLLTEVGVSGQGRDNALTLLIKAVPRKSLKDPNNSLTLWVIDQGLKKILEVGGSLQDPPGELAVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIKSWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESVIALCASEQEEEQLVAVEALIHAAGKAKRASFITANGVSLLKDLYKCSEKDSIRIRALVGLCKLGSAGGTDFSMKQFAEGSTLKLAKQCRKWLCNDQIDAGTRRWAVEGLAYLTFDADVKEEFVEDAAALKALFQLSRLEERSVLFAVASALVNCTNSYDYEEPDPKMVELAKYAKQHVPEQHPKDKPSFVRARVKKLLAAGVVSAMVCMVKTESPVLTSSCRELLSRVFLALVEEVEDRGTVVAQGGGRALIPLALEGTDVGQTKAAQALAKLTITSNPEMTFPGERIYEVVRPLVSLLHLNCSGLQNFEALMALTNLAGISERLRQKILKEKAVPMIEGYMFEEHEMIRRAATECMCNLAMSKEVQDLFEAQGNDRLKLLVLYSGEDDELLQRAAAGGLAMLTSMRPTLCSRIPQVTTHWLEILQALLLSSNQELQHRGAVVVLNMVEASREIASTLMESEMMEILSVLAKGDHSPVTRAAAACLDKAVEYGLIQPNQDGE
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
2Phosphorylation------MTVSGPGTP
------CCCCCCCCC
24.3127273156
2 (in isoform 2)Phosphorylation-24.3121406692
4Phosphorylation----MTVSGPGTPEP
----CCCCCCCCCCC
30.0627273156
4 (in isoform 2)Phosphorylation-30.0621406692
5 (in isoform 2)Phosphorylation-21.9625159151
8PhosphorylationMTVSGPGTPEPRPAT
CCCCCCCCCCCCCCC
27.8423401153
15O-linked_GlycosylationTPEPRPATPGASSVE
CCCCCCCCCCCCCHH
25.5730379171
15PhosphorylationTPEPRPATPGASSVE
CCCCCCCCCCCCCHH
25.5719664994
18UbiquitinationPRPATPGASSVEQLR
CCCCCCCCCCHHHHH
10.3929967540
19PhosphorylationRPATPGASSVEQLRK
CCCCCCCCCHHHHHH
40.6130266825
20PhosphorylationPATPGASSVEQLRKE
CCCCCCCCHHHHHHH
29.1927273156
21UbiquitinationATPGASSVEQLRKEG
CCCCCCCHHHHHHHC
5.1429967540
26UbiquitinationSSVEQLRKEGNELFK
CCHHHHHHHCCCCEE
77.79-
28UbiquitinationVEQLRKEGNELFKCG
HHHHHHHCCCCEECC
35.6327667366
33AcetylationKEGNELFKCGDYGGA
HHCCCCEECCCHHHH
50.3526051181
33UbiquitinationKEGNELFKCGDYGGA
HHCCCCEECCCHHHH
50.3529967540
45UbiquitinationGGALAAYTQALGLDA
HHHHHHHHHHHCCCC
11.5721890473
53PhosphorylationQALGLDATPQDQAVL
HHHCCCCCHHHHHHH
22.5825159151
55AcetylationLGLDATPQDQAVLHR
HCCCCCHHHHHHHHH
51.6019608861
55UbiquitinationLGLDATPQDQAVLHR
HCCCCCHHHHHHHHH
51.6029967540
55 (in isoform 2)Malonylation-51.6026320211
70AcetylationNRAACHLKLEDYDKA
CCEEHHCCCCHHHHH
26.6019608861
70MalonylationNRAACHLKLEDYDKA
CCEEHHCCCCHHHHH
26.6026320211
70UbiquitinationNRAACHLKLEDYDKA
CCEEHHCCCCHHHHH
26.6019608861
74PhosphorylationCHLKLEDYDKAETEA
HHCCCCHHHHHHHHH
15.2327642862
76AcetylationLKLEDYDKAETEASK
CCCCHHHHHHHHHHH
41.7226051181
78UbiquitinationLEDYDKAETEASKAI
CCHHHHHHHHHHHHH
53.5832015554
78 (in isoform 2)Malonylation-53.5826320211
83AcetylationKAETEASKAIEKDGG
HHHHHHHHHHHHCCC
61.5027452117
87AcetylationEASKAIEKDGGDVKA
HHHHHHHHCCCCHHH
56.4023749302
89UbiquitinationSKAIEKDGGDVKALY
HHHHHHCCCCHHHHH
45.3129967540
93MalonylationEKDGGDVKALYRRSQ
HHCCCCHHHHHHHHH
37.1026320211
93UbiquitinationEKDGGDVKALYRRSQ
HHCCCCHHHHHHHHH
37.1032015554
104UbiquitinationRRSQALEKLGRLDQA
HHHHHHHHHCCHHHH
58.0329967540
109UbiquitinationLEKLGRLDQAVLDLQ
HHHHCCHHHHHHHHH
32.7923000965
111UbiquitinationKLGRLDQAVLDLQRC
HHCCHHHHHHHHHHH
11.9623000965
111 (in isoform 2)Malonylation-11.9626320211
120PhosphorylationLDLQRCVSLEPKNKV
HHHHHHHCCCCCCHH
30.5528060719
124UbiquitinationRCVSLEPKNKVFQEA
HHHCCCCCCHHHHHH
61.0923000965
126MalonylationVSLEPKNKVFQEALR
HCCCCCCHHHHHHHH
51.0226320211
126UbiquitinationVSLEPKNKVFQEALR
HCCCCCCHHHHHHHH
51.0223000965
127UbiquitinationSLEPKNKVFQEALRN
CCCCCCHHHHHHHHH
9.2932015554
133MethylationKVFQEALRNIGGQIQ
HHHHHHHHHCCHHHH
39.50115919537
134UbiquitinationVFQEALRNIGGQIQE
HHHHHHHHCCHHHHH
37.8032015554
1422-HydroxyisobutyrylationIGGQIQEKVRYMSST
CCHHHHHHHHHHCCC
18.68-
142UbiquitinationIGGQIQEKVRYMSST
CCHHHHHHHHHHCCC
18.6832015554
145PhosphorylationQIQEKVRYMSSTDAK
HHHHHHHHHCCCCHH
12.3427259358
147PhosphorylationQEKVRYMSSTDAKVE
HHHHHHHCCCCHHHH
22.5827259358
148PhosphorylationEKVRYMSSTDAKVEQ
HHHHHHCCCCHHHHH
17.4927259358
149PhosphorylationKVRYMSSTDAKVEQM
HHHHHCCCCHHHHHH
32.4427259358
151UbiquitinationRYMSSTDAKVEQMFQ
HHHCCCCHHHHHHHH
20.2029967540
158UbiquitinationAKVEQMFQILLDPEE
HHHHHHHHHHHCHHH
21.7827667366
166UbiquitinationILLDPEEKGTEKKQK
HHHCHHHCCCHHHHH
70.2629967540
170UbiquitinationPEEKGTEKKQKASQN
HHHCCCHHHHHHHCC
61.41-
171UbiquitinationEEKGTEKKQKASQNL
HHCCCHHHHHHHCCE
51.29-
173AcetylationKGTEKKQKASQNLVV
CCCHHHHHHHCCEEE
59.917408287
173UbiquitinationKGTEKKQKASQNLVV
CCCHHHHHHHCCEEE
59.9127667366
175UbiquitinationTEKKQKASQNLVVLA
CHHHHHHHCCEEEEE
27.0021890473
175UbiquitinationTEKKQKASQNLVVLA
CHHHHHHHCCEEEEE
27.0021890473
175 (in isoform 2)Ubiquitination-27.0021890473
176UbiquitinationEKKQKASQNLVVLAR
HHHHHHHCCEEEEEE
52.7333845483
181UbiquitinationASQNLVVLAREDAGA
HHCCEEEEEECCCCH
2.6423503661
184UbiquitinationNLVVLAREDAGAEKI
CEEEEEECCCCHHHH
46.7521890473
190UbiquitinationREDAGAEKIFRSNGV
ECCCCHHHHHHCCHH
46.7627667366
190 (in isoform 1)Ubiquitination-46.7621890473
194PhosphorylationGAEKIFRSNGVQLLQ
CHHHHHHCCHHHHHH
27.4720068231
218PhosphorylationLMLAALRTLVGICSE
HHHHHHHHHHHHHCH
27.01-
224PhosphorylationRTLVGICSEHQSRTV
HHHHHHHCHHCCCCE
35.87-
232UbiquitinationEHQSRTVATLSILGT
HHCCCCEEEHHHCCC
11.3833845483
233PhosphorylationHQSRTVATLSILGTR
HCCCCEEEHHHCCCC
19.3922985185
235PhosphorylationSRTVATLSILGTRRV
CCCEEEHHHCCCCHH
16.0622985185
238UbiquitinationVATLSILGTRRVVSI
EEEHHHCCCCHHHEC
18.5929967540
239PhosphorylationATLSILGTRRVVSIL
EEHHHCCCCHHHECC
16.3222985185
264UbiquitinationACHLLQVMFDALKEG
HHHHHHHHHHHHHHH
1.3032015554
264 (in isoform 2)Malonylation-1.3026320211
266UbiquitinationHLLQVMFDALKEGVK
HHHHHHHHHHHHHHH
32.6621890473
269UbiquitinationQVMFDALKEGVKKGF
HHHHHHHHHHHHHCC
54.8921890473
274UbiquitinationALKEGVKKGFRGKEG
HHHHHHHHCCCCCCC
61.96-
279MalonylationVKKGFRGKEGAIIVD
HHHCCCCCCCEEEEC
49.0326320211
279UbiquitinationVKKGFRGKEGAIIVD
HHHCCCCCCCEEEEC
49.0333845483
306UbiquitinationLDLLTEVGVSGQGRD
HHHHHHHCCCCCCHH
11.1433845483
306 (in isoform 2)Ubiquitination-11.1421890473
311UbiquitinationEVGVSGQGRDNALTL
HHCCCCCCHHHHHHH
42.2923503661
314UbiquitinationVSGQGRDNALTLLIK
CCCCCHHHHHHHHHH
35.1721890473
314UbiquitinationVSGQGRDNALTLLIK
CCCCCHHHHHHHHHH
35.1721890473
314 (in isoform 2)Ubiquitination-35.1721890473
317PhosphorylationQGRDNALTLLIKAVP
CCHHHHHHHHHHHCC
19.6720873877
321AcetylationNALTLLIKAVPRKSL
HHHHHHHHHCCHHHC
43.2123236377
321UbiquitinationNALTLLIKAVPRKSL
HHHHHHHHHCCHHHC
43.2121906983
321 (in isoform 1)Ubiquitination-43.2121890473
326UbiquitinationLIKAVPRKSLKDPNN
HHHHCCHHHCCCCCC
54.8123503661
327PhosphorylationIKAVPRKSLKDPNNS
HHHCCHHHCCCCCCC
41.7620873877
329UbiquitinationAVPRKSLKDPNNSLT
HCCHHHCCCCCCCEE
77.5421890473
329 (in isoform 1)Ubiquitination-77.5421890473
334PhosphorylationSLKDPNNSLTLWVID
HCCCCCCCEEEEEEC
29.3920873877
336PhosphorylationKDPNNSLTLWVIDQG
CCCCCCEEEEEECHH
20.5620873877
338UbiquitinationPNNSLTLWVIDQGLK
CCCCEEEEEECHHHH
4.6421890473
345AcetylationWVIDQGLKKILEVGG
EEECHHHHHHHHCCC
44.5924471315
362UbiquitinationQDPPGELAVTANSRM
CCCCCCEEEECCCHH
7.7233845483
368UbiquitinationLAVTANSRMSASILL
EEEECCCHHHHHHHH
23.9229967540
370PhosphorylationVTANSRMSASILLSK
EECCCHHHHHHHHHH
20.1121406692
371UbiquitinationTANSRMSASILLSKL
ECCCHHHHHHHHHHH
7.4032015554
372PhosphorylationANSRMSASILLSKLF
CCCHHHHHHHHHHHH
13.3821406692
376PhosphorylationMSASILLSKLFDDLK
HHHHHHHHHHHHHHC
24.7021406692
377UbiquitinationSASILLSKLFDDLKC
HHHHHHHHHHHHHCC
53.8233845483
380UbiquitinationILLSKLFDDLKCDAE
HHHHHHHHHHCCHHH
71.4232015554
383AcetylationSKLFDDLKCDAEREN
HHHHHHHCCHHHHHH
36.7425953088
383UbiquitinationSKLFDDLKCDAEREN
HHHHHHHCCHHHHHH
36.7429967540
396UbiquitinationENFHRLCENYIKSWF
HHHHHHHHHHHHHHH
58.6321890473
396UbiquitinationENFHRLCENYIKSWF
HHHHHHHHHHHHHHH
58.6321890473
396 (in isoform 2)Ubiquitination-58.6321890473
401PhosphorylationLCENYIKSWFEGQGL
HHHHHHHHHHCCCCH
27.69-
4112-HydroxyisobutyrylationEGQGLAGKLRAIQTV
CCCCHHHHHHHHHHH
29.23-
411UbiquitinationEGQGLAGKLRAIQTV
CCCCHHHHHHHHHHH
29.2321890473
411 (in isoform 1)Ubiquitination-29.2321890473
468UbiquitinationLIHAAGKAKRASFIT
HHHHHHHHHHHHEEE
12.9721890473
468AcetylationLIHAAGKAKRASFIT
HHHHHHHHHHHHEEE
12.9719608861
468UbiquitinationLIHAAGKAKRASFIT
HHHHHHHHHHHHEEE
12.9721890473
468 (in isoform 2)Ubiquitination-12.9721890473
469UbiquitinationIHAAGKAKRASFITA
HHHHHHHHHHHEEEE
52.5729967540
472PhosphorylationAGKAKRASFITANGV
HHHHHHHHEEEECHH
22.6323403867
472UbiquitinationAGKAKRASFITANGV
HHHHHHHHEEEECHH
22.6329967540
475PhosphorylationAKRASFITANGVSLL
HHHHHEEEECHHHHH
16.4423403867
480PhosphorylationFITANGVSLLKDLYK
EEEECHHHHHHHHHH
29.4023403867
481UbiquitinationITANGVSLLKDLYKC
EEECHHHHHHHHHHC
6.8229967540
483AcetylationANGVSLLKDLYKCSE
ECHHHHHHHHHHCCH
51.4819608861
483UbiquitinationANGVSLLKDLYKCSE
ECHHHHHHHHHHCCH
51.4821890473
483 (in isoform 1)Ubiquitination-51.4821890473
486PhosphorylationVSLLKDLYKCSEKDS
HHHHHHHHHCCHHHH
21.7820860994
487AcetylationSLLKDLYKCSEKDSI
HHHHHHHHCCHHHHH
38.2825953088
487UbiquitinationSLLKDLYKCSEKDSI
HHHHHHHHCCHHHHH
38.28-
492UbiquitinationLYKCSEKDSIRIRAL
HHHCCHHHHHHHHHH
45.2924816145
493PhosphorylationYKCSEKDSIRIRALV
HHCCHHHHHHHHHHH
25.4929142712
501UbiquitinationIRIRALVGLCKLGSA
HHHHHHHHHHHHCCC
26.6332015554
507PhosphorylationVGLCKLGSAGGTDFS
HHHHHHCCCCCCCCC
33.8925159151
510UbiquitinationCKLGSAGGTDFSMKQ
HHHCCCCCCCCCHHH
23.1032015554
514PhosphorylationSAGGTDFSMKQFAEG
CCCCCCCCHHHHHCC
28.0724719451
515SulfoxidationAGGTDFSMKQFAEGS
CCCCCCCHHHHHCCH
3.9021406390
516UbiquitinationGGTDFSMKQFAEGST
CCCCCCHHHHHCCHH
40.8632015554
517 (in isoform 2)Malonylation-33.8526320211
523PhosphorylationKQFAEGSTLKLAKQC
HHHHCCHHHHHHHHH
38.4829496963
525AcetylationFAEGSTLKLAKQCRK
HHCCHHHHHHHHHHH
46.6225953088
525UbiquitinationFAEGSTLKLAKQCRK
HHCCHHHHHHHHHHH
46.6232015554
532MalonylationKLAKQCRKWLCNDQI
HHHHHHHHHHHCCCC
52.7426320211
553PhosphorylationWAVEGLAYLTFDADV
HHEEEEEEEEECCCC
16.0021949786
555PhosphorylationVEGLAYLTFDADVKE
EEEEEEEEECCCCCH
13.5421949786
562UbiquitinationTFDADVKEEFVEDAA
EECCCCCHHHHHHHH
57.4233845483
599UbiquitinationALVNCTNSYDYEEPD
HHHCCCCCCCCCCCC
10.9629967540
602UbiquitinationNCTNSYDYEEPDPKM
CCCCCCCCCCCCHHH
17.6029967540
611UbiquitinationEPDPKMVELAKYAKQ
CCCHHHHHHHHHHHH
39.2429967540
613UbiquitinationDPKMVELAKYAKQHV
CHHHHHHHHHHHHHC
6.8429967540
614UbiquitinationPKMVELAKYAKQHVP
HHHHHHHHHHHHHCC
59.3629967540
617UbiquitinationVELAKYAKQHVPEQH
HHHHHHHHHHCCCCC
37.5429967540
626UbiquitinationHVPEQHPKDKPSFVR
HCCCCCCCCCCHHHH
76.0229967540
628UbiquitinationPEQHPKDKPSFVRAR
CCCCCCCCCHHHHHH
49.0029967540
668PhosphorylationSSCRELLSRVFLALV
HHHHHHHHHHHHHHH
38.7424719451
692UbiquitinationVAQGGGRALIPLALE
EEECCCCEEEEEEEC
17.0821890473
692UbiquitinationVAQGGGRALIPLALE
EEECCCCEEEEEEEC
17.0833845483
692 (in isoform 2)Ubiquitination-17.0821890473
701PhosphorylationIPLALEGTDVGQTKA
EEEEECCCCCCHHHH
20.3820068231
706PhosphorylationEGTDVGQTKAAQALA
CCCCCCHHHHHHHHH
19.4020068231
707UbiquitinationGTDVGQTKAAQALAK
CCCCCHHHHHHHHHH
33.5633845483
707 (in isoform 1)Ubiquitination-33.5621890473
714UbiquitinationKAAQALAKLTITSNP
HHHHHHHHCCCCCCC
47.19-
718PhosphorylationALAKLTITSNPEMTF
HHHHCCCCCCCCCCC
19.74-
723SulfoxidationTITSNPEMTFPGERI
CCCCCCCCCCCCHHH
5.0221406390
724PhosphorylationITSNPEMTFPGERIY
CCCCCCCCCCCHHHH
25.6422210691
731PhosphorylationTFPGERIYEVVRPLV
CCCCHHHHHHHHHHH
14.6427273156
783PhosphorylationAVPMIEGYMFEEHEM
CCCCCCCCCHHHHHH
5.95-
785UbiquitinationPMIEGYMFEEHEMIR
CCCCCCCHHHHHHHH
8.2024816145
806UbiquitinationMCNLAMSKEVQDLFE
HHHHHHCHHHHHHHH
49.14-
826PhosphorylationRLKLLVLYSGEDDEL
CEEEEEEECCCCHHH
13.7225348772
827PhosphorylationLKLLVLYSGEDDELL
EEEEEEECCCCHHHH
31.3925348772
846PhosphorylationAGGLAMLTSMRPTLC
HCHHHHHHHCCCCHH
13.8528270605
847PhosphorylationGGLAMLTSMRPTLCS
CHHHHHHHCCCCHHH
14.6128270605
851PhosphorylationMLTSMRPTLCSRIPQ
HHHHCCCCHHHCCCH
29.9928270605
854PhosphorylationSMRPTLCSRIPQVTT
HCCCCHHHCCCHHHH
36.0428270605
893PhosphorylationVLNMVEASREIASTL
EECHHHHHHHHHHHH
19.5520068231
898PhosphorylationEASREIASTLMESEM
HHHHHHHHHHHHHHH
27.9526356563
899PhosphorylationASREIASTLMESEMM
HHHHHHHHHHHHHHH
22.5426356563
903PhosphorylationIASTLMESEMMEILS
HHHHHHHHHHHHHHH
19.4826356563
915UbiquitinationILSVLAKGDHSPVTR
HHHHHHCCCCCHHHH
32.0524816145
918PhosphorylationVLAKGDHSPVTRAAA
HHHCCCCCHHHHHHH
26.3026091039
930AcetylationAAAACLDKAVEYGLI
HHHHHHHHHHHHCCC
41.1926051181
930UbiquitinationAAAACLDKAVEYGLI
HHHHHHHHHHHHCCC
41.1924816145
934PhosphorylationCLDKAVEYGLIQPNQ
HHHHHHHHCCCCCCC
15.6128152594

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

Oops, there are no upstream regulatory protein records of UN45A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UN45A_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 UN45A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XPO2_HUMANCSE1Lphysical
22939629
WDR5_HUMANWDR5physical
22939629
UGGG1_HUMANUGGT1physical
22863883
FA83H_HUMANFAM83Hphysical
25036637
MARHA_HUMANMARCH10physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
VATA_HUMANATP6V1Aphysical
26344197
SNAA_HUMANNAPAphysical
26344197
PPME1_HUMANPPME1physical
26344197
GDS1_HUMANRAP1GDS1physical
26344197
BRE1A_HUMANRNF20physical
26344197
HS90A_HUMANHSP90AA1physical
18285346
HS90B_HUMANHSP90AB1physical
18285346
MYO5_YEASTMYO5physical
27888470
FA83H_HUMANFAM83Hphysical
28514442
CDK17_HUMANCDK17physical
28514442
MYH14_HUMANMYH14physical
28514442
S27A2_HUMANSLC27A2physical
28514442
MYO1E_HUMANMYO1Ephysical
28514442
MYO1C_HUMANMYO1Cphysical
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 UN45A_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-70 AND LYS-483, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-4; THR-8 AND THR-15, ANDMASS 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 THR-15, AND MASSSPECTROMETRY.
"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 THR-15, AND MASSSPECTROMETRY.

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