AF9_HUMAN - dbPTM
AF9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AF9_HUMAN
UniProt AC P42568
Protein Name Protein AF-9
Gene Name MLLT3 {ECO:0000312|HGNC:HGNC:7136}
Organism Homo sapiens (Human).
Sequence Length 568
Subcellular Localization Nucleus . Chromosome . Colocalizes with acylated histone H3 (PubMed:25417107, PubMed:27105114). Colocalizes with histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114).
Protein Description Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. [PubMed: 20159561]
Protein Sequence MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKESSKKPKENKPLKEEKIVPKMAFKEPKPMSKEPKPDSNLLTITSGQDKKAPSKRPPISDSEELSAKKRKKSSSEALFKSFSSAPPLILTCSADKKQIKDKSHVKMGKVKIESETSEKKKSTLPPFDDIVDPNDSDVEENISSKSDSEQPSPASSSSSSSSSFTPSQTRQQGPLRSIMKDLHSDDNEEESDEVEDNDNDSEMERPVNRGGSRSRRVSLSDGSDSESSSASSPLHHEPPPPLLKTNNNQILEVKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITNTTFDFDLCSLDKTTVRKLQSYLETSGTS
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
10AcetylationSSCAVQVKLELGHRA
CCCEEEEEEECCCCC
21.1025953088
58PhosphorylationVVFHLHESFPRPKRV
HHHHHHHHCCCCCCC
29.78-
71PhosphorylationRVCKDPPYKVEESGY
CCCCCCCCCCCCCCC
32.8126074081
76PhosphorylationPPYKVEESGYAGFIL
CCCCCCCCCCCEEEE
24.4926074081
78PhosphorylationYKVEESGYAGFILPI
CCCCCCCCCEEEEEE
16.9026074081
88PhosphorylationFILPIEVYFKNKEEP
EEEEEEEEECCCCCC
8.9526074081
123PhosphorylationHLRCEKLTFNNPTED
CEEEEECCCCCCCHH
35.0722817900
151PhosphorylationRSIHTSSSSSSSSSS
CCCCCCCCCCCCCCC
33.72-
152PhosphorylationSIHTSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
153PhosphorylationIHTSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
154PhosphorylationHTSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
155PhosphorylationTSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
156PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
157PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
158PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
159PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
160PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
161PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
162PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
163PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
164PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
165PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
166PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
167PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
168PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
169PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
170PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
171PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
172PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
173PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
174PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
175PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
176PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
177PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
178PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
179PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
180PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8719664994
181PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
182PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
183PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
184PhosphorylationSSSSSSSSSSSSSST
CCCCCCCCCCCCCCC
35.87-
192PhosphorylationSSSSSSTSFSKPHKL
CCCCCCCCCCCHHHH
29.4824719451
211O-linked_GlycosylationKEKPSKDSREHKSAF
HCCCCCCHHHHHHHH
43.2230379171
219AcetylationREHKSAFKEPSRDHN
HHHHHHHCCCCCCCC
69.3225953088
235AcetylationSSKESSKKPKENKPL
CCCHHCCCCCCCCCC
64.3719822071
237AcetylationKESSKKPKENKPLKE
CHHCCCCCCCCCCCH
80.80-
240AcetylationSKKPKENKPLKEEKI
CCCCCCCCCCCHHCC
53.4723749302
251AcetylationEEKIVPKMAFKEPKP
HHCCCCCCCCCCCCC
4.31-
254AcetylationIVPKMAFKEPKPMSK
CCCCCCCCCCCCCCC
64.6723749302
257AcetylationKMAFKEPKPMSKEPK
CCCCCCCCCCCCCCC
55.2126051181
264SumoylationKPMSKEPKPDSNLLT
CCCCCCCCCCCCCEE
63.65-
264SumoylationKPMSKEPKPDSNLLT
CCCCCCCCCCCCCEE
63.65-
278AcetylationTITSGQDKKAPSKRP
EEECCCCCCCCCCCC
42.8425953088
283AcetylationQDKKAPSKRPPISDS
CCCCCCCCCCCCCCH
68.7925953088
288PhosphorylationPSKRPPISDSEELSA
CCCCCCCCCHHHHHH
40.6425159151
290PhosphorylationKRPPISDSEELSAKK
CCCCCCCHHHHHHHH
26.6129978859
294PhosphorylationISDSEELSAKKRKKS
CCCHHHHHHHHCCCC
41.1225159151
296AcetylationDSEELSAKKRKKSSS
CHHHHHHHHCCCCCH
50.1325953088
300MethylationLSAKKRKKSSSEALF
HHHHHCCCCCHHHHH
60.65115973163
301PhosphorylationSAKKRKKSSSEALFK
HHHHCCCCCHHHHHH
41.9729116813
302PhosphorylationAKKRKKSSSEALFKS
HHHCCCCCHHHHHHH
40.8721815630
303PhosphorylationKKRKKSSSEALFKSF
HHCCCCCHHHHHHHH
33.7028464451
308MethylationSSSEALFKSFSSAPP
CCHHHHHHHHHCCCC
51.98115973171
309PhosphorylationSSEALFKSFSSAPPL
CHHHHHHHHHCCCCE
24.0325159151
311PhosphorylationEALFKSFSSAPPLIL
HHHHHHHHCCCCEEE
32.4525627689
312PhosphorylationALFKSFSSAPPLILT
HHHHHHHCCCCEEEE
42.6627251275
319PhosphorylationSAPPLILTCSADKKQ
CCCCEEEEEECCHHH
9.4525159151
321PhosphorylationPPLILTCSADKKQIK
CCEEEEEECCHHHHC
33.9821815630
324AcetylationILTCSADKKQIKDKS
EEEEECCHHHHCCHH
46.4225953088
330AcetylationDKKQIKDKSHVKMGK
CHHHHCCHHHCCCCE
37.1411794765
331PhosphorylationKKQIKDKSHVKMGKV
HHHHCCHHHCCCCEE
43.58-
334AcetylationIKDKSHVKMGKVKIE
HCCHHHCCCCEEEEE
36.1911794775
337AcetylationKSHVKMGKVKIESET
HHHCCCCEEEEEECC
36.5411794785
339SumoylationHVKMGKVKIESETSE
HCCCCEEEEEECCCC
44.22-
339AcetylationHVKMGKVKIESETSE
HCCCCEEEEEECCCC
44.2226051181
339SumoylationHVKMGKVKIESETSE
HCCCCEEEEEECCCC
44.2228112733
350PhosphorylationETSEKKKSTLPPFDD
CCCCCCCCCCCCCCC
44.0230576142
364PhosphorylationDIVDPNDSDVEENIS
CCCCCCCCHHHHHHC
50.6320873877
371PhosphorylationSDVEENISSKSDSEQ
CHHHHHHCCCCCCCC
43.2130576142
372PhosphorylationDVEENISSKSDSEQP
HHHHHHCCCCCCCCC
32.1727732954
385PhosphorylationQPSPASSSSSSSSSF
CCCCCCCCCCCCCCC
31.57-
386PhosphorylationPSPASSSSSSSSSFT
CCCCCCCCCCCCCCC
35.87-
387PhosphorylationSPASSSSSSSSSFTP
CCCCCCCCCCCCCCH
35.8728787133
388PhosphorylationPASSSSSSSSSFTPS
CCCCCCCCCCCCCHH
35.87-
389PhosphorylationASSSSSSSSSFTPSQ
CCCCCCCCCCCCHHH
31.7630576142
412PhosphorylationSIMKDLHSDDNEEES
HHHHHHHCCCCHHHC
54.6921712546
419PhosphorylationSDDNEEESDEVEDND
CCCCHHHCCCCCCCC
42.2121712546
429PhosphorylationVEDNDNDSEMERPVN
CCCCCCHHHCCCCCC
45.1321712546
446PhosphorylationGSRSRRVSLSDGSDS
CCCCCEEECCCCCCC
21.9730177828
448PhosphorylationRSRRVSLSDGSDSES
CCCEEECCCCCCCCC
32.2130177828
451PhosphorylationRVSLSDGSDSESSSA
EEECCCCCCCCCCCC
42.8430177828
453PhosphorylationSLSDGSDSESSSASS
ECCCCCCCCCCCCCC
40.8730177828
455PhosphorylationSDGSDSESSSASSPL
CCCCCCCCCCCCCCC
33.2830177828
456PhosphorylationDGSDSESSSASSPLH
CCCCCCCCCCCCCCC
26.3530177828
457PhosphorylationGSDSESSSASSPLHH
CCCCCCCCCCCCCCC
41.2630177828
459PhosphorylationDSESSSASSPLHHEP
CCCCCCCCCCCCCCC
34.1430177828
460PhosphorylationSESSSASSPLHHEPP
CCCCCCCCCCCCCCC
31.0630177828
473PhosphorylationPPPPLLKTNNNQILE
CCCCCCCCCCCCEEE
43.0524732914
483PhosphorylationNQILEVKSPIKQSKS
CCEEEECCCCCCCCC
36.7125159151
488PhosphorylationVKSPIKQSKSDKQIK
ECCCCCCCCCHHHCC
29.1722617229
557UbiquitinationLDKTTVRKLQSYLET
CCHHHHHHHHHHHHH
46.68-

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 AF9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AF9_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 AF9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APBP2_HUMANAPPBP2physical
16189514
BCOR_HUMANBCORphysical
12776190
RBM48_HUMANRBM48physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
PTN_HUMANPTNphysical
16169070
LRIF1_HUMANLRIF1physical
16169070
DOT1L_HUMANDOT1Lphysical
16636056
DOT1L_HUMANDOT1Lphysical
17332896
AFF4_HUMANAFF4physical
20431927
AFF1_HUMANAFF1physical
20431927
BCOR_HUMANBCORphysical
20431927
CDK9_HUMANCDK9physical
20431927
DOT1L_HUMANDOT1Lphysical
20431927
AFF3_HUMANAFF3physical
20431927
ACACA_HUMANACACAphysical
20431927
SIR1_HUMANSIRT1physical
20431927
CCNT1_HUMANCCNT1physical
20431927
NIPBL_HUMANNIPBLphysical
20431927
EAF1_HUMANEAF1physical
20431927
ELL3_HUMANELL3physical
20431927
PCGF1_HUMANPCGF1physical
20431927
ENL_HUMANMLLT1physical
20431927
EF2_HUMANEEF2physical
20431927
ELL_HUMANELLphysical
20431927
BCOR_HUMANBCORphysical
20854876
DOT1L_HUMANDOT1Lphysical
20854876
AFF1_HUMANAFF1physical
20854876
AFF3_HUMANAFF3physical
20854876
AFF4_HUMANAFF4physical
20854876
AF10_HUMANMLLT10physical
20854876
CCNT1_HUMANCCNT1physical
20854876
CCNT2_HUMANCCNT2physical
20854876
ENL_HUMANMLLT1physical
20854876
ELL_HUMANELLphysical
20854876
CDK9_HUMANCDK9physical
20854876
RING2_HUMANRNF2physical
20854876
DOT1L_HUMANDOT1Lphysical
21896721
KMT2A_HUMANKMT2Aphysical
21896721
AFF1_HUMANAFF1physical
21896721
AFF4_HUMANAFF4physical
21873227
CDK9_HUMANCDK9physical
21873227
ELL2_HUMANELL2physical
21873227
PAF1_HUMANPAF1physical
21873227
A4_HUMANAPPphysical
21832049
ELL_HUMANELLphysical
21729782
EAF1_HUMANEAF1physical
21729782
CDK9_HUMANCDK9physical
21729782
AFF4_HUMANAFF4physical
21729782
ELL2_HUMANELL2physical
21729782
AFF1_HUMANAFF1physical
21729782
ENL_HUMANMLLT1physical
21729782
CCNT1_HUMANCCNT1physical
21729782
CCNT2_HUMANCCNT2physical
21729782
ENPL_HUMANHSP90B1physical
20159978
H33_HUMANH3F3Aphysical
25417107
DOT1L_HUMANDOT1Lphysical
25417107
CDK9_HUMANCDK9physical
25417107
ELL2_HUMANELL2physical
25417107
AFF4_HUMANAFF4physical
25417107

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 AF9_HUMAN

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Related Literatures of Post-Translational Modification
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-412; SER-419 ANDSER-429, AND MASS SPECTROMETRY.
"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-288, 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-288; SER-294; SER-412;SER-419; SER-429 AND SER-483, 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-294; SER-412; SER-419;SER-429 AND SER-483, AND MASS SPECTROMETRY.

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