AFF1_HUMAN - dbPTM
AFF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AFF1_HUMAN
UniProt AC P51825
Protein Name AF4/FMR2 family member 1
Gene Name AFF1
Organism Homo sapiens (Human).
Sequence Length 1210
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MAAQSSLYNDDRNLLRIREKERRNQEAHQEKEAFPEKIPLFGEPYKTAKGDELSSRIQNMLGNYEEVKEFLSTKSHTHRLDASENRLGKPKYPLIPDKGSSIPSSSFHTSVHHQSIHTPASGPLSVGNISHNPKMAQPRTEPMPSLHAKSCGPPDSQHLTQDRLGQEGFGSSHHKKGDRRADGDHCASVTDSAPERELSPLISLPSPVPPLSPIHSNQQTLPRTQGSSKVHGSSNNSKGYCPAKSPKDLAVKVHDKETPQDSLVAPAQPPSQTFPPPSLPSKSVAMQQKPTAYVRPMDGQDQAPSESPELKPLPEDYRQQTFEKTDLKVPAKAKLTKLKMPSQSVEQTYSNEVHCVEEILKEMTHSWPPPLTAIHTPSTAEPSKFPFPTKDSQHVSSVTQNQKQYDTSSKTHSNSQQGTSSMLEDDLQLSDSEDSDSEQTPEKPPSSSAPPSAPQSLPEPVASAHSSSAESESTSDSDSSSDSESESSSSDSEENEPLETPAPEPEPPTTNKWQLDNWLTKVSQPAAPPEGPRSTEPPRRHPESKGSSDSATSQEHSESKDPPPKSSSKAPRAPPEAPHPGKRSCQKSPAQQEPPQRQTVGTKQPKKPVKASARAGSRTSLQGEREPGLLPYGSRDQTSKDKPKVKTKGRPRAAASNEPKPAVPPSSEKKKHKSSLPAPSKALSGPEPAKDNVEDRTPEHFALVPLTESQGPPHSGSGSRTSGCRQAVVVQEDSRKDRLPLPLRDTKLLSPLRDTPPPQSLMVKITLDLLSRIPQPPGKGSRQRKAEDKQPPAGKKHSSEKRSSDSSSKLAKKRKGEAERDCDNKKIRLEKEIKSQSSSSSSSHKESSKTKPSRPSSQSSKKEMLPPPPVSSSSQKPAKPALKRSRREADTCGQDPPKSASSTKSNHKDSSIPKQRRVEGKGSRSSSEHKGSSGDTANPFPVPSLPNGNSKPGKPQVKFDKQQADLHMREAKKMKQKAELMTDRVGKAFKYLEAVLSFIECGIATESESQSSKSAYSVYSETVDLIKFIMSLKSFSDATAPTQEKIFAVLCMRCQSILNMAMFRCKKDIAIKYSRTLNKHFESSSKVAQAPSPCIASTGTPSPLSPMPSPASSVGSQSSAGSVGSSGVAATISTPVTIQNMTSSYVTITSHVLTAFDLWEQAEALTRKNKEFFARLSTNVCTLALNSSLVDLVHYTRQGFQQLQELTKTP
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
5Phosphorylation---MAAQSSLYNDDR
---CCCCCHHCCCCH
19.9928060719
6Phosphorylation--MAAQSSLYNDDRN
--CCCCCHHCCCCHH
23.8528060719
8PhosphorylationMAAQSSLYNDDRNLL
CCCCCHHCCCCHHHH
20.6328060719
9 (in isoform 2)Phosphorylation-50.4226471730
10 (in isoform 2)Phosphorylation-42.5621815630
13 (in isoform 2)Phosphorylation-50.8826471730
15 (in isoform 2)Phosphorylation-4.9626471730
45PhosphorylationIPLFGEPYKTAKGDE
CCCCCCCCCCCCHHH
19.3727422710
64PhosphorylationIQNMLGNYEEVKEFL
HHHHHCCHHHHHHHH
16.2128796482
71 (in isoform 2)Phosphorylation-7.1527642862
74UbiquitinationVKEFLSTKSHTHRLD
HHHHHHCCCCHHCCC
36.54-
83PhosphorylationHTHRLDASENRLGKP
CHHCCCCCCCCCCCC
34.7672272945
89AcetylationASENRLGKPKYPLIP
CCCCCCCCCCCCCCC
42.827964611
91AcetylationENRLGKPKYPLIPDK
CCCCCCCCCCCCCCC
64.097964623
98AcetylationKYPLIPDKGSSIPSS
CCCCCCCCCCCCCCC
56.1726051181
171PhosphorylationLGQEGFGSSHHKKGD
CCCCCCCCCCCCCCC
25.0028555341
172PhosphorylationGQEGFGSSHHKKGDR
CCCCCCCCCCCCCCC
29.9525627689
188PhosphorylationADGDHCASVTDSAPE
CCCCCCCCCCCCCCC
30.8324144214
190PhosphorylationGDHCASVTDSAPERE
CCCCCCCCCCCCCHH
23.0324144214
192PhosphorylationHCASVTDSAPERELS
CCCCCCCCCCCHHCC
36.0424144214
199PhosphorylationSAPERELSPLISLPS
CCCCHHCCCCCCCCC
16.9522167270
203PhosphorylationRELSPLISLPSPVPP
HHCCCCCCCCCCCCC
41.7422167270
206PhosphorylationSPLISLPSPVPPLSP
CCCCCCCCCCCCCCC
43.7722167270
206 (in isoform 2)Phosphorylation-43.7727251275
212PhosphorylationPSPVPPLSPIHSNQQ
CCCCCCCCCCCCCCC
27.8129255136
213 (in isoform 2)Phosphorylation-35.6727251275
216PhosphorylationPPLSPIHSNQQTLPR
CCCCCCCCCCCCCCC
36.7329255136
219 (in isoform 2)Phosphorylation-49.6227251275
220PhosphorylationPIHSNQQTLPRTQGS
CCCCCCCCCCCCCCC
29.0329255136
237PhosphorylationVHGSSNNSKGYCPAK
CCCCCCCCCCCCCCC
31.5446159993
238AcetylationHGSSNNSKGYCPAKS
CCCCCCCCCCCCCCC
56.9018584413
240PhosphorylationSSNNSKGYCPAKSPK
CCCCCCCCCCCCCHH
10.0523403867
244AcetylationSKGYCPAKSPKDLAV
CCCCCCCCCHHHEEE
53.0518584425
245PhosphorylationKGYCPAKSPKDLAVK
CCCCCCCCHHHEEEE
39.0123401153
247AcetylationYCPAKSPKDLAVKVH
CCCCCCHHHEEEEEC
72.9018584437
252 (in isoform 2)Phosphorylation-28.3924719451
256AcetylationLAVKVHDKETPQDSL
EEEEECCCCCCCCCC
48.9226051181
281PhosphorylationFPPPSLPSKSVAMQQ
CCCCCCCCCCCCCCC
42.7424719451
283PhosphorylationPPSLPSKSVAMQQKP
CCCCCCCCCCCCCCC
21.3223186163
291PhosphorylationVAMQQKPTAYVRPMD
CCCCCCCCEEEECCC
37.3423186163
293PhosphorylationMQQKPTAYVRPMDGQ
CCCCCCEEEECCCCC
10.2423186163
305PhosphorylationDGQDQAPSESPELKP
CCCCCCCCCCCCCCC
54.4426657352
307PhosphorylationQDQAPSESPELKPLP
CCCCCCCCCCCCCCC
28.1926657352
311UbiquitinationPSESPELKPLPEDYR
CCCCCCCCCCCHHHH
42.73-
312 (in isoform 2)Phosphorylation-66.8127251275
324UbiquitinationYRQQTFEKTDLKVPA
HHHHHHCCCCCCCCC
43.05-
325PhosphorylationRQQTFEKTDLKVPAK
HHHHHCCCCCCCCCC
39.0920068231
328UbiquitinationTFEKTDLKVPAKAKL
HHCCCCCCCCCCCCC
49.32-
334UbiquitinationLKVPAKAKLTKLKMP
CCCCCCCCCCCCCCC
56.85-
339UbiquitinationKAKLTKLKMPSQSVE
CCCCCCCCCCCCCHH
50.77-
364PhosphorylationEEILKEMTHSWPPPL
HHHHHHHHHCCCCCC
17.5328450419
366PhosphorylationILKEMTHSWPPPLTA
HHHHHHHCCCCCCEE
31.9230108239
372PhosphorylationHSWPPPLTAIHTPST
HCCCCCCEEEECCCC
29.3728450419
376PhosphorylationPPLTAIHTPSTAEPS
CCCEEEECCCCCCCC
16.9082900347
378PhosphorylationLTAIHTPSTAEPSKF
CEEEECCCCCCCCCC
41.2130108239
379PhosphorylationTAIHTPSTAEPSKFP
EEEECCCCCCCCCCC
35.9228450419
383PhosphorylationTPSTAEPSKFPFPTK
CCCCCCCCCCCCCCC
38.1330108239
383 (in isoform 2)Phosphorylation-38.1327251275
384AcetylationPSTAEPSKFPFPTKD
CCCCCCCCCCCCCCC
68.7026051181
389PhosphorylationPSKFPFPTKDSQHVS
CCCCCCCCCCCCCHH
48.1130108239
390UbiquitinationSKFPFPTKDSQHVSS
CCCCCCCCCCCCHHH
56.47-
403AcetylationSSVTQNQKQYDTSSK
HHHCCCCHHCCCCCC
59.3725953088
403UbiquitinationSSVTQNQKQYDTSSK
HHHCCCCHHCCCCCC
59.37-
534PhosphorylationAPPEGPRSTEPPRRH
CCCCCCCCCCCCCCC
40.0128985074
544PhosphorylationPPRRHPESKGSSDSA
CCCCCCCCCCCCCCC
46.9372840311
560AcetylationSQEHSESKDPPPKSS
HHHHHHCCCCCCCCC
70.9226051181
582AcetylationPEAPHPGKRSCQKSP
CCCCCCCCCCCCCCC
45.6625953088
584PhosphorylationAPHPGKRSCQKSPAQ
CCCCCCCCCCCCCCC
25.1223403867
588PhosphorylationGKRSCQKSPAQQEPP
CCCCCCCCCCCCCCC
10.2923401153
595 (in isoform 2)Phosphorylation-41.0327251275
603AcetylationQRQTVGTKQPKKPVK
CCCCCCCCCCCCCCC
59.6925953088
617PhosphorylationKASARAGSRTSLQGE
CCHHCCCCCCCCCCC
31.2528555341
619PhosphorylationSARAGSRTSLQGERE
HHCCCCCCCCCCCCC
35.1718691976
620PhosphorylationARAGSRTSLQGEREP
HCCCCCCCCCCCCCC
20.0063731909
627 (in isoform 2)Phosphorylation-44.9827251275
660AcetylationAAASNEPKPAVPPSS
CHHCCCCCCCCCCCH
39.1626051181
666PhosphorylationPKPAVPPSSEKKKHK
CCCCCCCCHHHHHCC
45.0925159151
667PhosphorylationKPAVPPSSEKKKHKS
CCCCCCCHHHHHCCC
60.2425159151
680PhosphorylationKSSLPAPSKALSGPE
CCCCCCCCHHHCCCC
32.44113310181
681AcetylationSSLPAPSKALSGPEP
CCCCCCCHHHCCCCC
52.8919608861
684PhosphorylationPAPSKALSGPEPAKD
CCCCHHHCCCCCCCC
58.1023401153
687 (in isoform 2)Phosphorylation-62.5127251275
688AcetylationKALSGPEPAKDNVED
HHHCCCCCCCCCCCC
47.9819608861
697PhosphorylationKDNVEDRTPEHFALV
CCCCCCCCCCCEEEE
45.4029255136
704 (in isoform 2)Phosphorylation-3.0727251275
707PhosphorylationHFALVPLTESQGPPH
CEEEEECCCCCCCCC
27.7628464451
709PhosphorylationALVPLTESQGPPHSG
EEEECCCCCCCCCCC
34.8930576142
715PhosphorylationESQGPPHSGSGSRTS
CCCCCCCCCCCCCCC
40.1918691976
717PhosphorylationQGPPHSGSGSRTSGC
CCCCCCCCCCCCCCC
36.2925159151
719PhosphorylationPPHSGSGSRTSGCRQ
CCCCCCCCCCCCCCE
33.8027080861
734PhosphorylationAVVVQEDSRKDRLPL
EEEEECCCCCCCCCC
40.2430229599
750PhosphorylationLRDTKLLSPLRDTPP
CCCCCCCCCCCCCCC
32.1225159151
755PhosphorylationLLSPLRDTPPPQSLM
CCCCCCCCCCCCHHH
31.1225159151
757 (in isoform 2)Phosphorylation-41.4724719451
760PhosphorylationRDTPPPQSLMVKITL
CCCCCCCHHHHHHHH
24.9820068231
766PhosphorylationQSLMVKITLDLLSRI
CHHHHHHHHHHHHCC
14.4315302935
789AcetylationRQRKAEDKQPPAGKK
HHCCCCCCCCCCCCC
57.0926051181
803PhosphorylationKHSSEKRSSDSSSKL
CCCCCCCCCCCHHHH
49.9546159997
809AcetylationRSSDSSSKLAKKRKG
CCCCCHHHHHHHHHC
55.1825953088
826UbiquitinationERDCDNKKIRLEKEI
HHHCCCCCHHHHHHH
39.03-
831AcetylationNKKIRLEKEIKSQSS
CCCHHHHHHHHHCCC
70.1426051181
835PhosphorylationRLEKEIKSQSSSSSS
HHHHHHHHCCCCCCC
40.7410508641
837PhosphorylationEKEIKSQSSSSSSSH
HHHHHHCCCCCCCCC
39.00158919
838PhosphorylationKEIKSQSSSSSSSHK
HHHHHCCCCCCCCCC
26.9710509639
839PhosphorylationEIKSQSSSSSSSHKE
HHHHCCCCCCCCCCC
39.2127251275
840PhosphorylationIKSQSSSSSSSHKES
HHHCCCCCCCCCCCC
35.8727251275
841PhosphorylationKSQSSSSSSSHKESS
HHCCCCCCCCCCCCC
37.5030576142
842PhosphorylationSQSSSSSSSHKESSK
HCCCCCCCCCCCCCC
38.1124719451
843PhosphorylationQSSSSSSSHKESSKT
CCCCCCCCCCCCCCC
40.2927251275
847PhosphorylationSSSSHKESSKTKPSR
CCCCCCCCCCCCCCC
41.778656097
847 (in isoform 2)Phosphorylation-41.7727251275
848PhosphorylationSSSHKESSKTKPSRP
CCCCCCCCCCCCCCC
45.4930576142
849 (in isoform 2)Phosphorylation-70.6024719451
871PhosphorylationMLPPPPVSSSSQKPA
CCCCCCCCCCCCCCC
30.2126074081
872PhosphorylationLPPPPVSSSSQKPAK
CCCCCCCCCCCCCCC
33.9526074081
873PhosphorylationPPPPVSSSSQKPAKP
CCCCCCCCCCCCCCH
29.3125627689
874PhosphorylationPPPVSSSSQKPAKPA
CCCCCCCCCCCCCHH
44.1425627689
932PhosphorylationSSSEHKGSSGDTANP
CCCCCCCCCCCCCCC
35.6368698031
950PhosphorylationPSLPNGNSKPGKPQV
CCCCCCCCCCCCCCC
41.4446160003
1039PhosphorylationLKSFSDATAPTQEKI
CCCCCCCCCCCHHHH
37.8546160009
1042PhosphorylationFSDATAPTQEKIFAV
CCCCCCCCHHHHHHH
47.0746160015
1067MalonylationMAMFRCKKDIAIKYS
HHHHHCCHHHHHHHH
58.9726320211
1072MalonylationCKKDIAIKYSRTLNK
CCHHHHHHHHHHHHH
28.3126320211
1092 (in isoform 3)Phosphorylation-35.1130266825
1099 (in isoform 2)Phosphorylation-32.8830266825
1166PhosphorylationWEQAEALTRKNKEFF
HHHHHHHHHHCHHHH
46.7920071362
1209PhosphorylationQLQELTKTP------
HHHHHHCCC------
29.0622617229
1217 (in isoform 2)Phosphorylation-24719451

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
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:15221006

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AFF1_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 AFF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNT1_HUMANCCNT1physical
19956800
5NTD_HUMANNT5Ephysical
19956800
ENL_HUMANMLLT1physical
20153263
CCNT1_HUMANCCNT1physical
20153263
CDK9_HUMANCDK9physical
20153263
AFF4_HUMANAFF4physical
20153263
AFF1_HUMANAFF1physical
20153263
KMT2A_HUMANKMT2Aphysical
21030982
AFF1_HUMANAFF1physical
21030982
CCNT1_HUMANCCNT1physical
21030982
CDK9_HUMANCDK9physical
21030982
BRD4_HUMANBRD4physical
21030982
TF65_HUMANRELAphysical
21030982
NPM_HUMANNPM1physical
21030982
ENL_HUMANMLLT1physical
21030982
NEC1_HUMANPCSK1physical
21030982
AF9_HUMANMLLT3physical
21030982
AF10_HUMANMLLT10physical
21030982
DOT1L_HUMANDOT1Lphysical
21030982
RPB1_HUMANPOLR2Aphysical
21030982
DDX6_HUMANDDX6physical
21030982
HEXI1_HUMANHEXIM1physical
21030982
H31T_HUMANHIST3H3physical
21030982
SIAH1_HUMANSIAH1physical
15221006
SIAH2_HUMANSIAH2physical
15221006
AFF1_HUMANAFF1physical
15221006
ENL_HUMANMLLT1physical
15856011
ELL2_HUMANELL2physical
24367103
ENL_HUMANMLLT1physical
24367103
LARP7_HUMANLARP7physical
24367103
HEXI1_HUMANHEXIM1physical
24367103
CDK9_HUMANCDK9physical
24367103
CCNT1_HUMANCCNT1physical
24367103

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 AFF1_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-681, 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-206 AND SER-750, ANDMASS 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-206; SER-212; SER-216;SER-245; SER-588; THR-697; SER-750 AND THR-1209, 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-206; SER-212; THR-220;SER-750 AND THR-755, 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-199; SER-206; SER-212;SER-588; SER-750; THR-755 AND THR-1209, 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-588 AND THR-766, ANDMASS SPECTROMETRY.

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