MAP9_HUMAN - dbPTM
MAP9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAP9_HUMAN
UniProt AC Q49MG5
Protein Name Microtubule-associated protein 9
Gene Name MAP9
Organism Homo sapiens (Human).
Sequence Length 647
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle . Localizes to microtubules in interphase, associates with the mitotic spindle during mitosis, localizes to the central body during cytokinesis.
Protein Description Involved in organization of the bipolar mitotic spindle. Required for bipolar spindle assembly, mitosis progression and cytokinesis. May act by stabilizing interphase microtubules..
Protein Sequence MSDEVFSTTLAYTKSPKVTKRTTFQDELIRAITARSARQRSSEYSDDFDSDEIVSLGDFSDTSADENSVNKKMNDFHISDDEEKNPSKLLFLKTNKSNGNITKDEPVCAIKNEEEMAPDGCEDIVVKSFSESQNKDEEFEKDKIKMKPKPRILSIKSTSSAENNSLDTDDHFKPSPRPRSMLKKKSHMEEKDGLEDKETALSEELELHSAPSSLPTPNGIQLEAEKKAFSENLDPEDSCLTSLASSSLKQILGDSFSPGSEGNASGKDPNEEITENHNSLKSDENKENSFSADHVTTAVEKSKESQVTADDLEEEKAKAELIMDDDRTVDPLLSKSQSILISTSATASSKKTIEDRNIKNKKSTNNRASSASARLMTSEFLKKSSSKRRTPSTTTSSHYLGTLKVLDQKPSQKQSIEPDRADNIRAAVYQEWLEKKNVYLHEMHRIKRIESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEENAARKGEALQAFEKWKEKKMEYLKEKNRKEREYERAKKQKEEETVAEKKKDNLTAVEKWNEKKEAFFKQKEKEKINEKRKEELKRAEKKDKDKQAINEYEKWLENKEKQERIERKQKKRHSFLESEALPPWSPPSRTVFAKVF
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
2Acetylation------MSDEVFSTT
------CCCCCHHCE
42.3419413330
2Phosphorylation------MSDEVFSTT
------CCCCCHHCE
42.3423663014
7Phosphorylation-MSDEVFSTTLAYTK
-CCCCCHHCEECCCC
26.1723663014
8PhosphorylationMSDEVFSTTLAYTKS
CCCCCHHCEECCCCC
17.8619690332
9PhosphorylationSDEVFSTTLAYTKSP
CCCCHHCEECCCCCC
14.2723663014
12PhosphorylationVFSTTLAYTKSPKVT
CHHCEECCCCCCCCC
20.1523663014
13PhosphorylationFSTTLAYTKSPKVTK
HHCEECCCCCCCCCC
21.3123663014
15PhosphorylationTTLAYTKSPKVTKRT
CEECCCCCCCCCCCC
23.3523663014
19PhosphorylationYTKSPKVTKRTTFQD
CCCCCCCCCCCCCHH
22.4226074081
22PhosphorylationSPKVTKRTTFQDELI
CCCCCCCCCCHHHHH
33.2526074081
41PhosphorylationARSARQRSSEYSDDF
HHHHHHHCCCCCCCC
21.13-
79 (in isoform 2)Phosphorylation-30.3621406692
79PhosphorylationKMNDFHISDDEEKNP
HHCCCCCCCCCCCCH
30.3630266825
87PhosphorylationDDEEKNPSKLLFLKT
CCCCCCHHHEEEEEE
45.3823927012
128PhosphorylationCEDIVVKSFSESQNK
CCEEEEECCCHHCCC
23.54-
130PhosphorylationDIVVKSFSESQNKDE
EEEEECCCHHCCCCH
43.35-
132PhosphorylationVVKSFSESQNKDEEF
EEECCCHHCCCCHHH
37.5417525332
154PhosphorylationKPKPRILSIKSTSSA
CCCCCEEEEECCCCC
26.1224719451
157PhosphorylationPRILSIKSTSSAENN
CCEEEEECCCCCCCC
31.6729978859
158PhosphorylationRILSIKSTSSAENNS
CEEEEECCCCCCCCC
23.0029978859
159PhosphorylationILSIKSTSSAENNSL
EEEEECCCCCCCCCC
34.3429978859
160PhosphorylationLSIKSTSSAENNSLD
EEEECCCCCCCCCCC
39.4229978859
165PhosphorylationTSSAENNSLDTDDHF
CCCCCCCCCCCCCCC
38.9229978859
175PhosphorylationTDDHFKPSPRPRSML
CCCCCCCCCCCHHHH
33.8527251275
180PhosphorylationKPSPRPRSMLKKKSH
CCCCCCHHHHHHHHC
31.0227251275
209PhosphorylationSEELELHSAPSSLPT
HHHHHHHCCCCCCCC
55.2725921289
212PhosphorylationLELHSAPSSLPTPNG
HHHHCCCCCCCCCCC
44.2025921289
238PhosphorylationENLDPEDSCLTSLAS
CCCCHHHHHHHHHHH
14.9028348404
241PhosphorylationDPEDSCLTSLASSSL
CHHHHHHHHHHHHHH
26.4828348404
242PhosphorylationPEDSCLTSLASSSLK
HHHHHHHHHHHHHHH
14.6928348404
245PhosphorylationSCLTSLASSSLKQIL
HHHHHHHHHHHHHHH
26.2528348404
246PhosphorylationCLTSLASSSLKQILG
HHHHHHHHHHHHHHC
33.8028348404
247PhosphorylationLTSLASSSLKQILGD
HHHHHHHHHHHHHCC
36.7728348404
255PhosphorylationLKQILGDSFSPGSEG
HHHHHCCCCCCCCCC
26.3129978859
257PhosphorylationQILGDSFSPGSEGNA
HHHCCCCCCCCCCCC
32.1029978859
260PhosphorylationGDSFSPGSEGNASGK
CCCCCCCCCCCCCCC
45.7929978859
265PhosphorylationPGSEGNASGKDPNEE
CCCCCCCCCCCCCHH
50.8329978859
279PhosphorylationEITENHNSLKSDENK
HHHCCHHCCCCCCCC
29.6225627689
282PhosphorylationENHNSLKSDENKENS
CCHHCCCCCCCCCCC
56.2922617229
289PhosphorylationSDENKENSFSADHVT
CCCCCCCCCCHHHHH
22.9725849741
291PhosphorylationENKENSFSADHVTTA
CCCCCCCCHHHHHHH
32.3830377224
296PhosphorylationSFSADHVTTAVEKSK
CCCHHHHHHHHHHHH
12.9629449344
305PhosphorylationAVEKSKESQVTADDL
HHHHHHHHCCCHHHH
33.4225159151
336PhosphorylationVDPLLSKSQSILIST
CCHHHCCCCEEEEEC
26.2827251275
338PhosphorylationPLLSKSQSILISTSA
HHHCCCCEEEEECCC
26.8428348404
343PhosphorylationSQSILISTSATASSK
CCEEEEECCCCCCCC
18.52-
349PhosphorylationSTSATASSKKTIEDR
ECCCCCCCCCCHHHH
35.39-
363PhosphorylationRNIKNKKSTNNRASS
HCCCCCCCCCCCHHH
37.6726074081
364PhosphorylationNIKNKKSTNNRASSA
CCCCCCCCCCCHHHH
45.4526074081
369PhosphorylationKSTNNRASSASARLM
CCCCCCHHHHHHHHH
24.1726074081
370PhosphorylationSTNNRASSASARLMT
CCCCCHHHHHHHHHH
25.8426074081
372PhosphorylationNNRASSASARLMTSE
CCCHHHHHHHHHHHH
18.8326074081
377PhosphorylationSASARLMTSEFLKKS
HHHHHHHHHHHHHHC
29.6926074081
378PhosphorylationASARLMTSEFLKKSS
HHHHHHHHHHHHHCC
16.6426074081
385PhosphorylationSEFLKKSSSKRRTPS
HHHHHHCCCCCCCCC
49.08-
390PhosphorylationKSSSKRRTPSTTTSS
HCCCCCCCCCCCCCH
26.1429978859
392PhosphorylationSSKRRTPSTTTSSHY
CCCCCCCCCCCCHHH
37.4629978859
393PhosphorylationSKRRTPSTTTSSHYL
CCCCCCCCCCCHHHH
34.9829978859
394PhosphorylationKRRTPSTTTSSHYLG
CCCCCCCCCCHHHHH
29.0829978859
395PhosphorylationRRTPSTTTSSHYLGT
CCCCCCCCCHHHHHE
28.4629449344
396PhosphorylationRTPSTTTSSHYLGTL
CCCCCCCCHHHHHEE
17.0229978859
397PhosphorylationTPSTTTSSHYLGTLK
CCCCCCCHHHHHEEE
17.6629978859
399PhosphorylationSTTTSSHYLGTLKVL
CCCCCHHHHHEEEEC
14.5829978859
402PhosphorylationTSSHYLGTLKVLDQK
CCHHHHHEEEECCCC
22.3229978859
429PhosphorylationDNIRAAVYQEWLEKK
HHHHHHHHHHHHHHC
8.9327642862
451PhosphorylationHRIKRIESENLRIQN
HHHHHHHHHCHHCCH
29.4328857561
496AcetylationAKKRLEEKNKKKTEE
HHHHHHHHHHHHHHH
65.7720167786
603PhosphorylationDKQAINEYEKWLENK
HHHHHHHHHHHHHCH
20.51-
625PhosphorylationRKQKKRHSFLESEAL
HHHHHHHCHHHCCCC
35.2429514088
629PhosphorylationKRHSFLESEALPPWS
HHHCHHHCCCCCCCC
30.2529514088
636PhosphorylationSEALPPWSPPSRTVF
CCCCCCCCCCCCCEE
32.4827251275
639PhosphorylationLPPWSPPSRTVFAKV
CCCCCCCCCCEEEEC
43.9229449344

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
289SPhosphorylationKinasePLK1P53350
PSP
305SPhosphorylationKinaseAURKAO14965
GPS
625SPhosphorylationKinaseAURKAO14965
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAP9_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 MAP9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
22672907
EP300_HUMANEP300physical
22672907

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 MAP9_HUMAN

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Related Literatures of Post-Translational Modification
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-15 AND SER-257, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASSSPECTROMETRY.
"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 TYR-12, AND MASSSPECTROMETRY.

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