ZW10_HUMAN - dbPTM
ZW10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZW10_HUMAN
UniProt AC O43264
Protein Name Centromere/kinetochore protein zw10 homolog
Gene Name ZW10
Organism Homo sapiens (Human).
Sequence Length 779
Subcellular Localization Cytoplasm . Endoplasmic reticulum membrane
Peripheral membrane protein . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle . Dynamic pattern of localization during the cell cycle. In most cells at interphase, present diffusely
Protein Description Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. [PubMed: 11590237]
Protein Sequence MASFVTEVLAHSGRLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPSMQSAQGLITQVDKLSEDIDLLKSRIESEVRRDLHVSTGEFTDLKQQLERDSVVLSLLKQLQEFSTAIEEYNCALTEKKYVTGAQRLEEAQKCLKLLKSRKCFDLKILKSLSMELTIQKQNILYHLGEEWQKLIVWKFPPSKDTSSLESYLQTELHLYTEQSHKEEKTPMPPISSVLLAFSVLGELHSKLKSFGQMLLKYILRPLASCPSLHAVIESQPNIVIIRFESIMTNLEYPSPSEVFTKIRLVLEVLQKQLLDLPLDTDLENEKTSTVPLAEMLGDMIWEDLSECLIKNCLVYSIPTNSSKLQQYEEIIQSTEEFENALKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARNLMTSEIHNTVKIIPDSKINVPELPTPDEDNKLEVQKVSNTQYHEVMNLEPENTLDQHSFSLPTCRISESVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLQKLPQLAAIHHNNCMYIAHHLLTLGHQFRLRLAPILCDGTATFVDLVPGFRRLGTECFLAQMRAQKGELLERLSSARNFSNMDDEENYSAASKAVRQVLHQLKRLGIVWQDVLPVNIYCKAMGTLLNTAISEVIGKITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSEESKNKKYQEEVPVYVPKWMPFKELMMMLQASLQEIGDRWADGKGPLAAAFSSSEVKALIRALFQNTERRAAALAKIK
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------MASFVTEVL
------CCHHHHHHH
16.2125944712
3Phosphorylation-----MASFVTEVLA
-----CCHHHHHHHH
20.9625159151
6Phosphorylation--MASFVTEVLAHSG
--CCHHHHHHHHHCC
20.5429255136
12PhosphorylationVTEVLAHSGRLEKED
HHHHHHHCCCCCHHH
21.7229255136
17UbiquitinationAHSGRLEKEDLGTRI
HHCCCCCHHHHHHHH
62.21-
17UbiquitinationAHSGRLEKEDLGTRI
HHCCCCCHHHHHHHH
62.21-
22PhosphorylationLEKEDLGTRISRLTR
CCHHHHHHHHHHHHH
31.9321406692
35AcetylationTRRVEEIKGEVCNMI
HHHHHHHHHHHHHHH
52.9125953088
43PhosphorylationGEVCNMISKKYSEFL
HHHHHHHHHHHHHHH
16.6023401153
74UbiquitinationSEDIDLLKSRIESEV
HHHHHHHHHHHHHHH
45.0121906983
74UbiquitinationSEDIDLLKSRIESEV
HHHHHHHHHHHHHHH
45.01-
88PhosphorylationVRRDLHVSTGEFTDL
HHHHCCCCCCCCCCH
21.6822199227
89PhosphorylationRRDLHVSTGEFTDLK
HHHCCCCCCCCCCHH
39.3722199227
96AcetylationTGEFTDLKQQLERDS
CCCCCCHHHHHHHHH
38.5226822725
96UbiquitinationTGEFTDLKQQLERDS
CCCCCCHHHHHHHHH
38.52-
96UbiquitinationTGEFTDLKQQLERDS
CCCCCCHHHHHHHHH
38.5221906983
103PhosphorylationKQQLERDSVVLSLLK
HHHHHHHHHHHHHHH
21.9821712546
107PhosphorylationERDSVVLSLLKQLQE
HHHHHHHHHHHHHHH
21.7524719451
129UbiquitinationYNCALTEKKYVTGAQ
HHCHHHCCHHCCHHH
44.1429967540
130UbiquitinationNCALTEKKYVTGAQR
HCHHHCCHHCCHHHH
38.43-
130UbiquitinationNCALTEKKYVTGAQR
HCHHHCCHHCCHHHH
38.4329967540
131PhosphorylationCALTEKKYVTGAQRL
CHHHCCHHCCHHHHH
17.8220068231
133PhosphorylationLTEKKYVTGAQRLEE
HHCCHHCCHHHHHHH
24.5720068231
143UbiquitinationQRLEEAQKCLKLLKS
HHHHHHHHHHHHHHH
48.89-
143UbiquitinationQRLEEAQKCLKLLKS
HHHHHHHHHHHHHHH
48.8924816145
162UbiquitinationDLKILKSLSMELTIQ
CHHHHHHHCCEEEEH
5.5924816145
170UbiquitinationSMELTIQKQNILYHL
CCEEEEHHHHHHHHC
41.2727667366
195PhosphorylationKFPPSKDTSSLESYL
ECCCCCCCCHHHHHH
24.7724043423
196PhosphorylationFPPSKDTSSLESYLQ
CCCCCCCCHHHHHHH
42.9624043423
197PhosphorylationPPSKDTSSLESYLQT
CCCCCCCHHHHHHHH
37.9424043423
200PhosphorylationKDTSSLESYLQTELH
CCCCHHHHHHHHHHH
36.1124043423
201PhosphorylationDTSSLESYLQTELHL
CCCHHHHHHHHHHHH
8.0824043423
204PhosphorylationSLESYLQTELHLYTE
HHHHHHHHHHHHHCC
37.6124043423
209PhosphorylationLQTELHLYTEQSHKE
HHHHHHHHCCCCCCC
9.4824043423
210PhosphorylationQTELHLYTEQSHKEE
HHHHHHHCCCCCCCC
33.6324043423
213PhosphorylationLHLYTEQSHKEEKTP
HHHHCCCCCCCCCCC
30.2324043423
264UbiquitinationASCPSLHAVIESQPN
HCCCCHHHHHHCCCC
14.8527667366
314O-linked_GlycosylationLLDLPLDTDLENEKT
HCCCCCCCCCCCCCC
50.6028411811
318UbiquitinationPLDTDLENEKTSTVP
CCCCCCCCCCCCCCC
64.4624816145
326UbiquitinationEKTSTVPLAEMLGDM
CCCCCCCHHHHHHHH
5.6827667366
349PhosphorylationLIKNCLVYSIPTNSS
HHHCCEEEECCCCHH
6.4722817900
353PhosphorylationCLVYSIPTNSSKLQQ
CEEEECCCCHHHHHH
46.1725627689
355PhosphorylationVYSIPTNSSKLQQYE
EEECCCCHHHHHHHH
31.1825627689
356PhosphorylationYSIPTNSSKLQQYEE
EECCCCHHHHHHHHH
39.1825627689
357UbiquitinationSIPTNSSKLQQYEEI
ECCCCHHHHHHHHHH
50.5729967540
361PhosphorylationNSSKLQQYEEIIQST
CHHHHHHHHHHHHCH
11.5427642862
376UbiquitinationEEFENALKEMRFLKG
HHHHHHHHHCHHHCC
47.2429967540
382UbiquitinationLKEMRFLKGDTTDLL
HHHCHHHCCCHHHHH
52.62-
382UbiquitinationLKEMRFLKGDTTDLL
HHHCHHHCCCHHHHH
52.6224816145
386PhosphorylationRFLKGDTTDLLKYAR
HHHCCCHHHHHHHHH
29.4119664994
390UbiquitinationGDTTDLLKYARNINS
CCHHHHHHHHHHCCH
44.13-
390UbiquitinationGDTTDLLKYARNINS
CCHHHHHHHHHHCCH
44.1327667366
402UbiquitinationINSHFANKKCQDVIV
CCHHHCCCCHHHHHH
52.0429967540
403UbiquitinationNSHFANKKCQDVIVA
CHHHCCCCHHHHHHH
36.6129967540
403UbiquitinationNSHFANKKCQDVIVA
CHHHCCCCHHHHHHH
36.61-
404UbiquitinationSHFANKKCQDVIVAA
HHHCCCCHHHHHHHH
4.4522817900
420UbiquitinationNLMTSEIHNTVKIIP
HCCCHHCCCCEEECC
21.6227667366
424UbiquitinationSEIHNTVKIIPDSKI
HHCCCCEEECCCCCC
32.6429967540
430UbiquitinationVKIIPDSKINVPELP
EEECCCCCCCCCCCC
45.7629967540
438PhosphorylationINVPELPTPDEDNKL
CCCCCCCCCCCCCCE
56.8730266825
444UbiquitinationPTPDEDNKLEVQKVS
CCCCCCCCEEEEEEC
59.3429967540
455PhosphorylationQKVSNTQYHEVMNLE
EEECCCCCEEECCCC
9.6322817900
484UbiquitinationCRISESVKKLMELAY
CCCCHHHHHHHHHHH
49.8527667366
560UbiquitinationLTLGHQFRLRLAPIL
HHHCCHHHHHCHHEE
16.6022817900
568GlutathionylationLRLAPILCDGTATFV
HHCHHEECCCCCCHH
4.7322555962
571PhosphorylationAPILCDGTATFVDLV
HHEECCCCCCHHHCC
14.8520071362
597UbiquitinationLAQMRAQKGELLERL
HHHHHHHHHHHHHHH
54.06-
597UbiquitinationLAQMRAQKGELLERL
HHHHHHHHHHHHHHH
54.06-
611PhosphorylationLSSARNFSNMDDEEN
HHHCCCCCCCCCHHH
34.4920860994
619PhosphorylationNMDDEENYSAASKAV
CCCCHHHHHHHHHHH
11.7220860994
624UbiquitinationENYSAASKAVRQVLH
HHHHHHHHHHHHHHH
46.2921906983
624UbiquitinationENYSAASKAVRQVLH
HHHHHHHHHHHHHHH
46.29-
6342-HydroxyisobutyrylationRQVLHQLKRLGIVWQ
HHHHHHHHHCCCEEE
38.72-
634AcetylationRQVLHQLKRLGIVWQ
HHHHHHHHHCCCEEE
38.7225953088
655PhosphorylationIYCKAMGTLLNTAIS
HHHHHHHHHHHHHHH
18.2620071362
659PhosphorylationAMGTLLNTAISEVIG
HHHHHHHHHHHHHHH
25.9020068231
662PhosphorylationTLLNTAISEVIGKIT
HHHHHHHHHHHHHHH
24.2820068231
684PhosphorylationEDGDRLYSLCKTVMD
CCCHHHHHHHHHHHC
31.7028348404
687UbiquitinationDRLYSLCKTVMDEGP
HHHHHHHHHHHCCCC
49.8229967540
688PhosphorylationRLYSLCKTVMDEGPQ
HHHHHHHHHHCCCCC
21.7728348404
690SulfoxidationYSLCKTVMDEGPQVF
HHHHHHHHCCCCCCC
4.7421406390
708UbiquitinationSEESKNKKYQEEVPV
CHHHCCCCCCCCCCC
62.6529967540
708AcetylationSEESKNKKYQEEVPV
CHHHCCCCCCCCCCC
62.6525953088
719AcetylationEVPVYVPKWMPFKEL
CCCCCCCCCCCHHHH
46.1925953088
777AcetylationRRAAALAKIK-----
HHHHHHHHCC-----
52.4519608861
777UbiquitinationRRAAALAKIK-----
HHHHHHHHCC-----
52.4519608861

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 ZW10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZW10_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 ZW10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RINT1_HUMANRINT1physical
15029241
STX18_HUMANSTX18physical
15029241
A4_HUMANAPPphysical
21832049
KNTC1_HUMANKNTC1physical
15824131
ZWILC_HUMANZWILCHphysical
15824131
RINT1_HUMANRINT1physical
15824131
CS025_HUMANC19orf25physical
15824131
MD1L1_HUMANMAD1L1physical
15824131
MD2L1_HUMANMAD2L1physical
15824131
WASC5_HUMANKIAA0196physical
22863883
LMNA_HUMANLMNAphysical
22863883
PSD10_HUMANPSMD10physical
22863883
ROCK2_HUMANROCK2physical
22863883
ACTZ_HUMANACTR1Aphysical
26344197
ACTY_HUMANACTR1Bphysical
26344197
HSP74_HUMANHSPA4physical
26344197
KNTC1_HUMANKNTC1physical
26344197
MSH2_HUMANMSH2physical
26344197
STOM_HUMANSTOMphysical
27173435

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 ZW10_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-777, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, AND MASSSPECTROMETRY.

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