HAUS8_HUMAN - dbPTM
HAUS8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAUS8_HUMAN
UniProt AC Q9BT25
Protein Name HAUS augmin-like complex subunit 8
Gene Name HAUS8
Organism Homo sapiens (Human).
Sequence Length 410
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, spindle pole . During interphase, primarily cytoplasmic and associates with centrosomes and with the mitotic
Protein Description Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex..
Protein Sequence MADSSGRGAGKPATGPTNSSSAKKKDKRVQGGRVIESRYLQYEKKTTQKAPAGDGSQTRGKMSEGGRKSSLLQKSKADSSGVGKGDLQSTLLEGHGTAPPDLDLSAINDKSIVKKTPQLAKTISKKPESTSFSAPRKKSPDLSEAMEMMESQTLLLTLLSVKMENNLAEFERRAEKNLLIMCKEKEKLQKKAHELKRRLLLSQRKRELADVLDAQIEMLSPFEAVATRFKEQYRTFATALDTTRHELPVRSIHLEGDGQQLLDALQHELVTTQRLLGELDVGDSEENVQVLDLLSELKDVTAKKDLELRRSFAQVLELSAEASKEAALANQEVWEETQGMAPPSRWYFNQDSACRESGGAPKNTPLSEDDNPGASSAPAQATFISPSEDFSSSSQAEVPPSLSRSGRDLS
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------MADSSGRGA
------CCCCCCCCC
25.9519413330
5Phosphorylation---MADSSGRGAGKP
---CCCCCCCCCCCC
32.8126074081
7Methylation-MADSSGRGAGKPAT
-CCCCCCCCCCCCCC
33.46-
9 (in isoform 2)Phosphorylation-22.8329743597
11UbiquitinationSSGRGAGKPATGPTN
CCCCCCCCCCCCCCC
30.8324816145
14PhosphorylationRGAGKPATGPTNSSS
CCCCCCCCCCCCCCC
52.8226074081
17PhosphorylationGKPATGPTNSSSAKK
CCCCCCCCCCCCCCH
49.4229396449
19PhosphorylationPATGPTNSSSAKKKD
CCCCCCCCCCCCHHC
28.3125262027
20PhosphorylationATGPTNSSSAKKKDK
CCCCCCCCCCCHHCC
36.0625159151
21PhosphorylationTGPTNSSSAKKKDKR
CCCCCCCCCCHHCCC
43.8825159151
39PhosphorylationGRVIESRYLQYEKKT
CCEEHHHEEEEECCC
13.8729083192
42PhosphorylationIESRYLQYEKKTTQK
EHHHEEEEECCCCCC
27.4122817900
46PhosphorylationYLQYEKKTTQKAPAG
EEEEECCCCCCCCCC
45.5929083192
47PhosphorylationLQYEKKTTQKAPAGD
EEEECCCCCCCCCCC
36.6329083192
49AcetylationYEKKTTQKAPAGDGS
EECCCCCCCCCCCCC
55.0025953088
49UbiquitinationYEKKTTQKAPAGDGS
EECCCCCCCCCCCCC
55.0024816145
56PhosphorylationKAPAGDGSQTRGKMS
CCCCCCCCCCCCCCC
32.87-
59DimethylationAGDGSQTRGKMSEGG
CCCCCCCCCCCCCCC
34.79-
59MethylationAGDGSQTRGKMSEGG
CCCCCCCCCCCCCCC
34.79-
61"N6,N6-dimethyllysine"DGSQTRGKMSEGGRK
CCCCCCCCCCCCCHH
35.64-
61MethylationDGSQTRGKMSEGGRK
CCCCCCCCCCCCCHH
35.64-
67DimethylationGKMSEGGRKSSLLQK
CCCCCCCHHHHHHHH
46.68-
67MethylationGKMSEGGRKSSLLQK
CCCCCCCHHHHHHHH
46.68-
69PhosphorylationMSEGGRKSSLLQKSK
CCCCCHHHHHHHHHC
25.5126074081
70PhosphorylationSEGGRKSSLLQKSKA
CCCCHHHHHHHHHCC
35.8123911959
74UbiquitinationRKSSLLQKSKADSSG
HHHHHHHHHCCCCCC
54.6229967540
79PhosphorylationLQKSKADSSGVGKGD
HHHHCCCCCCCCCCH
33.5720068231
89PhosphorylationVGKGDLQSTLLEGHG
CCCCHHHHHHHCCCC
28.4618691976
90PhosphorylationGKGDLQSTLLEGHGT
CCCHHHHHHHCCCCC
23.5429978859
97PhosphorylationTLLEGHGTAPPDLDL
HHHCCCCCCCCCCCH
30.2527732954
105PhosphorylationAPPDLDLSAINDKSI
CCCCCCHHHHCCHHH
27.1125159151
109UbiquitinationLDLSAINDKSIVKKT
CCHHHHCCHHHHHHC
39.7129967540
110UbiquitinationDLSAINDKSIVKKTP
CHHHHCCHHHHHHCH
37.2829967540
111PhosphorylationLSAINDKSIVKKTPQ
HHHHCCHHHHHHCHH
35.1628555341
114UbiquitinationINDKSIVKKTPQLAK
HCCHHHHHHCHHHHH
49.6229967540
115UbiquitinationNDKSIVKKTPQLAKT
CCHHHHHHCHHHHHH
55.3229967540
116PhosphorylationDKSIVKKTPQLAKTI
CHHHHHHCHHHHHHH
15.5621712546
122PhosphorylationKTPQLAKTISKKPES
HCHHHHHHHCCCCCC
25.5221690413
124UbiquitinationPQLAKTISKKPESTS
HHHHHHHCCCCCCCC
39.6029967540
124PhosphorylationPQLAKTISKKPESTS
HHHHHHHCCCCCCCC
39.6026657352
125UbiquitinationQLAKTISKKPESTSF
HHHHHHCCCCCCCCC
69.3829967540
126UbiquitinationLAKTISKKPESTSFS
HHHHHCCCCCCCCCC
47.4229967540
129PhosphorylationTISKKPESTSFSAPR
HHCCCCCCCCCCCCC
37.5728450419
130PhosphorylationISKKPESTSFSAPRK
HCCCCCCCCCCCCCC
31.9328450419
131PhosphorylationSKKPESTSFSAPRKK
CCCCCCCCCCCCCCC
26.8725159151
133PhosphorylationKPESTSFSAPRKKSP
CCCCCCCCCCCCCCC
36.8126657352
139PhosphorylationFSAPRKKSPDLSEAM
CCCCCCCCCCHHHHH
27.0425159151
143PhosphorylationRKKSPDLSEAMEMME
CCCCCCHHHHHHHHH
30.5921690413
151PhosphorylationEAMEMMESQTLLLTL
HHHHHHHHHHHHHHH
15.5723917254
153PhosphorylationMEMMESQTLLLTLLS
HHHHHHHHHHHHHHH
28.75-
157PhosphorylationESQTLLLTLLSVKME
HHHHHHHHHHHHHHH
26.1424719451
160PhosphorylationTLLLTLLSVKMENNL
HHHHHHHHHHHHCCH
23.8624719451
175UbiquitinationAEFERRAEKNLLIMC
HHHHHHHHHHEEHHH
40.4429967540
176UbiquitinationEFERRAEKNLLIMCK
HHHHHHHHHEEHHHC
52.4929967540
202PhosphorylationLKRRLLLSQRKRELA
HHHHHHHHHHHHHHH
28.1024719451
220PhosphorylationDAQIEMLSPFEAVAT
HHHHHHCCHHHHHHH
26.6621690413
230UbiquitinationEAVATRFKEQYRTFA
HHHHHHHHHHHHHHH
40.39-
235PhosphorylationRFKEQYRTFATALDT
HHHHHHHHHHHHHHC
16.8221690413
238PhosphorylationEQYRTFATALDTTRH
HHHHHHHHHHHCCCC
24.4621690413
311PhosphorylationKDLELRRSFAQVLEL
HCHHHHHHHHHHHHH
20.6421690413
319PhosphorylationFAQVLELSAEASKEA
HHHHHHHCHHHHHHH
18.0628555341
347PhosphorylationMAPPSRWYFNQDSAC
CCCCHHHCCCCCHHH
7.4927642862
352PhosphorylationRWYFNQDSACRESGG
HHCCCCCHHHHHCCC
21.3624719451
357PhosphorylationQDSACRESGGAPKNT
CCHHHHHCCCCCCCC
24.1525159151
382PhosphorylationSSAPAQATFISPSED
CCCCCEEEEECCCCC
14.9325627689
385PhosphorylationPAQATFISPSEDFSS
CCEEEEECCCCCCCC
20.4125627689

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
19SPhosphorylationKinaseAURAO14965
PSP
20SPhosphorylationKinaseAURAO14965
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAUS8_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 HAUS8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAUS6_HUMANHAUS6physical
19369198
HAUS5_HUMANHAUS5physical
19369198
A4_HUMANAPPphysical
21832049
SEC20_HUMANBNIP1physical
28514442
RBP10_HUMANRANBP10physical
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 HAUS8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.

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