HAUS7_HUMAN - dbPTM
HAUS7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAUS7_HUMAN
UniProt AC Q99871
Protein Name HAUS augmin-like complex subunit 7
Gene Name HAUS7
Organism Homo sapiens (Human).
Sequence Length 368
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Localizes to interphase centrosomes and to mitotic spindle microtubules.
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 MGGARLGARNMAGQDAGCGRGGDDYSEDEGDSSVSRAAVEVFGKLKDLNCPFLEGLYITEPKTIQELLCSPSEYRLEILEWMCTRVWPSLQDRFSSLKGVPTEVKIQEMTKLGHELMLCAPDDQELLKGCACAQKQLHFMDQLLDTIRSLTIGCSSCSSLMEHFEDTREKNEALLGELFSSPHLQMLLNPECDPWPLDMQPLLNKQSDDWQWASASAKSEEEEKLAELARQLQESAAKLHALRTEYFAQHEQGAAAGAADISTLDQKLRLVTSDFHQLILAFLQVYDDELGECCQRPGPDLHPCGPIIQATHQNLTSYSQLLQVVMAVADTSAKAVETVKKQQGEQICWGGSSSVMSLATKMNELMEK
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
16PhosphorylationRNMAGQDAGCGRGGD
CCCCCCCCCCCCCCC		13.7933259812
25PhosphorylationCGRGGDDYSEDEGDS
CCCCCCCCCCCCCCC		20.7828796482
26PhosphorylationGRGGDDYSEDEGDSS
CCCCCCCCCCCCCCC		45.6322167270
32PhosphorylationYSEDEGDSSVSRAAV
CCCCCCCCCHHHHHH		43.4222167270
33PhosphorylationSEDEGDSSVSRAAVE
CCCCCCCCHHHHHHH		28.9321815630
35PhosphorylationDEGDSSVSRAAVEVF
CCCCCCHHHHHHHHH		20.3926552605
44 (in isoform 2)Ubiquitination-40.68-
44UbiquitinationAAVEVFGKLKDLNCP
HHHHHHHHHHHCCCC		40.6829967540
46 (in isoform 2)Ubiquitination-64.75-
46UbiquitinationVEVFGKLKDLNCPFL
HHHHHHHHHCCCCCC		64.7521963094
57PhosphorylationCPFLEGLYITEPKTI
CCCCCCEEECCCCCH		19.3625159151
88UbiquitinationWMCTRVWPSLQDRFS
HHHHHHCHHHHHHHH		23.4633845483
93MethylationVWPSLQDRFSSLKGV
HCHHHHHHHHHCCCC		22.01-
98UbiquitinationQDRFSSLKGVPTEVK
HHHHHHCCCCCCCHH		60.8621906983
98 (in isoform 2)Ubiquitination-60.86-
98AcetylationQDRFSSLKGVPTEVK
HHHHHHCCCCCCCHH		60.8671279
105UbiquitinationKGVPTEVKIQEMTKL
CCCCCCHHHHHHHHH		32.2329967540
105AcetylationKGVPTEVKIQEMTKL
CCCCCCHHHHHHHHH		32.2371281
105 (in isoform 2)Ubiquitination-32.23-
111 (in isoform 2)Ubiquitination-51.68-
111UbiquitinationVKIQEMTKLGHELML
HHHHHHHHHCCEEEE		51.6821963094
118UbiquitinationKLGHELMLCAPDDQE
HHCCEEEEECCCHHH		3.3532015554
125UbiquitinationLCAPDDQELLKGCAC
EECCCHHHHHHHCHH		64.1632015554
128 (in isoform 2)Ubiquitination-65.65-
128AcetylationPDDQELLKGCACAQK
CCHHHHHHHCHHHHH		65.6525953088
128UbiquitinationPDDQELLKGCACAQK
CCHHHHHHHCHHHHH		65.6521963094
135 (in isoform 2)Ubiquitination-35.98-
135AcetylationKGCACAQKQLHFMDQ
HHCHHHHHHHHHHHH		35.9825953088
135UbiquitinationKGCACAQKQLHFMDQ
HHCHHHHHHHHHHHH		35.9821963094
149PhosphorylationQLLDTIRSLTIGCSS
HHHHHHHHHHCCCHH		26.47-
158PhosphorylationTIGCSSCSSLMEHFE
HCCCHHHHHHHHHHH		28.5825954137
159PhosphorylationIGCSSCSSLMEHFED
CCCHHHHHHHHHHHH		35.7425954137
218 (in isoform 2)Ubiquitination-56.77-
218UbiquitinationQWASASAKSEEEEKL
HHHHHCCCCHHHHHH		56.7721906983
224 (in isoform 2)Ubiquitination-57.17-
224UbiquitinationAKSEEEEKLAELARQ
CCCHHHHHHHHHHHH		57.1721906983
238UbiquitinationQLQESAAKLHALRTE
HHHHHHHHHHHHHHH		40.2927667366
238AcetylationQLQESAAKLHALRTE
HHHHHHHHHHHHHHH		40.2925953088
238 (in isoform 2)Ubiquitination-40.29-
262PhosphorylationAAGAADISTLDQKLR
CCCCCCHHHHHHHHH		24.3821712546
267UbiquitinationDISTLDQKLRLVTSD
CHHHHHHHHHHHHCH		34.9322053931
267 (in isoform 2)Ubiquitination-34.93-
267UbiquitinationDISTLDQKLRLVTSD
CHHHHHHHHHHHHCH		34.9321963094
328 (in isoform 2)Ubiquitination-2.40-
340UbiquitinationAKAVETVKKQQGEQI
HHHHHHHHHHCCCEE		52.8927667366
341UbiquitinationKAVETVKKQQGEQIC
HHHHHHHHHCCCEEE		43.4429967540
354PhosphorylationICWGGSSSVMSLATK
EECCCHHHHHHHHHH		24.44-
360PhosphorylationSSVMSLATKMNELME
HHHHHHHHHHHHHHH		35.80-
361UbiquitinationSVMSLATKMNELMEK
HHHHHHHHHHHHHHC		33.8421963094
400 (in isoform 2)Ubiquitination--
420 (in isoform 2)Ubiquitination--
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 HAUS7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAUS7_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 HAUS7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAUS6_HUMANHAUS6physical
19369198
ATF4_HUMANATF4physical
19447967
HAUS1_HUMANHAUS1physical
26186194
ASPM_HUMANASPMphysical
26186194
SPDLY_HUMANSPDL1physical
26186194
HAUS4_HUMANHAUS4physical
26186194
HAUS3_HUMANHAUS3physical
26186194
HAUS8_HUMANHAUS8physical
26186194
GOLI4_HUMANGOLIM4physical
26186194
HAUS5_HUMANHAUS5physical
26186194
GLCE_HUMANGLCEphysical
26186194
CKAP4_HUMANCKAP4physical
26186194
FKRP_HUMANFKRPphysical
26186194
CETN3_HUMANCETN3physical
26186194
S27A2_HUMANSLC27A2physical
26186194
HAUS6_HUMANHAUS6physical
26186194
PMGT1_HUMANPOMGNT1physical
26186194
HAUS2_HUMANHAUS2physical
26186194
LEMD2_HUMANLEMD2physical
26186194
MUL1_HUMANMUL1physical
26186194
TCAL1_HUMANTCEAL1physical
26186194
SPRY7_HUMANSPRYD7physical
26186194
ALG11_HUMANALG11physical
26186194
ALG14_HUMANALG14physical
26186194
PP4P1_HUMANTMEM55Bphysical
26186194
SCPDL_HUMANSCCPDHphysical
26186194
GSTM1_HUMANGSTM1physical
26186194
VTI1B_HUMANVTI1Bphysical
26186194
GP1BB_HUMANGP1BBphysical
26186194
ARI1_HUMANARIH1physical
26186194
VAMP8_HUMANVAMP8physical
26186194
HAUS2_HUMANHAUS2physical
28514442
HAUS3_HUMANHAUS3physical
28514442
HAUS1_HUMANHAUS1physical
28514442
HAUS4_HUMANHAUS4physical
28514442
HAUS8_HUMANHAUS8physical
28514442
HAUS5_HUMANHAUS5physical
28514442
SPRY7_HUMANSPRYD7physical
28514442
HAUS6_HUMANHAUS6physical
28514442
SPDLY_HUMANSPDL1physical
28514442
GLCE_HUMANGLCEphysical
28514442
ALG14_HUMANALG14physical
28514442
S27A2_HUMANSLC27A2physical
28514442
GP1BB_HUMANGP1BBphysical
28514442
ALG11_HUMANALG11physical
28514442
GOLI4_HUMANGOLIM4physical
28514442
SCPDL_HUMANSCCPDHphysical
28514442
GSTM1_HUMANGSTM1physical
28514442
FKRP_HUMANFKRPphysical
28514442
VTI1B_HUMANVTI1Bphysical
28514442
LEMD2_HUMANLEMD2physical
28514442
ARI1_HUMANARIH1physical
28514442
MUL1_HUMANMUL1physical
28514442
TCAL1_HUMANTCEAL1physical
28514442
CKAP4_HUMANCKAP4physical
28514442
XXLT1_HUMANXXYLT1physical
28514442
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 HAUS7_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-26, 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-26, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY.

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