HAUS5_HUMAN - dbPTM
HAUS5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAUS5_HUMAN
UniProt AC O94927
Protein Name HAUS augmin-like complex subunit 5
Gene Name HAUS5
Organism Homo sapiens (Human).
Sequence Length 633
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 MELAQEARELGCWAVEEMGVPVAARAPESTLRRLCLGQGADIWAYILQHVHSQRTVKKIRGNLLWYGHQDSPQVRRKLELEAAVTRLRAEIQELDQSLELMERDTEAQDTAMEQARQHTQDTQRRALLLRAQAGAMRRQQHTLRDPMQRLQNQLRRLQDMERKAKVDVTFGSLTSAALGLEPVVLRDVRTACTLRAQFLQNLLLPQAKRGSLPTPHDDHFGTSYQQWLSSVETLLTNHPPGHVLAALEHLAAEREAEIRSLCSGDGLGDTEISRPQAPDQSDSSQTLPSMVHLIQEGWRTVGVLVSQRSTLLKERQVLTQRLQGLVEEVERRVLGSSERQVLILGLRRCCLWTELKALHDQSQELQDAAGHRQLLLRELQAKQQRILHWRQLVEETQEQVRLLIKGNSASKTRLCRSPGEVLALVQRKVVPTFEAVAPQSRELLRCLEEEVRHLPHILLGTLLRHRPGELKPLPTVLPSIHQLHPASPRGSSFIALSHKLGLPPGKASELLLPAAASLRQDLLLLQDQRSLWCWDLLHMKTSLPPGLPTQELLQIQASQEKQQKENLGQALKRLEKLLKQALERIPELQGIVGDWWEQPGQAALSEELCQGLSLPQWRLRWVQAQGALQKLCS
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
1Acetylation-------MELAQEAR
-------CHHHHHHH		9.5722814378
29PhosphorylationVAARAPESTLRRLCL
CEECCCHHHHHHHHH		31.5127135362
30PhosphorylationAARAPESTLRRLCLG
EECCCHHHHHHHHHC		23.7127135362
71PhosphorylationLWYGHQDSPQVRRKL
EEECCCCCHHHHHHH		15.6323403867
77UbiquitinationDSPQVRRKLELEAAV
CCHHHHHHHHHHHHH		35.43-
85PhosphorylationLELEAAVTRLRAEIQ
HHHHHHHHHHHHHHH		21.1823898821
97PhosphorylationEIQELDQSLELMERD
HHHHHHHHHHHHHHC		24.3927732954
105PhosphorylationLELMERDTEAQDTAM
HHHHHHCHHHHHHHH		39.1720860994
108UbiquitinationMERDTEAQDTAMEQA
HHHCHHHHHHHHHHH		42.2121890473
112SulfoxidationTEAQDTAMEQARQHT
HHHHHHHHHHHHHHC		4.2121406390
165UbiquitinationQDMERKAKVDVTFGS
HHHHHHHHCCEEHHH		41.84-
172PhosphorylationKVDVTFGSLTSAALG
HCCEEHHHHHHHHHC		25.0427251275
174PhosphorylationDVTFGSLTSAALGLE
CEEHHHHHHHHHCCC		20.3027251275
175PhosphorylationVTFGSLTSAALGLEP
EEHHHHHHHHHCCCC		19.48-
208UbiquitinationNLLLPQAKRGSLPTP
HCCCCHHHCCCCCCC		52.6322817900
208 (in isoform 1)Ubiquitination-52.6321890473
208 (in isoform 2)Ubiquitination-52.6321890473
208UbiquitinationNLLLPQAKRGSLPTP
HCCCCHHHCCCCCCC		52.6321890473
213UbiquitinationQAKRGSLPTPHDDHF
HHHCCCCCCCCCCCC		45.6527667366
236O-linked_GlycosylationSSVETLLTNHPPGHV
HHHHHHHHCCCCHHH		34.30OGP
282UbiquitinationPQAPDQSDSSQTLPS
CCCCCCCCCCCCHHH		46.8322817900
305UbiquitinationWRTVGVLVSQRSTLL
HHHHHHHHCCCHHHH		4.2122817900
313UbiquitinationSQRSTLLKERQVLTQ
CCCHHHHHHHHHHHH		54.7027667366
319PhosphorylationLKERQVLTQRLQGLV
HHHHHHHHHHHHHHH		16.8824260401
328UbiquitinationRLQGLVEEVERRVLG
HHHHHHHHHHHHHCC		42.0522505724
349S-nitrosylationLILGLRRCCLWTELK
HHHHHHHHHHHHHHH		1.4819483679
349S-nitrosocysteineLILGLRRCCLWTELK
HHHHHHHHHHHHHHH		1.48-
350S-nitrosylationILGLRRCCLWTELKA
HHHHHHHHHHHHHHH		3.1819483679
350S-nitrosocysteineILGLRRCCLWTELKA
HHHHHHHHHHHHHHH		3.18-
356UbiquitinationCCLWTELKALHDQSQ
HHHHHHHHHHHHHCH		42.54-
382 (in isoform 1)Ubiquitination-33.7221890473
382UbiquitinationLLRELQAKQQRILHW
HHHHHHHHHHHHHHH		33.7221906983
405 (in isoform 1)Ubiquitination-52.5921890473
405UbiquitinationEQVRLLIKGNSASKT
HHHHHHHCCCCCCCC		52.5921906983
406UbiquitinationQVRLLIKGNSASKTR
HHHHHHCCCCCCCCE		26.7422817900
417PhosphorylationSKTRLCRSPGEVLAL
CCCEECCCHHHHHHH		35.9420873877
428UbiquitinationVLALVQRKVVPTFEA
HHHHHHCCCCCCHHH		30.4122505724
461PhosphorylationLPHILLGTLLRHRPG
CHHHHHHHHHHCCCC		23.69-
471UbiquitinationRHRPGELKPLPTVLP
HCCCCCCCCCCCCCC		39.9629967540
487PhosphorylationIHQLHPASPRGSSFI
HHHCCCCCCCCCCCH		21.4125159151
506 (in isoform 1)Ubiquitination-55.2921890473
506UbiquitinationKLGLPPGKASELLLP
HHCCCCCCHHHHHHH		55.2922817900
530UbiquitinationLLLQDQRSLWCWDLL
HHHHCHHHHHHHHHH		22.1622505724
561UbiquitinationQIQASQEKQQKENLG
HHHHHHHHHHHHHHH		50.8529967540
564UbiquitinationASQEKQQKENLGQAL
HHHHHHHHHHHHHHH		46.1829967540
572UbiquitinationENLGQALKRLEKLLK
HHHHHHHHHHHHHHH		58.9329967540
576UbiquitinationQALKRLEKLLKQALE
HHHHHHHHHHHHHHH		64.81-
579UbiquitinationKRLEKLLKQALERIP
HHHHHHHHHHHHHCH		43.92-
630UbiquitinationQAQGALQKLCS----
HHHHHHHHHHC----		52.9222505724
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 HAUS5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAUS5_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 HAUS5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAUS6_HUMANHAUS6physical
19369198
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 HAUS5_HUMAN

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Related Literatures of Post-Translational Modification

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