HABP4_HUMAN - dbPTM
HABP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HABP4_HUMAN
UniProt AC Q5JVS0
Protein Name Intracellular hyaluronan-binding protein 4 {ECO:0000303|PubMed:10887182}
Gene Name HABP4 {ECO:0000312|HGNC:HGNC:17062}
Organism Homo sapiens (Human).
Sequence Length 413
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, Stress granule . Cytoplasm, sarcoplasm . Nucleus, Nuclear body . Nucleus, nucleolus . Nucleus speckle . Nucleus, Cajal body . Nucleus, gem . Transported into the nuclear compartment in activated leukocytes (PubMed:952
Protein Description RNA-binding protein that plays a role in the regulation of transcription, pre-mRNA splicing and mRNA translation. [PubMed: 14699138]
Protein Sequence MKGALGSPVAAAGAAMQESFGCVVANRFHQLLDDESDPFDILREAERRRQQQLQRKRRDEAAAAAGAGPRGGRSPAGASGHRAGAGGRRESQKERKSLPAPVAQRPDSPGGGLQAPGQKRTPRRGEQQGWNDSRGPEGMLERAERRSYREYRPYETERQADFTAEKFPDEKPGDRFDRDRPLRGRGGPRGGMRGRGRGGPGNRVFDAFDQRGKREFERYGGNDKIAVRTEDNMGGCGVRTWGSGKDTSDVEPTAPMEEPTVVEESQGTPEEESPAKVPELEVEEETQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSKYRDDMVKDDYEDDSHVFRKPANDITSQLEINFGNLPRPGRGARGGTRGGRGRIRRAENYGPRAEVVMQDVAPNPDDPEDFPALS
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
2Methylation------MKGALGSPV
------CCCCCCCHH		53.54-
7Phosphorylation-MKGALGSPVAAAGA
-CCCCCCCHHHHHHH		19.6321712546
36PhosphorylationHQLLDDESDPFDILR
HHHHCCCCCHHHHHH		58.54-
70MethylationAAAGAGPRGGRSPAG
HHCCCCCCCCCCCCC		60.3224129315
73MethylationGAGPRGGRSPAGASG
CCCCCCCCCCCCHHC		42.14-
74PhosphorylationAGPRGGRSPAGASGH
CCCCCCCCCCCHHCC		23.5225849741
79PhosphorylationGRSPAGASGHRAGAG
CCCCCCHHCCCCCCC		33.9328348404
82MethylationPAGASGHRAGAGGRR
CCCHHCCCCCCCCCC		37.94-
88MethylationHRAGAGGRRESQKER
CCCCCCCCCCCHHHH		37.97-
97PhosphorylationESQKERKSLPAPVAQ
CCHHHHHCCCCCCCC		45.8925159151
108PhosphorylationPVAQRPDSPGGGLQA
CCCCCCCCCCCCCCC		28.2929255136
121PhosphorylationQAPGQKRTPRRGEQQ
CCCCCCCCCCCCCCC		28.3428985074
124MethylationGQKRTPRRGEQQGWN
CCCCCCCCCCCCCCC		54.96-
133PhosphorylationEQQGWNDSRGPEGML
CCCCCCCCCCCHHHH		35.6028555341
198UbiquitinationGMRGRGRGGPGNRVF
CCCCCCCCCCCCHHH		49.8524816145
226UbiquitinationYGGNDKIAVRTEDNM
CCCCCCEEEEECCCC		7.1724816145
260PhosphorylationTAPMEEPTVVEESQG
CCCCCCCEEEECCCC		40.2329460479
265PhosphorylationEPTVVEESQGTPEEE
CCEEEECCCCCCCCC		22.0229970186
268PhosphorylationVVEESQGTPEEESPA
EEECCCCCCCCCCCC		21.6429507054
273PhosphorylationQGTPEEESPAKVPEL
CCCCCCCCCCCCCCC		33.1825850435
316PhosphorylationFNIRKPESTVPSKAV
CCCCCCCCCCCCCEE		43.1420068231
317PhosphorylationNIRKPESTVPSKAVV
CCCCCCCCCCCCEEE		34.4720068231
320PhosphorylationKPESTVPSKAVVIHK
CCCCCCCCCEEEEEC		28.9820068231
336UbiquitinationKYRDDMVKDDYEDDS
CCCCCCCCCCCCCCC		37.9424816145
339PhosphorylationDDMVKDDYEDDSHVF
CCCCCCCCCCCCCCC		31.2428796482
354PhosphorylationRKPANDITSQLEINF
CCCHHHHCCCEEEEC		17.1820873877
355PhosphorylationKPANDITSQLEINFG
CCHHHHCCCEEEECC		32.8523663014
375PhosphorylationGRGARGGTRGGRGRI
CCCCCCCCCCCCCCC		29.0328695742
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
354TPhosphorylationKinasePRKCAP17252
GPS
354TPhosphorylationKinasePRKCQQ04759
GPS
354TPhosphorylationKinasePRKCZQ05513
GPS
354TPhosphorylationKinasePKC-Uniprot
375TPhosphorylationKinasePRKCAP17252
GPS
375TPhosphorylationKinasePRKCQQ04759
GPS
375TPhosphorylationKinasePRKCZQ05513
GPS
375TPhosphorylationKinasePKC-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
354TPhosphorylation

14699138
375TPhosphorylation

14699138
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 HABP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RACK1_HUMANGNB2L1physical
14699138
ANM1_HUMANPRMT1physical
16169070
VIME_HUMANVIMphysical
16169070
CHD3_HUMANCHD3physical
16169070
RACK1_HUMANGNB2L1physical
16455055
CHD3_HUMANCHD3physical
16455055
TOPRS_HUMANTOPORSphysical
16455055
DAXX_HUMANDAXXphysical
16455055
PIAS3_HUMANPIAS3physical
16455055
HMGX4_HUMANHMGXB4physical
16455055
KAT5_HUMANKAT5physical
16455055
UBC9_HUMANUBE2Iphysical
16455055
PR15A_HUMANPPP1R15Aphysical
16455055
YBOX1_HUMANYBX1physical
16455055
C1QBP_HUMANC1QBPphysical
16455055
P53_MOUSETrp53physical
16455055
P53_HUMANTP53physical
16455055
HNRPQ_HUMANSYNCRIPphysical
19523114
SRSF1_HUMANSRSF1physical
19523114
SRSF9_HUMANSRSF9physical
19523114
YBOX1_HUMANYBX1physical
19523114
C1QBP_HUMANC1QBPphysical
19523114
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
DB08818Hyaluronan
Regulatory Network of HABP4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-97 AND SER-108, AND MASSSPECTROMETRY.
"Ki-1/57 interacts with RACK1 and is a substrate for thephosphorylation by phorbol 12-myristate 13-acetate-activated proteinkinase C.";
Nery F.C., Passos D.O., Garcia V.S., Kobarg J.;
J. Biol. Chem. 279:11444-11455(2004).
Cited for: FUNCTION, INTERACTION WITH GNB2L1, SUBCELLULAR LOCATION, ANDPHOSPHORYLATION.

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