HPS4_HUMAN - dbPTM
HPS4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HPS4_HUMAN
UniProt AC Q9NQG7
Protein Name Hermansky-Pudlak syndrome 4 protein
Gene Name HPS4
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization
Protein Description Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38. [PubMed: 23084991]
Protein Sequence MATSTSTEAKSASWWNYFFLYDGSKVKEEGDPTRAGICYFYPSQTLLDQQELLCGQIAGVVRCVSDISDSPPTLVRLRKLKFAIKVDGDYLWVLGCAVELPDVSCKRFLDQLVGFFNFYNGPVSLAYENCSQEELSTEWDTFIEQILKNTSDLHKIFNSLWNLDQTKVEPLLLLKAARILQTCQRSPHILAGCILYKGLIVSTQLPPSLTAKVLLHRTAPQEQRLPTGEDAPQEHGAALPPNVQIIPVFVTKEEAISLHEFPVEQMTRSLASPAGLQDGSAQHHPKGGSTSALKENATGHVESMAWTTPDPTSPDEACPDGRKENGCLSGHDLESIRPAGLHNSARGEVLGLSSSLGKELVFLQEELDLSEIHIPEAQEVEMASGHFAFLHVPVPDGRAPYCKASLSASSSLEPTPPEDTAISSLRPPSAPEMLTQHGAQEQLEDHPGHSSQAPIPRADPLPRRTRRPLLLPRLDPGQRGNKLPTGEQGLDEDVDGVCESHAAPGLECSSGSANCQGAGPSADGISSRLTPAESCMGLVRMNLYTHCVKGLVLSLLAEEPLLGDSAAIEEVYHSSLASLNGLEVHLKETLPRDEAASTSSTYNFTHYDRIQSLLMANLPQVATPQDRRFLQAVSLMHSEFAQLPALYEMTVRNASTAVYACCNPIQETYFQQLAPAARSSGFPNPQDGAFSLSGKAKQKLLKHGVNLL
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
6 (in isoform 4)Phosphorylation-24.82-
6 (in isoform 3)Phosphorylation-24.82-
167UbiquitinationLWNLDQTKVEPLLLL
HCCCCCCCCHHHHHH		38.68-
207 (in isoform 4)Ubiquitination-51.03-
212UbiquitinationLPPSLTAKVLLHRTA
CCHHHCHHHHHCCCC		28.34-
257PhosphorylationVTKEEAISLHEFPVE
EEHHHHHCCCCCCHH		30.62-
269PhosphorylationPVEQMTRSLASPAGL
CHHHHHHHHCCCCCC		21.0830266825
272PhosphorylationQMTRSLASPAGLQDG
HHHHHHCCCCCCCCC		22.1523401153
280PhosphorylationPAGLQDGSAQHHPKG
CCCCCCCCCCCCCCC		32.8029396449
289PhosphorylationQHHPKGGSTSALKEN
CCCCCCCCHHHHHHC		28.0527251275
298PhosphorylationSALKENATGHVESMA
HHHHHCCCCCCEEEE		39.1328270605
307PhosphorylationHVESMAWTTPDPTSP
CCEEEEEECCCCCCC		20.9329978859
308PhosphorylationVESMAWTTPDPTSPD
CEEEEEECCCCCCCC		18.2629978859
312PhosphorylationAWTTPDPTSPDEACP
EEECCCCCCCCCCCC		61.3426471730
313PhosphorylationWTTPDPTSPDEACPD
EECCCCCCCCCCCCC		35.4226471730
353PhosphorylationRGEVLGLSSSLGKEL
CCCCCEECCCCCHHH		18.9730266825
354PhosphorylationGEVLGLSSSLGKELV
CCCCEECCCCCHHHH		34.3330266825
355PhosphorylationEVLGLSSSLGKELVF
CCCEECCCCCHHHHH		37.4519664994
423PhosphorylationPPEDTAISSLRPPSA
CCCCCCHHHCCCCCH		22.3624719451
424PhosphorylationPEDTAISSLRPPSAP
CCCCCHHHCCCCCHH		23.4525954137
530PhosphorylationDGISSRLTPAESCMG
CCCCCCCCHHHHHHH		21.2428060719
534PhosphorylationSRLTPAESCMGLVRM
CCCCHHHHHHHHHHH		16.12-
544PhosphorylationGLVRMNLYTHCVKGL
HHHHHHHHHHHHHHH		6.88-
545PhosphorylationLVRMNLYTHCVKGLV
HHHHHHHHHHHHHHH		16.38-
597PhosphorylationLPRDEAASTSSTYNF
CCCCCCCCCCCCCCC		35.5525072903
598PhosphorylationPRDEAASTSSTYNFT
CCCCCCCCCCCCCCC		23.2125072903
599PhosphorylationRDEAASTSSTYNFTH
CCCCCCCCCCCCCCC		20.4225072903
600PhosphorylationDEAASTSSTYNFTHY
CCCCCCCCCCCCCCH		34.6925072903
601PhosphorylationEAASTSSTYNFTHYD
CCCCCCCCCCCCCHH		23.4225072903
602PhosphorylationAASTSSTYNFTHYDR
CCCCCCCCCCCCHHH		15.3825072903
605PhosphorylationTSSTYNFTHYDRIQS
CCCCCCCCCHHHHHH		18.8525072903
607PhosphorylationSTYNFTHYDRIQSLL
CCCCCCCHHHHHHHH		12.1225072903
634PhosphorylationRRFLQAVSLMHSEFA
HHHHHHHHHHHHHHH		24.0025072903
638PhosphorylationQAVSLMHSEFAQLPA
HHHHHHHHHHHCCHH		22.0525072903
647PhosphorylationFAQLPALYEMTVRNA
HHCCHHHHHHHCCCH		13.0325072903
650PhosphorylationLPALYEMTVRNASTA
CHHHHHHHCCCHHHH		12.3625072903
697UbiquitinationFSLSGKAKQKLLKHG
CCCCHHHHHHHHHCC		51.99-
702UbiquitinationKAKQKLLKHGVNLL-
HHHHHHHHCCCCCC-		49.07-
710 (in isoform 4)Ubiquitination--
715 (in isoform 4)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 HPS4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HPS4_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 HPS4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HPS4_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614073Hermansky-Pudlak syndrome 4 (HPS4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HPS4_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-355, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND MASSSPECTROMETRY.

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