Basic Information
Name | Beige protein homolog 1 |
Uniprot ID | P25356 |
Systematic gene name | YCR032W |
Standard gene name | BPH1 |
Gene names | BPH1 YCR032W YCR32W YCR591 YCR601 |
Description from SGD | YCR032W BPH1 SGDID:S000000628, Chr III from 179520-186023, Genome Release 64-3-1, Verified ORF, "Protein homologous to Chediak-Higashi syndrome and Beige proteins; both of which are implicated in disease syndromes in human and mouse, respectively, due to defective lysosomal trafficking; mutant phenotype and genetic interactions suggest a role in protein sorting" |
Protein length | 2167 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MNSIINAASK VLRLQDDVKK ATIILGDILI LQPINHEVEP DVENLVQHEL
TKIIQGYPIQ DNMIINSKKG TVEDDLCELN NYTCFALSKS FDLCHDSRNF
NIAQPKRWIQ LLETLTDSVS FAVIVQIILT LSNISLINKQ TLGKLKKLRI
RIFEILSNKN DSWKSTLLQK NLIEWYIFML SVDCTPLELQ NLYLHKELKF
CNGILNSLTL QVSDPRSQNY LQFENTYKLF QIQKSSRINN SFLFYIEFNS
VTSNRIMTIE RHIYLEIKEG QFCISNDNYI IGLFENFEFE AGTLYFIGVL
IDHNNRITLY VDGSMINQLT LFENSICQLS TCELGSMICS IKVYRFYLWD
GLLTEFAINI LQAIGTNYQY TFSKKKEGPE VLSLCQDFLI AKAHLMARPT
TEISSTKYID EIELLEMENI IIDVNPNDIL QDFTESSNFT VKFEESTNSK
NIPEVGKCYF YRSSNLVSKF VSIDSIRLAF LNMTESGSID DLFHHVSHLM
NLLRNIDILN WFKKDFGFPL FAYTLKQKIT QDLSQPLNIQ FFNLFLEFCG
WDFNDISKSI ILDTDAYENI VLNLDLWYMN EDQSSLASGG LEIIRFLFFQ
ISSLMEASIY SKFNSNKFND MNILEKLCLS YQAVTKRENQ NSKFNELSSD
LISVFVTLLK SNTDKRHLQW FLHLSYYFIK RKDVRSTEII LQAVDQLFSF
YLDQGSDENA KILSEIIPLK LILMIMDQIV ENNESNPITC LNILFKVVLT
NKPLFKQFYK NDGLKLILTM LCKVGKSYRE EIISLLLTYS IGNYTTANEI
FSGAEDMIGG ISNDKITAKE IIYLAVNFIE WHVINSNASD SSSVLDLNNH
ILRFVEDLKS LSAVPINESV FDPKKSYVMV SLLDLSIALN ESEDISKFKS
SSKVISELIK GNIMCALTKY AAYDFEVYMS TFFCHSTEYK LVYPKTVMNN
SSYLELSFIV TLLPEILNDL VDSNNNLNLM MLKHPYTMSN LLYFLRKFRP
DTSQIVMPKD FYFSSYTCLL HCVIQIDKSS FYHFKNVSKS QLLQDFKICI
MNLIYSNTLK QIIWEKEEYE MFSESLMAHQ EVLFAHGACD NETVGLLLIF
FANRLRDCGY NKAVFNCMKV IIKNKERKLK EVACFFDPAN KSEVLEGLSN
ILSCNNSETM NLITEQYPFF FNNTQQVRFI NIVTNILFKN NNFSPISVRQ
IKNQVYEWKN ARSEYVTQNN KKCLILFRKD NTSLDFKIKK SISRYTYNLK
TDREENAVFY RNNLNLLIFH LKHTLEIQSN PNSSCKWSSD FAEDFDGMKR
RLLPAWEPKY EPLINEEDAN QDTITGGNRQ RRESGSILSY EFIEHMETLE
SEPVGDLNEN RKILRLLKDN DSIATIWNCS LIIGLEIKEG ILIHGSNYLY
FVSDYYFSLE DKKILKLSEV SQESRDMTVS LINGPDVKRV STFLKHEVFV
WKLLDITFVT KRPFLLRDVA IELLFKERVS AFFSFYNKRV RDDVLRVLNK
IPKHLPADPI FSSVLQEIND RGNSIVARNG IGKASIASKF TSVFSANNSL
IDGFEISKKW VRGEISNFYY LLSINILAGR SFNDLTQYPV FPWVIADYES
NVLDLENPKT YRDLSKPMGA QSEKRKLQFI ERYEALASLE NADSAPFHYG
THYSSAMIVS SYLIRLKPFV ESFLLLQGGS FGPADRLFSS LERAWSSASS
ENTTDVRELT PEFFFLPEFL INVNSYDFGT DQSGKKVDDV VLPPWANGDP
KVFIQKNREA LESPYVSAHL HEWIDLIFGY KQKGDIAVKS VNVFNRLSYP
GAVNLDNIDD ENERRAITGI IHNFGQTPLQ IFQEPHPEKI ACNVQQLTTE
VWRKVPMKPI FEKTIFNLNE KNRSVDYVIH DPSYFDSLYW RGFAFPNLFF
RTEESLVSLR IVHKNWLKIG LDIFKKTHMA QITSFAYWKL GEFITGDKNG
LIKVWKYRKD KHSVSGNLEN KKTMFGHLCE LKEMRCYHDY NTLLTLDISG
LVYVWDMINF ELVRQITNDA QKVAISQHAG SIMVLTKNNA ISIFNLNGQI
YTSKKFEPAK IVSSIDFFDF TKLDAGYRKH IYWKEMEILL VGFEDGTIEI
YELFLNFHNE WAIKLLKQLC TEKGKAITSI KGQGKTYLSQ KRRKDTAEPH
EIEVIAGTLD GRLAIWY
TKIIQGYPIQ DNMIINSKKG TVEDDLCELN NYTCFALSKS FDLCHDSRNF
NIAQPKRWIQ LLETLTDSVS FAVIVQIILT LSNISLINKQ TLGKLKKLRI
RIFEILSNKN DSWKSTLLQK NLIEWYIFML SVDCTPLELQ NLYLHKELKF
CNGILNSLTL QVSDPRSQNY LQFENTYKLF QIQKSSRINN SFLFYIEFNS
VTSNRIMTIE RHIYLEIKEG QFCISNDNYI IGLFENFEFE AGTLYFIGVL
IDHNNRITLY VDGSMINQLT LFENSICQLS TCELGSMICS IKVYRFYLWD
GLLTEFAINI LQAIGTNYQY TFSKKKEGPE VLSLCQDFLI AKAHLMARPT
TEISSTKYID EIELLEMENI IIDVNPNDIL QDFTESSNFT VKFEESTNSK
NIPEVGKCYF YRSSNLVSKF VSIDSIRLAF LNMTESGSID DLFHHVSHLM
NLLRNIDILN WFKKDFGFPL FAYTLKQKIT QDLSQPLNIQ FFNLFLEFCG
WDFNDISKSI ILDTDAYENI VLNLDLWYMN EDQSSLASGG LEIIRFLFFQ
ISSLMEASIY SKFNSNKFND MNILEKLCLS YQAVTKRENQ NSKFNELSSD
LISVFVTLLK SNTDKRHLQW FLHLSYYFIK RKDVRSTEII LQAVDQLFSF
YLDQGSDENA KILSEIIPLK LILMIMDQIV ENNESNPITC LNILFKVVLT
NKPLFKQFYK NDGLKLILTM LCKVGKSYRE EIISLLLTYS IGNYTTANEI
FSGAEDMIGG ISNDKITAKE IIYLAVNFIE WHVINSNASD SSSVLDLNNH
ILRFVEDLKS LSAVPINESV FDPKKSYVMV SLLDLSIALN ESEDISKFKS
SSKVISELIK GNIMCALTKY AAYDFEVYMS TFFCHSTEYK LVYPKTVMNN
SSYLELSFIV TLLPEILNDL VDSNNNLNLM MLKHPYTMSN LLYFLRKFRP
DTSQIVMPKD FYFSSYTCLL HCVIQIDKSS FYHFKNVSKS QLLQDFKICI
MNLIYSNTLK QIIWEKEEYE MFSESLMAHQ EVLFAHGACD NETVGLLLIF
FANRLRDCGY NKAVFNCMKV IIKNKERKLK EVACFFDPAN KSEVLEGLSN
ILSCNNSETM NLITEQYPFF FNNTQQVRFI NIVTNILFKN NNFSPISVRQ
IKNQVYEWKN ARSEYVTQNN KKCLILFRKD NTSLDFKIKK SISRYTYNLK
TDREENAVFY RNNLNLLIFH LKHTLEIQSN PNSSCKWSSD FAEDFDGMKR
RLLPAWEPKY EPLINEEDAN QDTITGGNRQ RRESGSILSY EFIEHMETLE
SEPVGDLNEN RKILRLLKDN DSIATIWNCS LIIGLEIKEG ILIHGSNYLY
FVSDYYFSLE DKKILKLSEV SQESRDMTVS LINGPDVKRV STFLKHEVFV
WKLLDITFVT KRPFLLRDVA IELLFKERVS AFFSFYNKRV RDDVLRVLNK
IPKHLPADPI FSSVLQEIND RGNSIVARNG IGKASIASKF TSVFSANNSL
IDGFEISKKW VRGEISNFYY LLSINILAGR SFNDLTQYPV FPWVIADYES
NVLDLENPKT YRDLSKPMGA QSEKRKLQFI ERYEALASLE NADSAPFHYG
THYSSAMIVS SYLIRLKPFV ESFLLLQGGS FGPADRLFSS LERAWSSASS
ENTTDVRELT PEFFFLPEFL INVNSYDFGT DQSGKKVDDV VLPPWANGDP
KVFIQKNREA LESPYVSAHL HEWIDLIFGY KQKGDIAVKS VNVFNRLSYP
GAVNLDNIDD ENERRAITGI IHNFGQTPLQ IFQEPHPEKI ACNVQQLTTE
VWRKVPMKPI FEKTIFNLNE KNRSVDYVIH DPSYFDSLYW RGFAFPNLFF
RTEESLVSLR IVHKNWLKIG LDIFKKTHMA QITSFAYWKL GEFITGDKNG
LIKVWKYRKD KHSVSGNLEN KKTMFGHLCE LKEMRCYHDY NTLLTLDISG
LVYVWDMINF ELVRQITNDA QKVAISQHAG SIMVLTKNNA ISIFNLNGQI
YTSKKFEPAK IVSSIDFFDF TKLDAGYRKH IYWKEMEILL VGFEDGTIEI
YELFLNFHNE WAIKLLKQLC TEKGKAITSI KGQGKTYLSQ KRRKDTAEPH
EIEVIAGTLD GRLAIWY
Legend
- X Ubiquitination
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[450, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[1334, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[1428, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1428, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1430, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1430, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1484, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |