P38735

Name	ABC transporter ATP-binding protein/permease VMR1 (Vacuolar multidrug resistance protein 1)
Uniprot ID	P38735
Systematic gene name	YHL035C
Standard gene name	VMR1
Gene names	VMR1 YHL035C
Description from SGD	YHL035C VMR1 SGDID:S000001027, Chr VIII from 32756-27978, Genome Release 64-3-1, reverse complement, Verified ORF, "Vacuolar membrane protein; involved in multiple drug resistance and metal sensitivity; ATP-binding cassette (ABC) family member involved in drug transport; potential Cdc28p substrate; induced under respiratory conditions; VMR1 has a paralog, YBT1, that arose from the whole genome duplication"
Protein length	1592
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MGTDPLIIRN NGSFWEVDDF TRLGRTQLLS YYLPLAIIAS IGIFALCRSG
LSRYVRSAEC DLVNEYLFGA QEERKEDNSI ERLLRNSNTQ ANYVNVKKQG
RILKLRHFDI TTIDVKQIDA KNHGGLTFSR PSTSDHLRKS SEIVLMSLQI
IGLSFLRVTK INIELTNRDV TTLLLFWLIL LSLSILRVYK RSTNLWAICF
TAHTTIWIST WIPIRSVYIG NIDDVPSQIF YIFEFVITST LQPIKLTSPI
KDNSSIIYVR DDHTSPSREH ISSILSCITW SWITNFIWEA QKNTIKLKDI
WGLSMEDYSI FILKGFTRRN KHINNLTLAL FESFKTYLLI GMLWVLVNSI
VNLLPTILMK RFLEIVDNPN RSSSCMNLAW LYIIGMFICR LTLAICNSQG
QFVSDKICLR IRAILIGEIY AKGLRRRLFT SPKTSSDSDS ISANLGTIIN
LISIDSFKVS ELANYLYVTV QAVIMIIVVV GLLFNFLGVS AFAGISIILV
MFPLNFLLAN LLGKFQKQTL KCTDQRISKL NECLQNIRIV KYFAWERNII
NEIKSIRQKE LRSLLKKSLV WSVTSFLWFV TPTLVTGVTF AICTFVQHED
LNAPLAFTTL SLFTLLKTPL DQLSNMLSFI NQSKVSLKRI SDFLRMDDTE
KYNQLTISPD KNKIEFKNAT LTWNENDSDM NAFKLCGLNI KFQIGKLNLI
LGSTGSGKSA LLLGLLGELN LISGSIIVPS LEPKHDLIPD CEGLTNSFAY
CSQSAWLLND TVKNNIIFDN FYNEDRYNKV IDACGLKRDL EILPAGDLTE
IGEKGITLSG GQKQRISLAR AVYSSAKHVL LDDCLSAVDS HTAVWIYENC
ITGPLMKNRT CILVTHNVSL TLRNAHFAIV LENGKVKNQG TITELQSKGL
FKEKYVQLSS RDSINEKNAN RLKAPRKNDS QKIEPVTENI NFDANFVNDG
QLIEEEEKSN GAISPDVYKW YLKFFGGFKA LTALFALYIT AQILFISQSW
WIRHWVNDTN VRINAPGFAM DTLPLKGMTD SSKNKHNAFY YLTVYFLIGI
IQAMLGGFKT MMTFLSGMRA SRKIFNNLLD LVLHAQIRFF DVTPVGRIMN
RFSKDIEGVD QELIPYLEVT IFCLIQCASI IFLITVITPR FLTVAVIVFV
LYFFVGKWYL TASRELKRLD SITKSPIFQH FSETLVGVCT IRAFGDERRF
ILENMNKIDQ NNRAFFYLSV TVKWFSFRVD MIGAFIVLAS GSFILLNIAN
IDSGLAGISL TYAILFTDGA LWLVRLYSTF EMNMNSVERL KEYSSIEQEN
YLGHDEGRIL LLNEPSWPKD GEIEIENLSL RYAPNLPPVI RNVSFKVDPQ
SKIGIVGRTG AGKSTIITAL FRLLEPITGC IKIDGQDISK IDLVTLRRSI
TIIPQDPILF AGTIKSNVDP YDEYDEKKIF KALSQVNLIS SHEFEEVLNS
EERFNSTHNK FLNLHTEIAE GGLNLSQGER QLLFIARSLL REPKIILLDE
ATSSIDYDSD HLIQGIIRSE FNKSTILTIA HRLRSVIDYD RIIVMDAGEV
KEYDRPSELL KDERGIFYSM CRDSGGLELL KQIAKQSSKM MK

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[129, 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)
[825, 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)
[825, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)