wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor MAMYB (Membrane-anchored MYB) (Q9ASQ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the regulation of root hair development, possibly through auxin signaling. Its endoplasmic reticulum membrane localization is not compatible with its transcription factor activity in the nucleus. May be cleaved to target the nucleus.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21477080}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000305|PubMed:21477080}. Note=Its endoplasmic reticulum membrane localization is not compatible with its transcription factor activity in the nucleus. May be cleaved to target the nucleus. A truncated form of MAMYB (amino acids 84 to 309) lacking the 2 transmembrane domains is localized to the nucleus. {ECO:0000269|PubMed:21477080}.
Interaction partners:
- Probable pectate lyase 16
- Putative transcription factor bHLH086
Sequence:
MDFFDEDRPRFVFQSRPSSSHTAEEEEEARIPNKLFISISVSISLIILSLSFFYFESEPAKSLLLWLSLSFLVGPFAPSSLTGGKIRVGYGQILEPEQIHDESSTDNERESRRKSVNKRSKGSTKSDNPPENASAVTEVSRKVVIPQSKESGSVNETKDWTAEEIEILKKQLIKHPAGKPGRWETVASAFGGRYKTENVIKKAKEIGEKKIYESDDYAQFLKNRKASDPRLVDENEENSGAGGDAEGTKEIWSNGEDIALLNALKAFPKEAAMRWEKIAAAVPGKSKAACMKRVTELKKGFRSSKTPAN
Protein: Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease) (A0A494C0W0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPALSLNFPRCSFCLLHEVFIACYLAQEDLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFTAPSTVGKRNLSPSQEEAGLEDGVSGEISDTELEQTDSCAEPLSEGRKKAKKLKRMKKELSPAGSISKNSPATLFEVPDTW
Protein: ATP synthase subunit beta (EC 7.1.2.2) (Q6FSH4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit 4
- ATP synthase subunit delta, mitochondrial
- Candida glabrata strain CBS138 chromosome A complete sequence
- ATP synthase subunit gamma
- ATP synthase subunit d
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MVLPRLYAAPSSRAALQAARMASKFNSPVRFASTAALASGKVSAVIGAIVDVQFEESNLPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVVDTGAPISVPVGRETLGRIINVIGEPIDERGPINSKLRKPIHADPPSFAEQSTAAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGDSKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSISELGIYPAVDPLDSKSRLLDAAVVGEEHYNVATKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIEGKLVRLKDTISSFKAVLEGKYDDLPENAFYMVGGIEDVVAKAEKLAAEAS
Protein: Magnesium-chelatase 38 kDa subunit (EC 6.6.1.1) (Mg-protoporphyrin IX chelatase) (P26239)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Function: Involved in bacteriochlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Interaction partners:
- Magnesium-chelatase 60 kDa subunit
- Magnesium-chelatase subunit H
- Magnesium protoporphyrin IX methyltransferase
- Spheroidene monooxygenase
- Geranylgeranyl diphosphate reductase
- Magnesium-chelatase, BchO
- Bacteriochlorophyll synthase 33 kDa chain
- Phytoene synthase
- Ferrochelatase
- Phytoene desaturase
Sequence:
MTTAVARLQPSASGAKTRPVFPFSAIVGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEAVEGCPVSSPNVEMIPDWATVLSTNVIRKPTPVVDLPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGENVVERDGLSIRHPARFVLVGSGNPEEGDLRPQLLDRFGLSVEVLSPRDVETRVEVIRRRDTYDADPKAFLEEWRPKDMDIRNQILEARERLPKVEAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRRDPLDEAGSTARVARTVEETLP
Protein: UDP-glycosyltransferase 71B2 (EC 2.4.1.-) (Protein HYPOSTATIN RESISTANCE 1) (Q9LSY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glucosyltransferase that glucosylates the cell wall inhibitor hypostatin in vivo to form a bioactive glucoside.
Interaction partners:
- CRIB domain-containing protein RIC8
Sequence:
MKLELVFIPSPGDGHLRPLVEVAKLHVDRDDHLSITIIIIPQMHGFSSSNSSSYIASLSSDSEERLSYNVLSVPDKPDSDDTKPHFFDYIDNFKPQVKATVEKLTDPGPPDSPSRLAGFVVDMFCMMMIDVANEFGVPSYMFYTSNATFLGLQVHVEYLYDVKNYDVSDLKDSDTTELEVPCLTRPLPVKCFPSVLLTKEWLPVMFRQTRRFRETKGILVNTFAELEPQAMKFFSGVDSPLPTVYTVGPVMNLKINGPNSSDDKQSEILRWLDEQPRKSVVFLCFGSMGGFREGQAKEIAIALERSGHRFVWSLRRAQPKGSIGPPEEFTNLEEILPEGFLERTAEIGKIVGWAPQSAILANPAIGGFVSHCGWNSTLESLWFGVPMATWPLYAEQQVNAFEMVEELGLAVEVRNSFRGDFMAADDELMTAEEIERGIRCLMEQDSDVRSRVKEMSEKSHVALMDGGSSHVALLKFIQDVTKNIS
Protein: Mediator of RNA polymerase II transcription subunit 21 (Mediator complex subunit 21) (Suppressor of RNA polymerase B 7) (O94376)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 18
Sequence:
MACRCTQLQDTIDEVATQFYSSIHYLSSHHDFVPLPGQEKVSDSKVNPISAEELQFAQRDLAKDLVTKFMQIDTLINQLPGISTAPKHQLEKIKKLQNSIEEKQLERKSLESENEDLKLQLAKRIETFGRLSCVLFQP
Protein: Bromo domain-containing protein (Q57UR8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- TATA box-binding protein-like 1
- Uncharacterized protein
- Uncharacterized protein
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- RNA polymerase-like protein
- [RNA-polymerase]-subunit kinase
- DNA-direcetd RNA polymerase II, subunit 9, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA repair and transcription factor protein, putative
Sequence:
MSGGTSARRAPSCSPWQHLVSVDISNTFCTAFAQHLSTVQNPQEFSETLSTLMCKWRDRKWAEITVPSTSTGGRHFVIPTRRRKDRRSIANGGVENNGFLSENFSNGVPIGDTRRDGAVTAYYESIRVQRLMEEVLLLSSEVEAEREAELIKLGEVEGMKAQRRAWRRRCCLTRAVDELWRFSCTGGSDFLLPVTELEAPNYYQRVRRPVSLSTLYCSVWDATVADYADLKALLTLMSCNCEHYNGSDSILAAQCRKLVKIGYRAVRDAETYEKQQLEADQELFSTLCGQDTVGCGPRTGTGTGVLRRMMDANGDGISMEPLPADELAALFPSRYQAACDGAVQSADEKLVCDANGSRTDDTVSHQVNNGGRRLVLRRKPPVQSTENGKDAPVPAHADPSGKPPRPRLRLSLVSSTSTKTETRPSGGSEGEGGGILDEDDVWEKPDRVSSRQKEGAAISISSKSSQVLRAKHGRKSLKKEKESRRRVGQADLRRKKEKSDHERRQKPPKVKREKADRGSRISKVKSGRLGGRDNGKDSKRSKRRLEEYSSTEMLSPLPTSSSTSSSYYSSSSTSSSDDSDTFTRRAPPSISVERLGELEAMMNKLDKMPLQQDTIEEVILTLKRVENELN
Protein: Adenosylcobinamide-GDP ribazoletransferase (EC 2.7.8.26) (Cobalamin synthase) (Cobalamin-5'-phosphate synthase) (P36561)
Organism: Escherichia coli (strain K12)
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate (By similarity).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Bifunctional adenosylcobalamin biosynthesis protein CobU
- Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase
- Adenosylcobalamin/alpha-ribazole phosphatase
- Corrinoid adenosyltransferase
- Corrinoid adenosyltransferase EutT
- Inner membrane protein YbbJ
- Methionine synthase
Sequence:
MSKLFWAMLSFITRLPVPRRWSQGLDFEHYSRGIITFPLIGLLLGAISGLVFMVLQAWCGAPLAALFSVLVLVLMTGGFHLDGLADTCDGVFSARSRDRMLEIMRDSRLGTHGGLALIFVVLAKILVLSELALRGESILASLAAACAVSRGTAALLMYRHRYAREEGLGNVFIGKIDGRQTCVTLGLAAIFAAVLLPGMHGVAAMVVTMVAIFILGQLLKRTLGGQTGDTLGAAIELGELVFLLALL
Protein: Peroxiredoxin 6005 (EC 1.11.1.-) (Q9VQI7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutathione peroxidase
- Glutathione peroxidase
- Glutathione S transferase O3
- Pyrimidodiazepine synthase
- RE13973p
- Gamma-glutamyl transpeptidase, isoform A
- Uncharacterized protein, isoform C
- glutathione-specific gamma-glutamylcyclotransferase
- glutathione-specific gamma-glutamylcyclotransferase
- Glutathione S-transferase S1
Sequence:
MSGKALNIGDQFPNFTAETSEGRIDFYDWMQDSWAILFSHPADFTPVCTTELSRVAALIPEFQKRGVKPIALSCDTVESHKGWIEDIKSFGKLSSFDYPIIADDKRELALKFNMLDKDEINAEGIPLTCRAVFVVDDKKKLRLSILYPATTGRNFDEILRVIDSLQLTQTKSVATPADWKQGGKCMVLPTVKAEDVPKLFPDGIETIELPSGKSYLRITPQP
Protein: V-type proton ATPase subunit a (Q59R99)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- V-type proton ATPase subunit C
- H
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B
- H
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit
- V-type proton ATPase subunit G
Sequence:
MPEKEEAVFRSADMSLVQLYVPTEVARDIIYKVGQLDIIQFRDLNSKINEFQRSFVKELRKLDNVERQFNLFKRELDVRDIPIKLFPYDLDNVPPQTEIDELIEGSDLLEERVIQLRDSVETLYEKEKYLKQFKYTIQAVNNFFAVQGETTNDNEETALLSQLESGGATSGGGGDARSGSSFISGVINRDKVGVLQQILWRVLRGNLYYHNEDLPEEIYDFKNNTYVAKSSFIIFSHGSLIRERIRKICESLDAELYNVDSTSALRREQLDDVNTKTTDLSTVLGESENALNSELIAISRDLAKWWEIIAREKAVYKAMNNCDYDNSRKTLIAEGWTPTDSITELTTAIQEYDASQSVPTIINVLDTNKTPPTYTRTNKFTYAFQAICDAYGVPKYKEINPGLPTIVTFPFMFAIMFGDLGHGFIVTLAAAALVLNEKKLNAMKKDEIFDMAYTGRYVLLLMGVFSMYTGFIYNDVFSRSMSIFKSGWEWPEKFNVGETIYAKYVGTYSIGLDPAWHGTENALLFSNSYKMKLSILMGYIHMSYSYVFSLVNYTYFNSMIDVIGNFIPGLLFMQGIFGYLSLCIVYKWSVDWFATGRQPPGLLNMLINMFLQPGDVPEPLYSGQSTIQVFLLLIALICVPWLLLVKPLYMKRQLEKEANQHHGSYSQLANDEESGVAGQEQEQENAAEDDDEDHEEHNFGDIMIHQVIHTIEFCLNCVSHTASYLRLWALSLAHAQLSTVLWSMTIGNAFGPTGLIGTFMVVFLFAMWFVLSVCILVVMEGTSAMLHSLRLHWVESMSKYFEGGGSAFEPFTFKGLLDSVL
Protein: Transcription factor AP-2-alpha (AP-2 transcription factor) (Activating enhancer-binding protein 2-alpha) (Activator protein 2) (Q6NYI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLVHSFSAMDRHDGTSNGTARLPQLGSVGQSPYTSAPPLSHTPNSDFQPPYFPPPYQPIYPQSQDPYSHVNDPYSINSLHAQSQPQHPGWPGQRQSQESSLLHQHRGLPHQLCREYRREVLLPSGHGIDTGLTDSIPIHGIPHSLEDVQQVEDQGIHIPDQTVIKKGPVSISKNNSNISAIPINKDGLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAIAEYMNRQHSDPNEQVQRKNMLLATKQICKEFTDLLSQDRSPLGNSRPQPILEPGIQSCLTHFSLISHGFGTPAVCAALTALQNYLTEAIKAMDKMYLNNNPNSHSETGSKAGDKDEKHRK
Protein: Fcgbp protein (Q7TNG6)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
TVAGQVVGLARGPQVTVDGEVVTLPVATGHVSVTAEGRNIVLQTNKGMKVLFDGDAHILMSIPSSFRGRLCGLCGNFNGNWSDDFVLPSGAVAPNVEAFGTAWRAPGSSLGCGEGCGPQGCPVCLAEETQAYEKNDACGKIRDPHGPFAACHKVLSPLEYFRQCVYDMCAHKGDKAYLCRSLAAYTAACQAAGAAVKPWRTDSVCPLQCPAHSHYSICTRSCQGSCAALSGLTGCTTRCFEGCECDDHFLLSHGVCIPAQDCGCVHNGQYMPVNSSLMSSDCSERCFCSPNNGLTCHEAGCPSGHVCEIQAGVRECQAARGLCSISVGANLTTFDGAHNAISSPGVYELSSRCPGLQKNVPWYRVLADVQPCHNNDKIVSKVHIFFQDGLVTVIPSKGAWVNGLRVDLPATVLTSVSVRRMPDGSMLVHQKAGVTVWLGKDGLLDVMVGDDLAAMLCGACGNFDGDQTNDAYGSQGKTPIEKWRAQDFSPCSN
Protein: Probable proline-specific permease put4 (Q9URZ3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for high-affinity proline transport. May be responsible for proline recognition and probably also for proline translocation across the plasma membrane. Also functions as non-specific GABA permease. Can also transport alanine and glycine (By similarity).
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized transporter PB1C11.03
- Sexual differentiation process protein isp7
- Ribose-phosphate pyrophosphokinase 1
Sequence:
MDEKKALQYEESKRAEEITDIELVSVGGIDVEKKYGETKRALKSRHVQLIAIGGCIGTGLFVGSGSALSESGPASLFLSYVIMSFVIWTVMNALGEMCTYLPLSGASPITYIERYVDASLAFAAGWNYWYAYVFLVASEVTAASIVIEYWTYAVPTAGWIAILLFLVAVLNSFFVKWFGETEFWFAIIKVIAIVGLIILGVVIFFGGTPKHDRLGFRYWKHGLAFREYIVKGASGRFVGFWSAVIKSGFAFILAPELVIFSAGETEAPRRNIPKATSRFIYRLIFFYIFGSLTIGVITSSKDPRLLNAISSGASGAAASPFVIGIQNAEIPVLNHIINAVILTSACSSGNSFLFAGSRSIYSLAKEHQAPKIFKYCNRWGVPVISVAVTVLFACLAFLNASASAAVVFNWFCNLSTISGFLAWICVLVAYLQFRKAMILNNLWETRPYKTPFQPYATYLTLFLLALITLTNGFTVFVGHTFTAGNFIAAYITLPIFLVLYVAHKLWSRNWSFGKRIEEIDVTTGVAEAEALEQMYPAPVPRNIIEKIWFWIA
Protein: Guanine nucleotide-binding protein alpha-1 subunit (GP1-alpha) (P08539)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) that mediates mating pheromone signal transduction. Binding of alpha-factor or a-factor to its cognate transmembrane receptor STE2 and STE3, respectively, allows the receptor to serve as a guanine nucleotide exchange factor (GEF) on GPA1. The exchange of GDP for GTP on the G protein alpha subunit alters its interaction with the G protein beta subunit STE4, leading to dissociation of the G protein beta-gamma dimer STE4-STE18. The dissociated subunits activate downstream effectors to activate the mating response pathway and induce changes necessary to produce mating-competent cells. STE4-STE18 activate the downstream pheromone signaling MAP kinase cascade leading to expression of mating-specific genes, inducing cell cycle arrest in G1, promoting polarized cell growth to form mating projections (shmoos), and establishing the changes in plasma membrane, cell wall and nuclear envelope to permit cell-cell fusion (plasmogamy) and fusion of the two haploid nuclei (karyogamy). GPA1 transmits a signal that requires direct binding to the effector enzyme PI3K located at the endosome, promoting increased PI3 production. The intrinsic GTPase activity of GPA1 determines the duration of signaling, and is dramatically accelerated by the RGS protein SST2. In unstimulated cells, GDP-bound GPA1 sequesters the G protein beta-gamma subunit STE4-STE18, preventing it from activating the downstream effectors. Also down-regulates the signal by inhibiting the pheromone-induced accumulation of FUS3 in the nucleus.
Subcellular location: Cell membrane; Lipid-anchor; Cytoplasmic side. Endosome membrane; Lipid-anchor; Cytoplasmic side. Note=Localizes predominantly to the plasma membrane in its inactive, GDP-bound form, and is directed to endosomes once in its active, GTP-bound form. Concentrates at the tip of the mating projections.
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Protein SST2
- Guanine nucleotide-binding protein subunit beta
- Pheromone alpha factor receptor
- Mitogen-activated protein kinase FUS3
- Pheromone a factor receptor
- Serine/threonine-protein kinase STE11
- Protein STE5
- Serine/threonine-protein kinase STE7
- Regulator of G-protein signaling 2
Sequence:
MGCTVSTQTIGDESDPFLQNKRANDVIEQSLQLEKQRDKNEIKLLLLGAGESGKSTVLKQLKLLHQGGFSHQERLQYAQVIWADAIQSMKILIIQARKLGIQLDCDDPINNKDLFACKRILLKAKALDYINASVAGGSDFLNDYVLKYSERYETRRRVQSTGRAKAAFDEDGNISNVKSDTDRDAETVTQNEDADRNNSSRINLQDICKDLNQEGDDQMFVRKTSREIQGQNRRNLIHEDIAKAIKQLWNNDKGIKQCFARSNEFQLEGSAAYYFDNIEKFASPNYVCTDEDILKGRIKTTGITETEFNIGSSKFKVLDAGGQRSERKKWIHCFEGITAVLFVLAMSEYDQMLFEDERVNRMHESIMLFDTLLNSKWFKDTPFILFLNKIDLFEEKVKSMPIRKYFPDYQGRVGDAEAGLKYFEKIFLSLNKTNKPIYVKRTCATDTQTMKFVLSAVTDLIIQQNLKKIGII
Protein: Aspartate-beta-hydroxylase (A0A096MJA9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004157}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004157}.
Interaction partners:
Sequence:
MAPRKNAKGGGGNSSSSGSGSGSGSPSTGSSGSSSSPGARREAKHGGHKNGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLGLKERSTSERTFPPEEAETQAELEEQAPEGAEAQNVEDEVKEQIQSLLQESVHTDHDLEADGPAGEPQSEVEDFLTATDSDDRFEALEPGTVHEDTEDSYHVEETASQNHPNDAEEVMSEQESSEEVRHEDYDEPVYEPSENERIEISDNAIDDSNIISEEINVASVEEQQDTPPVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAASLPDAPTDLVKLSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPRETGYTELVKSLERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCTLLEKFSETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETRSWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
Protein: 2-hydroxy-palmitic acid dioxygenase mpo1 (EC 1.14.18.12) (Metabolism of phytosphingosine to odd-numbered fatty acids protein 1) (Metabolism of PHS to odd-numbered FA protein 1) (O13737)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Dioxygenase that catalyzes the alpha-oxidation of 2-hydroxy fatty acids in an iron-dependent manner (By similarity). Involved in metabolism of phytosphingosine and is required for proper endoplasmic reticulum stress response (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MTYLSRSYSFYAAYHSNPVNIKIHQVCIPLLLLTALVLLHNFVITLINSKLQINVAHLVGLAYQIFYVTLDPLDGLLYSPVLYLFSYILPSKLFTIFSRSLVNRSAAVVHVICWILQFIGHGVFEKRKPALLDNLIQSLFIAPLFAFLETGPFVGYYPSVVSKIRANIKLKDVGENYPNLSEFLFPPSMVEDAVSGVVEDASQLSYCIRPLRLSDIDDGIVF
Protein: Sv2b protein (Q8JZZ9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
PFWSRKVELINRQLMNSTFLEQKEGCHMDFEEDNDFLIYLVSFLGSLSVLPGNIISALLMDRIGRLKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTNQRATAFGILNGLCKFGAILGNTIFASFVGITKVVPILLAAASLVGGGLIALRLPETREQVLM
Protein: Nuclear transcription factor Y subunit A-4 (AtNF-YA-4) (Q8VY64)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit B-3
- Nuclear transcription factor Y subunit C-2
- Nuclear transcription factor Y subunit B-2
- bZIP transcription factor 28
- Nuclear transcription factor Y subunit C-3
- Nuclear transcription factor Y subunit C-9
- Nuclear transcription factor Y subunit B-6
- Nuclear transcription factor Y subunit C-1
- Nuclear transcription factor Y subunit B-1
- Nuclear transcription factor Y subunit C-4
Sequence:
MTSSVHELSDNNESHAKKERPDSQTRPQVPSGRSSESIDTNSVYSEPMAHGLYPYPDPYYRSVFAQQAYLPHPYPGVQLQLMGMQQPGVPLQCDAVEEPVFVNAKQYHGILRRRQSRAKLEARNRAIKAKKPYMHESRHLHAIRRPRGCGGRFLNAKKENGDHKEEEEATSDENTSEASSSLRSEKLAMATSGPNGRS
Protein: Sodium/glutamate symporter (Glutamate permease) (P0AER8)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the sodium-dependent, binding-protein-independent transport of glutamate.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02062, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:17269795, ECO:0000269|PubMed:17662058, ECO:0000269|PubMed:2537813}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02062, ECO:0000269|PubMed:17269795, ECO:0000269|PubMed:17662058}.
Interaction partners:
- Proton/glutamate-aspartate symporter
- Protein GltF
- Glutamate/aspartate import solute-binding protein
Sequence:
MFHLDTLATLVAATLTLLLGRKLVHSVSFLKKYTIPEPVAGGLLVALALLVLKKSMGWEVNFDMSLRDPLMLAFFATIGLNANIASLRAGGRVVGIFLIVVVGLLVMQNAIGIGMASLLGLDPLMGLLAGSITLSGGHGTGAAWSKLFIERYGFTNATEVAMACATFGLVLGGLIGGPVARYLVKHSTTPNGIPDDQEVPTAFEKPDVGRMITSLVLIETIALIAICLTVGKIVAQLLAGTAFELPTFVCVLFVGVILSNGLSIMGFYRVFERAVSVLGNVSLSLFLAMALMGLKLWELASLALPMLAILVVQTIFMALYAIFVTWRMMGKNYDAAVLAAGHCGFGLGATPTAIANMQAITERFGPSHMAFLVVPMVGAFFIDIVNALVIKLYLMLPIFAG
Protein: Thiamine transporter ThiT (Thiamine ECF transporter S component ThiT) (A2RI47)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Function: Probably a thiamine-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21135102}; Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
Interaction partners:
- Biotin transporter BioY
- Riboflavin transporter RibU
- Energy-coupling factor transporter transmembrane protein EcfT
- Energy-coupling factor transporter ATP-binding protein EcfA2
- Energy-coupling factor transporter ATP-binding protein EcfA1
- Pantothenic acid transporter PanT
- Niacin transporter NiaX
- Cys-tRNA
- Thiamine precursor transporter HmpT
- Aminopyrimidine aminohydrolase
Sequence:
MSNSKFNVRLLTEIAFMAALAFIISLIPNTVYGWIIVEIACIPILLLSLRRGLTAGLVGGLIWGILSMITGHAYILSLSQAFLEYLVAPVSLGIAGLFRQKTAPLKLAPVLLGTFVAVLLKYFFHFIAGIIFWSQYAWKGWGAVAYSLAVNGISGILTAIAAFVILIIFVKKFPKLFIHSNY
Protein: T-box transcription factor TBX5 (T-box protein 5) (P70326)
Organism: Mus musculus (Mouse)
Function: DNA-binding protein that regulates the transcription of several genes and is involved in heart development and limb pattern formation. Binds to the core DNA motif of NPPA promoter.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99593, ECO:0000255|PROSITE-ProRule:PRU00201}. Cytoplasm {ECO:0000250|UniProtKB:Q99593}. Note=Shuttles between the cytoplasm and the nucleus. Acetylation at Lys-339 promotes nuclear retention. {ECO:0000250|UniProtKB:Q99593}.
Interaction partners:
- Homeobox protein Nkx-2.5
- Transcription factor GATA-4
- Catenin beta-1
- Transcriptional coactivator YAP1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
- WW domain-containing transcription regulator protein 1
- Myocyte-specific enhancer factor 2C
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Heart- and neural crest derivatives-expressed protein 2
- Myosin-6
Sequence:
MADTDEGFGLARTPLEPDSKDRSCDSKPESALGAPSKSPSSPQAAFTQQGMEGIKVFLHERELWLKFHEVGTEMIITKAGRRMFPSYKVKVTGLNPKTKYILLMDIVPADDHRYKFADNKWSVTGKAEPAMPGRLYVHPDSPATGAHWMRQLVSFQKLKLTNNHLDPFGHIILNSMHKYQPRLHIVKADENNGFGSKNTAFCTHVFPETAFIAVTSYQNHKITQLKIENNPFAKGFRGSDDLELHRMSRMQSKEYPVVPRSTVRHKVTSNHSPFSSETRALSTSSNLGSQYQCENGVSGPSQDLLPPPNPYPLAQEHSQIYHCTKRKDEECSSTEHPYKKPYMETSPSEEDTFYRSGYPQQQGLSTSYRTESAQRQACMYASSAPPSEPVPSLEDISCNTWPSMPSYSSCTVTTVQPMDRLPYQHFSAHFTSGPLVPRLAGMANHGSPQLGEGMFQHQTSVAHQPVVRQCGPQTGLQSPGGLQPPEFLYTHGVPRTLSPHQYHSVHGVGMVPEWSENS