wanglab/gogpt-training-data huggingface dataset:
Protein: L-2-hydroxyglutarate dehydrogenase, mitochondrial (EC 1.1.99.2) (Duranin) (Q9H9P8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16005139}.
Interaction partners:
- D-2-hydroxyglutarate dehydrogenase, mitochondrial
- Citrate synthase, mitochondrial
- Fumarate hydratase, mitochondrial
- Glutamate dehydrogenase 1, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Glutamate dehydrogenase 2, mitochondrial
- Glutamine synthetase
- Glutaminase liver isoform, mitochondrial
- Glutaminase kidney isoform, mitochondrial
Sequence:
MVPALRYLVGACGRARGLFAGGSPGACGFASGRPRPLCGGSRSASTSSFDIVIVGGGIVGLASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALLYEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCRGLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPIVIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNIYPVPDSRFPFLGVHFTPRMDGSIWLGPNAVLAFKREGYRPFDFSATDVMDIIINSGLIKLASQNFSYGVTEMYKACFLGATVKYLQKFIPEITISDILRGPAGVRAQALDRDGNLVEDFVFDAGVGDIGNRILHVRNAPSPAATSSIAISGMIADEVQQRFEL
Protein: X-linked lymphocyte-regulated 4A (A2BI41)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MASKIKGRPPKQPKVTPALPSDDSQQLHENNPGNNLALETCGESSSSHGTGGPKPGPSKKTLNERKRKYGVSVNKTVQNIEWNVDHFLKVQHERRQELYKDYSHQFLTLVMMWNIDVDQIKKQAGKLSDILDEQQKLFQQFQSIHMQKIEEFKELCDRHLKNLQAIKCCRRKAIIEEARKLMDYLEKTVTEE
Protein: Single-stranded DNA-binding protein (Q8I415)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- DNA topoisomerase
- 40S ribosomal protein S5, putative
- 3'-5' exonuclease
- Large ribosomal subunit protein bL21m
- Ribosomal protein L21, apicoplast, putative
- Eukaryotic translation initiation factor 4C
Sequence:
MGKRMLCIVFPLLIYFNYVLHRTYGYIIGDVKVHQLNNIINKRIIKSRKISMFKINLQNDFNYENKRFYNNMNRNVMNEKSLNKIMLIGRVGCEPDIKILNGGDKVATFSLATNEFWRDRNTNELKSKTDWHRIVVYDQNIVDLIDKYLRKGRRVYVQGSLHTRKWHTNDMNSQPKQITEIILSYNKGDLIFLDDKRNFNQRNNSNNINSENQQHINNEHINNNNINNGNDFMPLNSNDKIIEDKEFTDRLDDNNEENNFQSNSETFDKQEGIYDKMNVQEFEE
Protein: Annexin A6 (Annexin VI) (Annexin-6) (P79134)
Organism: Bos taurus (Bovine)
Function: May associate with CD21. May regulate the release of Ca(2+) from intracellular stores.
Subcellular location: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}.
Interaction partners:
- Protein kinase C alpha type
Sequence:
MAKPAQGAKYRGSIRDFPDFNPSQDAETLYNAMKGFGSDKEAILELITSRSNRQRQEICQNYKSLYGKDLIADLKYELTGKFERLIVGLMRPPAYADAKEIKDAISGIGTDEKCLIEILASRTNEQIHQLVAAYKDAYERDLEADITGDTSGHFRKMLVVLLQGTREEDDVVSEDLVQQDVQDLYEAGELKWGTDEAQFIYILGNRSKQHLRLVFDEYLKTTGKPIEASIRGELSGDFEKLMLAVVKCIRSTAEYFAERLFKAMKGLGTRDNTLIRIMVSRSELDMLDIREIFRTKYEKSLYSMIKNDTSGEYKKTLLKLCGGDDDAAGQFFPEAAQVAYQMWELSAVARVELKGTVRPAGDFNPDADAKALRKAMKGLGTDEDTIIDIIAHRSNAQRQQIRQTFKSHFGRDLMADLKSELSGDLARLILGLMMPPAHYDAKQLKKAMEGAGTDEKALIEILATRTNAEIQAINKAYKEDYHKSLEDALSSDTSGHFKRILISLATGNREEGGEDRERAREDAQVAAEILEIADTTSGDKSSLETRFMMILCTRSYPHLRRVFQEFIKMTNYDVEHTIKKEMSGDVRDVFVAIVQSVKNKPLFFADKLYKSMKGAGTDEKTLTRIMVSRSEIDLLNIRREFIEKYDKSLHQAIEGDTSGHFLKALLAICGGED
Protein: Outer dense fiber protein 2 (Cenexin) (Outer dense fiber of sperm tails protein 2) (A0A024R8A5)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}.
Interaction partners:
Sequence:
MKDRSSTPPLHVHVDENTPVHVHIKKLPKPSATSSQKSHKRGMKGDTVNVRRSVRVKTKNPPHCLEITPPSSEKLVSVMRLSDLSTEDDDSGHCKMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERMKEEKDFTILQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGALLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRSKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKESLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKEKGDLELEIIVLNDRVTDLVNQQQTLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKILKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSLKVDELERKLEATSAQNIEFLQVIAKREEAIHQSQLRLEEKTRECGTLARQLESAIEDARRQVEQTKEHALSKERAAQNKILDLETQLSRTKTELSQLRRSRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKSSYANVFGDGPYSTFLTSSPIRSRSPPA
Protein: Sideroflexin-3 (Q9JHY2)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial serine transporter that mediates transport of serine into mitochondria, an important step of the one-carbon metabolism pathway. Mitochondrial serine is converted to glycine and formate, which then exits to the cytosol where it is used to generate the charged folates that serve as one-carbon donors.
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BWM7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGDLPLNINIQEPRWDQSTFLGRARHFFTVTDPRNLLLSGKQLEASRNIVQNYRAGVVTPGLTEDQLWRAKYVYDSAFHPDTGEKVVLIGRMSAQVPMNMTITGCMLTFYRKTPTMVFWQWVNQSFNAIVNYSNRSGDAPITVQQLGTAYVSATTGAVATALGLKSLTKHLPPLVGRFVPFAAVAAANCINIPLMRQRELQVGIPVTDEAGQRLGHSVTAAKQGIFQVVVSRIGMAIPAMAIPPVIMNTLEKKDFLKRRPWLGAPLQVGLVGFCLVFATPLCCALFPQRSSIHVTRLEPELRAQIQAQKPSIDVVYYNKGL
Protein: Autophagy-related protein 22 (P25568)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Vacuolar effluxer which mediate the efflux of leucine and other amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17021250}; Multi-pass membrane protein {ECO:0000269|PubMed:17021250}. Note=Vacuole and punctate structures.
Interaction partners:
- Vacuolar amino acid transporter 3
- Vacuolar amino acid transporter 4
- Putative lipase ATG15
- Autophagy-related protein 8
- Ubiquitin-like modifier-activating enzyme ATG7
- Tryptophan synthase
- Serine/threonine-protein kinase ATG1
- Autophagy-related protein 9
- Autophagy-related protein 3
- Endoplasmic reticulum chaperone BiP
Sequence:
MSYGTINDMNESVTNYRIKKAQNNIKGWYAYSFSSEPFVVSAVSTYIPLLLQQFASINGVKVHDHSIPCLSETGSDSDKCVLGLFNNRIFVDTSSFALYVFSLSVLFQTIIVISVSGIVDLWGSVKFKGRILVWFGIVGALSTVAISKLNDTQIYSLAGLYIVANGCFGVINVVGNSLLPIFVKDSLKCQSQGAYEPDKVDSLTTVISGRGASLGYSSALIVQIVSMFLVASKKGSKQDVQVAVLFVGIWWFVWQLPMIWLIDDVTIPIRVDDSTLASARSPYPGEQDALGQLNWKNYLSYGWVSLFESFKHARLLKDVMIFLIAWFIISDSITTINSTAVLFSKAELHMSTLNLIMISVLTVVNAMLGAFMIPQFLATKFRWTSSQTLMYIIIWASFIPFYGILGFFFNAFGLKHKFEMFLLAIWYGLSLGGLSAVSRSVFSLIVPPGKESTFFSMFSITDKGSSILGPFLVGLLTDKTHNIRYSFYFFFLLLMLSLPVLNCLDVKRGRREAEELSQVLPESERRLD
Protein: Catechol O-methyltransferase A (EC 2.1.1.6) (F4ZGF2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Shows highest activity towards catecholestrogens and dobutamine. Also has lower activity towards L-DOPA, dopamine and epinephrine. Active towards the xenobiotic compounds methyl-DOPA, carbidopa, isoproterenol, and apomorphine.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Amine oxidase [flavin-containing]
- Amine oxidase.
- Aromatic-L-amino-acid decarboxylase
- Dopamine beta-hydroxylase
- Uncharacterized protein.
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Cytochrome P450 1A
- Cytochrome P450 1A
- Transmembrane O-methyltransferase homolog
Sequence:
MLWVVLAVVVVLASVLVLLRQSSGLLALLWHDVVHQRLLNFFTGLSRPQRILKAVQKNATKGNPESVIAAIDHYCRHSEWAMNVGDEKGLILDSVVTEVNPSTALELGTYCGYSTVRIARLLSPGTKLITLEFNPDYAAIARQIIAYAGLQDKVILVEGPSGDLIPKMKQQHGIKSFDFVFLDHWKDRYVPDTKLLEECGLLRKGSVLLADNVICPGTPEYLKYVRNDPRYESRYFKSNLEYTKVEDGLEKSVFLG
Protein: Oligosaccharyltransferase complex subunit OSTC (Hydrophobic protein HSF-28) (Q9NRP0)
Organism: Homo sapiens (Human)
Function: Specific component of the STT3A-containing form of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:21768116}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Protein transport protein Sec61 subunit gamma
Sequence:
METLYRVPFLVLECPNLKLKKPPWLHMPSAMTVYALVVVSYFLITGGIIYDVIVEPPSVGSMTDEHGHQRPVAFLAYRVNGQYIMEGLASSFLFTMGGLGFIILDRSNAPNIPKLNRFLLLFIGFVCVLLSFFMARVFMRMKLPGYLMG
Protein: ABC transporter A family member 7 (ABC transporter ABCA.7) (AtABCA7) (Probable ABC2 homolog 6) (Q9STT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ABC transporter D family member 2, chloroplastic
- ABC transporter C family member 7
- Probable inactive receptor kinase At2g26730
- ABC transporter C family member 6
Sequence:
MADPGPASFSTRANALLRKNLTYQKRNLWSNIRLIMIPFYLCILLVIIQILFDTQVNNSADNRCGCECIERNRAGKCQRELCGLEHSKPDQAFFCSIPRPPLWPPLLQIPRPESRDVRGLRDDSCRRTGSCPVTILFTGNNRSLGTTVSENLFTSSVSANASEILRTLANNVLGTTVEADFTNYLDPGIASNLSIYNIQPRCILNATFPFSFEQPPLKFEKELRCVQGSNLWTNTSKEVNDKIFKGYKKGNPEGKINEIAAAYDLLNTDRNNFNVHIWYNSTYKDDAGNRLIKLIRVPRSVNLVSNAYLQFLQGPGTRMLFEYVKEMPKPETSLRLDIASLIGPLFFTWVILLLFPVILSSLVYEKQQHLRIIMKMHGLGDGPYWMISYAYFLTISVLYVICLMIFGSAIGLKFFRLNSYSIQFVFYFLYLNLQIALAFLVSSVFSKVKTSTVASYIYVFGSGLLGLFLLNFLIEDSSFPRGWIIVMELYPGFSLYRGLYELAQFAFRGNLRGEDGMKWKDFGDSAMDDVFYIIVVEWFLALIAAYYIDKISSSGRNPLFFLQNPFKKSPSLRRPSLQRQGSKVSVDMEKPDVTHESKKVERLMLESSTSHAIVCDNLKKVYPGRDGNPPKLAVRGLSLAVPSGECFGMLGPNGAGKTSFINMMTGLLKPTSGTALVQGLDICNDMDRVYTSMGVCPQHDLLWETLTGREHLLFYGRLKNLKGADLNQAVEESLKSVNLFHGGVADKPAGKYSGGMKRRLSVAISLIGNPKVVYMDEPSTGLDPASRKNLWTVIKRAKQNTAIILTTHSMEEAEFLCDRLGIFVDGGLQCIGNPKELKGRYGGSYVFTMTTSSEHEQNVEKLIKDVSPNAKKIYHIAGTQKFELPKEEVRISEVFQAVEKAKSNFTVFAWGLADTTLEDVFIKVVRNGQAFNVFS
Protein: FI07923p (Karyopherin beta 3, isoform A) (Karyopherin beta 3, isoform B) (Q9VN44)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- D-Importin 7/RanBP7
- Importin subunit alpha
- Importin subunit alpha
- Importin subunit alpha
- Importin subunit beta
- GTP-binding nuclear protein Ran
- Exportin-1
- Cell division cycle 14, isoform A
- GMP synthase
- GTP-binding nuclear protein Ran-like
Sequence:
MAADQAHFQQLLASLLSTDNDVRQQAEEAYNNLSRELKVTHLLGNIQNGQQSEEARQMAAVLLRRLFTTEFFDFYKGLPAESQNQLLQQILLAVQQEVTPQLRRKICEVVAEVARNLIDEDCNNQWPDILQFLFQCANSPTPQLQESALRIFSSVPSIFGNQEAQYIDLIKQMLAKSMDAGSDPEVRVQAVRAVGAFILYHDKENETAIHKHFADMLPRMIHITGETIEAQDDQSLLKLLIEMTENCPKFLRPQLEFIFEVCMKVFSSQDFEDSWRHLVLEVMVSLAENAPSMIRKRADKYIVALIPLILHMMTDLDDDENWSTADVVDDDDHSDNNVIAESSLDRLACGLGGKIVLPLVMNALPVMLGHADWKHRFAALMAISAIGEGCHKQMEAILDEVMSGVLNFLSDPHPRVRYAACNAIGQMSTDFAQTFEKKFHSQVIPGLLSLLDDVENPRVQAHAGAALVNFSEDCPKNILTRYLDGIMAKLETILNSKFKELVEKGNKLVLEQVVTTIASVADTCESEFVAYYDRLMPCLKFIIQNANSDDLRMLRGKTIECVSLIGLAVGREKFIGDAGEVMDMLLVNHTEGGELADDDPQTSYLITAWARMCKILGKQFEQYLPLVMGPVMRTATMKPEVAMLDNDEVEDIDGDVDWSFINLGEQQNFAIRTAGMDDKASACEMLVCYARELKEGFAEYAEDVVRQMLPMLKFYFHDGVRTAAAESLPYLLDCAKIKGPQYLEGMWMFICPELLKVIVTEPEPDVQSELLNSLAKCIETLGPNCLNEDAMKQVLEIINKYVLEHFERADKRLAARNEEDYDDGVEEELAEQDDTDVYILSKIVDITHALFQTNKAQFLPAFEQVAPHFVKLLEPSRPVADRQWGLCVFDDLIEFCGPACAPYQQIFTPALVQYVCDKAPEVRQAAAYGCGVLGQFAGEQFAHTCAQIIPLLVQVINDPKAREIENISPTENAISAFAKILKYNNSALSNVDELIGVWFSWLPVSEDSEEAAHIYGYLCDLIEGNHPVILGANNGNLPRIVSIIAESFCTKVVEAQSATGTRMLTIVKQVESNPEVMAACASTLSPEQQQALQDAYRELANVAPA
Protein: tRNA (cytidine(34)-2'-O)-methyltransferase (EC 2.1.1.207) (tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmL) (P44868)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01885}.
Interaction partners:
- Ribosomal RNA large subunit methyltransferase H-methyltransferase)
- Ribosomal RNA small subunit methyltransferase D
- tRNA
Sequence:
MLDIVLYEPEIPQNTGNIIRLCANTGFRLHLIEPLGFTWDDKRLRRSGLDYHEFAEIKRHKTFEAFLESEKPKRLFALTTKGCPAHSQVKFKLGDYLMFGPETRGIPMSILNEMPMEQKIRIPMTANSRSMNLSNSVAVTVYEAWRQLGYKGAVNLPEVK
Protein: HL08110p (Z band alternatively spliced PDZ-motif protein 66, isoform A) (Z band alternatively spliced PDZ-motif protein 66, isoform J) (Q9VSN2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEYVQFKNGSPVYYKEQPDLNECIQYQPYRTTPLVLPGAKVKKDAPTTESYLRHYPNPAVRAHPGHDYHDSIMKQRVADTMLHKVVGSEADTGRVFHKQFNSPIGLYSNNNIEDTIRSTVPFATSESNRLKDSPLHRPLPTKLNGYKKTVQYDPRNSETYRAIQEEGGYSNYGQSSPQEVTIPVQTKVYQPNRLVPGKKPVSAPVSRPPYNVVNTHDENIRQSGSFNRLMYSVIGATEY
Protein: D-lactate dehydrogenase (cytochrome) (EC 1.1.2.4) (A0A8I5Y6D8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MCGWGPGGWSPPFFPPATGHVCGFCCLSYDPCTVSPLQGGLSQDFVEALKAVVGSPHVSTASAVRQHHGHDESMHRCRPPDAVVWPQNVDQVSRLASLCYNQGVPIIPFGTGTGVEGGVCAVQGGVCISLTHMDQIMELNTEDFSVVVEPGVTRKALNTHLRNSGLWFPVDPGADASLCGMAATGASGTNAVRYGTMRDNVINLEVVLPDGRLLHTAGRGRHYRKSAAGYNLTGLFVGSEGTLGIITSATLRLHPAPEATVAATCAFPSVQAAVDSTVQILQAAVPVARIEFLDEVMMDACNRHSKLNCPVAPTLFLEFHGSQQALAEQLQRTEAITQDNGGSHFSWAKEAEKRNELWAARHNAWYAALALRPGRVIVGHVGDGNFHCILLVNPDDVEEQRRVKAFAENLGRRALALHGTCTGEHGIGLGKRQLLQEEVGPVGVETMRQLKDTLDPRGLMNPGKVL
Protein: Flagellar basal body rod protein FlgB (P24500)
Organism: Bacillus subtilis (strain 168)
Function: Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
Subcellular location: Bacterial flagellum basal body {ECO:0000269|PubMed:9159525}.
Interaction partners:
- Flagellar basal-body rod protein FlgC
- Flagellar hook-basal body complex protein FliE
- FlaA locus uncharacterized protein YlxG
- Flagellar basal-body rod protein FlgG
- Flagellar M-ring protein
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliG
- Flagellar hook-associated protein 1
- Flagellar biosynthetic protein FliQ
- Flagellar motor switch phosphatase FliY
Sequence:
MSLFSGTIQNLENALSRADIKQKVITNNIANIDTPNYKAKKVSFQNLLDQESSRLEAIKTDYRHVDFSDTDSNYSIVASGDTSYQQNGNNVDVDKEMTELAQNQINYQALVERMNGKFNSLKTVLTGGK
Protein: ESAT-6-like protein (A0A0H3LCA2)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MATRFMTDPHAMRDMAGRFEVHAQTVEDEARRMWASAQNISGAGWSGMAEATSLDTMAQMNQAFRNIVNMLHGVRDGLVRDANNYEQQEQASQQILSS
Protein: Prefoldin subunit 6 (Q17Q89)
Organism: Bos taurus (Bovine)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Interaction partners:
- Prefoldin subunit 5
- Prefoldin subunit 3
- Prefoldin subunit 1
- Prefoldin subunit 2
- Prefoldin subunit 4
- Prefoldin subunit 4
- Unconventional prefoldin RPB5 interactor
- RNA polymerase II-associated protein 3
- Protein UXT
- RuvB-like helicase
Sequence:
MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYESQLRDLEQQSEQQRETLAQLQQEFQRAQAAKAGAPGKA
Protein: Glucose sensor (Q5ANE1)
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:
- Carbon catabolite-derepressing protein kinase
- Rgt1p
Sequence:
MKNLSVFPFLTRIMYDASLEDEYYRQMRQKSSSISAFKVGLVAAMGGFLYGYDTGLINDLLEMEYVYTHFPSNNKSFTSHERSILVAILSLGTFIGALIAPLASDRYGRKFSIMMSSGLIFITGNILQIASASIALMCVGRFVSGVSVGILSAIVPLYQAEVSPKWSRGSVVFTYQWSITAGLLVSSAVCQGTRKINNSESYRIPIGLQFLWALILFFGMSFLPESPRYYVQQDNLQSALDSLCKLRKLPPDDDDLIEELVDIKANYDYELSYGKTTVLDCFKSGGGRHKQGLRMLTGIGVQFFQQCSGINFIFYYGVNFFSSTGINNYYIMSFITYLVNVIFTVPGIMMIDVVGRRPLLFWGGVGMAVCNFIIAIAGVSVKNDEVNGILCVSFACVFIAFFASTWGGCTWALCSDIYGISIRQKAVALTAATNWLVNFIFAFITPYLIDTGQHTAAIGSKIFFIWGSFNACGAIFVFFTVYETKGLKLEEVDYMYVHCDNARVSTKFISTKIDFAHLDENYNPIPMTQLPDSTSSNEMYHDKGSDENSSPQQLPHYHQQQPLYNGEDQNNLTIIPYDNSSTISSVNSIEERRDSIPSTNGLSFTSSSQSHPQSNSYSHSNSHSATYRSKSHNSMISNDYQSYLESIQREYSQHYQNSSAMIKQLSRNSRNNGSDQEERHEPIQKQEIIDSPLNINSINHINNIPTTVIATPFFAHPPSDSDSSDDEEEEEVVVEQEGVKINDVTTIK
Protein: Diaminopimelate decarboxylase (DAP decarboxylase) (DAPDC) (EC 4.1.1.20) (P00861)
Organism: Escherichia coli (strain K12)
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate.
Interaction partners:
- Diaminopimelate epimerase
- Lysine-sensitive aspartokinase 3
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- 4-hydroxy-tetrahydrodipicolinate synthase
- 4-hydroxy-tetrahydrodipicolinate reductase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- Succinyl-diaminopimelate desuccinylase
- Constitutive lysine decarboxylase
Sequence:
MPHSLFSTDTDLTAENLLRLPAEFGCPVWVYDAQIIRRQIAALKQFDVVRFAQKACSNIHILRLMREQGVKVDSVSLGEIERALAAGYNPQTHPDDIVFTADVIDQATLERVSELQIPVNAGSVDMLDQLGQVSPGHRVWLRVNPGFGHGHSQKTNTGGENSKHGIWYTDLPAALDVIQRHHLQLVGIHMHIGSGVDYAHLEQVCGAMVRQVIEFGQDLQAISAGGGLSVPYQQGEEAVDTEHYYGLWNAAREQIARHLGHPVKLEIEPGRFLVAQSGVLITQVRSVKQMGSRHFVLVDAGFNDLMRPAMYGSYHHISALAADGRSLEHAPTVETVVAGPLCESGDVFTQQEGGNVETRALPEVKAGDYLVLHDTGAYGASMSSNYNSRPLLPEVLFDNGQARLIRRRQTIEELLALELL
Protein: Tyrosine-protein kinase transmembrane receptor Ror (dRor) (EC 2.7.10.1) (Q24488)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tyrosine-protein kinase receptor that functions during early stages of neuronal development.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Frizzled-3
- Frizzled
- Frizzled-2
- Frizzled-4
- Protein Wnt-5
Sequence:
MNKYSAFIVCISLVLLFTKKDVGSHNVDSRIYGFQQSSGICHIYNGTICRDVLSNAHVFVSPNLTMNDLEERLKAAYGVIKESKDMNANCRMYALPSLCFSSMPICRTPERTNLLYFANVATNAKQLKNVSIRRKRTKSKDIKNISIFKKKSTIYEDVFSTDISSKYPPTRESENLKRICREECELLENELCQKEYAIAKRHPVIGMVGVEDCQKLPQHKDCLSLGITIEVDKTENCYWEDGSTYRGVANVSASGKPCLRWSWLMKEISDFPELIGQNYCRNPGSVENSPWCFVDSSRERIIELCDIPKCADKIWIAIVGTTAAIILIFIIIFAIILFKRRTIMHYGMRNIHNINTPSADKNIYGNSQLNNAQDAGRGNLGNLSDHVALNSKLIERNTLLRINHFTLQDVEFLEELGEGAFGKVYKGQLLQPNKTTITVAIKALKENASVKTQQDFKREIELISDLKHQNIVCILGVVLNKEPYCMLFEYMANGDLHEFLISNSPTEGKSLSQLEFLQIALQISEGMQYLSAHHYVHRDLAARNCLVNEGLVVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPSESILYGKFTTESDVWSFGVVLWEIYSYGMQPYYGFSNQEVINLIRSRQLLSAPENCPTAVYSLMIECWHEQSVKRPTFTDISNRLKTWHEGHFKASNPEM
Protein: Potassium voltage-gated channel subfamily KQT member 5 (KQT-like 5) (Potassium channel subunit alpha KvLQT5) (Voltage-gated potassium channel subunit Kv7.5) (Q9NR82)
Organism: Homo sapiens (Human)
Function: Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. As the native M-channel, the potassium channel composed of KCNQ3 and KCNQ5 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10787416, ECO:0000269|PubMed:11159685}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 3
- Potassium voltage-gated channel subfamily KQT member 2
- Potassium voltage-gated channel subfamily KQT member 4
- Potassium voltage-gated channel subfamily KQT member 1
- ATP-sensitive inward rectifier potassium channel 12
- ATP-sensitive inward rectifier potassium channel 14
- Inward rectifier potassium channel 2
- Inward rectifier potassium channel 4
- Inward rectifier potassium channel 18
- Neurocalcin-delta
Sequence:
MPRHHAGGEEGGAAGLWVKSGAAAAAAGGGRLGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAATLGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGTDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQITSDKKSREKITAEHETTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALALASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLSRSTSANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPISQSDGSAVAATNTIANQINTAPKPAAPTTLQIPPPLPAIKHLPRPETLHPNPAGLQESISDVTTCLVASKENVQVAQSNLTKDRSMRKSFDMGGETLLSVCPMVPKDLGKSLSVQNLIRSTEELNIQLSGSESSGSRGSQDFYPKWRESKLFITDEEVGPEETETDTFDAAPQPAREAAFASDSLRTGRSRSSQSICKAGESTDALSLPHVKLK