wanglab/gogpt-training-data huggingface dataset:
Protein: Anoctamin-3 (Transmembrane protein 16C) (A2AHL1)
Organism: Mus musculus (Mouse)
Function: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity. Seems to act as potassium channel regulator and may inhibit pain signaling; can facilitate KCNT1/Slack channel activity by promoting its full single-channel conductance at very low sodium concentrations and by increasing its sodium sensitivity.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Note=Shows an intracellular localization. {ECO:0000250}.
Interaction partners:
Sequence:
MVHHSGSIQSFKQQKGMNISKSEITTEASLKPSRRSLPCLAQSYAHSKSLSQSASLFQSTESESQAPTSVTFLSADKPEHVTSEESRKDSTLKCSFADLSDFCLALGKDKDYLDESEHANYDRSRLLNDFVTKDKPASKTKLSKNDMSYIASSGLLFKDGKKRIDYILVYRKTNIQYDKRNTFEKNLRAEGLMLEKEPAIANPDIMFIKIHIPWDTLCKYAERLNIRVPFRKKCYYTDQKNKSKSRVQNYFKRIKKWMSQNPMVLDKSAFPELEESDCYTGPFSRARIHHFIINNKDTFFSNATRSRIVYHMLERTKYENGISKVGIRKLITNGSYIAAFPPHEGAYKSSLPIKTHGPQNNRHLLYERWARWGMWYKHQPLDLIRMYFGEKIGLYFAWLGWYTGMLIPAAVVGLCVFFYGLVTMNESQVSQEICKATEVFMCPLCDKNCSLQRLNDSCIYAKVTYLFDNGGTVFFAIFMAIWATVFLEFWKRRRSILTYTWDLIEWEEEEETLRPQFEAKYYRMEVINPITGKPEPHQPSSDKVTRLLVSVSGIFFMISLVITAVFAVVVYRLVVMEQFASFKWNFVKQHWQFATSGAAVCINFIIIMLLNLAYEKIAYLLTNLEYPRTESEWENSFALKMFLFQFVNLNSSIFYIAFFLGRFVGHPGKYNKLFERWRLEECHPSGCLIDLCLQMGVIMFLKQIWNNFMELGYPLIQNWWSRHKIKRGIQDASIPQWENDWNLQPMNIHGLMDEYLEMVLQFGFTTIFVAAFPLAPLLALLNNIIEIRLDAYKFVTQWRRPLPARATDIGIWLGILEGIGILAVITNAFVIAITSDYIPRFVYEYKYGPCANHVKQNENCLKGYVNNSLSFFDLSELGMGKSGYCRYRDYRGPPWSSKPYEFTLQYWHILAARLAFIIVFEHLVFGIKSFIAYLIPDIPKGLRERIRREKYLVQEMMYEAELEHLQQQRRKSGQPIHHEWP
Protein: Sugar transport protein 4 (Hexose transporter 4) (Q39228)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport. Can transport glucose, methylglucose, galactose, xylose and mannose, but not fructose.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sucrose transport protein SUC1
- Sucrose transport protein SUC4
- At2g39500/F12L6.16
Sequence:
MAGGFVSQTPGVRNYNYKLTPKVFVTCFIGAFGGLIFGYDLGISGGVTSMEPFLEEFFPYVYKKMKSAHENEYCRFDSQLLTLFTSSLYVAALVSSLFASTITRVFGRKWSMFLGGFTFFIGSAFNGFAQNIAMLLIGRILLGFGVGFANQSVPVYLSEMAPPNLRGAFNNGFQVAIIFGIVVATIINYFTAQMKGNIGWRISLGLACVPAVMIMIGALILPDTPNSLIERGYTEEAKEMLQSIRGTNEVDEEFQDLIDASEESKQVKHPWKNIMLPRYRPQLIMTCFIPFFQQLTGINVITFYAPVLFQTLGFGSKASLLSAMVTGIIELLCTFVSVFTVDRFGRRILFLQGGIQMLVSQIAIGAMIGVKFGVAGTGNIGKSDANLIVALICIYVAGFAWSWGPLGWLVPSEISPLEIRSAAQAINVSVNMFFTFLVAQLFLTMLCHMKFGLFFFFAFFVVIMTIFIYLMLPETKNVPIEEMNRVWKAHWFWGKFIPDEAVNMGAAEMQQKSV
Protein: Tubulin polymerization-promoting protein family member 3 (TPPP/p20) (Q9BW30)
Organism: Homo sapiens (Human)
Function: Regulator of microtubule dynamic that has microtubule bundling activity. Required for embryo implantation; possibly by regulating beta-catenin (By similarity). Also required for decidualization via regulation of beta-catenin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30667362}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:17105200}.
Interaction partners:
Sequence:
MAASTDMAGLEESFRKFAIHGDPKASGQEMNGKNWAKLCKDCKVADGKSVTGTDVDIVFSKVKGKSARVINYEEFKKALEELATKRFKGKSKEEAFDAICQLVAGKEPANVGVTKAKTGGAVDRLTDTSRYTGSHKERFDESGKGKGIAGRQDILDDSGYVSAYKNAGTYDAKVKK
Protein: Skeleton-binding protein 1 (Q8I487)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Membrane associated histidine-rich protein 1
- Ring-exported protein 1
Sequence:
MCSAARAFDFFTDLADEPTQLQDAVPETTEKLAEVVSDAATNVTDAVSDTASGIGSLVGEAASSLGNLVGEAASGIGNIVGGAASGIGNIVGGAASGIGSLVGDAASGLGNLVGDAAEALATTELKDVIPENTESTTDLVPSEVSPPVDDYLDDDGFSSFREFLESTPCWQRRMAQEALLNEYEVESPAESMSPILRVQFFADFAKQAVHVAKQNYLYVVIFLFFVINILLFINFYNLGKRKGYYLAKKQKKEQMLEQNPEQNPEQNAQQNAQQNAQQNAQQNAQQNAQQNAQQNTQQNTQQKTQQNPQQNAQQNTQQNTQQQSTTKSTTKTVARET
Protein: Oligodendrocyte transcription factor 2 (G3V612)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Glial fibrillary acidic protein
- Transcription factor SOX-10
- Platelet-derived growth factor receptor alpha
- Myelin basic protein
- Paired box protein Pax-6
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- DNA-binding protein inhibitor ID-4
- RNA binding protein fox-1 homolog 3
- NK2 homeobox 2
- Nestin
Sequence:
MDSDASLVSSRPSSPEPDDLFLPARSKGGSSSGFTGGTVSSSTPSDCPPELSSELRGAMGTAGAHPGDKLGGGGFKSSSSSTSSSTSSAATSSTKKDKKQMTEPELQQLRLKINSRERKRMHDLNIAMDGLREVMPYAHGPSVRKLSKIATLLLARNYILMLTNSLEEMKRLVSEIYGGHHAGFHPSACGGLAHSTPLPTATAHPAAAAHAAHHPAVHHPILPPAAAAAAAAAAAAAVSSASLPGSGLSSVGSIRPPHGLLKSPSAAAAAPLGGGGGGSGGSGGFQHWGGMPCPCSMCQVPPPHHHVSAMGAGTLPRLTSDAK
Protein: Uncharacterized protein (Q38CZ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRPLRAWFAMCLVAILLFTVVDVSALYVRGKATRAIFIAVMASSVWICYVLLLFIFLYRPLRRCTALYRTGCCCRNGSSAANNGVRLWFKEQHSLDVCVEELRNGMVDIEGLKRT
Protein: Niemann-Pick disease, type C1 variant (Q59GR1)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
PPASAALRGHSMTARGLALGLLLLLLCPAQVFSQSCVWYGECGIAYGDKRYNCEYSGPPKPLPKDGYDLVQELCPGFFFGNVSLCCDVRQLQTLKDNLQLPLQFLSRCPSCFYNLLNLFCELTCSPRQSQFLNVTATEDYVDPVTNQTKTNVKELQYYVGQSFANAMYNACRDVEAPSSNDKALGLLCGKDADACNATNWIEYMFNKDNGQAPFTITPVFSDFPVRGMEPMNNATKGCDESVDEVTAPCSCQDCSIVCGPKPQPPPPPAPWTILGLDAMYVIMWITYMAFLLVFFGAFFAVWCYRKRYFVSEYTPIDSNIAFSVNASDKGEASCCDPVSAAFEGCLRRLFTRWGSFCVRNPGCVIFFSLVFITACSSGLVFVRVTTNPVDLWSAPSSQARLEKEYFDQHFGPFFRTEQLIIRAPLTDKHIYQPYPSGADVPFGPPLDIQILHQVLDLQIAIENITASYDNETVTLQDICLAPLSPYNTNCTILSVLNYFQNSHSVLDHKKGDDFFVYADYHTHFLYCVRAPASLNDTSLLHDPCLGTFGGPVFPWLVLGGYDDQNYNNATALVITFPVNNYYNDTEKLQRAQAWEKEFINFVKNYKNPNLTISFTAERSIEDELNRESDSDVFTVVISYAIMFLYISLALGHMKSCRRLLVDSKVSLGIAGILIVLSSVACSLGVFSYIGLPLTLIVIEVIPFLVLAVGVDNIFILVQAYQRDERLQGETLDQQLGRVLGEVAPSMFLSSFSETVAFFLGALSVMPAVHTFSLFAGLAVFIDFLLQITCFVSLLGLDIKRQEKNRLDIFCCVRGAEDGTSVQASESCLFRFFKNSYSPLLLKDWMRPIVIAIFVGVLSFSIAVLNKVDIGLDQSLSMPDDSYMVDYFKSISQYLHAGPPVYFVLEEGHDYTSSKGQNMVCGGMGCNNDSLVQQIFNAAQLDNYTRIGFAPSSWIDDYFDWVKPQSSCCRVDNITDQFCNASVVDPACVRCRPLTPEGKQRPQGGDFMRFLPMFLSDNPNPKCGKGGHAAYSSAVNILLGHGTRVGATYFMTYHTVLQTSADFIDALKKARLIASNVTETMGINGSAYRVFPYSVFYVFYEQYLTIIDDTIFNLGVSLGAIFLVTMVLLGCELWSAVIMCATIAMVLVNMFGVMWLWGISLNAVSLVNLVMSCGISVEFCSHITRAFTVSMKGSRVERAEEALAHMGSSVFSGITLTKFGGIVVLAFAKSQIFQIFYFRMYLAMVLLGATHGLIFLPVLLSYIGPSVNKAKSCATEERYKGTERERLLNF
Protein: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 (EC 2.4.1.149) (Beta-1,3-N-acetylglucosaminyltransferase 1) (BGnT-1) (Beta-1,3-Gn-T1) (Beta3Gn-T1) (Beta-1,3-galactosyltransferase 7) (Beta-1,3-GalTase 7) (Beta3Gal-T7) (Beta3GalT7) (b3Gal-T7) (Beta-3-Gx-T7) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2) (BGnT-2) (Beta-1,3-Gn-T2) (Beta-1,3-N-acetylglucosaminyltransferase 2) (Beta3Gn-T2) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7) (Q9Z222)
Organism: Mus musculus (Mouse)
Function: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Probably constitutes the main polylactosamine synthase.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 4
- Type 2 lactosamine alpha-2,3-sialyltransferase
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 3
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Galactoside alpha-
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
- Alpha-
Sequence:
MSVGRRRVKLLGILMMANVFIYLIVEVSKNSSQDKNGKGGVIIPKEKFWKPPSTPRAYWNREQEKLNRWYNPILNRVANQTGELATSPNTSHLSYCEPDSTVMTAVTDFNNLPDRFKDFLLYLRCRNYSLLIDQPKKCAKKPFLLLAIKSLIPHFARRQAIRESWGRETNVGNQTVVRVFLLGKTPPEDNHPDLSDMLKFESDKHQDILMWNYRDTFFNLSLKEVLFLRWVSTSCPDAEFVFKGDDDVFVNTHHILNYLNSLSKSKAKDLFIGDVIHNAGPHRDKKLKYYIPEVFYTGVYPPYAGGGGFLYSGPLALRLYSATSRVHLYPIDDVYTGMCLQKLGLVPEKHKGFRTFDIEEKNKKNICSYIDLMLVHSRKPQEMIDIWSQLQSPNLKC
Protein: Sec-independent protein translocase protein TatA (A1YH68)
Organism: Providencia stuartii
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162, ECO:0000256|HAMAP-Rule:MF_00236}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162, ECO:0000256|HAMAP-Rule:MF_00236}.
Interaction partners:
- Twin arginine-targeting protein translocase TatB
- Twin arginine-targeting protein translocase TatC
- Rhomboid protease AarA
- Glutamine-hydrolyzing GMP synthase
- Rhomboid family intramembrane serine protease GlpG
Sequence:
MESTIATAAFGSPWQLIIIALLIILIFGTKKLRSLGSDLGESLKGFKKAMNDDEAAKAAKEEQEKQDADFAPKNITEQQQAADKKDSPVESKNKEQG
Protein: Medium-chain fatty acid ethyl ester synthase/esterase 2 (Alcohol O-acetyltransferase) (EC 2.3.1.84, EC 3.1.1.-) (Ethanol hexanoyl transferase 1) (P38295)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Displays enzymatic activity both for medium-chain fatty acid (MCFA) ethyl ester synthesis and hydrolysis (esterase activity). MCFA are toxic for yeast and this enzyme could thus be involved in their detoxification by esterification.
Interaction partners:
- Isoamyl acetate-hydrolyzing esterase
- Alcohol O-acetyltransferase 1
- Ethanol acetyltransferase 1
- Very long-chain fatty acid transport protein
- Monoglyceride lipase
- Long-chain-fatty-acid--CoA ligase 1
Sequence:
MSEVSKWPAINPFHWGYNGTVSHIVGENGSIKLHLKDNKEQVDFDEFANKYVPTLKNGAQFKLSPYLFTGILQTLYLGAADFSKKFPVFYGREIVKFSDGGVCTADWLIDSWKKDYEFDQSTTSFDKKKFDKDEKATHPEGWPRLQPRTRYLKDNELEELREVDLPLVVILHGLAGGSHEPIIRSLAENLSRSGRFQVVVLNTRGCARSKITTRNLFTAYHTMDIREFLQREKQRHPDRKLYAVGCSFGATMLANYLGEEGDKSPLSAAATLCNPWDLLLSAIRMSQDWWSRTLFSKNIAQFLTRTVQVNMGELGVPNGSLPDHPPTVKNPSFYMFTPENLIKAKSFKSTREFDEVYTAPALGFPNAMEYYKAASSINRVDTIRVPTLVINSRDDPVVGPDQPYSIVEKNPRILYCRTDLGGHLAYLDKDNNSWATKAIAEFFTKFDELVV
Protein: Probable transport protein HsrA (High-copy suppressor of rspA) (P31474)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator YieP
- Multidrug export protein EmrA
- Nickel-responsive regulator
- Probable multidrug resistance protein EmrK
Sequence:
MSDKKKRSMAGLPWIAAMAFFMQALDATILNTALPAIAHSLNRSPLAMQSAIISYTLTVAMLIPVSGWLADRFGTRRIFTLAVSLFTLGSLACALSNSLPQLVVFRVIQGIGGAMMMPVARLALLRAYPRNELLPVLNFVAMPGLVGPILGPVLGGVLVTWATWHWIFLINIPIGIAGLLYARKHMPNFTTARRRFDITGFLLFGLSLVLFSSGIELFGEKIVASWIALTVIVTSIGLLLLYILHARRTPNPLISLDLFKTRTFSIGIVGNIATRLGTGCVPFLMPLMLQVGFGYQAFIAGCMMAPTALGSIIAKSMVTQVLRRLGYRHTLVGITVIIGLMIAQFSLQSPAMAIWMLILPLFILGMAMSTQFTAMNTITLADLTDDNASSGNSVLAVTQQLSISLGVAVSAAVLRVYEGMEGTTTVEQFHYTFITMGIITVASAAMFMLLKTTDGNNLIKRQRKSKPNRVPSESE
Protein: Antigen 43 (AG43) (Fluffing protein) [Cleaved into: Antigen 43 alpha chain; Antigen 43 beta chain] (P39180)
Organism: Escherichia coli (strain K12)
Function: Controls colony form variation and autoaggregation. May function as an adhesin.
Subcellular location: [Antigen 43]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Antigen 43 alpha chain]: Secreted. Cell surface {ECO:0000269|PubMed:22466966}. Note=The cell surface component is about 60 kDa and can be released by mild heat treatment (PubMed:22466966).; SUBCELLULAR LOCATION: [Antigen 43 beta chain]: Cell outer membrane {ECO:0000305|PubMed:25341963}; Multi-pass membrane protein {ECO:0000305}. Note=May form a beta-barrel.
Interaction partners:
- Inner membrane protein YeeR
- Probable autotransporter YfaL
- Uncharacterized fimbrial-like protein SfmH
- Type 1 fimbrin D-mannose specific adhesin
- Type-1 fimbrial protein, A chain
- DNA-binding transcriptional dual regulator OxyR
- Prophage integrase IntE
- Inverse autotransporter adhesin YeeJ
- Translocation and assembly module subunit TamB
- Uncharacterized fimbrial-like protein SfmA
Sequence:
MKRHLNTCYRLVWNHMTGAFVVASELARARGKRGGVAVALSLAAVTSLPVLAADIVVHPGETVNGGTLANHDNQIVFGTTNGMTISTGLEYGPDNEANTGGQWVQDGGTANKTTVTSGGLQRVNPGGSVSDTVISAGGGQSLQGRAVNTTLNGGEQWMHEGAIATGTVINDKGWQVVKPGTVATDTVVNTGAEGGPDAENGDTGQFVRGDAVRTTINKNGRQIVRAEGTANTTVVYAGGDQTVHGHALDTTLNGGYQYVHNGGTASDTVVNSDGWQIVKNGGVAGNTTVNQKGRLQVDAGGTATNVTLKQGGALVTSTAATVTGINRLGAFSVVEGKADNVVLENGGRLDVLTGHTATNTRVDDGGTLDVRNGGTATTVSMGNGGVLLADSGAAVSGTRSDGKAFSIGGGQADALMLEKGSSFTLNAGDTATDTTVNGGLFTARGGTLAGTTTLNNGAILTLSGKTVNNDTLTIREGDALLQGGSLTGNGSVEKSGSGTLTVSNTTLTQKAVNLNEGTLTLNDSTVTTDVIAQRGTALKLTGSTVLNGAIDPTNVTLASGATWNIPDNATVQSVVDDLSHAGQIHFTSTRTGKFVPATLKVKNLNGQNGTISLRVRPDMAQNNADRLVIDGGRATGKTILNLVNAGNSASGLATSGKGIQVVEAINGATTEEGAFVQGNRLQAGAFNYSLNRDSDESWYLRSENAYRAEVPLYASMLTQAMDYDRIVAGSRSHQTGVNGENNSVRLSIQGGHLGHDNNGGIARGATPESSGSYGFVRLEGDLMRTEVAGMSVTAGVYGAAGHSSVDVKDDDGSRAGTVRDDAGSLGGYLNLVHTSSGLWADIVAQGTRHSMKASSDNNDFRARGWGWLGSLETGLPFSITDNLMLEPQLQYTWQGLSLDDGKDNAGYVKFGHGSAQHVRAGFRLGSHNDMTFGEGTSSRAPLRDSAKHSVSELPVNWWVQPSVIRTFSSRGDMRVGTSTAGSGMTFSPSQNGTSLDLQAGLEARVRENITLGVQAGYAHSVSGSSAEGYNGQATLNVTF
Protein: Microfibrillar-associated protein 5 (MFAP-5) (MP25) (Microfibril-associated glycoprotein 2) (MAGP-2) (Q28022)
Organism: Bos taurus (Bovine)
Function: May play a role in hematopoiesis. In the cardiovascular system, could regulate growth factors or participate in cell signaling in maintaining large vessel integrity (By similarity). Component of the elastin-associated microfibrils (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Fibrillin-1
- Microfibrillar-associated protein 2
- Elastin
- Fibulin-5
- Lysyl oxidase homolog 1
- Fibrillin-2
- Multiple EGF like domains 6
- Microfibril-associated glycoprotein 3
- Microfibril-associated glycoprotein 4
- Myocilin
Sequence:
MTFFGPKVLLLLTALIMSSGRTPLGVSGQRGDDVTTVTSETFTEDPNLVNDPATDETVLADIQPSTDDLASLNDKNTTTECRDEKFACTRLYSVHRPIKQCLHQICFTSSRRMYVINNEICSRLVCKEHEAMKDELCRQKAGLPPRRLRRSNYFRLPPCDNVNLQGPSGL
Protein: E3 ubiquitin-protein ligase DTX4 (EC 2.3.2.27) (Protein deltex-4) (Deltex4) (RING finger protein 155) (RING-type E3 ubiquitin transferase DTX4) (Q9Y2E6)
Organism: Homo sapiens (Human)
Function: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations (By similarity). Functions as a ubiquitin ligase protein in vivo, mediating 'Lys48'-linked polyubiquitination and promoting degradation of TBK1, targeting to TBK1 requires interaction with NLRP4.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 4
- Serine/threonine-protein kinase TBK1
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 4
Sequence:
MLLASAVVVWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRAGGSVVLGQVDSRLAPYIIDLQSMNQFRQDTGTLRPVRRNYYDPSSAPGKGVVWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDLTSIGFSYVIDFNTMGQINRQTQRQRRVRRRLDLIYPMVTGTLPKAQSWPVSPGPATSPPMSPCSCPQCVLVMSVKAAVVNGSTGPLQLPVTRKNMPPPGVVKLPPLPGSGAKPLDSTGTIRGPLKTAPSQVIRRQASSMPTGTTMGSPASPPGPNSKTGRVALATLNRTNLQRLAIAQSRVLIASGVPTVPVKNLNGSSPVNPALAGITGILMSAAGLPVCLTRPPKLVLHPPPVSKSEIKSIPGVSNTSRKTTKKQAKKGKTPEEVLKKYLQKVRHPPDEDCTICMERLTAPSGYKGPQPTVKPDLVGKLSRCGHVYHIYCLVAMYNNGNKDGSLQCPTCKTIYGVKTGTQPPGKMEYHLIPHSLPGHPDCKTIRIIYSIPPGIQGPEHPNPGKSFSARGFPRHCYLPDSEKGRKVLKLLLVAWDRRLIFAIGTSSTTGESDTVIWNEVHHKTEFGSNLTGHGYPDANYLDNVLAELAAQGISEDSTAQEKD
Protein: Tyrosine 3-monooxygenase (EC 1.14.16.2) (Tyrosine 3-hydroxylase) (Q9PU40)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
- Aromatic-L-amino-acid decarboxylase
- Pterin-4-alpha-carbinolamine dehydratase
- Pterin-4-alpha-carbinolamine dehydratase 2
- Dopamine beta-hydroxylase.
- Sepiapterin reductase.
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Dihydropteridine reductase
- Tyrosinase
- Tyrosine aminotransferase
Sequence:
MPTPNISTSAAKGFRRAVSELDSKQAEAIMSPRFIGRRQSLIEDARKEREAAAAATDAAESTETIVFEEKDGRAMLNLFFMLKGAKTSPLSRALKVFETFEAKIHHLETRLSRKPREGTAELEYFVRCEVHSSDLNTFISSIKRVAEDVRTTKEDKFHWFPRKICELDKCHHLVTKFDPDLDLDHPGYSDQVYRQRRKSIAEIAFHYKHGDPIPRVEYTAEETATWKEVYSTLKSLYPTHACKEYLEAFNLLEKFCGYNENNIPQLEEVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADKTFAQFSQDIGLASLGATDEEIEKLATLYWFTVEFGLCRQNGIVKAYGAGLLSSYGELIHSLSDEPEVRDFDPDAAAVQPYQDQNYQPVYFVSESFSDAKNKLRNYAAHIKRPFSVKYEPYTHSIELLDSPQTICHSLESVRDELHSLINALNVIS
Protein: RNA-directed RNA polymerase subunit beta (EC 2.7.7.48) (RNA replicase beta chain) (RNA-directed RNA polymerase subunit II) (P14647)
Organism: Escherichia virus Qbeta (Bacteriophage Q-beta)
Function: This is the catalytic subunit of the viral RNA-dependent RNA polymerase complex. This complex is involved in viral RNA replication that produces (+)-stranded genomes via a complementary, (-)-stranded intermediate. Binds RNA cooperatively with the host ribosomal protein S1.
Interaction partners:
Sequence:
MSKTASSRNSLSAQLRRAANTRIEVEGNLALSIANDLLLAYGQSPFNSEAECISFSPRFDGTPDDFRINYLKAEIMSKYDDFSLGIDTEAVAWEKFLAAEAECALTNARLYRPDYSEDFNFSLGESCIHMARRKIAKLIGDVPSVEGMLRHCRFSGGATTTNNRSYGHPSFKFALPQACTPRALKYVLALRASTHFDIRISDISPFNKAVTVPKNSKTDRCIAIEPGWNMFFQLGIGGILRDRLRCWGIDLNDQTINQRRAHEGSVTNNLATVDLSAASDSISLALCELLLPPGWFEVLMDLRSPKGRLPDGSVVTYEKISSMGNGYTFELESLIFASLARSVCEILDLDSSEVTVYGDDIILPSCAVPALREVFKYVGFTTNTKKTFSEGPFRESCGKHYYSGVDVTPFYIRHRIVSPADLILVLNNLYRWATIDGVWDPRAHSVYLKYRKLLPKQLQRNTIPDGYGDGALVGSVLINPFAKNRGWIRYVPVITDHTRDRERAELGSYLYDLFSRCLSESNDGLPLRGPSGCDSADLFAIDQLICRSNPTKISRSTGKFDIQYIACSSRVLAPYGVFQGTKVASLHEA
Protein: Uncharacterized protein (Q38CC8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLFAQRKRRQRIAGKIGHDDSEYEIDHHHNIGILPQGQPRNTPRAYNGGPPATPRRQPHYVEQQQQQPWQQQQPSALMERFDVNFTPLQVNGNALGNNYRGGLVSNFGQALPPLPPPPVQPAAAWAPLPPVVNKNPLWFKPMLGACAPVSHPLIAPGVNACYHQSPPQYLYNCAPAAPNNLPPLQLPPVNAGTPRAETPLPYINNPIGRSCSRGDFHRPRSAAVGTLPNLNAFEDSAEAKRAARQRAIEFQQENARLCEERRRQQQLERQLQMEEERRREDAARAERLRLGQKEQSEMEREHSEAAGRVKKGRGGGRSNWTSDEQLREDLMRQINDKKQRQEDERRAAELEMQKEKENNKNSVYSNFYSDNGTDHLRGGRGGSPEPLEHTAPGAEPLGNGAAAGNDPVTNMAIPAGQLPGGNPHTLPQSYLPFAPHPLGTPRPFPAFQLDPILPLQRPGVVAGMASAASVPAAGNDYITPHLPPFPSIEISTPRDRAPTREAERVESHLRDMINEHESITRMLESEVPTKPSEIPLYRPQPIAHTKVSFTSPTVDNLRWNPCGTPPAAAGTGTGTASAPAFAMGYAAACGGGSDELSAEPSTFVGAQLAGNNA
Protein: 1-alkyl-2-acetylglycerophosphocholine esterase (EC 3.1.1.47) (G5EGT1)
Organism: Caenorhabditis elegans
Interaction partners:
- Lissencephaly-1 homolog
- Intracellular phospholipase A2
- phospholipase A2
- Phospholipase A2
- Phospholipase A2
- Platelet-activating factor acetylhydrolase homolog 2
Sequence:
MGGYLSSPQILTRKMPGQFKVGCMDLMIEEAAGSGLFMRLFFPTDSEITGPSSLPVWIPRPEYAYGVGEYLGHSPHQMDLISSLVIGDKRVDCIDNAQLSTKSDKWPVLVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEHRDSSACWTYKLVEKNGTLVEKPMKIKLVDRNDKDQFKIRNEQVGKRAEECAKAVKILEQLDSGNVKDKVIIGNNANLEFFKNKLLTTTASIIGHSFGGATSIASSSSDFQKAIVLDGWMYPLDQNQQEQAKQPIMFLNVGDWQWNENLEVMRKILPNNEGNILLTLSGAVHQSFTDFPFVFPNWLAKQFGVHGPTEPYLCMQSAIELTLSFLKDGKDGVQKLKDEKYTTFITNEIYGRVKLIV
Protein: Cyclic di-GMP phosphodiesterase PdeL (EC 3.1.4.52) (P21514)
Organism: Escherichia coli (strain K12)
Function: Acts both as an enzyme and as a c-di-GMP sensor to couple transcriptional activity to the c-di-GMP status of the cell. Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG. Also acts as a transcription factor to control its own expression.
Interaction partners:
- Probable diguanylate cyclase DgcC
- Diguanylate cyclase DgcM
- Diguanylate cyclase DgcP
- Diguanylate cyclase DgcN
- Probable diguanylate cyclase DgcT
- Diguanylate cyclase DosC
- Probable diguanylate cyclase DgcJ
- Probable diguanylate cyclase DgcF
- Diguanylate cyclase DgcZ
- Probable diguanylate cyclase DgcE
Sequence:
MNSCDFRVFLQEFGTTVHLSLPGSVSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDITFWRDIFFQYNPEIISATGSNSHRYINDNHYHHIVTPEAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKHLLPDNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYATYRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPGNKFISEWVMKAGG
Protein: MIP16848p (Q9VQ14)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cathepsin B, isoform A)
- Cathepsin L1
- cathepsin L
- FI04419p
- Cathepsin F
- Uncharacterized protein, isoform A
- IP19042p
- Peptidase A1 domain-containing protein
- Uncharacterized protein, isoform B
Sequence:
MNIRVIILLFCLIVFVGGKKVHRFRLERRSHRHHKIPHAHLHLQFRNALRRKYGFTPLRTVNAVNVTSESGKGVVITEPLINSYDTNFFGVVSVGDQSFTMQFDTGSSDFWVPSSHCRFCIKTCGNKFFRKSNSKSFRSSGTPFSITYGSGSVKGIVASDNVGFGDLKIQNQGIGLVNISDSCSVFDGIAGFAFQQLSMTKSVPSFQQMIDQQLVEQPIFSFHLKSGSSDGGSMILGGSNSSLYYGPLTYTNVTEAKYWSFKLDFIAVHGKGSRSSRTGNKAIMDTGTSLIVGPVLEVLYINKDIGAEHNKTYNLYTVACESIPQLPIIVFGIAGKEFFVKPHTYVIRYDNFCFSAFMDMLGLQYWILGDAFMRENYVEFDWARRRMGIAPAV
Protein: Ribosome modulation factor (RMF) (Hibernation factor RMF) (Protein E) (P0AFW2)
Organism: Escherichia coli (strain K12)
Function: During stationary phase, converts 70S ribosomes to an immature dimeric form (90S ribosomes) which are converted to inactive 100S ribosomes (a process called ribosomal hibernation) by the hibernation promoting factor HPF. Inactivates ribosomes by covering the peptidyl transferase (PTase) center of the 23S rRNA and the entrance of peptide exit tunnel. However crystallization with T.thermophilus 70S ribosomes shows it binds near the 3'-end of the 16S rRNA near the anti-Shine-Dalgarno sequence, where it would sterically hinder translation inititation. In this crystal binding of RMF induces movement of the 30S head domain away from the rest of the ribosome, presumably so they would more easily form dimers. Also involved in protection against heat stress, but this role is not dependent on the maintenance of ribosome dimers.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ribosome hibernation promoting factor
- Ribosome-associated inhibitor A
- Elongation factor Tu 2
- Elongation factor Tu 1
- Cold shock-like protein CspC
- Uncharacterized protein YaeQ
- Cell division topological specificity factor
- Uncharacterized protein YodC
- Protein YobF
- Protease 7
Sequence:
MKRQKRDRLERAHQRGYQAGIAGRSKEMCPYQTLNQRSQWLGGWREAMADRVVMA
Protein: Large ribosomal subunit protein eL43 (60S ribosomal protein L37a) (P61513)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL36
- Large ribosomal subunit protein uL15
Sequence:
MAKRTKKVGIVGKYGTRYGASLRKMVKKIEISQHAKYTCSFCGKTKMKRRAVGIWHCGSCMKTVAGGAWTYNTTSAVTVKSAIRRLKELKDQ