wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-directed RNA polymerase (EC 2.7.7.48) (Q54UI6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Uncharacterized protein
- Putative RNaseIII
- DNA
- Argonaut-like protein
- Argonaut-like protein
- Argonaut-like protein
Sequence:
MSNYNNNNNNIPILKNNVKPRQYQEDAFNQCISRNTILVLPTGTGKTLVSILTFLKMFEINEKKNNDKVALFLVNNILLGKQQTETIKNLTDKRVMVLSGDDLSFQTKKKNYDIVVATPQILMNLINKNKIRIDNFHFIIFDEVHNATGLDNYCKIMSLVKNLDPPFRPRILGLTASVLKNASNYTTERATNEIKKLEDIMLSKIYCPLIEIFKDQQQQQQQQQQQHHHHQSPNFEIYEPSIQQTKLTSIISKLIIDKTRYLSKKNGHKDVKLEQIELPILKFIQSLSSLKPKLTSERDSSEYATIVNLCNSLTTLSIEGPQQCLTSITDGFVNGIIYQQLIDYDSEENQQQQEEEEEEEKEDEDDGIEMKTNKFKSLLKLLSIEIKENNINDKINCIVFVETRDTGKKLLNLLISEKEISKLNPKLIYGHNGRNGMKHSEQQQIIQQFKEGVCQVLVSTNVLEEGIDIKECNSVICFDNLYSLKSLIQRRGRDRTCSSFTLILEQDQRLRLEDLIKSEIIINRSLIDIMTDRMRQKELSTSSSSTSSSSSSSSNNSISMVSSLSSSSLSPSLSTSSSGVVTDEENSIYDYQTFFLPIFHIKENEYESFKEYCFKYNIKCSKEAADIDDDSDDDDENDSDSDSDSDGDSDSDNNSNSDNNSDRDEAIKLKNGPLVICSIEKKGNEFHEPYLSKFLLLNIKVDSTEKDTLINKFTIYLSKRFGYWINYSHYIDAIELDNEQEINNTFELVKETSRPSEAKTKFEFGNILNSPPLQFNKVDHFNSNIESIIIRKDHIVFKSVQNSSGNIYYLHHMSCRDVEQYCLYTPPTLIRTGSSKLTNSYDFYFLVIRPITLVRVKYDCKSKRTFTDEIEIENKNFGRSFVYKFTINLNFEKVNRLLSQLKYIGFDLYLFRNVNNNENNNNNNNNNTNKNINSNNIIINNNNNNNGNNINNINNGNELNFQNINNEEIYYLINSLNSERSFGRIINQDFVNQIIDLLKSNRIEEARYIIGVASTKKTKFFDYSKLFKKVISLNGNFNNIDSGDINDNNNGNYNIIEELYKDKPIQSNNGWVLINEIFVTPSRIVLKPPRLTLGNRILRKFSPEKFILFNFTDENLEPFRGLNKSSPLTKTIERIFNNGIEIIQGSGKKYFFIGCSQSQVRNYSAWFVLEDKVTNEKSALNWSGIKYESLQMIKVFRNLCLLFSTTLKSQVIYKIEMIPDIISKEGHNFTEGCGFIGSKLVELINQQNNYNSSTCAYQIRLGGSKGVLVLNENIDEMSLQIRPSMSKFELDYKSGQLDEEHKTLEIVSASTTSRCKLNRQAITLLSNAGVEDSTFLQMLEVELNQNAQTLVDVNLSKELLGDFFQHITEYELFNDYYIRSILLKLYKSKLIKIQDKCWIEVKESRNLLGVCDTSGTLPEDTVYIEVEELDPIDNLMKPKVIIGRVAVLKNPCHHPGDVRFLKAIDHPPLNGKRNVLFFSTNGMVPNFKQCSGSDLDGDRYFVIYDQTLIREDLITHEPYLGEEQTVNPLIGEEDSDDDQYENDDNDITIPTSTTTKSTNNTPTKLSDIYLKNVDKSKLGTISNTHLAISDIEKVSSINSIKVAIQCAIEVDSVKTSVHGIIPRDVKSILKEKGYPHFMKIKNGSTFEYKGGNQRKYYISDRVIGKIYDSAENLLWFGDFLPEAKVDESLLVQGYKEYLNHENFTTYMDYKSKINSILRRFGAQSEEDLLIGFMDPQFSEKLSIEAKAHFKSNYNSIQKLFYHNFLNEFRKKSNNNNNNNNNLSMLQIEEEEELINENYTEIEKKVCAWYFISYSDPENDKTLGFYRSVKGLLKTTEINNFETQKHNDKKPLNLSILSFAKEMKDTLLFGYQEKLLIFDEIKEILNDHLLENQLNDHFIFNLLFSGQQQNNNHQQEEQQQQQQQQQQQQQQQEEEDVEQSNIPSFYLYLQPLENEIENEKLLLVLKEKLESSFSNNLFEIIKITSTILEFEFKKIKFIIDFNSNSWYQSKVISLYITKHPSLVPTLLVIIEHIKNISLLLNSNKNTTTTTTTTTTSTTTTTTTISYNNNNNIKEKIENFSISPIGLVILFIRYAIENGLIKEFEESDIEFELSNNNNNIYSYEDLKDLLKIECEVGQSDNLLGFYRYYSEIFLLGVYSKKESFKLKSFGKSSIGVDNEVTITNDPQQLSLLSSQFKFAYNGICATVNVHKFLDSCLIISKRSILIQIGVDQIDNLIKNQLAIRESIELLNVSIQFIYNSPKSCTIDINGLPNRLTKARDKIREFLK
Protein: N-terminal acetyltransferase B complex auxiliary subunit NAA25 (N-terminal acetyltransferase B complex auxiliary subunit TCU2) (NatB N-alpha-terminal acetylation complex non-catalytic subunit) (Protein TRANSCURVATA 2) (F4KEY9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxiliary subunit of the NatB N-alpha-acetyltransferase complex. Required for flowering time regulation and for vegetative and reproductive plant development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24244708}.
Interaction partners:
- N-terminal acetyltransferase B complex catalytic subunit NAA20
- N-terminal acetyltransferase A complex catalytic subunit NAA10
- AT3g04860/T9J14_19
- AT5g28150/T24G3_80
- N-alpha-acetyltransferase MAK3
- MAK10 homologue
- Nuclear pore complex protein NUP58
- Sorting nexin 2A
- Acyl-CoA N-acyltransferases
- N-terminal acetyltransferase A complex auxiliary subunit NAA15
Sequence:
MRRWGLWEQETNVHTVAESDNFQSFPDRVEILCLTGTESFDVKGQQLIKTLQKGFPTKFLSSQMSSKFGLAGGIPERRVRPIWDAIDSRQFKNALKLVTSLLAKYPKSPYALALKALIHERMGKTDEALSVCLDAKELLYKDDLALMDDLTLSTLQIVLQRLDHLDLATSCYAHACGKYPNNLELMMGLFNCYVREYSFVKQQQTAIKMYKLAGEERFLLWAVCSIQLQVLCDKSGEKLLLLAEGLLKKHIASHSMHEPEALMVYISLLEQQSKYNDALEVLSGDLGSLLMIEVDKLRIQGRLLARANDYSAAVDVYKKILELSPDDWECFLHYLGCLLEDDSIWKYFDNIDQIHPTKHIECKFSHLTEEMFDSRISSASDLVQKLQRDAENSNLRGPYLAELEIEKRKFLFGKKNEDKLLESLLQYFLKFGHLACYASDVEAYLQVLSPNKKAGFVEMLVKNSDSSASATKVLGQTTTILKVQELTGNIFGLPTDEIEASAVKLAKLYCQNLSLSKDLDPQESMFGEELLSLISNMLVQLFWRTRDFGYLAEAIMVLELGLTIRGHVWQYKILLLHIYSYVGALPLAFERYKALDVKNILTETVSHHILRQMLESPMWVDLSNLLKDYLKFMDDHLRESADLTFLAYRHRNYSKVIEFVLFKQRLQHSNQYQAARVEASVLQLKQNADSFEEEERILENLKSGVQLVELSNEIGSRTLKFNEDMQTRPWWTPCPEKNYLLGPFEEISYCPPKENVKEEREENMKRAIQRKSLLPRMIYLSIQCTPTALKESVETNGSGGDIDVCEELKCLLEDYTKMLGCSLSDAVEMITEISQGARTSESLGSNLVDWLNFAVFWNAWSLSSQEHWHVLNSLFERLILDRVRSMGSSDMSSCYSDVQVLVQIITEPLAWHSLIIQACTRSSLPSGKKKKKNQHSDQLSSSPISQAIKDSIQLLCSTIQDVSNWLLNQLNNPEDGQVEGFLTTLKRDGNAAGPGQILGVLESFIASSEESEVGNRIFQALKSWNTADTARKTVMAQQRVLREFLQICESKRKLLETLKQQMSHV
Protein: Sorting assembly machinery 35 kDa subunit (Mitochondrial 38 kDa outer membrane protein) (TOB complex 38 kDa subunit) (P14693)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:14699090, ECO:0000269|PubMed:15326197}.
Interaction partners:
- Sorting assembly machinery 50 kDa subunit
- Mitochondrial distribution and morphology protein 10
- Mitochondrial import receptor subunit TOM40
- Sorting assembly machinery 37 kDa subunit
- Mitochondrial import receptor subunit TOM22
- Mitochondrial import receptor subunit TOM5
- Mitochondrial import receptor subunit TOM7
- Mitochondrial import receptor subunit TOM20
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM6
Sequence:
MVSSFSVPMPVKRIFDTFPLQTYAAQTDKDEAVALEIQRRSYTFTERGGGSSELTVEGTYKLGVYNVFLEANTGAALATDPWCLFVQLALCQKNGLVLPTHSQEQTPSHTCNHEMLVLSRLSNPDEALPILVEGYKKRIIRSTVAISEIMRSRILDDAEQLMYYTLLDTVLYDCWITQIIFCASDAQFMELYSCQKLSGSIVTPLDVENSLLQKLSAKSLKISLTKRNKFQFRHREIVKSMQGVYHNHHNSVNQEQVLNVLFENSKQVLLGLKDMLKSDGQPTYLHLKIASYILCITNVKEPIKLKTFVENECKELVQFAQDTLKNFVQ
Protein: Sphingolipid long chain base-responsive protein PIL1 (P53252)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Sphingolipid long chain base-responsive protein LSP1
- Protein SUR7
- Serine/threonine-protein kinase PKH1
- Eisosome protein SEG1
- Eisosome protein 1
- Non-classical export protein 2
- Uncharacterized protein MRP8
- Serine/threonine-protein kinase PKH2
- Uncharacterized protein YGR130C
- Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
Sequence:
MHRTYSLRNSRAPTASQLQNPPPPPSTTKGRFFGKGGLAYSFRRSAAGAFGPELSRKLSQLVKIEKNVLRSMELTANERRDAAKQLSIWGLENDDDVSDITDKLGVLIYEVSELDDQFIDRYDQYRLTLKSIRDIEGSVQPSRDRKDKITDKIAYLKYKDPQSPKIEVLEQELVRAEAESLVAEAQLSNITRSKLRAAFNYQFDSIIEHSEKIALIAGYGKALLELLDDSPVTPGETRPAYDGYEASKQIIIDAESALNEWTLDSAQVKPTLSFKQDYEDFEPEEGEEEEEEDGQGRWSEDEQEDGQIEEPEQEEEGAVEEHEQVGHQQSESLPQQTTA
Protein: As/Sb Reductase (EC 1.20.4.1) (Q4Q501)
Organism: Leishmania major
Interaction partners:
- Possible hypothetical 85.8 Kd protein
- Thiol-dependent reductase 1
- Protein kinase domain-containing protein
- Putative mitogen-activated protein kinase kinase 3
- 14-3-3 protein I
- 14-3-3 protein II
- Serine/threonine-protein kinase PLK
- Serine/threonine-protein kinase PLK
- Protein kinase domain-containing protein
Sequence:
MHRSPFSCEGIAILARVLLCHLTAFFFFVVLTVLLFEHSDGRRALYFALRRLSASLGGGHDVLLTREAVCTLWLRVVRECVPFTGAASYATLLLYPLLGCVAMTNYTYIKPEELVELLDNPDSLVKAAVIDCRDSDRDCGFIVNSINMPTISCTEEMYEKLAKTLFEEKKELAVFHCAQSLVRAPKGANRFALAQKKLGYVLPAVYVLRGGWEAFYHMYGDVRPDLMYV
Protein: Cngb1 protein (Q80VQ4)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
LPDKMRLDLAIDVNYSIVSKVALFQGCDRQMIFDMLKRLRSVVYLPNDYVCKKGEIGREMYIIQAGQVQVLGGPDGKAVLVTLKAGSVFGEISLLAVGGGNRRTANVVAHGFTNLFILDKKDLNEILVHYPESQKLLRKKARRMLRNNNKPKEEKSVLILPPRAGTPKLFNAALAAAGKMGPRGAKGGKLAHLRARLKELAALEAAARQQQLLEQAKSSQEAGGEEGSGATDQPAPQEPPEPKDPPKPPGPPEPSAQSSPPPASAKPEESTGEAAGPPEPSVRIRVSPGPDPGEQTLSVEVLEEKKEGAE
Protein: Ubiquinone biosynthesis protein COQ9, mitochondrial (Q05779)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16027161}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16027161}; Matrix side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16027161}.
Interaction partners:
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4, mitochondrial
- Atypical kinase COQ8, mitochondrial
- MIOREX complex component 2
- Hexaprenyl pyrophosphate synthase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- RING-box protein HRT1
Sequence:
MLCRNTARTGCKFFRLYHSNPIEHVKPIHIKPLTYGKESPQYKVLSLALQKFVPEHGFSERSIVESLNELGYPSSMISSIGAPNSPSFFHSSTAVMELIKFQLVDKRYRLTEGINPDVTPQYKLPSLEHLLLKRLEMDKPIGGHLSELMSQLAIPSAFLFETAIPELHRLSDDMIYFSNEKDHHDSAWYAKRLAVSSTYIGSKLFMAQDKSHNYKETFTFAKDKLHRVMRLGEYYNNTEEFAWYTLMSTVNLIKSQLVRG
Protein: Kinesin, putative (Q57ZA9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Tubulin alpha chain
- separase
- Zeta tubulin
- AAA+ ATPase domain-containing protein
- Tubulin beta chain
- Rev7, putative
- Structural maintenance of chromosomes protein
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
Sequence:
MSNIKVAVRCRPLFESERPAAGLSFVNGRRVMLDNKSYDPDYIFPPTATQDDVYAICEPILQSVKDGLHGTVMVYGQTGTGKTFTMLGGAGGSSGIAHRMIGSMLEHVQQRTVEGAQCALTLSMIEIYNEKLIDMLSKDGETEVTLVGGFPVSNEKLTLSRVADAFAAIQKGLSRRHIASTLMNERSSRSHVVIIVDYEEFNEYTNSVDVTHLFMVDLAGSESLKKSHASGAAAGETGKINKSLLALKNVFLALSNSNDTTRPNHVPYRDSKLTEILRDSIGGSARTLMIACISSVGRDIEETKSTLMYAVKARSIRNQANTEREKLMIRLRSFEAENQRLRNRLQERVAERGGYYISREDHERYQQLEEEYTELKSNVDTLLKERRENEGLQHITDSQTSVLKAMIEEKEEELVRFKQVYHEALLKFDSQVGTLQLVVQDAVRDAHNTAKRGTEAVFQRLEQWRLDTLMGQVEEGDDECRDEGSKGNAEEGSEGRKRGSTFGVSTRQYEDDMARCVVRINENFASLGQNIVAMTQKHVAAVHSLQKRRRASLEGVQERLKSQLQETLSAYVREQMILDDELECEQRLYEDSISMTTKLPTPADVLPFRHALQNACRAAVESSKDIFTDLEMNDEVAGSLQQINEALRVSATGASLGAFLQIGNMPPLRPSTSSQSSNAVCAAASASASASLRNDTSTTLPDTQTRRLSMKDKNQSVVSSRGGAVKRLRSSSNVSDSRRASAPSEK
Protein: Bifunctional glucose-6-phosphate 1-dehydrogenase/6-phosphogluconolactonase (PfGluPho) [Includes: 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31); Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)] (Q8IKU0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Bifunctional enzyme which catalyzes the first two steps of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis.
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphotransferase
- Phosphoglycerate mutase
- Pyruvate dehydrogenase E1 component subunit alpha
- Enolase
- Phosphoglucomutase, putative
- Pyruvate kinase
- pyruvate kinase
Sequence:
MDYENFVKSAEEINNLHNVNYLETKDLNDFNWKAAYYICKEIYDKQQINKDGYVVIGLSGGRTPIDVYKNMCLIKDIKIDKSKLIFFIIDERYKSDDHKFSNYNNIKFLFHNLNINEKEQLYKPDTTKSIVDCILDYNDKIKIMIEKYKKVDIAILGMGSDFHIASLFPNIFYNIYMNNYQNNYIYNEKTLDFINNDQDNDNLKYLKEYVYFTTTNQFDVRKRITVSLNLLANASSKIFLLNSKDKLDLWKNMLIKSYIEVNYNLYPATYLIDTSCTNENVNINNNNNNNNKNKNNYCYSNTTVISCGYENYTKSIEEIYDSKYALSLYSNSLNKEELLTIIIFGCSGDLAKKKIYPALFKLFCNNSLPKDLLIIGFARTVQDFDTFFDKIVIYLKRCLLCYEDWSISKKKDLLNGFKNRCRYFVGNYSSSESFENFNKYLTTIEEEEAKKKYYATCYKMNGSDYNISNNVAEDNISIDDENKTNEYFQMCTPKNCPDNVFSSNYNFPYVINRMLYLALPPHIFVSTLKNYKKNCLNSKGTDKILLEKPFGNDLDSFKMLSKQILENFNEQQIYRIDHYLGKDMVSGLLKLKFTNTFLLSLMNRHFIKCIKITLKETKGVYGRGQYFDPYGIIRDVMQNHMLQLLTLITMEDPIDLNDESVKNEKIKILKSIPSIKLEDTIIGQYEKAENFKEDENNDDESKKNHSYHDDPHIDKNSITPTFCTCILYINSINWYGVPIIFKSGKGLNKDICEIRIQFHNIMGSSDENMNNNEFVIILQPVEAIYLKMMIKKTGCEEMEEVQLNLTVNEKNKKINVPEAYETLLLECFKGHKKKFISDEELYESWRIFTPLLKELQEKQVKPLKYSFGSSGPKEVFGLVKKYYNYGKNYTHRPEFVRKSSFYEDDLLDIN
Protein: Protein kinase domain-containing protein (G5EB22)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Polo-like kinase
- G2/mitotic-specific cyclin-B
- Cyclin-dependent kinase 1
- Protein arginine N-methyltransferase
- Tyrosine-protein phosphatase cdcA
- Protein phosphatase PP2A regulatory subunit B
- Double-strand-break repair protein rad21
- M-phase inducer phosphatase
- Dis1/XMAP215 protein AlpA
- G2/mitotic-specific cyclin
Sequence:
MVATFSPHRDAGGTLHLSSHSGIHHIDANTAIRQLRRSFSRSPSKSSSFSLLTSRNHSPSKNTSYVSSPLSPSRRSAQGNFVLFPSSSQQSPFAIPYPPSAKISRPTMRRARTSPRSPVKRALNVSSDQGNAKPLHETPVTPGVENSSTIPEISLSPDDIGGGFSTCSNESSIYAEGTPNPRPSASRIEKRRSGTFNSAVSPMKRSDGIMNLDRASRGSPSAKRRSVQAVNLPGDFSIFDSENVTNTPEDPKTEETDLEKDAIFFPTSTTPPFSPFATVPRRTSSLRRSTLQQRSNDRSLFSRPRTMGDSEDLDAGTPLTVRSRQSLDANTPQPHRESLFSPRPAQVSSLFSNSNGATSRPAAHPLSRTITQSSSSSSLVDDSPTHEPPQKSDRPRAIINFSKSLPAGATRPSGARHLTREDSTSSTDSFATPENYKLVKPLPAAFMSTGLISKKNRNADDSHSLLGFSKNMPDTPCKRPVNLFAASQKAQPDGPLGRPAWSNAVDMPPPSPFNPSSARPKQGPFARGMGIFGTNFNRQGASRRGSLASIDGDDGYGLQTQSPSNRQNSQPLSESDFPPTPTKQSFFPSRTYPPTASQIASLERLSEARGTNSSPLHDRFQHESPRPNDRQSAQPDFNPLNLPATPTGPRDSFVGKRPSLPLNIHNTPDVDACLTSRFERVELVGTGEFSQVYRVSQPNGVSLPSIFSTTPKSLNSLPDQVWAVKKSKQPYSGLKDRERRIREVDALKALTNYDHIISFADSWEDNGHLYIQTEYCEEGSLDVFLAQVGLKARLDDFRIWKILLELSTGLKHIHDSGFIHLDLKPANILVTFEGVLKIADFGMASRWPAEEGIEGEGDREYIGPEILMGRYDKPADIFSLGLIIFEIAGNVELPDNGLSWQKLRNGDMSDVPSLTWSSETTVFRDASGNPISEEPSFEELCASDFGDDDFGTTDLFGSNRERKPVPFTRSSELADPPAFMIDAGHEQSLDKIVRWMISPEPLDRPTADHILESYGVQFVASRRRAGATVYEGNWGPADDVLAEDAEMIDV
Protein: Prostamide/prostaglandin F synthase (Prostamide/PG F synthase) (Prostamide/PGF synthase) (EC 1.11.1.20) (Peroxiredoxin-like 2B) (Q9DB60)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reduction of prostaglandin-ethanolamide H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor. Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18006499}.
Interaction partners:
- Prostaglandin E synthase
- Thromboxane-A synthase
- Prostaglandin G/H synthase 2
- Hematopoietic prostaglandin D synthase
- Prostaglandin-H2 D-isomerase
- Prostacyclin synthase
- Prostaglandin G/H synthase 1
- Carbonyl reductase 1])
- Prostaglandin E synthase 2
- Prostaglandin E synthase 3
Sequence:
MNVVDLGRVGACVLKHAVTGEAVELRSLWQEKACVVAGLRRFGCMVCRWIAQDLSNLRSILDQHDVRLVGVGPEALGLQEFLDGGYFSGELYLDESKQIYKELGFKRYNSLSILPAALGKPVRDVASKAKAVGIQGNLSGDLLQSGGLLVVSKGGDKVLLHFIQKSPGDYVPQENILQALGISAEVCSSKPPQCDEEVCGR
Protein: 2-hydroxychromene-2-carboxylate isomerase (HCCA isomerase) (EC 5.99.1.4) (Q52462)
Organism: Pseudomonas sp. (strain C18)
Function: Involved in the naphthalene catabolic pathway. Catalyzes the reversible glutathione-dependent isomerization of 2-hydroxychromene-2-carboxylate (HCCA) to trans-O-hydroxybenzylidenepyruvate (THBPA) (Probable).
Interaction partners:
Sequence:
MLLCRLLFLECLIVIVDFYFDFLSPFSYLANHRLSKLAQDYGFSIRYYAIDLARVKIAIGNVGPSNRDLIVKLDYLKVDLQRWAELYEIPLVFPANYNSRRMNTGLYYSGAMAQTGAYVNVVFNAVWGDGIAPDLESLPALVSEKLGWDRSAFEDFISSDAATERYDEQTHAAIERKVFGVPTMFLGDEMWWGNDRLFMLENAVGGAPVNGE
Protein: SKP1-like protein 4 (AtSK4) (Q9LNT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- Cullin-2
- Putative cullin-like protein 2
- Putative cullin-like protein 1
- Cullin-like protein 3
- RING-box protein 1a
- RING-box protein 1b
- F-box protein 7
- Elongin-C
- Cullin-3A
Sequence:
MAETKKMIILKSSDGESFEIEEAVAVKSQTIKHMIEDDCADNGIPLPNVTGAILAKVIEYCKKHVEAAAEAGGDKDFYGSAENDELKNWDSEFVKVDQPTLFDLILAANYLNIGGLLDLTCKAVADQMRGKTPEQMRAHFNIKNDYTPEEEAEVRNENKWAFE
Protein: LD42058p (Short spindle 2, isoform A) (Short spindle 2, isoform C) (Q9VUA5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein xmas
- Nuclear cap-binding protein subunit 2
- NTF2-related export protein
- Protein mini spindles
Sequence:
MDILDIDEALKDDSYIFLADKTHDDVSNILQQWKTNNQPPLQQLHLQYNNEAFKNNSKTFTRPKRRNLDFSQNGAGNDSGVGTGSVAGAPAMLQLEIGGLVTTNMHKSFLQDTSPPSSICSSMNTERMNNSLITSADFTNLNFLQSTIGLEQDPNLTTTLTNQTTDNMGIGGSIGGYTLSDMIRDRKALESLTMCEDDGTLIKDSHIGQIDEISLTLSKTASGCSTMDNSTDSMSIPLAADRTMPVVVSAVCPALQRTMILGEEMIGDTTFNLVDSLTTSALQSESESLPVDGNATFKRPTASATTADETQVLTGRQMNTTFTDGCNTPEGRCETPENIDRKLALLTMESSTPLTTNMRSHCYHNNNNNNKAGYTPTLKGRGDMNLSPIVGATPQKPTGTAPGRLNNTFEPVAKTAPFNGEKFVLDTMELLEQIEQPLDGTYNLQMSEQHRQMQCVMDLAEAEVEMLAQQGDEEQFENMLAELGKVNTLNEEQLKMQKSLDTIKRRFHRDEAEAEEREEELQQSAAEKVDTPVLNQSHSSSNSSGGGGERLLSRRSRLYDDVNLSAMHGSNGSSTSTNSASFIVQRRDMPQVEQPAPDPDPEPAEEPPKSQVTAEIDPASYKLPERRERDRDRFKTIKISKEMRLQPEIIVPCIDDEPQQLEDEQKQLVEDVRYEEDQRQGSPPGRLSRRDQTTAISNNADASASNYLTYKKPKEKSLIQRRPQQQEAPLLAEPAPASTLPQPRSLSRPRYISGLQKFTTVSKATSAGAGLNATPAAAMPTTVTVPANGNGELKSPMGIKSKSFHNLSSTMSGVGSGALPRPSLGGGLRRPSAQPSKLMSGLRGPTQAQEDDSAVFKVPKLVSGLRAPGLAPKRAGANGLARPSSGYYSLSVKTAPEADTPESLSSASSRGSLYGHKDSGRTVNGGNVPQQNPQQTFDMQALTSKLTQVTTGATGIPKPSGLRPPSQIKRSGLPRPSSIVRR
Protein: Protein Wnt-4 (XWnt-4) (P49338)
Organism: Xenopus laevis (African clawed frog)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Plays an important role in embryonic kidney development. Acts downstream of Notch signaling during pronephric kidney development. During early pronephros development, patterns the proximal pronephric anlagen to promote glomus and nephrostome formation. Also required later in pronephros development for tubulogenesis.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:19223472}.
Interaction partners:
Sequence:
MTPEYFLRSLLMMILAVFSANASNWLYLAKLSSVGSISEEETCEKLKGPIQRQVQMCKRNLEVMDSVRRGAQLAIEECQYQFRNRRWNCSTLDTLPVFGKVVTQGTREAAFVYAISSAGVAFAVTRACSSGDLEKCGCDRTVHGVSPQGFQWSGCSDNILYGVAFSQSFVDVRERSKGGSSSRALMNLHNNEAGRKAILNNMRVECKCHGVSGSCEVKTCWKAMPTFRKVGNVLKEKFDGATEVEQKKIGSTKVLVPKNSQFKPHTDEDLVYLDSSPDFCDHDLKNGVLGTTGRQCNKTSKAIDGCELMCCGRGFHTEEVEIVERCSCKFHWCCFVKCKQCHKVVEMHTCR
Protein: Metalloproteinase inhibitor 2 (Tissue inhibitor of metalloproteinases 2) (Q7SZM6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKSVRSCIGTLVVLVLFRVGEIAEACSCSPVHPQQAFCNADVVIRAKVVGKKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDRHIDVVFTAPSSAVCGVTNLDTNGKKEYLISGKAEANGKMHVTLCDLIMPWESMSATQKKSLSQRYQMGCDCKITRCATFPCEISAPEECLWTDWVTEKIIHGRQSDHYACIKRGDGSCAWYRGVAPPKKEFLEVEDP
Protein: Mitochondrial import protein 2 (Transcripts altered in meiosis protein 7) (G2TRP0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the mitochondrial outer import machinery (MIM) complex that mediates transport of proteins into mitochondrial compartments. Promotes the insertion of tom70 into the outer mitochondrial membrane. Promotes the insertion of atg43 into the outer mitochondrial membrane. Involved in import of the subset of proteins with multiple alpha-helical transmembrane segments (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3E798}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial import protein 1
- Probable mitochondrial import receptor subunit tom70
- Cytochrome c oxidase assembly factor 3, mitochondrial
- Mitophagy receptor atg43
- Vacuolar protein sorting-associated protein ist1
- Vacuolar protein-sorting-associated protein 46
- Vacuolar protein sorting-associated protein vts1
- Mitochondrial import receptor subunit tom20
- Mitochondrial import receptor subunit tom22
- Uncharacterized protein tam5
Sequence:
MAEVLDLEIDPISDGEDDTYSSELDDDLKDSIEQLERVLCLVVFPLLGKFLGRKFAFHAWARWLERRRLVSN
Protein: Uncharacterized protein (Q57V60)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSFHDDNHFVVDDDEQESSVELPSSNSSFHEEMEGVSNEEGTYEESDGKGGTVMGEEDDDDEGDEEEEEEAVDDEGDEEEEEEAVDDEGDEEEEEEAVDDEGDEEEEEEAVDDEGDEEEGEGDEECYDESEMMIDDCSGASAEEDHKEGEKYSVGGTQGDEGGEGLNVDECNSLEPSCQGSAWPSPSESSNVSPPPVILDPSVWGSSLSGAVAGSAASAVEGPSFPTQLKAEVPNSTCEQATDISSGVVLENTGYVRSAQLLDSSTSAGVTPSQSSFSFKRPRPKSQNEEAAAAKALLGMFKLCFPTTRFDGRLKDLLAGSA
Protein: Shikimate kinase (SK) (EC 2.7.1.71) (P9WPY3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- 3-dehydroquinate synthase
- Chorismate synthase
- Probable shikimate 5-dehydrogenase AroE
- 3-phosphoshikimate 1-carboxyvinyltransferase
- 3-dehydroquinate dehydratase
- Possible non-heme haloperoxidase Hpx
- Prephenate dehydrogenase
- Prephenate dehydratase
Sequence:
MAPKAVLVGLPGSGKSTIGRRLAKALGVGLLDTDVAIEQRTGRSIADIFATDGEQEFRRIEEDVVRAALADHDGVLSLGGGAVTSPGVRAALAGHTVVYLEISAAEGVRRTGGNTVRPLLAGPDRAEKYRALMAKRAPLYRRVATMRVDTNRRNPGAVVRHILSRLQVPSPSEAAT
Protein: Membrane-bound lytic murein transglycosylase B (EC 4.2.2.n1) (35 kDa soluble lytic transglycosylase) (Murein hydrolase B) (Slt35) (P41052)
Organism: Escherichia coli (strain K12)
Function: Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division.
Subcellular location: Cell outer membrane; Lipid-anchor; Periplasmic side.
Interaction partners:
- Membrane-bound lytic murein transglycosylase D
- Soluble lytic murein transglycosylase
- Membrane-bound lytic murein transglycosylase A
- Membrane-bound lytic murein transglycosylase F
- Endo-type membrane-bound lytic murein transglycosylase A
- Membrane-bound lytic murein transglycosylase C
- Endolytic peptidoglycan transglycosylase RlpA
- Anhydromuropeptide permease
- Endolytic murein transglycosylase
- Outer membrane protein assembly factor BamE
Sequence:
MFKRRYVTLLPLFVLLAACSSKPKPTETDTTTGTPSGGFLLEPQHNVMQMGGDFANNPNAQQFIDKMVNKHGFDRQQLQEILSQAKRLDSVLRLMDNQAPTTSVKPPSGPNGAWLRYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFNYPRRAEYFSGELETFLLMARDEQDDPLNLKGSFAGAMGYGQFMPSSYKQYAVDFSGDGHINLWDPVDAIGSVANYFKAHGWVKGDQVAVMANGQAPGLPNGFKTKYSISQLAAAGLTPQQPLGNHQQASLLRLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVWQLGQAVALARVQ