wanglab/gogpt-training-data huggingface dataset:
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q8CIN3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRRLLEPCWWILFLKITSSVLHYVVCFPALTEGYVGTLQESRQGSSVQIRRRKASGDPYWAYSGAYGPEHWVTSSVSCGGSHQSPIDILDHHARVGEEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGAGLPGRFKAEKVEFHWGHSNGSAGSEHSVNGRRFPVEMQIFFYNPDDFDSFQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEIVEWIVFRRPVPISYHQLEAFYSIFTTEQQDHVKSVEYLRNNFRPQQALNDRVVSKSAVRDAWNHDLADFLDNPLGTEASKVCSSPPIHMKVQPLNQTALQVSWSQPETIYHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKATISHISPDSLYLFRVQAVCRNDMRSDFSQTMLFQANTTRIFQGTRIVKTGVPTASPASSADMAPISSGSSTWTSSGIPFSFVSMATGMGPSSSGSQATVASVVTSTLLAGLGFGGGGISSFPSTVWPTRLPTASAASKQAGRPVLATTEALASPGPDGDSAPTKDGEGAEEGEKEEKSESEDGEREQEEEEKDSEKKEKSEATHTAAESDQTAPAPTPSSPHRTAQEGGHQTIPGHRQDHSAPVTDQPGHVDPGLDTLVDTATQVPPTATEEHYSGSDPKRPEMPSKKPISRGDRFSEDSKFITVNPAEKNTSGMISRPSPGRMEWIIPLIVVSALTFVCLVLLIAVLVYWRGCNKIKSKGFPRRSREVPSSGERGEKGSRKCFQTAHFYVEDSSSPRVVPNESIPIIPIPDDMEAIPVKQFGKSQHGFSGDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIIMITNLVEKGRRKCDQYWPTENTEEYGNIIVTLKSTEVHACYTVRRFSVRNTKVKKGQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPDMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAILGKETEVSSSQLHSYVNSILIPGVGGKTRLEKQFKLITQCNAKYVECFSAQKECNKEKNRNSSVVPAERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQAPISSTFELINVIKEEALARDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFVYKAMLSLVSTKENGNGPMTGDKNGAVLTAEESDPAESMESLV
Protein: Flagellar radial spoke protein-like, putative (Q57WA5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
- GTP-binding nuclear protein
- Nucleoporin
Sequence:
MASLTDDDIRVSPLWEHMKKVLLQVVQQQPSCALEAVVPASLTVQTGTSVPPRVTTEFGDHRPKVVNTVPPDALENLRWASSFGTALVPPKPRRKPQEDEEDMIPEDIEEEEEEVLGEVGDVVAEQAIFNSVGEGLPPEEAFRLVVGMKQLMRTEPLANVRFWGKFYGSVGDYYIVETKIDPNRIPEEGDEDGFDEVDEEEDGEPVENIADVLFAHGPKAHADTGVESSGTGLNEFVYYAANTTDPTRWARLPDVTPTQIIAARLIRRGFTGDLEATVDTHPRFPGCEKHYVRAQIARINCTCRVAPIDMYTTEGAVPVEEDEDGNLLPPPATVPAYSVLPPLIPQEVPDEEDAEAIEPVKSWFYGYRDDELLQGKYWVHIAPTLLLNGRTVASEQETAGDDDGRGGEVDHSEKIHPFLCEVSRDEPLRYTCHSRSQLPAWSFRKAFHDESSKKRTYVARSCLWPGAYTYVVTELGKPGSSFQSVYIGSGLKSLQGVNYAPKLPPRCLVEYPEVDLLLQRDGTLDDELEYAPPPPKPEDAGEDEEEYD
Protein: Protein NDRG1-A (xNDRG1-A) (Q641F2)
Organism: Xenopus laevis (African clawed frog)
Function: May be involved in pronephros development, after specification of the pronephros.
Interaction partners:
Sequence:
MSAEMTDLNFAEGRPLMTDKEDGITVLLQEYVTQEHDIETAHGIVHVTMCGTPKLNRPVILTYHDIGLNHKTCFNSLFNFEDMHEISQHFSVCHVDAPGQQEGAASFPAGYMYPSMDQLAEMLPGVVQQLGLRTVMGLGIGAGAYILTRFALNHPSMVEGLVLININPCAEGWMDWAATKISGWTNALPDMVISHLFSKDEVHSNPELVETYRQHILHDINQNNVQHFVKSYNSRRDLEIERPIPGTNAVTLKCPALLVVGDSSPAVDAVVECNSKLDPTKTTLLKMSDCGGFPQVIQPAKLAEAFKYFVQGMGYMPAASMTRLMRSRTGSAASSSSQDGNRSRSHTNEGSRSRSHTGDGNRSRAHTGDGNRSRSHTDTNNINSDQNSPKSMEVSC
Protein: FI01566p (SAGA-associated factor 29kDa, isoform A) (SAGA-associated factor 29kDa, isoform B) (Q9W2I4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 12
- SAGA complex subunit Spt3
- Ada2a-containing complex component 2
- Enhancer of yellow 2 transcription factor
- SAGA-associated factor 11 homolog
- Transcriptional adapter 2b
- SAGA complex subunit Spt7
- Transcription initiation factor TFIID subunit 9
- Transcriptional adapter 1-2
- SAGA factor-like TAF6
Sequence:
MPLTAESAAQQIQDRLKDIQQNIHNVDEERRRAENSIASLVRSLHATNQKVKPLLKASLTEAAQEEATIRAALAKIHEIRSIRNERRIQARNAGNKEAIRRGALMKMVQLSAQTLPLFVGKLGERAPALCGAIPAEGNYVAKVGDNVAALAKGIDEEENWILAEVVQFLHRQNKYDVIDIDEEQKDRHVLSKRKVIPLPLMRANPETDGHALFPKDTVVMALYPQTTCFYKAIVHRLPQTATEDYEVLFEDSSYTNGYAEPLPVAQRYVIAYRPTKKGAGSGSGNLSSA
Protein: Mitochondrial protein import protein MAS5 (Yeast dnaJ protein 1) (P25491)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex.
Subcellular location: Cytoplasm. Cytoplasm, perinuclear region. Note=Concentrated in a perinuclear ring as well as in the cytoplasm.
Interaction partners:
- ATP-dependent molecular chaperone HSC82
- ATP-dependent molecular chaperone HSP82
- Heat shock protein 104
- Heat shock protein SSA1
- Heat shock protein SSA2
- Heat shock protein homolog SSE1
- Heat shock protein SSA3
- Heat shock protein STI1
- Zuotin
- Protein SIS1
Sequence:
MVKETKFYDILGVPVTATDVEIKKAYRKCALKYHPDKNPSEEAAEKFKEASAAYEILSDPEKRDIYDQFGEDGLSGAGGAGGFPGGGFGFGDDIFSQFFGAGGAQRPRGPQRGKDIKHEISASLEELYKGRTAKLALNKQILCKECEGRGGKKGAVKKCTSCNGQGIKFVTRQMGPMIQRFQTECDVCHGTGDIIDPKDRCKSCNGKKVENERKILEVHVEPGMKDGQRIVFKGEADQAPDVIPGDVVFIVSERPHKSFKRDGDDLVYEAEIDLLTAIAGGEFALEHVSGDWLKVGIVPGEVIAPGMRKVIEGKGMPIPKYGGYGNLIIKFTIKFPENHFTSEENLKKLEEILPPRIVPAIPKKATVDECVLADFDPAKYNRTRASRGGANYDSDEEEQGGEGVQCASQ
Protein: Equilibrative nucleoside transporter 2 (rENT2) (Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter) (Equilibrative NBMPR-insensitive nucleoside transporter) (Nucleoside transporter, ei-type) (Solute carrier family 29 member 2) (O54699)
Organism: Rattus norvegicus (Rat)
Function: Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is insensitive (EI) to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) and is sodium-independent. Specific for nucleosides, but may also transport hypoxanthine. May also play a role in the efflux of inosine and hypoxanthine from muscle cells during the net degradation of purine nucleotides that occurs during strenuous exercise and/or in the reuptake of these purines during the recovery process (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:23639800}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q14542}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the apical membrane of Sertoli cells. {ECO:0000269|PubMed:23639800}.
Interaction partners:
- Equilibrative nucleoside transporter 3
- Equilibrative nucleoside transporter 1
- Sodium/nucleoside cotransporter 2
- Sodium/nucleoside cotransporter 1
- Solute carrier family 28 member 3
- Adenosine kinase
Sequence:
MAHGNAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQGRLAGTNSSAETPSTNHTSPTDTFNFNNWVTLLSQLPLLLFTLLNSFLYQCIPESVRILGSLLAILLLFALTAALVKVDLSPGLFFSITMASVWFINSFCAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLTSLASGVDPQTSALGYFITPCVGILLSIICYLSLPHLKFARYYLTKKPQAPVQELETKAELLGADEKNGIPVSPQQAGPTLDLDPEKELELGLEEPQKPGKPSVFVVFRKIWLTALCLVLVFTVTLSVFPAITAMVTTSSNSPGKWSQFFNPICCFLLFNVMDWLGRSLTSYFLWPDEDSQLLPLLVCLRFLFVPLFMLCHVPQRARLPIIFWQDAYFITFMLLFAISNGYFVSLTMCLAPRQVLPHEREVAGALMTFFLALGLSCGASLSFLFKALL
Protein: Peptide ABC transporter, permease protein (Q88AW8)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Inner membrane ABC transporter permease protein YejB
- ABC-type dipeptide transporter
- Bacterial extracellular solute-binding protein, family 5
- Peptide ABC transporter, permease protein
- ABC transporter, permease protein
- Inner membrane ABC transporter permease protein YejB
- Inner membrane ABC transporter permease protein YejB
- ABC transporter, periplasmic substrate-binding protein
- Peptide ABC transporter, periplasmic peptide-binding protein
- ABC transporter, periplasmic substrate-binding protein
Sequence:
MFEFSPQTQRRFALFKANRRGWWSLWIFIGLMLVCLCGELIANDKPLLINYDGQMYYPVLHTYMETDFGGELPFEPDYASDYVRKLIAAKNGWMLFAPIPFSYDTINYDLDAPSPSPPDGTNWLGTDEQARDVLARVLFGARISILFALLLTVISTVIGVCAGAIQGYYGGMTDLIGQRIQEIWSGLPVLYLLIILSGFVSPSFWWLLGIMALFSWLSLVDVVRAEFLRGRNLEYVKAARALGLTDAALMWRHILPNAMTSTLTYLPFIITGAIATLTALDFLGFGMPAGSASLGELIGEAKRNLQAPWLGLTAFVALALILSLLVFIGEACRDAFDPRS
Protein: Protein DETOXIFICATION 33 (AtDTX33) (Multidrug and toxic compound extrusion protein 33) (MATE protein 33) (Q9SX83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidate cytidylyltransferase, mitochondrial
- Protein PHLOEM UNLOADING MODULATOR
- HSR201-like protein
- Protein DETOXIFICATION 42
- Protein DETOXIFICATION 43
- Chloride channel protein CLC-c
Sequence:
MGKDKTLPLLDPREPPELTGTKSASKVWAKEFGEESKRLWELAGPAIFTAISQYSLGALTQTFSGRLGELELAAVSVENSVISGLAFGVMLGMGSALETLCGQAYGAGQIRMMGIYMQRSWVILFTTALFLLPVYIWAPPILSFFGEAPHISKAAGKFALWMIPQLFAYAANFPIQKFLQSQRKVLVMAWISGVVLVIHAVFSWLFILYFKWGLVGAAITLNTSWWLIVIGQLLYILITKSDGAWTGFSMLAFRDLYGFVKLSLASALMLCLEFWYLMVLVVVTGLLPNPLIPVDAISICMNIEGWTAMISIGFNAAISVRVSNELGAGNAALAKFSVIVVSITSTLIGIVCMIVVLATKDSFPYLFTSSEAVAAETTRIAVLLGFTVLLNSLQPVLSGVAVGAGWQALVAYVNIACYYIIGLPAGLVLGFTLDLGVQGIWGGMVAGICLQTLILIGIIYFTNWNKEAEQAESRVQRWGGTAQE
Protein: GDP-L-fucose synthase (EC 1.1.1.271) (GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase) (Protein FX) (Red cell NADP(H)-binding protein) (Short-chain dehydrogenase/reductase family 4E member 1) (Q13630)
Organism: Homo sapiens (Human)
Function: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Interaction partners:
- GDP-mannose 4,6 dehydratase
- Fucose-1-phosphate guanylyltransferase
- Ubiquitin-like protein FUBI
- Ubiquitin-conjugating enzyme E2 L5
- L-fucose kinase
- UDP-glucose 4-epimerase
- UDP-glucose 6-dehydrogenase
Sequence:
MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTPFKQAVKETCAWFTDNYEQARK
Protein: Cyclopropane mycolic acid synthase 1 (CMAS) (EC 2.1.1.79) (Cyclopropane-fatty-acyl-phospholipid synthase) (CFA synthase) (Cyclopropane fatty acid synthase) (Mycolic acid methyltransferase) (MA-MT) (S-adenosylmethionine-dependent methyltransferase) (AdoMet-MT) (SAM-MT) (A5U866)
Organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Function: Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MPDELKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHTITGLHPKEIHERGLPMSFTFARFLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQFTCQK
Protein: Cornetto, isoform E (M9PBT2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSATLFEMDSQTEEQQQTVCLEEQQLVVGMTSLELSESVVTPGNCDGSDSGLDVASCCHSRITLQRGLSSTSGGYTSSNGLEEIYDSCELKVTTVAQTPSETGSEKTSPPRRTGSVKKKVAMFEPEPTGTPAKDQLRGRVANLKRAESLPRNSAAPGTPGTPSTHRDKARLSTSSFRVPSTTGTPSSSRLARPQKPDTLPNALNRAQSVQRLTQVQRTPSLSRARTPGTPSDDGRWPANRGAARRGMSVTPEVTTNRMRGSPAPGGTLPRRRKQQSVEDLTGGRLSRSNSISRAAIVDARMTSSVMVVPTSRRSLAPAAAKVNSLRRPQPATPRTRIYHETAVQTALTSEDLEQVLGGGLLQTRAVDAVEQRNQSTQAEPDQREFELEQLRHEVRQLSGKLQREREEKLAMQQELHLNTERVMGMLELARVVSASAGTPTSEDSGDGSGHDSLLMLESQIQISGHELFERQQEIGQLRSMCRALQLEMRRSLATQQLLLQEKAAIEQESSELQDFLQHEKAAQCDALRDLEADYQAVKLQLANREEEAKVLRDECRHLVRLNEQRRQENRLLQTKFTALENKSRELIHQQNASVAGASTALSGLHSRLDGLVEQLVYSYSISEQDLEDIRFQAETEHVQNGQRPNGLDLPICPAASGDAIHTLVLASDGSLSPQRNQSFIAAVIGAIRQATTHSGKRLSLRQAGKKNGVGLGSAQAVSAGTQGQEPQGNGDDSDSTEMLDSETEPCLLMMDNVLEDVVHHDSHSHNMVSSCTGMISQIELPTELISQCSHQNNINGGAGGDDSLQQLSQAITNRQQMELHMHKMNGMPMNPRDQCNTEELSCHDSLAELTELPSLMEYSTAQAVVDQVIEVDTLVTKLLKVLRLVQLDNDNCIQQLIVDKNKLQQHKEDMLEKLKDLEDVNLKLQDELMDATQELMIKGSDLSGAKAEMQRHRNEIDSQIKFKSALFRLK
Protein: Ribosomal protein S6 kinase alpha-4 (S6K-alpha-4) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 4) (Nuclear mitogen- and stress-activated protein kinase 2) (RSK-like protein kinase) (RLSK) (Q9Z2B9)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 12
- Ribosomal protein S6 kinase alpha-5
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-dependent transcription factor ATF-2
- Cyclic AMP-dependent transcription factor ATF-6 beta
Sequence:
MGDEDEDEGCAVELQITEANLTGHEEKVSVENFALLKVLGTGAYGKVFLVRKTGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSFCGTIEYMAPEIIRSKAGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPLRIGPVAQDLLQRLLCKDPKKRLGAGPQGAQEVKSHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYSPAGSPPPGDPRIFQGYSFVAPSILFDHNNAVMADVLQAPGAGYRPGRAAVARSAMMQDSPFFQQYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEENTQREVAALRLCQSHPNVVNLHEVLHDQLHTYLVLELLRGGELLEHIRKKRLFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPAEPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRSSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKREGFFLKSVENAPLAKRRKQKLRSAAASRRGSPVPASSGRLPASAAKGTTRRANGPLSPS
Protein: Protein SPH1 (SPA2 homolog 1) (Q06160)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Polarity-determining protein which forms a conjugate with the ubiquitin-like modifier HUB1. Involved in bud site selection and cellular morphogenesis during conjugation. Required for pseudohyphal growth.
Subcellular location: Bud tip. Bud neck. Cytoplasm, cytoskeleton. Note=Sites of polarized growth as bud tip, bud neck and mating projection. Hub1 is necessary for the proper location to mating projections after pheromone alpha treatment.
Interaction partners:
- Bud site selection protein 6
- Protein PEA2
- Putative pterin-4-alpha-carbinolamine dehydratase
- GTPase-activating protein MSB4
Sequence:
MISSELTNDQIIDLISDYKNFKRIIEASVPEDDRRRNQNRQNRNKDLTKLSNVQFWQLTTDVNDELMKRLTDSGADASLNDLDLKRGKAQSKLSRLKDAKFHKLILDIFTEIERRNLHHLDMGTHNNGLDEGDLNFYLNDTLFESFKINDDFMSVNGIISIEVFRELKTQFTLYFQNTLHRIDPVDTTTTRLPILLETIIKIAKLIGDLLPVLSSVSLQSSLENEIVYLKSALSHAITSTRYFLTYGDLIPRIVAQSSISEVIFAFCNIAQIVKIKSTSRDDISRNEGELSDIEAGMKPLKIIEKVKNEKNGKDISSLGDSGSTAVSFPSSGKPITKKSDMPVVVASPSISIIEKSESSIRESGKVRNNTSGETNLASVSPLKNTKNSSRITSEPSPREGLPLKVVSNSRSPSPQGNTLPLIGKFRQDYQASPPKKVITKPVAETAKPYANIPPAADVLYSPTVTKMRKFREKVQKFAPNSGLGLRISTSEENLNNSDVNSTTHNANINNLVEFVESKSMVVLPMAQGILNDVQASKSKLFKSARSVSRLCQNSIEIIPILESVIDMTTKAMVQKSFKLDLGEHCKEIIERLTDCSQKLSELCTYGCDSTKLGKKRFYQKLADILMEVTKRTRELVECVKMANRQTLSQDLSSFFNYRSVQ
Protein: Polyadenylate-binding protein 3 (PABP-3) (Poly(A)-binding protein 3) (O64380)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the cytoplasm, affects both translation and mRNA decay. Inhibits the polyadenylated RNA degradation by the Rrp41p 3'-->5' exonuclease in vitro. Binds with the 5'UTRs of PAB2, PAB3 and with a lower affinity with the 5'UTR of PAB5.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Initiation factor eIF-4 gamma, MA3
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 4E-1
- Eukaryotic translation initiation factor 6-1
- Plant intracellular Ras-group-related LRR protein 6
- Plant intracellular Ras-group-related LRR protein 7
- Plant intracellular Ras-group-related LRR protein 4
- Immune-associated nucleotide-binding protein 4
- Polyadenylate-binding protein-interacting protein 3
Sequence:
MAAAVATGVAPATMVDQVPSPTAQTSVQVPVSIPLPSPVVVADQTHPNSSLYAGDLDPKVTEAHLFDLFKHVANVVSVRVCRDQNRRSLGYAYINFSNPNDAYRAMEALNYTPLFDRPIRIMLSNRDPSTRLSGKGNIFIKNLDASIDNKALFETFSSFGTILSCKVAMDVTGRSKGYGFVQFEKEESAQAAIDKLNGMLMNDKQVFVGHFIRRQERARDENTPTPRFTNVYVKNLPKEIGEDELRKTFGKFGVISSAVVMRDQSGNSRCFGFVNFECTEAAASAVEKMNGISLGDDVLYVGRAQKKSEREEELRRKFEQERINRFEKSQGANLYLKNLDDSVDDEKLKEMFSEYGNVTSSKVMLNPQGMSRGFGFVAYSNPEEALRALSEMNGKMIGRKPLYIALAQRKEDRRAHLQALFSQIRAPGPMSGFHHPPGGPMPGPPQHMYVGQNGASMVPSQPIGYGFQPQFMPGMRPGSGPGNFIVPYPLQRQPQTGPRMGFRRGATNVQQHIQQQQLMHRNPSPGMRYMNGASNGRNGMDSSVPQGILPPIIPLPIDASSISHQKAPLLPISKLTSSLASASPADRTRMLGEQLYPLVERHEPLHVAKVTGMLLEMDQAEILHLMESPEALKSKVSEALDVLRLSVDPTDHDLGFSTTD
Protein: N-succinylarginine dihydrolase (EC 3.5.3.23) (O50175)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
Interaction partners:
- Arginine N-succinyltransferase subunit beta
- N-succinylglutamate 5-semialdehyde dehydrogenase
- Arginine N-succinyltransferase subunit alpha
- Succinylglutamate desuccinylase
- Succinylornithine transaminase/acetylornithine aminotransferase
- NAD-specific glutamate dehydrogenase
- Arginine/ornithine transport ATP-binding protein AotP
- Topoisomerase II
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
Sequence:
MNAHEVNFDGLVGPTHNYGGLSYGNVASQSNSQAVSNPKEAAKQGLAKMKALMEMGFKQGVLAPQARPDTAALRSLGFSGSDEEVIRRAAKEAMPLLAACSSASSMWTANAATVSPSADTADGRVHFTAANLNCKFHRSIEHPTTSRVLAAMFNDERHFAHHAALPAVSQFGDEGAANHTRFCKDYGDAGVEFFVFGRSAFDSRFPAPQRYPARQTLEACQAVARLHGLSEAGVVYAQQNPAVIDQGVFHNDVISVGNGEVLFHHEDAFLDTEKVLAELHDKLGRRGGRFRAICVPRDQVAVEDAVKSYLFNSQLLSKADGSMLLVVPEECRNNPRVWNYLDQLTGDDGPIREVKVFDLKQSMQNGGGPACLRLRVALQERELAAVNPGVIMSAGLYDTLVAWVDRHYRDRLSETDLADPQLLLECRTALDELTQILKLGSVYSFQLD
Protein: 26S proteasome non-ATPase regulatory subunit 6 homolog (26S proteasome regulatory subunit RPN7) (AtRPN7) (26S proteasome regulatory subunit S10 homolog) (Q93Y35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 4 homolog A
- Proteasome subunit beta type-6
- 26S proteasome regulatory subunit 7 homolog A
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- ARM repeat superfamily protein
- 26S proteasome regulatory subunit 7 homolog B
Sequence:
MDGGAEGSQQPHLILANKLFLLTHPDVPDIEKVQLKSEVLDFIRSHGMAPLYETLIASSVLDLDQSLLESMRAANEEELKKLDEKIADAEENLGESEVREAHLAKALYFIRISDKEKALEQLKLTEGKTVAVGQKMDVVFYTLQLAFFYMDFDLVSKSIDKAKKLFEEGGDWERKNRLKVYEGLYCMSTRNFKKAASLFLDSISTFTTYEIFPYETFIFYTVLTSIITLDRVSLKQKVVDAPEILTVLGKIPFLSEFLNSLYECQYKAFFSAFAGMAVQIKYDRYLYPHFRFYMREVRTVVYSQFLESYKSVTVEAMAKAFGVSVDFIDQELSRFIAAGKLHCKIDKVAGVLETNRPDAKNALYQATIKQGDFLLNRIQKLSRVIDL
Protein: Large ribosomal subunit protein uL5 (60S ribosomal protein L11) (P46222)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm {ECO:0000250|UniProtKB:P0C0W9}.
Interaction partners:
- Large ribosomal subunit protein eL37A
- Large ribosomal subunit protein eL30
- 40S ribosomal protein S15
- Elongation factor Ts, mitochondrial
- Eukaryotic translation initiation factor 5A
- Ribosomal protein S30, isoform A
- DSec61alpha
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL13
Sequence:
MAAVTKKIKRDPAKNPMRDLHIRKLCLNICVGESGDRLTRAAKVLEQLTGQQPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILERGLKVREYELRRENFSSTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGYNVNHRKRKSGTVGFQHRLTKEDAMKWFQQKYDGIILNTKK
Protein: Carboxypeptidase N subunit 2 (Carboxypeptidase N 83 kDa chain) (Carboxypeptidase N large subunit) (Carboxypeptidase N polypeptide 2) (Carboxypeptidase N regulatory subunit) (P22792)
Organism: Homo sapiens (Human)
Function: The 83 kDa subunit binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit.
Subcellular location: Secreted.
Interaction partners:
- Carboxypeptidase N catalytic chain
- Carboxypeptidase B
Sequence:
MLPGAWLLWTSLLLLARPAQPCPMGCDCFVQEVFCSDEELATVPLDIPPYTKNIIFVETSFTTLETRAFGSNPNLTKVVFLNTQLCQFRPDAFGGLPRLEDLEVTGSSFLNLSTNIFSNLTSLGKLTLNFNMLEALPEGLFQHLAALESLHLQGNQLQALPRRLFQPLTHLKTLNLAQNLLAQLPEELFHPLTSLQTLKLSNNALSGLPQGVFGKLGSLQELFLDSNNISELPPQVFSQLFCLERLWLQRNAITHLPLSIFASLGNLTFLSLQWNMLRVLPAGLFAHTPCLVGLSLTHNQLETVAEGTFAHLSNLRSLMLSYNAITHLPAGIFRDLEELVKLYLGSNNLTALHPALFQNLSKLELLSLSKNQLTTLPEGIFDTNYNLFNLALHGNPWQCDCHLAYLFNWLQQYTDRLLNIQTYCAGPAYLKGQVVPALNEKQLVCPVTRDHLGFQVTWPDESKAGGSWDLAVQERAARSQCTYSNPEGTVVLACDQAQCRWLNVQLSPQQGSLGLQYNASQEWDLRSSCGSLRLTVSIEARAAGP
Protein: RNA polymerase-like protein (Q381Y8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Spt4/RpoE2 zinc finger domain-containing protein
- Transcription initiation protein, putative
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase II, putative
- DNA-direcetd RNA polymerase II, subunit 9, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase subunit beta
- General transcription factor IIH subunit 4
- TATA box-binding protein-like 1
Sequence:
MFYKMKLERNIKVEPHLLERTLHRHLEEYLRKAVEGTPLHLSLGNALRSGLARTNQNSSAVIIAVLDILNTSSLEGRVLDDGSVSFFVKYEGLVFKLHRGEVIDVIVSSVEREGWWGDVMGVGRMYISRGQMGNEWVYESDGMRGIWITKDGARSVKEGEIVRVRVVAETPQSEGVLAVGSMVGNYLGPL