wanglab/gogpt-training-data huggingface dataset:
Protein: Nonsense-mediated mRNA decay factor SMG7 (Protein SMG7) (SMG7 homolog) (A9QM73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays multiple roles in growth and development. Involved in nonsense-mediated mRNA decay (NMD). May provide a link to the mRNA degradation machinery to initiate NMD and serve as an adapter for UPF proteins function. Required for meiotic progression through anaphase II of pollen mother cells. May counteract cyclin-dependent kinase (CDK) activity at the end of meiosis. May play a role in plant defense through its involvement in NMD. Together with EXA1, helps to restrict cell death induction during pathogen infection in a salicylic acid- (SA) and reactive oxygen species- (ROS) independent manner.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:22974464, ECO:0000269|PubMed:29073135}.
Interaction partners:
- Regulator of nonsense transcripts UPF3
- Regulator of nonsense transcripts 1 homolog
- Regulator of nonsense transcripts UPF2
- Telomerase reverse transcriptase
- RNA-binding protein Y14
- Nuclear cap-binding protein subunit 1
- Protein POLLENLESS 3
- Nuclear cap-binding protein subunit 2
- Protein mago nashi homolog
- Eukaryotic initiation factor 4A-III homolog
Sequence:
MMTLQMDKTTASSSWERAKSIYDEIAELANKRQKAGNPPDPNLLQLLREKYEAIILESHTFSEQHNIEIPLWQLHYKRIEYFRLHINRVLASSTSTAAQNVKGPSKAEQIAQLKLQFRTFLSEATGFYHDMILKIRSKYGLPLGSFSEDQQSQNLSDKDGKELAEVQKALKSCHRCLIYLGDLARYKGMYAEGDSRSRQYASASSYYLQAASLWPASGNPHHQLAIVASYSRDEFVTTYRYFRSLAVEYPFPTARDNLIVAFDKNRQSYEKLFVPSKDSSKRLTGKGRGKGADISLKDATLVAGPEKDKVTIANEMLKAFSIRFVHLNGILFTRTSLETFFDVLASTSSSLREVISLGSAKELTLGIDTSDSALFIVRVVTMLIFSVHNSKKETEGQSYAEIVQRVEPARNSLTASFELLGLVIEKCVQLGDPSSSYFLPGVLVFVEWLACCPDIALGSDPDDRQTAVRNSFWNQFVVFFNQVLSLGPTFIDDVEDETCFSNMSLYDERETENRLALWEDYELRGFLPLLPAQTILNFSRKHSFGTEGPKEKKARIKRIFAAGKALTSVIKVDQNHVYFDSKKKKFLVGVKPADDFLDSHSSPPKACNALQDNQVMIDHNSPIMQLDQQIYMGEEDDDDEVIVFKPLVTEKRKEASDQIYVPSGGFRKSDQVTTMGDFKALSGSDVAFHENQILQARGNASIQVPASVGANLLGPLQPSTQSQAMHMQQVQTQVQVPASVGANLLGLLLTSTQSQAMHMQQVQTQAVNPQPAQSLAASRLQPIQSQVAQPLPSRVVHFQQTQAQVSHVSPAHSQSTSFGGGSKWSPEEAASLASSLSGFAQLGNGHVMRNEMQGNHGVSYYPAHSLPVHQSYNGNGMGGMPYSQSRTPEAVFPPKIDPVLSSGVVADGLGVQSSLAKKNPISRAFRHLGPPPGFNSVPAKLQKEPAPGSELSGNNHLPVDDYSWLDGYQAQSSRGVGLNSSLNYATSGKPEHLGSTGNGLNGPANFPFPGKQVPTSQVQADFPYFQNPQKDNFVDKNHQSTQLPEQYQGQSTWSSRHFV
Protein: Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic (ZmBSD2) (Q9XF14)
Organism: Zea mays (Maize)
Function: Chloroplast chaperone required for RuBisCo complex biogenesis and translational regulation of the RuBisCo large subunit (RbcL). Stabilizes an end-state assembly intermediate of eight RbcL subunits until the small subunits (RBCSs) become available to produce a complete stable RuBisCo complex containing eight small and eight large subunits (By similarity). Involved in the differentiation of bundle sheath cells, especially chloroplast structure.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:10330470}. Note=Associates with chloroplastic polysomes. {ECO:0000269|PubMed:10330470}.
Interaction partners:
- 4a-hydroxytetrahydrobiopterin dehydratase
- Rubisco accumulation factor 1
- Ribulose bisphosphate carboxylase large chain
- BSD domain-containing protein
- Ribulose bisphosphate carboxylase small subunit, chloroplastic
- Photosystem II stability/assembly factor
Sequence:
MAATASLTTTAPSPPALLKASAPLLISFRPVSRHCKNLCIKTKATENDQSAKKHQKVKSILCQDCEGNGAIVCTKCEGNGVNSVDYFEGRFKAGSLCWLCRGKREILCGNCNGAGFLGGFLSTFDETAQ
Protein: Nuclear receptor coactivator (Q7TPU7)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR038181}.
Interaction partners:
Sequence:
MSGMGENTSDPSRAETRKRKECPDQLGPSPKRSTEKRNREQENKYIEELAELIFANFNDIDNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMMLEALDGFFFVVNLEGSVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSMVNGGSWSGEPPRRSSHTFNCRMLVKPLPDSEEEGHDSQEAHQKYEAMQCFAVSQPKSIKEEGEDLQSCLICVARRVPMKERPTLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLVRRCIQKFHTQHEGESLSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQTTNEPQLVISLHMLHREQNVCVMNPDLTGQAMGKPLNPISSSSPAHQALCSGNPGQDMTLGSNINFPMNGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPGQASSVLSPRQRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSNTGNSHSYTNSSLNALQALSEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQAEASCHPEEQKGPNDSSMPQAASGDRAEGHSRLHDSKGQTKLLQLLTTKSDQMEPSPLPSSLSDTNKDSTGSLPGPGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKELSQESSSTAPGSEVTVKQEPASPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTKLIAMKTVKEEVSFEPSDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPTGSVDKQAIINDLMQLTADSSPVPPAGAQKAALRMSQSRMIGSSTSRPSMPSGEWAPQSPAVRVTCAATTGAMNRPVQGGMIRNPTASIPMRANSQPGQRQMLQSQVMNIGPSELEMNMGGPQYNQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALLDQLYLALRNFDGLEEIDRALGIPELVSQSQAVDAEQFSSQESSIMLEQKPPVFPQQYASQAQMAQGGYNPMQDPNFHTMGQRPNYTTLRMQPRPGLRPTGIVQNQPNQLRLQLQHRLQAQQNRQPLMNQISSVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMQQQVQQRTLMMRGQGLNVTPSMVAPAGLPAAMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATTPQSPLMSPRMAHTQSPMMQQSQANPAYQPTSDMNGWAQGSMGGNSMFSQQSPPHFGQQANTSMYSNNMNISVSMATNTGGLSSMNQMTGQMSMTSVTSVPTSGLPSMGPEQVNDPALRGGNLFPNQLPGMDMIKQEGDASRKYC
Protein: Retinol dehydrogenase 14 (EC 1.1.1.300) (Q17QW3)
Organism: Bos taurus (Bovine)
Function: Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol. Shows a very weak activity towards 13-cis-retinol. Has no activity towards steroid.
Interaction partners:
- Retinol dehydrogenase 8
- Short-chain dehydrogenase/reductase family 9C member 7
Sequence:
MAVGTAAALLAALGGILWLAARRFVGSSVQRLHQGRDSGLMRGKTVLITGANSGLGRATAAELLRLGARVIMGCRDRERAEEAAGQLRREVCPAGGPDSGPNSGGAGELVVKELDLASLSSVRSFCQEMLQEEPRLDVLINNAGVFQCPYMKTEDGFEMQFGVNHLGHFLLTNLLLGLLKSSAPSRIVVVSSKLYKYGDINFEDLNSEQSYNKSFCYSRSKLANILFTRELARRLEGTSVTVNVLHPGIVRTNLGRHIHIPLLVRPLFNLVSWAFFKTPEEGAQTAVYLASSPEVEGVSGRYFGDCKEEELLPKAMDESVARKLWDISEVMVGILK
Protein: PSP proline-rich domain-containing protein (O16997)
Organism: Caenorhabditis elegans
Interaction partners:
- Matrin-type domain-containing protein
- Splicing factor 3B subunit 3
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 1 domain-containing protein
- Splicing factor 3B subunit 4
- Pre-mRNA-splicing factor SYF1
- Splicing factor 3A subunit 2
- Splicing factor 3B subunit 6-like protein
- Probable U2 small nuclear ribonucleoprotein A'
- RRM domain-containing protein
Sequence:
MSGEDDYNSDDEANKNLSKKELQELKRKQQKSKKKKESKKRAKATKQAEIETREEPKKEEENGDDLDVEIDYIGETIEIEPDNPHAQYFSAIFDAFKISTDSEDGFSYGHHVSKGEKKDDLGKVGQAERIIQEEMEERAKENTEEKLSRRKLRISLQPSIAKLKETTLRADVVEWADVTSRDPYLLVAMKSYRNSVPVPRHWNAKRKYLAGKRGFERPPFELPDFIKRTGIQDMREALLEKEESQSLKSKMRERARPKLGKIDIDYQKLHDAFFKWQTKPAMTKMGELYYEGKEMEAMMRDKKPGEMSDELRIALGMPIGSNAFKFPPPWLIAMQRYGPPPSFPHIKIPGLNAPIPEGCAFGYHAGGWGKPPVDEYGHPLYGDVFGLAAPAFEPEDESQIERRYWGEIGSDESSDEEESEEEEHADDDDADVEGGFQTPAPVEGMITPSGMTTGITGIETPDTIELRKGKESSVLGTDTPAAAYHIIPEKKNERIGGQMMASSHTYDLSKKHAVRDDGVQISLDPESIDMDEQGLAARYEEQLRKQKHRDDDDEDREDLTDMVAEHAAKQNRKRKVQDDKKNKTSSSSSSGSSGKKHKDFKF
Protein: Lethal giant larvae homologue 2 domain-containing protein (TOM-1 isoform E) (G5EE26)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDRAKKKFASAIDGLRSLHNRTEINVDEKIQSEHCRFTRVVRHGLPEDPRCFAYDPVQRLIAIGTGRGHIRIIGDAGVDYLLKHESGEPVLHMQFLVNEGGLITSCGTDSIHLWNYRQKTAEIVHTVQLSKESVSCIHLPVAGKWLFIGTDKGNVYFLCLNSFLLSPYVINWNKAIDLSCRVHPGPVRQLAVSPAENTKLLIVYDKGIVVQWNLGTREVDRYPLDPPIKSVNWHFDGRQILTGNVDGSISLYNHKKSTEAIQRTTPHGSGPCRPIQQVEWKHMSETESIIMFSGGMPTDDGLPMPALTILKGGKSATVLEMDWPIIQFIPLNQNIWNSIPQCPHSVAVLLKHDFMVLDLNQNGHPVIESPHAMNIHESPVTCMAYYSDCPLDLIGALTLVGTKQRNKEFSARSWPVTGGLGRECATGHQELVVTGHKDGSLKFWQETGEHLQILYKLKSSSHFERLEEMETSDKVSHAVKYIELCLESRQLLVAGISGQVTLFRFTKQEICGTIAVVNIPLLGNLSSNLPNNDFDKSPVPNGPGKEIRRQRKIVSRESTNSLDTSDSGDERIVPFKVRGAPVKRPPGFVPELACFVPWHSHAKVDQITTICLNSSYGIIAIGTSSGLALVDTTQCALIYSWTTNELYGSDPTPAIQLSMQLSDAASPLESPISLEAPKRIISEQKQRSFDARRPQLFKTQSVVENGSLSRGDSQRESPSSGRQLNTSSPSTSSQSLERSMSTQPQESITSLSFIHSYSKKNDSKMSPCLWVGTSAGASLALNLILPEDRFTSTIVVAPSVRGRKHCYYGTVVRLKGQVISQSFMDNTFCIISPASESYKEAAKEQSATSPDRSLLNRVNTKASLAPQYSSSIDSNDEISQILIVAAENEVKVVALPTFSQLYVQKFDEIPLVKATPTHIRGYPCLMCLSAAGQIIMLSLPSLRILQTSTIFPHSVEIDDPLCQKTAFSDHGLGVYMASQTEMEKYTMCSEIAEQTGESLGELFVPCEMPEQPKNNSFLKGVSSIFGGTPRNDPNDIDAILSENMGVKNSSGVNPMRSVARTIPGPSVQMDRAQAGGVSAGQAAAMALQNLNERTEKLNATVDATENLKNNAMSLSSRTGKLVEKYEKKKWYNF
Protein: ARF GTPase-activating protein GIT1 isoform X1 (G protein-coupled receptor kinase-interacting ArfGAP 1) (A0A0R4IPR8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSRKVQRSEVCADCSAPDPGWSSINRGVLICDECCSVHRSLGRHISIVKHLRHSGWPPSLLQMVQTLASNGANSIWEHSLLDPAQVQSGRRKPNPQDKVHPTKSEFIRAKYQMLAFVHKLPCRDDDGVTTKDLSKQLHSSVRTGSLETCLRLLSLGAQANFFHPEKGTTPLHVAAKAGQVLQAELLVVYGADPGAPDINGRTPIDYARQAGHVELAERLVECQYELTDRLAFYLCGRRPDHKNGHYIIPQMADRARPKCPTQSLDLSELAKAAKKKLQALNNRLFEELAMDVYDEVDRRENDAVWLTTQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSDAKRRQHGKGLTSPTDPLDLSQVDDDQHDYDSVASDEDTDSELTAQNNNNTQRNNRAKSMDSSDLSDGPITLQEYLEVKKALASSEAKVQQLMKVNNNLSEELRRLQKEISRMQTENSALRGAQAGSGATMTGGGVPGHWPDRVRGMGGGGGLSGDSSLIAPSSTPHRRDRQAFSMYEPVGTTSKVLSPALDPLTCRLQPLSPVRKGAPAGPTPYGGAHLSASTDGRYNHPKAGEKYGSGTDSDYDNSQTYDVSIGVGRSSEEDSRGDVDDTEGDPDPTLPCTEDVILKTEQVTKNIQELLRAAQEFKHDSFVPCSEKIHLAVTEMASLFPKRPALDAVRSSLKLLAASASRLQVECRKAAPSDSSASTVDYQLLTQQVIQCAYDIAKAAKQLVTITTREKKQ
Protein: Interleukin-1 receptor-associated kinase 1-binding protein 1 (IRAK1-binding protein 1) (Q5VVH5)
Organism: Homo sapiens (Human)
Function: Component of the IRAK1-dependent TNFRSF1A signaling pathway that leads to NF-kappa-B activation and is required for cell survival. Acts by enhancing RELA transcriptional activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MSLQKTPPTRVFVELVPWADRSRENNLASGRETLPGLRHPLSSTQAQTATREVQVSGTSEVSAGPDRAQVVVRVSSTKEAAAEAKKSVCRRLDYITQSLQQQGVQAENITVTKDFRRVENAYHMEAEVCITFTEFGKMQNICNFLVEKLDSSVVISPPQFYHTPGSVENLRRQACLVAVENAWRKAQEVCNLVGQTLGKPLLIKEEETKEWEGQIDDHQSSRLSSSLTVQQKIKSATIHAASKVFITFEVKGKEKRKKHL
Protein: Carbonic anhydrase 4 (EC 4.2.1.1) (Carbonate dehydratase IV) (Carbonic anhydrase IV) (CA-IV) (P48283)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Catalyzes the reversible hydration of carbon dioxide into bicarbonate and protons and thus is essential to maintaining intracellular and extracellular pH. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P22748}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P22748}.
Interaction partners:
Sequence:
MQLLFALLALGALRPLAGEELHWCYEIQASNYSCLGPDKWQEDCQKSRQSPINIVTTKAEVDHSLGRFHFSGYDQREARLVENNGHSVMVSLGDEISISGGGLPARYRATQLHLHWSQELDRGSEHSLDGERSAMEMHIVHQKETGTSGNEVQDSDDSIAVLAFLVEAGPTMNEGFQPLVTALSAISIPGTNTTMAPSSLWDLLPAEEELRHYFRYMGSLTTPACSETVVWTVFQEPIRLHRDQILEFSSKLYYDQERKMNMKDNVRPLQRLGDRSVFKSQAAGQLLPLPLPTLLVPTLACVMAGLLR
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (Brain cyclic nucleotide-gated channel 2) (BCNG-2) (Q9UL51)
Organism: Homo sapiens (Human)
Function: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10228147, ECO:0000269|PubMed:10524219}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
- Cdc42 effector protein 5
Sequence:
MDARGGGGRPGESPGATPAPGPPPPPPPAPPQQQPPPPPPPAPPPGPGPAPPQHPPRAEALPPEAADEGGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKVSFSCRGAASGPAPGPGPAEEAGSEEAGPAGEPRGSQASFMQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPRNCWVSINGMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLNSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPPQVTSAIATLQQAAAMSFCPQVARPLVGPLALGSPRLVRRPPPGPAPAAASPGPPPPASPPGAPASPRAPRTSPYGGLPAAPLAGPALPARRLSRASRPLSASQPSLPHGAPGPAASTRPASSSTPRLGPTPAARAAAPSPDRRDSASPGAAGGLDPQDSARSRLSSNL
Protein: Photosystem II reaction center protein L (PSII-L) (Q2LIJ7)
Organism: Oryza grandiglumis (Wild rice) (Oryza sativa var. grandiglumis)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid, chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01317}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01317}.
Interaction partners:
Sequence:
MTQSNPNEQNVELNRTSLYWGLLLIFVLAVLFSNYFFN
Protein: Adenylate kinase (AK) (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (P9WKF5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with GTP or UTP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
Interaction partners:
- Protein translocase subunit SecY
- Methionine aminopeptidase 1
- Adenosine kinase
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- ATP synthase subunit b-delta
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL5
- Nucleoside diphosphate kinase
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MRVLLLGPPGAGKGTQAVKLAEKLGIPQISTGELFRRNIEEGTKLGVEAKRYLDAGDLVPSDLTNELVDDRLNNPDAANGFILDGYPRSVEQAKALHEMLERRGTDIDAVLEFRVSEEVLLERLKGRGRADDTDDVILNRMKVYRDETAPLLEYYRDQLKTVDAVGTMDEVFARALRALGK
Protein: Ciliated left-right organizer metallopeptidase (EC 3.4.24.-) (Leishmanolysin-like peptidase 2) (A0A1L8HYT7)
Organism: Xenopus laevis (African clawed frog)
Function: Putative metalloprotease playing a role in the process of LR patterning.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- LOC496290 protein
Sequence:
MTVSFSMFQIYRLVWLSFMTSMCLSACIHDSVLQETPVVSSNIISSRVPRLFPRSTSSDYFQPLRVTPWYLLGENAFISQGQIRQLKIALQEVTQMLSSTLSVHRSEGSLLLNRDISRFCRSVWRAPNDNKCAYMQTSYQGEKCLDVTIPDFHLQGVKVWSDLEKEPRTVIEDGAGVPDTDFLLYVQVAQTQKCAAQPSVIAYASYCQQDPTGRPLAGVIVFCTDHLREEEYNQRHIIQVALHELLHTLGFSSSLYASWLDCSLAEYGEACSSRTRVTNTDENGQFRIYTPTVMQKMGEHLGVEGVGAPLENKGFPNLASSHWESRFFQGSIMTALLSPPHLTHLDPITLAAFTDMGWYKVNATIKSQLMWGKGAGRYFGLPTTCQDSSTGFFCTGSKLGCHHLHLDKGNCSTDSYLEGCHIYSPLIHGGECWRHQNSGDPDEIFHAQSRCFYSNLTKGASPNQEFRGRCYLHQCLGENHFQVKVHESEWTDCPAGAWIQVAGYEGFIQCPSGCLCLGFQTPHVATLTPTYVTGQITTVKENNVYPTEGIVQFRVQVEVSQRHKWTSEIKSFLLDEVLGVIAQKAGVQRCFLQSHMKEDLDLSFAIVGKWSTDCPPTPEADTAAFSLLTLNQDGAPYIIYNSSYFSTVSIRFIDSDPPALYVSHMLYSYVIGGGCCAVCGAAIIFALFWYKLRRQFLRVGSSYPPETSNHERPQIPADLV
Protein: MAGA (O13314)
Organism: Pyricularia grisea (Crabgrass-specific blast fungus) (Magnaporthe grisea)
Interaction partners:
Sequence:
MMGACMSASSEESEQKKRSQKIDKDLEEDSKRLRRECKILLLGSGESGKSTIVKQMKIIHLKGYSDDELYNYRPTVFKNLIECAKAVISAMRQFDIEPQLEGNKELCDYLLDYMVESGPQAEIDPKVGQAVQSIWNDPAREQLMDRQTEFYLMDSAEYFFQEVLRIVSPDYLPNEMDVLRARTKTTGIYETRFQMGQLSIHMFDVGGQRSERKKWIHCFENVTSIIFCVALSEYDQVLLEESSQNRMMESLLLFDSVVNSRWFMRTSIILFLNKVDIFKQKLGRSPLGNYFPDYSGGNDVNKADKYLLWRFNQVNRAHLNLYPHLTQATDTSNIRLVFAAVKETILNNALKDSGIL
Protein: Acyl-CoA wax alcohol acyltransferase 1 (EC 2.3.1.75) (Diacylglycerol O-acyltransferase 2-like protein 3) (Diacylglycerol acyltransferase 2) (Long-chain-alcohol O-fatty-acyltransferase 1) (Q58HT5)
Organism: Homo sapiens (Human)
Function: Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters. Shows a strong preference for decyl alcohol (C10), with less activity towards C16 and C18 alcohols. Shows a strong preference for saturated acyl-CoAs.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6E213}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Very long chain fatty acid elongase 2
- Very long chain fatty acid elongase 3
- Long-chain fatty acid transport protein 1
- Diacylglycerol O-acyltransferase 1
- Fatty acid-binding protein, adipocyte
- Very long chain fatty acid elongase 1
Sequence:
MAHSKQPSHFQSLMLLQWPLSYLAIFWILQPLFVYLLFTSLWPLPVLYFAWLFLDWKTPERGGRRSAWVRNWCVWTHIRDYFPITILKTKDLSPEHNYLMGVHPHGLLTFGAFCNFCTEATGFSKTFPGITPHLATLSWFFKIPFVREYLMAKGVCSVSQPAINYLLSHGTGNLVGIVVGGVGEALQSVPNTTTLILQKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHKDSRMYKFQSCFRRIFGFYCCVFYGQSFCQGSTGLLPYSRPIVTVVGEPLPLPQIEKPSQEMVDKYHALYMDALHKLFDQHKTHYGCSETQKLFFL
Protein: TOX high mobility group box family member 2 (Granulosa cell HMG box protein 1) (GCX-1) (Q76IQ7)
Organism: Rattus norvegicus (Rat)
Function: Putative transcriptional activator involved in the hypothalamo-pituitary-gonadal system.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:14764631}.
Interaction partners:
Sequence:
MSDGNPELLSTSQTYNSQGESNEDYEIPPITPPNLPEPSLLHLGDHEAGYHSLCHGLAPNGLLPAYSYQAMDLPAIMVSNMLAQDGHLLSGQLPTIQEMVHSEVAAYDSGRPGPLLGRPAMLASHMSALSQSQLISQMGLRSGIAHSSPSPPGSKSATPSPSSSTQEEESDAHFKISGEKRPSTDPGKKAKNPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPSATFGDVSKIVASMWDSLGEEQKQAYKRKTEAAKKEYLKALAAYRASLVSKSPPDQGEAKNAQANPPAKMLPPKQPMYAMPGLASFLTPSDLQAFRSAASPASLARTLGSKALLPGLSTSPPPPSFPLSPSLHQQLPLPPHAQGTLLSPPLSMSPAPQPPVLPAPMALQVQLAMSPSPPGPQDFPHISDFPSGSGSRSPGPSNPSSSGDWDGSYPSGERGLGTCRLCRSSPPPTTSPKNLQEPSAR
Protein: Actin, cytoplasmic 1 (EC 3.6.4.-) (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed] (P60711)
Organism: Rattus norvegicus (Rat)
Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60709}. Nucleus {ECO:0000250|UniProtKB:P60709}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P60709}.
Interaction partners:
- Actin, cytoplasmic 2
- Caspase-3
- Profilin-2
- Cofilin-1
- Tight junction protein ZO-1
- Alpha-centractin
- Actin-related protein 10
- Myosin-9
- Integrin beta-1
- Transforming protein RhoA
Sequence:
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Phytochrome B (P93527)
Organism: Sorghum bicolor (Sorghum) (Sorghum vulgare)
Function: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion.
Interaction partners:
Sequence:
MASGSRATPTRSPSSARPEAPRHAHHHHHHHSQSSGGSTSRAGGGGGGGGGGGGTAATATATATESVSKAVAQYTLDARLHAVFEQSGASGRSFDYSQSLRAPPTPSSEQQIAAYLSRIQRGGHIQPFGCTLAVADDSSFRLLAFSENAADLLDLSPHHSVPSLDSAAPPPVSLGADARLLFSPSSAVLLERAFAAREISLLNPLWIHSRVSSKPFYAILHRIDVGVVIDLEPARTEDPALSIAGAVQSQKLAVRAISRLQALPGGDIKLLCDTVVEHVRELTGYDRVMVYRFHEDEHGEVVAESRRDNLEPYLGLHYPATDIPQASRFLFRQNRVRMIADCHATPVRVIQDPGMSQPLCLVGSTLRAPHGCHAQYMANMGSIASLVMAVIISSGGDDEQTGRGGISSAMKLWGLVVCHHTSPRCIPFPLRYACEFLMQAFGLQLNMELQLAHQLSEKHILRTQTLLCDMLLRDSPTGIVTQSPSIMDLVKCDGAALYYHGKYYPLGVTPTESQIKDIIEWLTVCHGDSTGLSTDSLADAGYLGAAALGDAVCGMAVAYITPSDYLFWFRSHTAKEIKWGGAKHHPEDKDDGQRMHPRSSFKAFLEVVKSRSLPWENAEMDAIHSLQLILRDSFRDAAEGTSNSKAIVNGQVQLGELELRGINELSSVAREMVRLIETATVPIFAVDTDGCINGWNAKIAELTGLSVEEAMGKSLVNDLIFKESEEIVEKLLSRALRGEEDKNVEIKLKTFGSEQSNGAIFVIVNACSSRDYTQNIVGVCFVGQDVTGQKVVMDKFINIQGDYKAIVHNPNPLIPPIFASDENTSCSEWNTAMEKLTGWSRGEVVGKFLIGEVFGSFCRLKGPDALTKFMVVIHNAIGGQDYEKFPFSFFDKNGKYVQALLTANTRSKMDGKSIGAFCFLQIASAEIQQAFEIQRQQEKKCYARMKELAYICQEIKNPLSGIRFTNSLLQMTDLNDDQRQFLETCSACEKQMSKIVKDATLQSIEDGSLVLEKSEFSFGDVMNAVVSQAMLLLRERDLQLIRDIPDEIKDASAYGDQFRIQQVLADFLLSMVRSAPSENGWVEIQVRPNVKQNSDGTDTELFIFRFACPGEGLPADIVQDMFSNSQWSTQEGVGLSTCRKILKLMGGEVQYIRESERSFFLIVLELPQPRPAADREIS
Protein: Proton myo-inositol cotransporter (H(+)-myo-inositol cotransporter) (Hmit) (H(+)-myo-inositol symporter) (Solute carrier family 2 member 13) (Q921A2)
Organism: Rattus norvegicus (Rat)
Function: H(+)-myo-inositol cotransporter. Can also transport related stereoisomers.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11500374}; Multi-pass membrane protein {ECO:0000269|PubMed:11500374}.
Interaction partners:
Sequence:
MSRKASEDVEYTLRSLSSLMGERRRRQPEPGAPGGERSLLAAESAASLQGAELERAARRQFQRDETPAFVYAAAAFSALGGFLFGYDTGVVSGAMLLLRRQMRLGAMWQELLVSGAVGAAAVAALAGGALNGALGRRSAILLASALCTVGSAVLAAAANKETLLAGRLVVGLGIGIASMTVPVYIAEVSPPNLRGRLVTINTLFITGGQFFASVVDGAFSYLQKDGWRYMLGLAAIPAVIQFLGFLFLPESPRWLIQKGQTQKARRILSQMRGNQTIDEEYDSIRNSIEEEEKEASAAGPIICRMLSYPPTRRALAVGCGLQMFQQLSGINTIMYYSATILQMSGVEDDRLAIWLASITAFTNFIFTLVGVWLVEKVGRRKLTFGSLAGTTVALTILALGFLLSAQVSPRVTFRPTAPSGQNATCTEYSYCNECMLDPDCGFCYKINSSAVIDSSCVPVNKASTNEAAWGRCENETKFKAEDVHWAYSFCPTPYSWTALVGLVLYLVFFAPGMGPMPWTVNSEIYPLWARSTGNACSAGINWIFNVLVSLTFLHTAEYLTYYGAFFLYAGFAAVGLLFVYGCLPETKGKKLEEIESLFDHRLCTCGTADSDEGRYIEYIRVKGSNYHLSDNDASDVE
Protein: Probable acetyl-CoA acyltransferase FadA2 (3-ketoacyl-CoA thiolase) (Beta-ketothiolase) (O86361)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable fatty oxidation protein FadB
- 3-hydroxyacyl-thioester dehydratase X
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Probable 3-hydroxybutyryl-CoA dehydrogenase FadB3
- 3-hydroxybutyryl-CoA dehydrogenase
- Acetyl-coenzyme A synthetase
- Malate synthase G
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B
- 2-isopropylmalate synthase
- Conserved protein
Sequence:
MAPAAKNTSQTRRRVAVLGGNRIPFARSDGAYADASNQDMFTAALSGLVDRFGLAGERLDMVVGGAVLKHSRDFNLMRECVLGSELSPYTPAFDLQQACGTGLQAAIAAADGIAAGRYEVAAAGGVDTTSDPPIGLGDDLRRTLLKLRRSRSNVQRLKLVGTLPASLGVEIPANSEPRTGLSMGEHAAVTAKQMGIKRVDQDELAAASHRNMADAYDRGFFDDLVSPFLGLYRDDNLRPNSSVEKLATLRPVFGVKAGDATMTAGNSTPLTDGASVALLASEQWAEAHSLAPLAYLVDAETAAVDYVNGNDGLLMAPTYAVPRLLARNGLSLQDFDFYEIHEAFASVVLAHLAAWESEEYCKRRLGLDAALGSIDRSKLNVNGSSLAAGHPFAATGGRILAQTAKQLAEKKAAKKGGGPLRGLISICAAGGQGVAAILEA