wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor LUX (Protein LUX ARRHYTHMO) (Protein PHYTOCLOCK 1) (Q9SNB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that is essential for the generation of the circadian clock oscillation. Is necessary for activation of CCA1 and LHY expression. Is coregulated with TOC1 and seems to be repressed by CCA1 and LHY by direct binding of these proteins to the evening element in the LUX promoter. Directly regulates the expression of PRR9, a major component of the morning transcriptional feedback circuit, by binding specific sites on PRR9 promoter. Binds to its own promoter, inducing a negative auto-regulatory feedback loop within the core clock. Binds to ELF3 and associates with ELF4 in a diurnal complex which is required for the expression of the growth-promoting transcription factors PIF4 and PIF5 and subsequent hypocotyl growth in the early evening.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:16164597, ECO:0000269|PubMed:22327739}.
Interaction partners:
- Protein EARLY FLOWERING 3
- Protein EARLY FLOWERING 4
- Two-component response regulator-like APRR1
- Protein CCA1
- Protein LHY
- Two-component response regulator-like APRR9
- Two-component response regulator-like APRR7
- Transcription factor PIF4
- Two-component response regulator-like APRR5
- Protein GIGANTEA
Sequence:
MGEEVQMSDYDVSGDGDRVSEWEMGLPSDEDLASLSYSLIPPNLAMAFSITPERSRTIQDVNRASETTLSSLRGGSSGPNTSSSNNNVEEEDRVGSSSPGSDSKKQKTSNGDGDDGGGVDPDSAMAAEEGDSGTEDLSGKTLKRPRLVWTPQLHKRFVDVVAHLGIKNAVPKTIMQLMNVEGLTRENVASHLQKYRLYLKRMQGLTNEGPSASDKLFSSTPVPPQSFQDIGGGGGSSGNVGVPIPGAYGTQQMMQMPVYAHHMGMQGYHHQNHNHDPYHQNHRHHHGAGGNGAFESNPYMMQQNKFGSMASYPSVGGGSANEN
Protein: Cytochrome P450, family 705, subfamily A, polypeptide 8 (Putative cytochrome P450) (Q9ZVD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH10
Sequence:
MGEIMNVDFVNCLILILLCLLSILCYSFFFKKPKDGFNLPPSPPSLPIIGHLHHLLSLFMHRSLQKLSSKYGPLLYLHVFNVPILLVSSPSIAYEIFRAQDVNVSTRDFPTNEGSLFLGSFSFITAPYGEYWKFMKKLIVTKLLGPQALERSQRIRANEVERFYSNLLDKAMKKESVEIADEAMKLVNNIICKMIMGRTCSEENGEAERIRGLVTKSDALLKKFLLAAILRKPLKKIGITLFKKVFMDISLKFDEVLEKILVENEERLEENQQGTDIMDKLLEVYGDKTSEYKITRDHIKSLFVDLFFAGTDTATHTIEWTMAEIMNNSLILERLREEIDSVVGKTRLIQETDLPNLLYLQATVKEGLRLHPTIPLVLRTFQDGCTIGGFSIPKKTKLVVNGYAIMRDPDNWEDPLEFKPERFLASSRSSQKDAIKEEVLKYLSFGSGRRGCPGVNLAYVSVETAIGVMVQCFDWKIDGHKINMNEVAGKGTLSMAHPLKCTLVPRSVTPLTSK
Protein: Cystinosis nephropathic isoform 1 (A0A0S2Z3I9)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MIRNWLTIFILFPLKLVEKCESSVSLTVPPVVKLENGSSTNVSLTLRPPLNATLVITFEITFRSKNITILELPDEVVVPPGVTNSSFQVTSQNVGQLTVYLHGNHSNQTGPRIRFLVIRSSAISIINQVIGWIYFVAWSISFYPQVIMNWRRKSVIGLSFDFVALNLTGFVAYSVFNIGLLWVPYIKEQFLLKYPNGVNPVNSNDVFFSLHAVVLTLIIIVQCCLYERGGQRVSWPAIGFLVLAWLFAFVTMIVAAVGVTTWLQFLFCFSYIKLAVTLVKYFPQAYMNFYYKSTEGWSIGNVLLDFTGGSFSLLQMFLQSYNNDQWTLIFGDPTKFGLGVFSIVFDVVFFIQHFCLYRKRPGLQAARTGSGSRLRQDWAPSLQPKALPQTTSVSASSLKG
Protein: Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (C1P634)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQRVRRLLLAAKLRRTQSEDVPSSNSMQKEKTMMMKGHLYGTPRPVECYADDDMMLMGSEGLLPPNWETAYTENGDKYFIDHNTGTTTWDDPRELPPGWEQVDDQNYGTFYVDHINRKTQYERPYGFGGSSATIDQPVKYGTLPSSTNHNHNNIYSHYNSGTLKSSSSPRDSGFDSSPTRYRKFGDPPETATSSADYDHHSKMFSRSSNPLFTTDPARLGGELISTKIVKGAKGLGFTLIGNDSSSRGDEFIQVKSVLSGGPAAANGVLRSGDILVRVNGRLLLGATQKEACDVFVAIPVNEAVDIQVCRGYELFIDPANRIVTENVYAAAKSRDLHEIDIFKGSEGFGFTIADNLNGQRIKKILFPSQCPNLMEGDTIVELDGRNVRPIPHTQLVDMLRERPIGYRGKLVVKRGSPKTRSRTPSAAFRYGEPQTNMMDSAAPLPVRSKTPAERQTSRTEEDQNVRNTLQRQPAVTSEWEGMSSAIPASRMRPSSTTLGFATPNYIPLSQYNQKPSDLITVSLIRKPVGFGFRLLGGVESKTPLSVGQIVIGGAAEEDGRLQEGDEIVEIDGHNVEGASHSEAVVLLEAAAQNKHVKLIVRRPSRTDPARRGSLNSAGPSGSYDVLLHRNENDGFGFVLMSSQHKNGSTVGQIQPGSPAARCGRLSVGDRVIAVNGIDILSLSHPDTISLIKDSGLSVRLTIAPPNTAGPVLPMVSATLGRNFTMNGHYESNYGLPPPPPSVYEKHPPPSYLAFDGLSINDRMSMNGNLIDVTLERGTKGFGFSIRGGQEFGSMPLFVLRIADDGPAKADGRLQVGDQLTTINGQSTKGMSHDDAIRIIKQHTMVNLTVLRNRLP
Protein: Meiotic driver wtf18 (A0A482ARC8)
Organism: Schizosaccharomyces pombe (Fission yeast)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele.
Subcellular location: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
Interaction partners:
Sequence:
MKNKGYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTETTNPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFFVTIGITCPILLITIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAVFLAKCIKVTAVFLAKCVKVTAVFLAKCIKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV
Protein: Trimethylamine-N-oxide reductase 1 (TMAO reductase 1) (Trimethylamine oxidase 1) (EC 1.7.2.3) (P33225)
Organism: Escherichia coli (strain K12)
Function: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.
Subcellular location: Periplasm {ECO:0000269|PubMed:2512991}.
Interaction partners:
- Cytochrome c-type protein TorC
- Chaperone protein TorD
- Cytochrome c-type protein TorY
- Tat proofreading chaperone DmsD
- Trimethylamine-N-oxide reductase 2
- Cell division protein FtsP
- TorCAD operon transcriptional regulatory protein TorR
- Sec-independent protein translocase protein TatC
- Sec-independent protein translocase protein TatB
- Periplasmic protein TorT
Sequence:
MNNNDLFQASRRRFLAQLGGLTVAGMLGPSLLTPRRATAAQAATDAVISKEGILTGSHWGAIRATVKDGRFVAAKPFELDKYPSKMIAGLPDHVHNAARIRYPMVRVDWLRKRHLSDTSQRGDNRFVRVSWDEALDMFYEELERVQKTHGPSALLTASGWQSTGMFHNASGMLAKAIALHGNSVGTGGDYSTGAAQVILPRVVGSMEVYEQQTSWPLVLQNSKTIVLWGSDLLKNQQANWWCPDHDVYEYYAQLKAKVAAGEIEVISIDPVVTSTHEYLGREHVKHIAVNPQTDVPLQLALAHTLYSENLYDKNFLANYCVGFEQFLPYLLGEKDGQPKDAAWAEKLTGIDAETIRGLARQMAANRTQIIAGWCVQRMQHGEQWAWMIVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRKGVILSGFSGSTSIPPVHDNSDYKGYSSTIPIARFIDAILEPGKVINWNGKSVKLPPLKMCIFAGTNPFHRHQQINRIIEGLRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQYGNHSNRGIIAMKQVVPPQFEARNDFDIFRELCRRFNREEAFTEGLDEMGWLKRIWQEGVQQGKGRGVHLPAFDDFWNNKEYVEFDHPQMFVRHQAFREDPDLEPLGTPSGLIEIYSKTIADMNYDDCQGHPMWFEKIERSHGGPGSQKYPLHLQSVHPDFRLHSQLCESETLRQQYTVAGKEPVFINPQDASARGIRNGDVVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWYDPDKGGEPGALCKYGNPNVLTIDIGTSQLAQATSAHTTLVEIEKYNGTVEQVTAFNGPVEMVAQCEYVPASQVKS
Protein: Protein TFG (C9JJP5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNGQLDLSGKLIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFVNGQPRPLESSQVKYLRRELIELRNKVNRLLDSLEPPGEPGPSTNIPENDTVDGREEKSASDSSGKQSTQVMAASMSAFDPLKNQDEINKNV
Protein: Serine and arginine rich splicing factor 2 (J3QL05)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRSRSRSRSRSRSRSRSRYSRSKS
Protein: C2H2-like zinc finger protein (Q9SZH7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVSPFSMPFIAQTSGFVNYSQVFITQTIAKRYHALIPTSNMVIVQNDNDRVNRFMTSYPPILKSTVNPPNDFDKQYETFTPKPIDFFCSQQDYACRQHLDIFSSSPKHYHEQYVHKNGRSVKYICKPTEVLEEIHDEIDYEKDGGWIYSLPFEKDSSFICLKCNSLFDTSQMLVVHTELIHSKNETKKRLKLHHQEFHGKSHKINKDQTGGQSCRRKLRQ
Protein: Hemomucin (Q58SN0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VTPPKDLKGALESNFHLEGAERLLEWRVYGPECLIARNNEIYTGIHGGEVIKLTSNHVTHVTKIGQPCEDIYEESRCGRPLGLAFDTQGNNLIIADAYYGLWQVDLGTNKKTLLVSLAQELAGKSINRPAKIFNGVTVSKEGDVYWTDSSSDFTIEDLVFASFANPSGRLFKYNRSKNVSEVLLDELAFANGLALSPNEDFIVVAETGAMRLTKYHLKGAKAGQSEVFVDGLPGLPDNLTPDAEGIWVPLVQSADSEHPNGFTLFTRFPSVRLFLARMLALFELPFRYLNSVYPNKFSQRFIHFVGHMESITVLAPKRTTVVRVDWNGNIVGSLHGFDKSAATISHVLEFQDFLFLGSPTNQYLARVKSPKAKQPTLKVRNVRVEGEGLEASIGVPPSKATPKPKAAPSTTTPKPTTTTTTTTPKPTTKTTTTTTTPKPTTTTTTKKPTTTTTTTTTTPKPTTTKPPTAKPSTTTTTTTTPKPTTTTTPTTPTTPTPEPSKPKVKRTVPEKPAPVEEEIPSD
Protein: S-arrestin (48 kDa protein) (Retinal S-antigen) (S-AG) (Rod photoreceptor arrestin) (P10523)
Organism: Homo sapiens (Human)
Function: Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO (By similarity). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:3720866}. Membrane {ECO:0000250|UniProtKB:P20443}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20443}. Note=Highly expressed in photoreceptor outer segments in light-exposed retina. Evenly distributed throughout rod photoreceptor cells in dark-adapted retina (By similarity). Predominantly dectected at the proximal region of photoreceptor outer segments, near disk membranes (PubMed:3720866). {ECO:0000250|UniProtKB:P08168, ECO:0000269|PubMed:3720866}.
Interaction partners:
- Rhodopsin
- Rhodopsin kinase GRK1
- Beta-2 adrenergic receptor
- Rhodopsin kinase GRK7
- Recoverin
- Beta-adrenergic receptor kinase 1
- G protein-coupled receptor kinase 3
- Proto-oncogene tyrosine-protein kinase Src
- Kinesin-like protein KIF3A
- Neurabin-2
Sequence:
MAASGKTSKSEPNHVIFKKISRDKSVTIYLGNRDYIDHVSQVQPVDGVVLVDPDLVKGKKVYVTLTCAFRYGQEDIDVIGLTFRRDLYFSRVQVYPPVGAASTPTKLQESLLKKLGSNTYPFLLTFPDYLPCSVMLQPAPQDSGKSCGVDFEVKAFATDSTDAEEDKIPKKSSVRLLIRKVQHAPLEMGPQPRAEAAWQFFMSDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVVLYSSDYYVKPVAMEEAQEKVPPNSTLTKTLTLLPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVLGILVSYQIKVKLTVSGFLGELTSSEVATEVPFRLMHPQPEDPAKESYQDANLVFEEFARHNLKDAGEAEEGKRDKNDVDE
Protein: 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha) (P11960)
Organism: Rattus norvegicus (Rat)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P12694}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyl dehydrogenase, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Branched-chain-amino-acid aminotransferase, cytosolic
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Ac1164
- L-lactate dehydrogenase B chain
Sequence:
SAAKIWRPSRGLRQAALLLLGRPGARGLARFHPSRQQQQQFPSLDDKPQFPGASAEFVDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPQEEVLKLYRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMAQCYGNVSDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANQIVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAERKLKPNPSLLFSDVYQEMPAQLRRQQESLARHLQTYGEHYPLDHFDK
Protein: SNRPN upstream reading frame protein (Q9WU12)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000269|PubMed:10318933}.
Interaction partners:
- Small nuclear ribonucleoprotein-associated protein N
- Small nuclear ribonucleoprotein-associated protein B
- U1 small nuclear ribonucleoprotein A
- Splicing factor 3B subunit 1
- U1 small nuclear ribonucleoprotein 70 kDa
- Splicing factor 3A subunit 1
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MERGRDRLHLRRTTEQHVPEVEVQVKRRRTASLSNQECHLYPRRSQQQQVPVVDFQAELRQAFLAETPRGG
Protein: Kruppel-like protein (Q9QZP7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEMEQLTFRDVAVDFSPDEWECLDPPQQRLYRDVMVENYRNLVSVALSHHCTQNFSPEQILKYSFTEVTNGSYSLQHLYLREDCANVGGNKAAACHGRHKQCLITSNTKDNRDQEQKTALKKPHARTDTFDEPCVYNCKYPQEIFQHDLTLKESWEDLIDRLIFSLKQFHRQRIKKPEDRSLKVIKSSLPILEEPYSFSQAKYQFFLWPKSTILNDXGLPATDPLLHSQNLDTDVWETPYMYKEISKGFSSGSLLNSCNDVVILEKSGQRDKVQNDFDHCLSPNNHQCNLPKKLFNCDNFFTQCSKLTIQQCNYIQDNHYKRYRL
Protein: Dual specificity protein phosphatase 22 (EC 3.1.3.16) (EC 3.1.3.48) (JNK pathway associated phosphatase) (JKAP) (Low molecular weight dual specificity phosphatase 2) (LMW-DSP2) (Q99N11)
Organism: Mus musculus (Mouse)
Function: Activates the Jnk signaling pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NRW4}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 1
- Unconventional myosin-If
- Tropomodulin-3
- PDZ and LIM domain protein 4
- Myosin XVIIIb
- Ras-related C3 botulinum toxin substrate 3
- Actin, cytoplasmic 2
- Cytospin-A
- Espin
- Unconventional myosin-Ic
Sequence:
MGSGMSQILPGLYIGNFKDARDAEQLSRNKVTHILSVHDTARPMLEGVKYLCIPAADTPSQNLTRHFKESIKFIHECRLQGESCLVHCLAGVSRSVTLVIAYIMTVTDFGWEDALHTVRAGRSCANPNLGFQRQLQEFEKHEVHQYRQWLREEYGENPLRDAEEAKNILAAPGILKYWAFLRRL
Protein: cytokine receptor family member B1 (A0FJH7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKTSSSYTGRLFLIHLYFTVIYAIPAPVNFTIWSHNFRHILHWNYGVNSPPQSVFNLQRFEKGKQTEHLNIRNTTMDVSEACQDIYIPCTFLIWASLDNMNSSVIEKKFIPYEDTIIGPPVIFLSGCGDCLNISISLPNESRKDDKLRRFYNSVSYSISWKKHGNNEVREILRSQEPSKQYVLENLQPGVQYCVKVLPQINSNQNTQPSSWQCEYTSKEEAQRVLYFMSWLLGATLSGSCVMMLAWILVYTGFLCKPKNPPLKSLSNIVPATYLIPEQTLSESLSLTEVQLIHLSYDTTENNSQLKNPEKREYEGSVLKSDTEDEEDSNDEDEVKCVYMSCEIDDISCQNNSTKKDIVSALPFNKSSIVCYTKEPAMEKIQYDDLKSEKELLSELFEEGHGHLEVTNTQLKTEGNEKGSTNTPGNINLFSVTVRTFGAEDDLDKEDVYKPLLPKLFVKTDKWTEELLPVSNKIQISIPIETGMKTDDLIHLDSQNDLVHVCSLAHNVETNPDTTMSAYMMNHIGKMHDQNKDLLEETNCDTSYITR
Protein: N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) (EC 3.5.1.114) (Acylase III) (Aminoacylase-3) (ACY-3) (Aspartoacylase-2) (Hepatitis C virus core-binding protein 1) (HCBP1) (HCV core-binding protein 1) (Q96HD9)
Organism: Homo sapiens (Human)
Function: Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:19486448}; Peripheral membrane protein {ECO:0000269|PubMed:19486448}. Cytoplasm {ECO:0000269|PubMed:19486448}. Note=Predominantly localized in the apical membrane of cells in the S1 segment. In the proximal straight tubules (S2 and S3 segments) is expressed diffusely throughout the cytoplasm.
Interaction partners:
- Aminoacylase-1
- Aspartoacylase
Sequence:
MCSLPVPREPLRRVAVTGGTHGNEMSGVYLARHWLHAPAELQRASFSAVPVLANPAATSGCRRYVDHDLNRTFTSSFLNSRPTPDDPYEVTRARELNQLLGPKASGQAFDFVLDLHNTTANMGTCLIAKSSHEVFAMHLCRHLQLQYPELSCQVFLYQRSGEESYNLDSVAKNGLGLELGPQPQGVLRADIFSRMRTLVATVLDFIELFNQGTAFPAFEMEAYRPVGVVDFPRTEAGHLAGTVHPQLQDRDFQPLQPGAPIFQMFSGEDLLYEGESTVYPVFINEAAYYEKGVAFVQTEKFTFTVPAMPALTPAPSPAS
Protein: Ras guanyl-releasing protein 3 (Calcium and DAG-regulated guanine nucleotide exchange factor III) (Guanine nucleotide exchange factor for Rap1) (Q8IV61)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) for Ras and Rap1.
Interaction partners:
- Ras-related protein Rap-1A
- GTPase HRas
- Ras-related protein Rap-1b
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- GTPase NRas
- GTPase KRas
- Son of sevenless homolog 1
- Son of sevenless homolog 2
- Diacylglycerol kinase iota
- RAS guanyl-releasing protein 1
Sequence:
MGSSGLGKAATLDELLCTCIEMFDDNGELDNSYLPRIVLLMHRWYLSSTELAEKLLCMYRNATGESCNEFRLKICYFMRYWILKFPAEFNLDLGLIRMTEEFREVASQLGYEKHVSLIDISSIPSYDWMRRVTQRKKVSKKGKACLLFDHLEPIELAEHLTFLEHKSFRRISFTDYQSYVIHGCLENNPTLERSIALFNGISKWVQLMVLSKPTPQQRAEVITKFINVAKKLLQLKNFNTLMAVVGGLSHSSISRLKETHSHLSSEVTKNWNEMTELVSSNGNYCNYRKAFADCDGFKIPILGVHLKDLIAVHVIFPDWTEENKVNIVKMHQLSVTLSELVSLQNASHHLEPNMDLINLLTLSLDLYHTEDDIYKLSLVLEPRNSKSQPTSPTTPNKPVVPLEWALGVMPKPDPTVINKHIRKLVESVFRNYDHDHDGYISQEDFESIAANFPFLDSFCVLDKDQDGLISKDEMMAYFLRAKSQLHCKMGPGFIHNFQEMTYLKPTFCEHCAGFLWGIIKQGYKCKDCGANCHKQCKDLLVLACRRFARAPSLSSGHGSLPGSPSLPPAQDEVFEFPGVTAGHRDLDSRAITLVTGSSRKISVRLQRATTSQATQTEPVWSEAGWGDSGSHTFPKMKSKFHDKAAKDKGFAKWENEKPRVHAGVDVVDRGTEFELDQDEGEETRQDGEDG
Protein: Protein arginine methyltransferase 2 isoform 1 (A0A0S2Z3N3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATSGDCPRSESQGEEPAECSEAGLLQEGVQPEEFVAIADYAATDETQLSFLRGEKILILRQTTADWWWGERAGCCGYIPANHVGKHVDEYDPEDTWQDEEYFGSYGTLKLHLEMLADQPRTTKYHSVILQNKESLTDKVILDVGCGTGIISLFCAHYARPRAVYAVEASEMAQHTGQLVLQNGFADIITVYQQKVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDAWLKEDGVIWPTMAALHLVPCSADKDYRSKVLFWDNAYEFNLSALKSLAVKEFFSKPKYNHILKPEDCLSEPCTILQLDMRTVQISDLETLRGELRFDIRKAGTLHGFTAWFSVHFQSLQEGQPPQVLSTGPFHPTTHWKQTLFMMDDPVPVHTGDVVTGSVVLQRNPVWRRHMSVALSWAVTSRQDPTSQKVGEKVFPIWR
Protein: Glycerate 2-kinase (EC 2.7.1.165) (Glycerate kinase 1) (GK1) (P23524)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of the phosphate group from adenosine triphosphate (ATP) to (R)-glycerate to form (2R)-2-phosphoglycerate, an enzymatic step in (L)-glucarate/galactarate catabolic pathway.
Interaction partners:
- 2-hydroxy-3-oxopropionate reductase
- 2-hydroxy-3-oxopropionate reductase
- Glyoxylate/hydroxypyruvate reductase B
- Glycerate 3-kinase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Probable phosphoglycerate mutase GpmB
- Glyoxylate/hydroxypyruvate reductase A
- tRNA-specific adenosine deaminase
- 5-keto-4-deoxy-D-glucarate aldolase
Sequence:
MKIVIAPDSYKESLSASEVAQAIEKGFREIFPDAQYVSVPVADGGEGTVEAMIAATQGAERHAWVTGPLGEKVNASWGISGDGKTAFIEMAAASGLELVPAEKRDPLVTTSRGTGELILQALESGATNIIIGIGGSATNDGGAGMVQALGAKLCDANGNEIGFGGGSLNTLNDIDISGLDPRLKDCVIRVACDVTNPLVGDNGASRIFGPQKGASEAMIVELDNNLSHYAEVIKKALHVDVKDVPGAGAAGGMGAALMAFLGAELKSGIEIVTTALNLEEHIHDCTLVITGEGRIDSQSIHGKVPIGVANVAKKYHKPVIGIAGSLTDDVGVVHQHGIDAVFSVLTSIGTLDEAFRGAYDNICRASRNIAATLAIGMRNAG
Protein: HTH-type transcriptional regulator AdiY (P33234)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Arginine/agmatine antiporter
- Transcriptional regulator GadE
- Biodegradative arginine decarboxylase
Sequence:
MRICSDQPCIVLLTEKDVWIRVNGKEPISLKANHMALLNCENNIIDVSSLNNTLVAHISHDIIKDYLRFLNKDLSQIPVWQRSATPILTLPCLTPDVFRVAAQHSMMPAETESEKERTRALLFTVLSRFLDSKKFVSLMMYMLRNCVSDSVYQIIESDIHKDWNLSMVASCLCLSPSLLKKKLKSENTSYSQIITTCRMRYAVNELMMDGKNISQVSQSCGYNSTSYFISVFKDFYGMTPLHYVSQHRERTVA
Protein: RH50269p (Serine protease homolog 93) (Q9VJD7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LP21446p
Sequence:
MKHCWAIGTLLLASVLMGNACRHTCVTRNFCLYEEPTFDYRSSNCGNTKICCAVLRKPGGTVLIEPNGPEDDKVGVNGINAQLSPTRELTRDRPNTIESQVKEINDFSGRPTNNERNPATEPNNGGYTTPNGGYPVNNGGYPVNNGGYPSNNGGYPSNNGGYPVNNGGYPVNNGGYPANNGGYPANNGGYPTTNVGNPTNNGGNPTTNFGNPTNNGGNPTTNVGSSELLSPSCGMSNANGLQMVEGITIDQARPAQYPWAVAIFHNGQYLAGGSLIQPNVVLTVAHRVITIETELVVRAGDWDLKSDREIFLSEQREVERAVIHEGFDFKSGANNLALLFLNSPFKLNDHIRTICLPTPNKSFAGRRCTVAGWGKMRYEDQRYSTVLKKVQLLVVNRNVCEKFLRSTRLGAKFELPKNIICAGGELGRDTCTGDGGSALFCSIGGENSGVYEQAGIVNWGVGCGQEGIPAIYTEVSKFTNWITEKLLPFDYRSG
Protein: Bypass of Response to Pheromone in yeast (Q9U1S2)
Organism: Caenorhabditis elegans
Interaction partners:
- Beta,beta-carotene 9',10'-oxygenase
- Sugar phosphate transporter domain-containing protein
- DOMON domain-containing protein
Sequence:
MTKLGAQPGVHGSEDVEKESIKIDPKVFTVLQPTVIPMPAPPMKPAPSPAFQAMRACFHCMFFATCLLLVTLIGFYFLAATPDLFKKTETSVNKPQMEALLAQPIDGSSEKTINSAENPGMMAIPLARVVVVEDISNNEGQKKTTVDGSVEEKSSTNLDRPLHPDEIEQYRMMEARQQFQQIMEERMYMQQMMAMRMMRMRRLQAAYYQQQQMKMAYMQQQQQQMQEEAARQQWAERSRYEEEQRRQYEAQQTYAQQQRAQAFWQQHQLEMQAQTQQAQAQAQWQQQEQQPQEQQRQRFWPRPMMHQQQWERPTVWQQPPQQFFFPSQQQQQHQQQPQQTQQPEDRFPQAPQFFQPIPQPSVHDKIYEELQKKSQNIPVNAPTRQIWTAITPTPAPEAASGTADVTASPINTAFPAVVTSSTPMPEDAAEVSDTILRDIFSAFDEQKNSEAANKELNSATPSTTEEPELEGKGAIVIEDSFPRIEERTTTPEPMESEEDAEHTSSEDNHEKELDPFAAVLKFFENNPPREALEAAGAETAATTQKPLKPLIV
Protein: Ras-related protein Rab-2B (EC 3.6.5.2) (Q8WUD1)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Regulates the compacted morphology of the Golgi (Probable). Promotes cytosolic DNA-induced innate immune responses. Regulates IFN responses against DNA viruses by regulating the CGAS-STING signaling axis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P59279}; Lipid-anchor {ECO:0000250|UniProtKB:P59279}; Cytoplasmic side {ECO:0000250|UniProtKB:P59279}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P59279}; Lipid-anchor {ECO:0000250|UniProtKB:P59279}; Cytoplasmic side {ECO:0000250|UniProtKB:P59279}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P59279}; Lipid-anchor {ECO:0000250|UniProtKB:P59279}; Cytoplasmic side {ECO:0000250|UniProtKB:P59279}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P59279}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P59279}; Lipid-anchor {ECO:0000250|UniProtKB:P59279}; Cytoplasmic side {ECO:0000250|UniProtKB:P59279}. Note=Localized in the Golgi apparatus in the round spermatids and in the acrosome in the elongating spermatid. {ECO:0000250|UniProtKB:P59279}.
Interaction partners:
- Golgi-associated RAB2 interactor protein 1A
- Ras-related protein Rab-2A
Sequence:
MTYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMVNIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLTSWLEDARQHSSSNMVIMLIGNKSDLESRRDVKREEGEAFAREHGLIFMETSAKTACNVEEAFINTAKEIYRKIQQGLFDVHNEANGIKIGPQQSISTSVGPSASQRNSRDIGSNSGCC