wanglab/gogpt-training-data huggingface dataset:
Protein: Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 11 (AthCYSTM11) (Q8LG30)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance to abiotic stress.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29272523}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29272523}.
Interaction partners:
Sequence:
MSDPKYAYPYPAPGNYPQGPPPPVGVPPQYYPPPPPPPPPPPPPRKVGFLEGLLAALCCCCLVDECCCDPTIICFD
Protein: Isopenicillin N epimerase component 2 (IPN epimerase component 2) (EC 5.1.1.17) (Isopenicillin N epimerase acyl-CoA racemase component) (EC 5.1.99.-) (Q8J0F0)
Organism: Hapsidospora chrysogena (Acremonium chrysogenum)
Function: Together with cefD1, catalyzes the reversible isomerization between isopenicillin N and penicillin N. This two-component IPN epimerase system may function by two sequential steps, an activation of isopenicillin N by the acyl-CoA synthase component cefD1, followed by epimerization by the acyl-CoA racemase component cefD2.
Interaction partners:
Sequence:
MDPSRPHPLSGKLVVELAGLAPGPFCGMLLADYGASVLRIDGPRSPKGDVLARNKSSICIDLKHPPSRKVLLSILSRADVLIDPFRPGVLERLGLSPTEVLLKANARLVVARLTGFRRDGKYQDMAGHDINYLAVSGVLAMLGRAGENPFPPANILGDFAGGGAMCVVGILLALVSRDATGLGQVVEANMVDGSAYLATMPRLATKTPFWGSPRGENVLDGGCPWYATYRTKDPGGKYMAVGALEPHFYEVLVRGLGLDKTDLPPREDRANWPRLRALFEAKFAERTRSEWAEVFDGTDACVTPVLEQGELEKAGFEQRLPVNLGATPGKPILPGQGDWTGRTLAKGHGGEEILRRWIGWERGVDYHVEENSGILVACSREKL
Protein: Peripheral plasma membrane protein CASK (hCASK) (EC 2.7.11.1) (Calcium/calmodulin-dependent serine protein kinase) (Protein lin-2 homolog) (O14936)
Organism: Homo sapiens (Human)
Function: Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking. Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q62915}. Cytoplasm {ECO:0000250|UniProtKB:Q62915}. Cell membrane {ECO:0000250|UniProtKB:Q62915}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62915}.
Interaction partners:
- Amyloid-beta A4 precursor protein-binding family A member 1
- Protein lin-7 homolog A
- Protein lin-7 homolog B
- Protein lin-7 homolog C
- Disks large homolog 1
- Caskin-1
- Liprin-alpha-2
- Whirlin
- Syndecan-2
- Epidermal growth factor receptor kinase substrate 8
Sequence:
MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDILQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY
Protein: Exocyst complex component 5 (Exocyst complex component Sec10) (B0BLY0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Exocyst complex component 8.
- Exocyst complex component Sec8
- Exocyst complex component 2
- Exocyst complex component 3-like 2b
- Exocyst complex component 1.
- Exocyst complex component
- Exocyst complex component 7
- Exocyst complex component 3.
- Exocyst complex component 3-like protein
- Exocyst complex component
Sequence:
MATTAQLFEEPFDADEYIERLAWRTPGGGSKGGAEAFDPKKLLEEFVNHIEELKLLDERIQRKVEKLEQQCHREAKEFAHKVQDLQRSNQVAFQHFQELDEHISYVATKVCHLGDQLEGVNTPRQRAVEAQRLMTYFNEFLDGELRSDVFNNPEKIKEAADIIQKLHLIAQELPFDRFSDVKAKIASKYHDLERQLIQEFTAAQRRGEIGRMREVAAVLLHFKGYAHCVDVYIKQCQEGAYMRNDVFEDIAILCQRVNKQVGEVFCSPETVMAKLIQSIFENKIQAHVKERLDETRNSDVEQYLKNLYDLYTRTTALAAKLTDYNLGSDKHTFLSKLIKNIFSCYLESYIDMERQYLQNRSGMILQRYYDSKNHQKRPVGTGSIQELKERIRQRTNLPLGPSIDTHGETLLSQEVVVNLLQETRHAFERCNKLSDPADLPKNAFSIFLILVEYLCVDHIDYALEIGLSAIPSADAKNANLYFLDVVQQANTIFHLFDKQFNDHLMPLISSSPKLTECLHKKKEVIEQMEVKLDTGIDRTLNCMIGQMKYILTTEQKKTDFKPEDENNVMIQYTTACSKVCAYVGKQVERVRRSMDGKNVDTVLTELGVRFHRLIHEHLQQFSYSSMGGMLAICDVAEYRRSAKDFRVPLVLQLFDTLHALCNLLVVAPDNLKQVCSGEQLTNLDRNLLHAFVQLRVDYRSARLGRHFS
Protein: Branchpoint-bridging protein (Q9VEJ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367126}.
Interaction partners:
- Splicing factor 3A subunit 2
- Splicing factor 3A subunit 1
- Probable ATP-dependent RNA helicase DDX46
- Cell division cycle 5, isoform A
- LD21442p
- Splicing factor U2AF 50 kDa subunit
- Splicing factor U2AF subunit
- LD24714p
- Splicing factor 3B subunit 1
- Splicing factor 3A subunit 3
Sequence:
MSATPPDLLSLAASREVSAAVAVAASANGGSGRSADKERSRSRDRGRDKDKDRDKDRKKRDKDSRDRDSRRRDDRGDRDRDRERDRDSRSHRSKSRNYDDGDRRRKRSRSRDRDRDRKRDRDRDSRSRRSSSRGGRDDYDRSRRRRSRSRSYERRRNDRGSQRDQRDQHSQRSSRERTHVNPFDTSNSRNSLNQDHDQSRIPSLFDRQQGLETIREEGREQRFDLTQTIQELMGNAGGNKGFASFFNSQNSNDSTSNGAFDNSADSAAERKRKRKSRWGGSENDKTFIPGMPTILPSTLDPAQQEAYLVQFQIEEISRKLRTGDLGITQNPEERSPSPEPIYSSDGKRLNTREFRYRKRLEEQRHQLIVKMQTVNPEFKPPADYKPPVTRVSDKVLIPQEQHPDINFVGLLIGPRGNTLKAMEKDTGAKIIIRGKGSVKEGKVGRKDGQPLPGEDEPLHAFITAPNPEAVRKAVDKIKDVIRQGIEVPEGHNDLRRMQLRELAQLNGTLRENDIQRCTCGSTDHKSWQCPDKPIITNTIVCTSCGGTGHLTKDCRNKRPGSGVPGMACEDSQAKIDEEYMSLMAELGEGPPPPSASAKTDPPASNGPQLHRASYSIFDKKPSQMQAIQSPPSSSSRDHQRDLGGWGAAAHEHGMGMEHGMGLDQHGHGLAAMDHGMSLGMEHAMAAYVPAPPGTQAPPPMPPPLMPWMSAPQPPPPATEPLNPPIPGTLPPLIPPPPGTSAPPMPPWGGGAYSGWGGGYAPPPPPPCAPPPPALSLSQPPPPPPPSA
Protein: Cbp/p300-interacting transactivator with Glu/Asp-rich carboxy-terminal domain 1 (Q4V8P1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- SIX homeobox 2.
Sequence:
MPTMSRPALDVKGGTTSGKEDANQEMNSLAYSNLGVKDRKAVTVLHYPGVTANGAKANGVPTSPSGSSSPTGSPTATPSTKPPSFNLHPTPHLLASMQLQKLNSQYQGAAATAAAALAAPSQPGEDEPLLNWGTGIQAGAGGSPGSVSPAGAQSPAIIDSDPVDEEVLMSLVVELGLDRANELPELWLGQNEFDFTADFPSGC
Protein: Paromamine 6'-oxidase (EC 1.1.3.43) (6'''-hydroxyneomycin C oxidase) (EC 1.1.3.44) (Neomycin biosynthesis protein 11) (Neo-11) (Neomycin biosynthesis protein Q) (Q53U15)
Organism: Streptomyces fradiae (Streptomyces roseoflavus)
Function: Glucosaminyl-6'-oxidase involved in the biosynthetic pathway of neomycin by mediating FAD-dependent dehydrogenation of paromamine to 6'-dehydro-6'-oxoparomamine. Works in combination with neamine transaminase to replace the 6-hydroxy group of paromamine with an amino group. Also able to collaborate with neomycin C transaminase to replace the 6'''-hydroxy group of 6'''-hydroxyneomycin C with an amino group.
Interaction partners:
Sequence:
MKRLRGTLPSDARHAWHPEPLGPAHRDGWDTRDDDRVWDVVVIGSGASGSVAADRLVRQGLDVLMIEEGFRLSPDLGNPELDDMCRTALARDGQGGWTDEGWPWTTSNLGGGTVFYGGASWRYRPFDFDPSELVDAGGLDVRWPYGLAELAPYYDVLERRLGVCGGEEGEGSRGPAHPPTAAAEVLYEAGTALGYEPFPTPLAINRHAHGGRSACERNSLCVSHQCSTGAKGDAVAVFLAPLAAHPNFTLRTGVRALRLNQDRPDAVGSVTCLDRLGRTTHRVRARSFVVACNAIQSAALLLRSRGGRAPDGVGNHSGLVGRGLTMKLSEYVSGVVDAPSAATLADWRAHAGPFSTIAFLDHYLDADCPTGVGGMIYESKNDMPSRIRDDVLELRIETILADHPNLDNRVRLSSHADEDGVPAVVIDYTPDPRDLRRLAYMTDVCERLLRKAGATGIAHEESGFAQGSCHLHGTCRAGDDPATSVVDGWGRVHSAPNVYVVDGGFMPYPGGLNPTLTIQAHALRSAKAVAGDLVSRHTAHV
Protein: tRNA dimethylallyltransferase (EC 2.5.1.75) (Dimethylallyl diphosphate:tRNA dimethylallyltransferase) (DMAPP:tRNA dimethylallyltransferase) (DMATase) (Isopentenyl-diphosphate:tRNA isopentenyltransferase) (IPP transferase) (IPPT) (IPTase) (P16384)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Interaction partners:
- RNA-binding protein Hfq
- tRNA-2-methylthio-N
- GTPase HflX
- DNA mismatch repair protein MutL
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaE
- N-acetylmuramoyl-L-alanine amidase AmiB
- Modulator of FtsH protease HflK
- Modulator of FtsH protease HflC
- Bifunctional NAD
- tRNA pseudouridine synthase A
Sequence:
MSDISKASLPKAIFLMGPTASGKTALAIELRKILPVELISVDSALIYKGMDIGTAKPNAEELLAAPHRLLDIRDPSQAYSAADFRRDALAEMADITAAGRIPLLVGGTMLYFKALLEGLSPLPSADPEVRARIEQQAAEQGWESLHRQLQEVDPVAAARIHPNDPQRLSRALEVFFISGKTLTELTQTSGDALPYQVHQFAIAPASRELLHQRIEQRFHQMLASGFEAEVRALFARGDLHTDLPSIRCVGYRQMWSYLEGEISYDEMVYRGVCATRQLAKRQITWLRGWEGVHWLDSEKPEQARDEVLQVVGAIAG
Protein: Probable NADPH dehydrogenase (EC 1.6.99.1) (Estrogen-binding protein) (EBP) (A0A1D8PPK1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Oxidoreductase that binds mammalian estrogens with high affinity.
Interaction partners:
- Probable NADPH dehydrogenase
- Oye32p
- enoyl-[acyl-carrier-protein] reductase
- Enoyl reductase
Sequence:
MTIESTNSFVVPSDTELIDVTPLGSTKLFQPIKVGNNVLPQRIAYVPTTRFRASKDHIPSDLQLNYYNARSQYPGTLIITEATFASERGGIDLHVPGIYNDAQAKSWKKINEAIHGNGSFSSVQLWYLGRVANAKDLKDSGLPLIAPSAVYWDENSEKLAKEAGNELRALTEEEIDHIVEVEYPNAAKHALEAGFDYVEIHGAHGYLLDQFLNLASNKRTDKYGCGSIENRARLLLRVVDKLIEVVGANRLALRLSPWASFQGMEIEGEEIHSYILQQLQQRADNGQQLAYISLVEPRVTGIYDVSLKDQQGRSNEFAYKIWKGNFIRAGNYTYDAPEFKTLINDLKNDRTIIGFSRFFTSNPDLVEKLKLGKPLNYYNREEFYKYYNYGYNSYDESEKQVIGKPLA
Protein: Collagen alpha-2(I) chain (Alpha-2 type I collagen) (P02467)
Organism: Gallus gallus (Chicken)
Function: Type I collagen is a member of group I collagen (fibrillar forming collagen).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Integrin beta-1
- Link domain-containing protein.
- Integrin subunit alpha 11
- Collagen IV NC1 domain-containing protein.
- Fibrillar collagen NC1 domain-containing protein.
- Integrin alpha-V
- Integrin alpha-8
- Collagen alpha-1
- Integrin beta
- Periostin
Sequence:
MLSFVDTRILLLLAVTSYLATSQHLFQASAGRKGPRGDKGPQGERGPPGPPGRDGEDGPPGPPGPPGPPGLGGNFAAQYDPSKAADFGPGPMGLMGPRGPPGASGPPGPPGFQGVPGEPGEPGQTGPQGPRGPPGPPGKAGEDGHPGKPGRPGERGVAGPQGARGFPGTPGLPGFKGIRGHNGLDGQKGQPGTPGTKGEPGAPGENGTPGQPGARGLPGERGRIGAPGPAGARGSDGSAGPTGPAGPIGAAGPPGFPGAPGAKGEIGPAGNVGPTGPAGPRGEIGLPGSSGPVGPPGNPGANGLPGAKGAAGLPGVAGAPGLPGPRGIPGPPGPAGPSGARGLVGEPGPAGAKGESGNKGEPGAAGPPGPPGPSGEEGKRGSNGEPGSAGPPGPAGLRGVPGSRGLPGADGRAGVMGPAGNRGASGPVGAKGPNGDAGRPGEPGLMGPRGLPGQPGSPGPAGKEGPVGFPGADGRVGPIGPAGNRGEPGNIGFPGPKGPTGEPGKPGEKGNVGLAGPRGAPGPEGNNGAQGPPGVTGNQGAKGETGPAGPPGFQGLPGPSGPAGEAGKPGERGLHGEFGVPGPAGPRGERGLPGESGAVGPAGPIGSRGPSGPPGPDGNKGEPGNVGPAGAPGPAGPGGIPGERGVAGVPGGKGEKGAPGLRGDTGATGRDGARGLPGAIGAPGPAGGAGDRGEGGPAGPAGPAGARGIPGERGEPGPVGPSGFAGPPGAAGQPGAKGERGPKGPKGETGPTGAIGPIGASGPPGPVGAAGPAGPRGDAGPPGMTGFPGAAGRVGPPGPAGITGPPGPPGPAGKDGPRGLRGDVGPVGRTGEQGIAGPPGFAGEKGPSGEAGAAGPPGTPGPQGILGAPGILGLPGSRGERGLPGIAGATGEPGPLGVSGPPGARGPSGPVGSPGPNGAPGEAGRDGNPGNDGPPGRDGAPGFKGERGAPGNPGPSGALGAPGPHGQVGPSGKPGNRGDPGPVGPVGPAGAFGPRGLAGPQGPRGEKGEPGDKGHRGLPGLKGHNGLQGLPGLAGQHGDQGPPGNNGPAGPRGPPGPSGPPGKDGRNGLPGPIGPAGVRGSHGSQGPAGPPGPPGPPGPPGPNGGGYEVGFDAEYYRADQPSLRPKDYEVDATLKTLNNQIETLLTPEGSKKNPARTCRDLRLSHPEWSSGFYWIDPNQGCTADAIRAYCDFATGETCIHASLEDIPTKTWYVSKNPKDKKHIWFGETINGGTQFEYNGEGVTTKDMATQLAFMRLLANHASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELRAEGNSRFTFSVLVDGCSKKNNKWGKTIIEYRTNKPSRLPILDIAPLDIGGADQEFGLHIGPVCFK
Protein: Carbon catabolite repressor protein 4 homolog 4 (CCR4 homolog 4) (EC 3.1.13.4) (Protein HESPERIN) (AtHESP) (AtHesperin) (A8MS41)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Transcriptional regulator of circadian rhythms with poly(A)-degrading activity that affects the expression and rhythmicity of the clock core oscillator genes TOC1 and CCA1. Deadenylation may be a mechanism involved in the regulation of the circadian clock. May play a negative role in response against oxidative stress. Possesses magnesium-dependent poly(A)-specific exoribonuclease activity in vitro and is almost inactive with poly(U), poly(C) and poly(G) as substrates.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P31384}. Cytoplasm {ECO:0000269|PubMed:31093672}.
Interaction partners:
- Transcription regulator
- Transcription regulator NOT2/NOT3/NOT5 family protein
- Ubiquitin carboxyl-terminal hydrolase family protein
- Transmembrane protein
- Nucleic acid binding / zinc ion binding protein
- Methyltransferase-like protein 5
- Pentatricopeptide repeat-containing protein At4g18975
- Pentatricopeptide repeat-containing protein At4g01030
- NOT2 / NOT3 / NOT5 family
- Probable NOT transcription complex subunit VIP2
Sequence:
MFSSTTLHHLPRPNLLLPRKVISRRMSTNPAIEPKVRKFESVEGVDIGSRNKSDGFFAIPLYLSKLVALYNCISLSRIGTSNENFVFSGIRFRLVSYNILAQVYVKSALLPHSPPACLKWKARSHAILSVLKNLQADFFCLQEVDEYDSFYRNNMDSLGYSGIYIQRTGQRKRDGCAIFYKPSCAELVTKERIEYNDLVDSIKADSVSCSEQKIETSNEGKDSRKDSRDLNDPLVRLKRDCVGIMAAFRINKPFQHIVIVANTHLYWDPELADVKLAQAKYLLSRLAQFKTLISDEFECTPSLLLAGDFNSIPGDMVYSYLVSGNAKPTETIEEEEAPVPLSSVYEVTRGEPKFTNCTPGFTNTLDYIFISPSDFIKPVSILQLPEPDSPDVVGFLPNHHHPSDHLPIGAEFEIRRE
Protein: L-lysine 2,3-aminomutase (LAM) (EC 5.4.3.-) (EF-P post-translational modification enzyme B) (P39280)
Organism: Escherichia coli (strain K12)
Function: With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine). Cannot use (S)-ornithine or (R)-alpha-lysine as a substrate.
Interaction partners:
- Elongation factor P
- Elongation factor P--
- Elongation factor P lysine hydroxylase
- Elongation factor P-like protein
- Uncharacterized protein YjeJ
- Chemotaxis protein methyltransferase
- Biotin synthase
- Pyruvate formate-lyase 2-activating enzyme
- Putative pyruvate formate-lyase 3-activating enzyme
- Trp operon repressor
Sequence:
MAHIVTLNTPSREDWLTQLADVVTDPDELLRLLNIDAEEKLLAGRSAKKLFALRVPRSFIDRMEKGNPDDPLLRQVLTSQDEFVIAPGFSTDPLEEQHSVVPGLLHKYHNRALLLVKGGCAVNCRYCFRRHFPYAENQGNKRNWQTALEYVAAHPELDEMIFSGGDPLMAKDHELDWLLTQLEAIPHIKRLRIHSRLPIVIPARITEALVECFARSTLQILLVNHINHANEVDETFRQAMAKLRRVGVTLLNQSVLLRDVNDNAQTLANLSNALFDAGVMPYYLHVLDKVQGAAHFMVSDDEARQIMRELLTLVSGYLVPKLAREIGGEPSKTPLDLQLRQQ
Protein: Transcription factor HES-3 (Hairy and enhancer of split 3) (Q61657)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor of genes that require a bHLH protein for their transcription.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MEKKRRARINVSLEQLRSLLERHYSHQIRKRKLEKADILELSVKYMRSLQNSLQGLWPVPSGVDYPSGFQGGLRGVSQRLRPGEGDSGLRCPLLLQRREGSTTDSANPQATSVLNPCLPAIWAPSRAAGGSHSPQSPLPLPGGLLESSTDVVAPHPASNCQAESTRPGFRVWRPW
Protein: Threonylcarbamoyl-AMP synthase (TC-AMP synthase) (EC 2.7.7.87) (L-threonylcarbamoyladenylate synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein Sua5) (tRNA threonylcarbamoyladenosine biosynthesis protein Sua5) (Q9UYB2)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Likely catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Does not bind tRNA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Serine hydroxymethyltransferase
- Hexosyltransferase, glycosyltransferase family 1
- GalE-2 UDP-glucose 4-epimerase)
- ApeH acylamino-acid-releasing enzyme
- tRNA N6-adenosine threonylcarbamoyltransferase
- tRNA-guanine
- KEOPS complex subunit Bud32
Sequence:
MTIIINVRERIEEWKIRIAAGFIREGKLVAFPTETVYGLGANALDENAVKRIFEAKGRPADNPLIIHIASFEQLEVLAKEIPEEAEMLAKRFWPGPLTLVLPKSEVVPRVITGGLDTVAVRMPAHEIALKLIELSERPIAAPSANISGKPSPTSAHHVAEDFYGKIECIIDGGETRIGVESTVIDLTEWPPVLLRPGGLPLEEIEKVIGEIRIHPAVYGKSVDTAKAPGMKYRHYAPSAEVIVVEGPRDKVRRKIEELIAKFKEEGKKVGVIGSGSYDADEVFYLGDTVEEIARNLFKALRHMDRTGVDVILAEGVEEKGLGLAVMNRLRKASGYRIIKV
Protein: Receptor expression enhancing protein A, isoform H (A0A0B4JD44)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MISSLFSRLIILFCGTLYPAYASYKAVRTKDVKEYVKWMMYWIVFAFFTCIETFTDIFISWLPFYYEVKVALVFWLLSPATKGSSTLYRKFVHPMLTRHEQEIDEYVNQAKERGYSAVLQLGSKGVNYATNVLMQTAIKGGGNLVQTIKRSYSLSDLSEPDMHRTQDELDDVMMSSMTSSAVVMRSTATGARLLRPRNQTPVGRSGSGTRHSTGMYFTEVDVTAKNAGDFNYNIRSQDDISSGYSSAEPVSGLSRTSSMTNASKARAKSKRNELLEEMRDEVYLDNQLYFQGVQRKSSVPEAEELKIVESSESIQSQELEKVLKEENIDAEDEAFFETLPLIEEHINEVVANYGRDEKLLPQERKHNSIEEEQFEDALFEEPQKCVSDEVDAKNIEEILTDRSQNQTPNGSAETTDSGTPSQNKPYVHPPIDPFLLVLSASASAPDPFMPERPRPMSPREMRETLEEIKHSFRAQLEAEPSVSASPSPSLRPKANHGKGRAPPPPLPPKKHSLSPQPDAISQTSTGSVERKSGIGQLFKNIKANVLRNKANPSQQQPEDEQLAAKETQI
Protein: Sodium/hydrogen exchanger 1 (APNH) (Na(+)/H(+) antiporter, amiloride-sensitive) (Na(+)/H(+) exchanger 1) (NHE-1) (Solute carrier family 9 member 1) (P19634)
Organism: Homo sapiens (Human)
Function: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14680478, ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:15677483, ECO:0000269|PubMed:17073455, ECO:0000269|PubMed:32130622, ECO:0000269|PubMed:34108458}; Multi-pass membrane protein {ECO:0000269|PubMed:34108458}. Basolateral cell membrane {ECO:0000250|UniProtKB:P48762}; Multi-pass membrane protein {ECO:0000269|PubMed:34108458}. Note=Localized basolaterally in every epithelial cell, except in the choroid plexus where SLC9A1 is expressed luminally. {ECO:0000269|PubMed:19369449}.
Interaction partners:
- Ezrin
- Moesin
- Calcineurin B homologous protein 1
- Radixin
- Calmodulin-1
- Calcineurin B homologous protein 3
- Calcineurin B homologous protein 2
- Rho-associated protein kinase 1
- Carbonic anhydrase 2
- Calmodulin-1
Sequence:
MVLRSGICGLSPHRIFPSLLVVVALVGLLPVLRSHGLQLSPTASTIRSSEPPRERSIGDVTTAPPEVTPESRPVNHSVTDHGMKPRKAFPVLGIDYTHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLMYAVCLVGGEQINNIGLLDNLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFANYEHVGIVDIFLGFLSFFVVALGGVLVGVVYGVIAAFTSRFTSHIRVIEPLFVFLYSYMAYLSAELFHLSGIMALIASGVVMRPYVEANISHKSHTTIKYFLKMWSSVSETLIFIFLGVSTVAGSHHWNWTFVISTLLFCLIARVLGVLGLTWFINKFRIVKLTPKDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLFLTAIITVIFFTVFVQGMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIEDICGHYGHHHWKDKLNRFNKKYVKKCLIAGERSKEPQLIAFYHKMEMKQAIELVESGGMGKIPSAVSTVSMQNIHPKSLPSERILPALSKDKEEEIRKILRNNLQKTRQRLRSYNRHTLVADPYEEAWNQMLLRRQKARQLEQKINNYLTVPAHKLDSPTMSRARIGSDPLAYEPKEDLPVITIDPASPQSPESVDLVNEELKGKVLGLSRDPAKVAEEDEDDDGGIMMRSKETSSPGTDDVFTPAPSDSPSSQRIQRCLSDPGPHPEPGEGEPFFPKGQ
Protein: Transmembrane protein 237 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein) (Q96Q45)
Organism: Homo sapiens (Human)
Function: Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:22152675}. Note=Localizes at the proximal region of primary cilia were observed, consistent with localization to the transition zone. Anchored to the transition zone by RPGRIP1L.
Interaction partners:
- Meckelin
- Transmembrane protein 231
- Nephrocystin-1
- B9 domain-containing protein 1
- Coiled-coil and C2 domain-containing protein 2A
- Transmembrane protein 17
- Protein fantom
- Transmembrane protein 216
- Tectonic-1
- Transmembrane protein 107
Sequence:
MRTDSGARLEEGHLRPPRALPPVPSQDDIPLSRPKKKKPRTKNTPASASLEGLAQTAGRRPSEGNEPSTKELKEHPEAPVQRRQKKTRLPLELETSSTQKKSSSSSLLRNENGIDAEPAEEAVIQKPRRKTKKTQPAELQYANELGVEDEDIITDEQTTVEQQSVFTAPTGISQPVGKVFVEKSRRFQAADRSELIKTTENIDVSMDVKPSWTTRDVALTVHRAFRMIGLFSHGFLAGCAVWNIVVIYVLAGDQLSNLSNLLQQYKTLAYPFQSLLYLLLALSTISAFDRIDFAKISVAIRNFLALDPTALASFLYFTALILSLSQQMTSDRIHLYTPSSVNGSLWEAGIEEQILQPWIVVNLVVALLVGLSWLFLSYRPGMDLSEELMFSSEVEEYPDKEKEIKASS
Protein: Thioredoxin F2, chloroplastic (AtTrxf2) (Thioredoxin F1) (AtTrxf1) (Q9XFH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol-disulfide oxidoreductase involved in the redox regulation of enzymes of both reductive pentose phosphate pathway (Calvin-Benson cycle) and oxidative pentose phosphate pathway.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19259774}.
Interaction partners:
- Thioredoxin M4, chloroplastic
- NADPH-dependent thioredoxin reductase 3
- Ferredoxin/thioredoxin reductase subunit A
- Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
- Thioredoxin M3, chloroplastic
- Thioredoxin-like protein CITRX, chloroplastic
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Thioredoxin-like protein CDSP32, chloroplastic
- Thioredoxin-like 4, chloroplastic
- Uncharacterized protein At2g41810
Sequence:
MPLSLRLAPSPTSFRYSPITSTGAGGFSPVKQHCRIPNSGVATKIGFCSGGGGVLDSGRRIGSCVVRCSLETVNVTVGQVTEVDKDTFWPIVKAAGDKIVVLDMYTQWCGPCKVIAPKYKELSEKYQDMVFLKLDCNQDNKPLAKELGIRVVPTFKILKDNKVVKEVTGAKYEDLLAAIEAARSG
Protein: choline-phosphate cytidylyltransferase (EC 2.7.7.15) (Q3HKC4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPQRKRTMDSPQEEDVEVKKKATEVEYVVRSLASDEPAPFSDEALAITTREAVDYSKKITLAMAEANEAGRPVRIYADGIYDLFHHGHANQLRQVKKMFPNVYLIVGVCGDRDTHKYKGRTVTSEEERYDGVRHCRYVDEVYREAPWFCTVEFLKNLKVDFIAHDAIPYVAPGEEDLYEKFRREGMFLETERTEGVSTSDVVCRIIRDYDKYVRRNLQRGYSPKELNVGFLAASKYQIQNKVDSLKSKGIELLSTWKSKSDDIIRDFIDTFHKDGGLNAFGGRLKGIMSMSRSPSPSPHEGSPTGIEHHLETQDEEEEEEALEEEKVVEQKIVEKKEVVKKRSSRNKAKTPLEY
Protein: Crumbs homolog 3a (Crumbs-like protein 3a) (Q1A5L0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Protein PALS1
- Crumbs-like protein 3b.
- Par-6 family cell polarity regulator alpha.
- Par-6 partitioning defective 6 homolog beta
- Par-6 family cell polarity regulator gamma b
- Par-6 family cell polarity regulator gamma a.
- Protein lin-7 homolog
- PATJ crumbs cell polarity complex component.
- V-myb avian myeloblastosis viral oncogene homolog-like 2b.
Sequence:
MIQQVGLLAGSFLLLLVRNVSAQGENSTMSSFTTSSPESTGPNIVAIVVPTVVLGLLAILTAVLVFLFCVVKKKRQTEGTYRPSAEEQTGARSVEAPDALKLPKEERLI
Protein: Olfactory receptor 2S2 (Olfactory receptor OR9-3) (Q9NQN1)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MEKANETSPVMGFVLLRLSAHPELEKTFFVLILLMYLVILLGNGVLILVTILDSRLHTPMYFFLGNLSFLDICFTTSSVPLVLDSFLTPQETISFSACAVQMALSFAMAGTECLLLSMMAFDRYVAICNPLRYSVIMSKAAYMPMAASSWAIGGAASVVHTSLAIQLPFCGDNVINHFTCEILAVLKLACADISINVISMEVTNVIFLGVPVLFISFSYVFIITTILRIPSAEGRKKVFSTCSAHLTVVIVFYGTLFFMYGKPKSKDSMGADKEDLSDKLIPLFYGVVTPMLNPIIYSLRNKDVKAAVRRLLRPKGFTQ