wanglab/gogpt-training-data huggingface dataset:
Protein: Down syndrome cell adhesion molecule 1, isoform AD (Q0E9J6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVNQFYGADILMEYVIRGNAAVLKCSIPSFVADFVRVESWIDEEGTELRPSENYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVAPKISVENRLKNAEARIGSTFTLFCPGQAYPVPFFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVAPKIAPFDFGDEPSNFGESASVQCLVTSGDFPVSFAWLFNGREINENVYDVSMVKLGKKISALSIDIVRDHHAGNYTCVAVNRATSVNFTAELVVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Ribosomal RNA small subunit methyltransferase C (EC 2.1.1.172) (16S rRNA m2G1207 methyltransferase) (rRNA (guanine-N(2)-)-methyltransferase RsmC) (P39406)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ribosomal RNA large subunit methyltransferase K/L
- Ribosomal RNA small subunit methyltransferase E
- Ribosomal RNA small subunit methyltransferase B
- Ribosomal RNA small subunit methyltransferase D
- Ribosomal RNA small subunit methyltransferase F
- Ribosomal RNA small subunit methyltransferase A
- DNA polymerase III subunit psi
Sequence:
MSAFTPASEVLLRHSDDFEQSRILFAGDLQDDLPARLDTAASRAHTQQFHHWQVLSRQMGDNARFSLVATADDVADCDTLIYYWPKNKPEAQFQLMNLLSLLPVGTDIFVVGENRSGVRSAEQMLADYAPLNKVDSARRCGLYFGRLEKQPVFDAEKFWGEYSVDGLTVKTLPGVFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVLSVAFARHSPKIRLTLCDVSAPAVEASRATLAANGVEGEVFASNVFSEVKGRFDMIISNPPFHDGMQTSLDAAQTLIRGAVRHLNSGGELRIVANAFLPYPDVLDETFGFHEVIAQTGRFKVYRAIMTRQAKKG
Protein: Augmin complex subunit wac (wee Augmin component) (Q9W0S8)
Organism: Drosophila melanogaster (Fruit fly)
Function: As part of the augmin complex, plays a role in centrosome-independent generation of spindle microtubules. The complex is required for mitotic spindle assembly through its involvement in localizing gamma-tubulin to spindle microtubules. wac is dispensable for somatic mitosis and for assembly of spindle microtubules in oocytes during female meiosis but is required during female meiosis for chromosome alignment and segregation. It is required for microtubule assembly near spindle poles in oocytes. It is also required for acentrosomal microtubule nucleation and meiotic spindle formation during male meiosis. wac binds to microtubules in vitro.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19289792, ECO:0000269|PubMed:19369198}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:23785300}. Note=Enriched at spindle poles during meiosis in oocytes. {ECO:0000269|PubMed:23785300}.
Interaction partners:
- Augmin complex subunit msd1
- Augmin complex subunit dgt2
- Augmin complex subunit msd5
- Augmin complex subunit dgt6
- Augmin complex subunit dgt5
- Augmin complex subunit dgt4
- Augmin complex subunit dgt3
- Grip71
Sequence:
MQNLKIQEEVNSLMRLGQHFDDQLKLASVELGDFSDDDLALLDKCAQYYSLLHIHDINLNYLRDFYCAKKRECIENRQTTVQQRVELQRILSSIEEATRDVVMLERFNAAAEERLIPDIVVMQRNAQQLATKQALLDRQKTLKIPKDFSIESVIEKVDSLEQR
Protein: Afp99p (Q5ANN8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ornithine decarboxylase
- Spermidine synthase
- Agmatinase
- Polyamine oxidase
- Corticosteroid-binding protein
- Protein ARG5,6
- Arginine biosynthesis bifunctional protein ArgJ
Sequence:
MKLYIFVLVACVSSQTIFRSPSLLDQLYGELHGRTNTAPNLQVQAEDPNQMVTQKVLAMRSKLTLPDKDDTSDIAIDQNMFGGILTYAHFNHFNCFISDDFDKHSTTDQQTTKNIDIAIVGAPFDTGTSYRPGARFGPESIRSNSRRLGSAWKSTKKRFNYPVNPYDETTHNYSIIDCGDVAMTPFDNRIALNQLYRGHRSISKHPGNVNQHPKIITLGGDHTITLMAIKNAHEQLRTKIRVFHFDSHIDTWDPKKLGGGITDYMSLNHGTFLHYATELGYIETKGNYHVGIRAPYIDANYDKQHDADCGFHIIQANDIDKIGVQGIIDELAKDPNIPTYISVDIDVLDPAYAPGTGTMEAGGFTTRELLSILDGLKNKVNVIGGDVVEVSPPYDTNSEITSLAATSVVDSLLKLMIV
Protein: Transcriptional activator protein CUP2 (Copper-fist transcription factor) (P15315)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Trans-acting regulatory protein that activates transcription of the CUP1 gene (metallothionein) in response to copper ions. Binds to the CUP1 UAS sequence 5'-GCTTCTTTTCCGCTGA-3'. Binds DNA only in presence of copper or silver. Copper seems to alter the conformation of the protein.
Subcellular location: Nucleus.
Interaction partners:
- Copper metallothionein 1-1
- Copper transport protein CTR3
- Superoxide dismutase
- Copper-transporting ATPase
Sequence:
MVVINGVKYACETCIRGHRAAQCTHTDGPLQMIRRKGRPSTTCGHCKELRRTKNFNPSGGCMCASARRPAVGSKEDETRCRCDEGEPCKCHTKRKSSRKSKGGSCHRRANDEAAHVNGLGIADLDVLLGLNGRSSDVDMTTTLPSLKPPLQNGEIKADSIDNLDLASLDPLEQSPSISMEPVSINETGSAYTTTNTALNDIDIPFSINELNELYKQVSSHNSHSQ
Protein: Neuromedin-B receptor (NMB-R) (Neuromedin-B-preferring bombesin receptor) (O54799)
Organism: Mus musculus (Mouse)
Function: Receptor for neuromedin-B (By similarity). Contributes to the maintenance of basal sigh rate through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity. Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR-expressing neurons in the sneeze-evoking region of the brainstem. These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response. Contributes to induction of acute itch, possibly through its activation on dorsal root ganglion neurons by the NMB peptide. Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6. Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to the positive regulation of the expression of the CSF1 receptor CSF1R.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuromedin-B
- Gastrin-releasing peptide
- Gastrin-releasing peptide receptor
- Bombesin receptor subtype-3
- Toll-like receptor 4
- Neurotensin/neuromedin N
- Neuromedin-S
Sequence:
MPPRSLSNLSFPTEANESELVPEVWEKDFLPDSDGTTAELVIRCVIPSLYLIIISVGLLGNIMLVKIFLTNSAMRNVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWVFGKLGCKLIPAIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGVLLWTSLKAVGIWVVSVLLAVPEAVFSEVARIGSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLVIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFVFCWFPNHVLYLYRSFNYKEIDPSLGHMIVTLVARVLSFSNSCVNPFALYLLSESFRKHFNSQLCCGRKSYPERSTSYLLSSSAVRMTSLKSNTKNVVTNSVLLNGHSTKQEIAL
Protein: E3 ubiquitin-protein ligase CIP8 (EC 2.3.2.27) (COP1-interacting protein 8) (RING-type E3 ubiquitin transferase CIP8) (Q9SPL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. Probably forms a minimal ubiquitin ligase complex in cooperation with the E2 enzyme UBC8. Its interaction with COP1 suggests that it may participate in proteasome-mediated degradation of HY5 in vivo.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:10488108}.
Interaction partners:
- E3 ubiquitin-protein ligase COP1
- COP1-interacting protein 7
- At5g40190
- Transport/golgi organization-like protein
- RING-H2 finger protein ATL14
- Eukaryotic aspartyl protease family protein
- Myosin heavy chain-like protein
- Transcription factor HY5
- Protein DETOXIFICATION 56
- Protein COP1 SUPPRESSOR 2
Sequence:
MSDAPSSSPDATASHWCYHCNKRVVVETLDDFVVCCECNKGFVESIQPTPAAYSSPAPPQPLSPDLNVEDSSIGSHFLQMLRLLAHAPSQRSPPRHLDVLSYEDDFFRLELNSRNEIDDDEDEDEDDGDEEEEDEEENLTVNDEEDEEDDLRRRNRFPLTTTQSRTGRNRILDWAEILMGIEDNSIEFRMESDRYAGNPADYIDDAAGYEALLQNLAEGDGGGGGGRRGAPPAAKSAIEALETFEVSSSEGEMVMVCAVCKDGMVMGETGKKLPCGHCYHGDCIVPWLGTRNSCPVCRFQLETDDAEYEEERKKRTSTVSDSAAASSSSSTSRY
Protein: E3 ubiquitin-protein ligase TRIM41 (EC 2.3.2.27) (RING finger-interacting protein with C kinase) (RINCK) (Tripartite motif-containing protein 41) (Q8WV44)
Organism: Homo sapiens (Human)
Function: E3 ligase that plays essential roles in innate antiviral response. Directly binds to influenza A virus or vesicular stomatitis virus nucleoproteins and targets them for ubiquitination and proteasomal degradation, thereby limiting viral infections. Activates the innate antiviral response by catalyzing monoubiquitination of CGAS, thereby activating CGAS. Also involved in innate antiviral response by mediating 'Lys-63'-linked polyubiquitylation of BCL10 which in turn hubs NEMO for activation of NF-kappa-B and IRF3 pathways (By similarity). Catalyzes the ubiquitin-mediated degradation of other substrates including protein kinase C, ZSCAN21 or TOP3B suggesting additional roles besides its function in immune response.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16022281, ECO:0000269|PubMed:29899090, ECO:0000269|PubMed:31979016}. Nucleus {ECO:0000269|PubMed:16022281, ECO:0000269|PubMed:29899090, ECO:0000269|PubMed:31979016}.
Interaction partners:
- DNA topoisomerase 3-beta-1
- T-cell receptor-associated transmembrane adapter 1
- PTPN13-like protein, Y-linked
- Mitochondrial inner membrane m-AAA protease component paraplegin
- E3 ubiquitin-protein ligase TRIM45
- Gamma-butyrobetaine dioxygenase
- Mitochondrial antiviral-signaling protein
Sequence:
MAAVAMTPNPVQTLQEEAVCAICLDYFTDPVSIGCGHNFCRVCVTQLWGGEDEEDRDELDREEEEEDGEEEEVEAVGAGAGWDTPMRDEDYEGDMEEEVEEEEEGVFWTSGMSRSSWDNMDYVWEEEDEEEDLDYYLGDMEEEDLRGEDEEDEEEVLEEVEEEDLDPVTPLPPPPAPRRCFTCPQCRKSFPRRSFRPNLQLANMVQVIRQMHPTPGRGSRVTDQGICPKHQEALKLFCEVDEEAICVVCRESRSHKQHSVVPLEEVVQEYKAKLQGHVEPLRKHLEAVQKMKAKEERRVTELKSQMKSELAAVASEFGRLTRFLAEEQAGLERRLREMHEAQLGRAGAAASRLAEQAAQLSRLLAEAQERSQQGGLRLLQDIKETFNRCEEVQLQPPEVWSPDPCQPHSHDFLTDAIVRKMSRMFCQAARVDLTLDPDTAHPALMLSPDRRGVRLAERRQEVADHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHKEKVGPGGSSVGSGDASSSRHHHRRRRLHLPQQPLLQREVWCVGTNGKRYQAQSSTEQTLLSPSEKPRRFGVYLDYEAGRLGFYNAETLAHVHTFSAAFLGERVFPFFRVLSKGTRIKLCP
Protein: Beta-alanine synthase (Pyd3 (EC 3.5.1.6)) (Q9VI04)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dihydropyrimidine dehydrogenase [NADP
- aldehyde dehydrogenase
- dihydropyrimidinase
- (S)-3-amino-2-methylpropionate transaminase (GABA aminotransferase) (Gamma-amino-N-butyrate transaminase) (L-AIBAT)
- aldehyde dehydrogenase
- Aldehyde dehydrogenase type III, isoform Q
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Uncharacterized protein, isoform B
- Carnosine dipeptidase 2, isoform A
- Glutamate decarboxylase
Sequence:
MSAFELKNLNDCLEKHLPPDELKEVKRILYGVEEDQTLELPTSAKDIAEQNGFDIKGYRFTAREEQTRKRRIVRVGAIQNSIVIPTTAPIEKQREAIWNKVKTMIKAAAEAGCNIVCTQEAWTMPFAFCTREKFPWCEFAEEAENGPTTKMLAELAKAYNMVIIHSILERDMEHGETIWNTAVVISNSGRYLGKHRKNHIPRVGDFNESTYYMEGNTGHPVFETEFGKLAVNICYGRHHPQNWMMFGLNGAEIVFNPSATIGRLSEPLWSIEARNAAIANSYFTVPINRVGTEQFPNEYTSGDGNKAHKEFGPFYGSSYVAAPDGSRTPSLSRDKDGLLVVELDLNLCRQVKDFWGFRMTQRVPLYAESFKKASEHGFKPQIIKET
Protein: UDP-glycosyltransferase 13 (MiUGT13) (EC 2.4.1.-) (C-glycosyltransferase) (MiCGT) (A0A0M4KE44)
Organism: Mangifera indica (Mango)
Function: Benzophenone C-glycosyltransferase involved in the biosynthesis of mangiferin. Exhibits a robust regio- and stereospecific C-glycosylation activity toward over 35 substrates from 18 structurally different types with UDP-glucose. Also able to produce O- and N-glycosides and to use UDP-xylose as sugar donor. Generates only C-glycosides with 2,4,6-tri-hydroxy acceptors at the A ring, both C- and O- glycosides with 2,4-di-hydroxyl acceptors at the A ring, and only O-glycosides with 2- or 4-mono-hydroxy acceptors at the A ring.
Interaction partners:
Sequence:
MSASDALNSCPHVALLLSSGMGHLTPCLRFAATLVQHHCRVTIITNYPTVSVAESRAISLLLSDFPQITEKQFHLLPFDPSTANTTDPFFLRWEAIRRSAHLLNPLLSSISPPLSALVIDSSLVSSFVPVAANLDLPSYVLFTSSTRMCSLEETFPAFVASKTNFDSIQLDDVIEIPGFSPVPVSSVPPVFLNLNHLFTTMLIQNGQSFRKANGILINTFEALEGGILPGINDKRAADGLPPYCSVGPLLPCKFEKTECSAPVKWLDDQPEGSVVYVSFGSRFALSSEQIKELGDGLIRSGCRFLWVVKCKKVDQEDEESLDELLGRDVLEKIKKYGFVIKNWVNQQEILDHRAVGGFVTHGGWNSSMEAVWHGVPMLVWPQFGDQKINAEVIERSGLGMWVKRWGWGTQQLVKGEEIGERIKDLMGNNPLRVRAKTLREEARKAIEVGGSSEKTLKELIENWKKTSRKT
Protein: Equilibrative nucleotide transporter 3 (AtENT3) (Nucleoside transporter ENT3) (Protein FLUOROURIDINE RESISTANT 1) (Q9M0Y3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleoside transporter that functions as a pyrimidine nucleoside carrier in all organs. Has high affinity for adenosine and uridine when expressed in a heterologous system (yeast). Mediates proton-dependent adenosine or uridine transport in Xenopus oocytes.
Subcellular location: Cell membrane {ECO:0000305|PubMed:12810710}; Multi-pass membrane protein {ECO:0000305|PubMed:12810710}. Note=Plasma membrane. {ECO:0000305|PubMed:12810710}.
Interaction partners:
- Nucleoside hydrolase 3
- Putative defensin-like protein 101
- Putative defensin-like protein 135
- Purine permease 2
- Putative defensin-like protein 62
- Defensin-like protein 90
- Putative F-box protein At4g05475
- Allantoinase
- Mitochondrial substrate carrier family protein
- Purine permease 14
Sequence:
MADRYENQPPEKLQGKYQAMVVCCILGIGSLVSWNSMLTIADYYYKVFPDYHPSRVLTLVYQPFALGTILILAYHESKINTRKRNLIGYILFTISTFLLIVLDLATKGRGGIGPYIGLCAVVASFGLADATVQGGMIGDLSLMCPELVQSFMGGLAVSGALTSALRLITKAAFEKTNDGPRKGAMMFLAISTCIELLCVFLYAYVFPKLPIVKYYRRKAASEGSKTVSADLAAAGIQNQSDLTDDDSKNQRLSNKELLIQNIDYAVNLFLIYVCTLSIFPGFLYENTGQHGLGDWYALVLVAMYNCWDLVGRYTPLVKWLKIENRKLITIAVLSRYLLIPAFYFTAKYGDQGWMIMLISVLGLTNGHLTVCIMTIAPKGYKGPEQNALGNLLVIFLLGGIFAGVALDWLWLIGKKNAF
Protein: Sexual differentiation process protein isp7 (P40902)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Sexual differentiation process protein isp4
- Transcription factor gaf1
- Uncharacterized amino-acid permease P7G5.06
- Probable proline-specific permease put4
- Uncharacterized MFS-type transporter PB1E7.08c
Sequence:
MLSQLIERSTQYVREASLEEQNRIMPLIDFGPYVNQEPGAHERIIQQLRAACESTGFFQIVNSPISPDVVKNAFRASKQFFELPFDEKLTLSKDMFSNRGYELMEDFVLEGEEDSSSPLEISGIDFEAGSYPGEAPLPPSSIGYVLPPSSLANGEGSSMFDADMTTSNAVAHGDESISNEFRESFYFGNDNLSKDRLLRPFQGPNKWPSTAGSSFRKALVKYHDQMLAFANHVMSLLAESLELSPDAFDEFCSDPTTSIRLLRYPSSPNRLGVQEHTDADALTLMSQDNVKGLEILDPVSNCFLSVSPAPGALIANLGDIMAILTNNRYKSSMHRVCNNSGSDRYTIPFFLQGNIDYVVAPLPGLGPSTAEPIAVEDLLRDHFQNSYTSHTTSLEVA
Protein: tRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33) (Transfer RNA methyltransferase 8) (tRNA (guanine(46)-N(7))-methyltransferase) (tRNA(m7G46)-methyltransferase) (Q96WV1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03055}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- Multifunctional methyltransferase subunit trm112
- tRNA
- tRNA pseudouridine synthase 4
- tRNA
- tRNA
- 18S rRNA
Sequence:
MSATAKKSAAQLQREEEEARKKLKRLSKQGGVEGRLPMKRLFRQRAHANVLSDHELEYPRSPSEMDWSPYYPDFDVESNKKVEIVDIGCGYGGLTVALGPQFPDTLVLGMEIRMQVSDYLKEKIQALRYRADHEEPVPGGYKNISVLRMNCQKFLPNFFEKGQLSKMFFCFPDPHFKARKHKNRIITSTLASEYAYFIRPHGTLYTITDVEELHVWMAQHLDAHPLFRRFTKEEEENDICVTLMTNETEEGKKVARNGGKKFVACYERIPNPK
Protein: DNA repair protein Rev1 (EC 2.7.7.-) (Reversionless protein 1) (Q9W0P2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents (By similarity). During homologous recombination (HR) repair of DNA double-strand breaks (DSBs) regulates the extent of repair synthesis. Possibly recruits the DNA polymerase zeta complex or another translesion polymerase to early DSB repair intermediates to initiate repair synthesis, while also blocking the access of more processive polymerases preventing them from acting during the initial stages of HR repair.
Subcellular location: Nucleus {ECO:0000255|PIRNR:PIRNR036573}.
Interaction partners:
- DNA polymerase zeta subunit 2
- DNA polymerase zeta catalytic subunit
- DNA polymerase eta
- DNA polymerase iota
- DNA polymerase delta subunit 3
- Proliferating cell nuclear antigen
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- DNA repair protein Rad51 homolog
- Proliferating cell nuclear antigen 2
Sequence:
MTRDEDNGFSEWGGYFEAKKSKLEEQFAAASDPFRKSDLFQGISIFVNGRTDPSADELKRIMMVHGGTFHHYERSHTTYIIASVLPDVKVRNMNLSKFISAKWVVDCLEKKKIVDYKPYLLYTNQKTSQPMLIFGKPKDNGANESKSDVEPPKDKAEVEVDSTKDETQMELGGILKNLQQAVATSPEKEASASESKITNLSTTSNNSTTARTAADPNFLSEFYKNSRLHHIATLGAGFKQYVCRLRQKHGTQGFPKRETLKSLANSHHNCLERYVMHIDMDCFFVSVGLRTRPELRGLPIAVTHSKGGNAATDVPVHPQADRKAELELFAQRFEHHFHDGDKAEKVRSGFDKKMSLSEIASCSYEAREKGIRNGMFVGQALKLCPELKTIPYDFEGYKEVAFTLYDTVAQYTLNIEAVSCDEMFVELTDLAHELNVDVMAFVSHLRQEVYSKTGCPCSAGVAGNKLLARMATKEAKPNGQFLLDSSNDILAYMAPMSLDLLPGVGSSISHKLKQAGLNNCGDVQNTTLEKMEKVLGKKLGQNLFQNCRGIDDRPLAYEQIRKTVSAEMNFGIRFTNSVECEQFLCQLSEEVTKRLVEIRRKARSINLKIMVRAAEAPVETSKYMGHGVCDIINKSSLIKYATDDVNVITTVVLDLMKDADIPPDELRGLGIHLTRLEDANEVRKENNIKEMFGKMSEMRKDKPIPQGAVGDKSIGDDKVNKPLVFENKPKPREPRNVLSMLTAAAVSRKSVTEDRSQRGTSKPITRPLSLVPKLDEDVLAQLPEDIRLEVIANREEHLCIAEYDGYRSPQYPTLRSPPLLNPYVTTNVSPLKATDLKPSTSRAAVARLQKRKERKEQEHYIRSDQIVADYIDDLPDFVNPHILKLISHPVEMPELLMGDNYKDLLNDWVSREEVPKPNDVDLILKQVSRMIKNDQLDHVCDVMKYWCRIINMKRSSSCCWHVAYKHIEESIQNQMLTIEGYSLLFIEYIRCIKCS
Protein: Translocating chain-associated membrane protein 1 (Protein TRAM1) (Q01685)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Involved in the translocation of nascent protein chains into or through the endoplasmic reticulum (ER) membrane by facilitating the proper chain positioning at the SEC61 channel. Regulates the exposure of nascent secretory protein chain to the cytosol during translocation into the ER. May affect the phospholipid bilayer in the vicinity of the lateral gate of the SEC61 channel, thereby facilitating ER protein transport. Intimately associates with transmembrane (TM) domain of nascent membrane proteins during the entire integration process into the ER membrane. Associates with the second TM domain of G-protein-coupled receptor opsin/OPSD nascent chain in the ER membrane, which may facilitate its integration into the membrane. Under conditions of ER stress, participates in the disposal of misfolded ER membrane proteins during the unfolded protein response (UPR), an integrated stress response (ISR) pathway, by selectively retrotranslocating misfolded ER-membrane proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1315422}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Translocating chain-associated membrane protein
Sequence:
MAIRKKSTKSPPVLSHEFILQNHADIVSCVAMVFLLGLMFEITAKASIIFVTLQYNVTLPATEEQATESTSLYYYGIKDLATVFFYMLVAIIIHAIIQEYVLDKINRRMHFSKTKHSKFNESGQLSAFYLFSCIWGTFILISENYISDPTILWRAYPHNLMTFQMKFFYIAQLAYWFHAFPELYFQKTKKEDIPRQLVYIGLYLFHIAGAYLLNLNHLGLVLLVLHYFVEFLFHISRLFYFSDEKYQKGFSLWAVLFVLGRLLTLILSVLTVGFGLARAENQKLDFSAGNFNVLAVRIAVLASICITQAFMMWKFINFQLRRWREHSTFQAPVVKKKPTVTKGRSSRKGTENGVNGTVTSNGADSPRNRKEKSS
Protein: ATPase inhibitor, mitochondrial (ATP synthase F1 subunit epsilon) (Inhibitor of F(1)F(o)-ATPase) (IF(1)) (IF1) (Q9UII2)
Organism: Homo sapiens (Human)
Function: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12110673}.
Interaction partners:
- Eukaryotic translation initiation factor 5B
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- Cytochrome b-c1 complex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 12
Sequence:
MAVTALAARTWLGVWGVRTMQARGFGSDQSENVDRGAGSIREAGGAFGKREQAEEERYFRAQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLKHDD
Protein: Rho guanine nucleotide exchange factor 26 (Q7JNG6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVIKCFTCLRKQSSEVWIVTADFDGQVEGHLTVHKGDRVEIVEDQATDCAEYVQVVLCDQPTKHGLVPASIIAPPESGSVPDRPDDSNASGSTVSKRKSLRRIFANSSKERAAAANSSSSNNNSPATRQSTSTSSPVTANGHTTESSTSAPIGVLSSGEPTSSNSIPSSSTPTHTVPSSVPATVIPIVVAEDEKAEDCLPPPMENITINNSIDEKDMNEDSVAASDAVEPEVALPAKVEKTPEETARFKRSYVLMELVETEQDYVKDLTSVVEGYIGNLNKMDLPADLVGKDKIIFANIVNILEFHKTNFLKEIEKCSENYEAAGAAFVKYERRLHTLYVTYCQNKPKSDYLLAQDDFEAFFADTKAKLGHKVALCDLLIKPVQRIMKYQLLLKDILKFTERAKDKTDTLKKALQVMHVVPKACDDMMQVGRLQNFDKSLSAQGKLIHQGTLQISESIAGNVQKPKDRRIFLFEQSAIIADHIPPKKEFGNPTYIFKSQFMVNKMVFEPNVPDDPLRFVIKSSDPTQPTSFIANAQSQEEKDEWNRKMSELLDQQKRLLAALVDPRRYNDMSSGMGDLSLGAPGGDRRGAPSSANRSAASSSKKPAESPKKEGKSKSSLFSFGKKPAKSPTSPPPLDAAAAGKFQKVADDQVNLETDEKVKVLDVKNGYASVKKADGTVGKCPSYFLTMSDIPGTNFAEQIQYRREWQRRVDETDVEYGPSAFDTATSSTDNFDVLLELTTCERPVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIWHGPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGVTSTVAFLSVISIPDPPTDFTVKISGDHEVRLKWKAESGLKYCIEYRILDDSSPENWLIASTNIEKTHVSLRNFARNSYSFRVFAYNQRVRSAPSQCICICFDGTEM
Protein: Retinoid-inducible serine carboxypeptidase (EC 3.4.16.-) (Serine carboxypeptidase 1) (Q9HB40)
Organism: Homo sapiens (Human)
Function: May be involved in vascular wall and kidney homeostasis.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MELALRRSPVPRWLLLLPLLLGLNAGAVIDWPTEEGKEVWDYVTVRKDAYMFWWLYYATNSCKNFSELPLVMWLQGGPGGSSTGFGNFEEIGPLDSDLKPRKTTWLQAASLLFVDNPVGTGFSYVNGSGAYAKDLAMVASDMMVLLKTFFSCHKEFQTVPFYIFSESYGGKMAAGIGLELYKAIQRGTIKCNFAGVALGDSWISPVDSVLSWGPYLYSMSLLEDKGLAEVSKVAEQVLNAVNKGLYREATELWGKAEMIIEQNTDGVNFYNILTKSTPTSTMESSLEFTQSHLVCLCQRHVRHLQRDALSQLMNGPIRKKLKIIPEDQSWGGQATNVFVNMEEDFMKPVISIVDELLEAGINVTVYNGQLDLIVDTMGQEAWVRKLKWPELPKFSQLKWKALYSDPKSLETSAFVKSYKNLAFYWILKAGHMVPSDQGDMALKMMRLVTQQE
Protein: GM01994p (Q95SD9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MLIANGMENEALLQRQRVKELEDYLDNLLLRVMETHPKILQNPYSRTTSAKRYGTWSFWSSSRTRATPTH