wanglab/gogpt-training-data huggingface dataset:
Protein: Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B] (P20918)
Organism: Mus musculus (Mouse)
Function: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells (By similarity).
Subcellular location: Secreted {ECO:0000250}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity). {ECO:0000250}.
Interaction partners:
- Histidine-rich glycoprotein
- Tissue-type plasminogen activator
- Annexin A2
- Alpha-enolase
- Alpha-2-antiplasmin
- Vitronectin
- Fibrinogen alpha chain
- Antithrombin-III
- Angiomotin
- Protein S100-A10
Sequence:
MDHKEVILLFLLLLKPGQGDSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKRVYLSECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRCTTPPPPPSPTYQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCESSASPDQSDSSVPPEEQTPVVQECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRCSETGGSVVELPTVSQEPSGPSDSETDCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPLCASASSFECGKPQVEPKKCPGRVVGGCVANPHSWPWQISLRTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRPEFYKVILGAHEEYIRGLDVQEISVAKLILEPNNRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFGAGRLKEAQLPVIENKVCNRVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIEREMRNN
Protein: Probable conserved ATP-binding protein ABC transporter (O33189)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Transport permease protein
- HTH tetR-type domain-containing protein
- Multidrug efflux system permease protein Rv1217c
- Putative 3-methyladenine DNA glycosylase
- Probable second part of macrolide-transport ATP-binding protein ABC transporter
- Fatty acid ABC transporter ATP-binding/permease protein
- Uncharacterized ABC transporter ATP-binding protein Rv1273c
- Mycobactin import ATP-binding/permease protein IrtB
- Probable first part of macrolide-transport ATP-binding protein ABC transporter
Sequence:
MMISSSDELLRDGADPAVIIDQLRVIRGKRLALQDVSVRVACGTITGLLGPSGSGKTTLIRCIVGSQIIASGSVSVLGQPAGSAELRHRVGYMPQDPTIYNDLRVIDNIRYFAELCGVDRQAADEVIEAVDLRDHRTARCANLSGGQRARVSLACALVGRPDLLVLDEPTIGLDPVLRVELWDRFTALARRGTTLLVSSHVMDEADRCGDLLLLRQGQLLAHTTPHRLRKETGCTSLEEAFLSIVRRTTTVPAAG
Protein: Tubulin glycylase 3D (EC 6.3.2.-) (Q23K29)
Organism: Tetrahymena thermophila (strain SB210)
Function: Probable glycylase which modifies tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of tubulin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19531357}. Note=Present in the cell body and not in cilia.
Interaction partners:
Sequence:
MINSHHTSQQTLNKESKSQMDKSYNIDDSIVDAKFENYTKKYQDDKLNKILHTYIKNPQILMDEEKEIKERFLAKQMKDVAATKQKFDTKNKLQQLELENENSQNNSYKTSNNLSKEEVIAVLQKQNRKSQVNSVLADNSNIQNDFYPQYRKPKNPTTKKRQSTDYTKRNTFQLENLNIQQQLNNKDSLNQQNQQQQDLAKNRVDNSQNQDIQARLYERTELQKLRIKQKEEEQAALKNKRQTNRSQSIEQNVNFVQNDNQKLIDRHKEYLKQLKQQVTIEKETQKQLKKKDEENKIRLRNSVLASIKNDLTEQRKLIQENHNLFLSKSTVSQSAKQISLPEINQSLTICLEKQKSEVEQEKKAVLTSQAFFRQSSLREIEETNEKIESKTNLSKVKKLRPLPFISSMVEWKKKQRIPADSKIFIVMGGYKDFKKALLKRGWIENPQTNSPCFDLKWTLLGKDIDYDNILPNQIVNHFENNSKICSKIGLLNSLKNLYWFDNADLNCFFPQCFDMNDPDEFNDFVKNFKLSKAVSVLKKYLRLYLEKDEKYNNCKIQAQVALQVLTRYYNDINNVIDDEKQASEYFKSIPDDEWEILASDEMSNEDLAKKKHFEWIKKIKLAYQGIKVKAQVKKKKKKSLAMIKKMISNEAIKRKQDGEKQQIDSSDSEDEEVEMDDFTSAVNQFLNQREKCDPQFNLKGEDNIWIVKPAGLSRGRGITCYKNLVEIIDHAKSMELQMIVQKYIENPVLIKQRKFDIRIWVLVTDWNPLAIWYFDECYVRFSADSYSTKNLSNKFQHLTNNAISKKKAQQGQDEITLQGNMYTQEQLENFFIETEGYNVFQQKIKPQIINIIKWSILSCSDTVESRKNSMELFGYDIMIDTNFNPWLLEVNTSPSLEYSTEITKKLVKQVLEDVAKVVVDYGMAQKSGIKKSELQKIGTGKFIKIYQGLEIQDKGINSIQKNFICEGSKMKIRKPKKQKKNTKLDKKQNLQQDLTINNQINHDQKQFSSQQANNIETYSRPQTAKSQTQSSKKL
Protein: Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase) (Q62658)
Organism: Rattus norvegicus (Rat)
Function: Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62942}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P62943}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62943}; Cytoplasmic side {ECO:0000250|UniProtKB:P62943}.
Interaction partners:
- Ryanodine receptor 1
- Serine/threonine-protein kinase mTOR
- Ryanodine receptor 2
- TGF-beta receptor type-1
- Regulatory-associated protein of mTOR
- Target of rapamycin complex subunit LST8
- Calmodulin-like protein 3
- Calmodulin-1
- Ribosomal protein S6 kinase beta-1
- Calmodulin-like protein 4
Sequence:
MGVQVETISSGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISPDYAYGATGHPGIIPPHATLVFDVELLKLE
Protein: Metalloendopeptidase (EC 3.4.24.-) (Q49IJ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EHEAKLQRLREELSRPVIEGHHRQSHHQKQAQHRQHHQSHHRKKHRRQQQHHRRRGQSTTQYVNHSPPGFNQSQQAQQQSVPEMDLLKAETSKDEEPLRHRVARAVTAKKERIWDYGVIPYEIDGNFSGIHKALFKLAMRHWENSTCIKFVERDPEIHPNYIVFTVRSCGCCSFVGKRGNGPQAISIGRNCDKFGIVVHELGHVVGFWHEHTRPDREKHVVIEHNNIMKGQDYNFNMLSPDEVDSLGMAYDYDSIMHYARNTFSKGTYLDTILPIEMKGRKRPEIGQRLRLSQGDIAQANLLYKCPKCGRTFQESSGIFASPSHYTAGALSNETEHCEWRITATYGERVELKLENMNIFKSNNCETDYLEIRDGYFEKSPLIGRFCGKVDKEVIRTESSRMLLTYVNTHRIEGFRGFKAEFD
Protein: GM09915p (Q95S39)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPVFESQSPSSPIATTLPKSQASSNGKLEKQISLLDSDSGISLSSINTCSTTAANSSPTYRAPNGFHSFPSHTLSFETLGDEYHEDEDTLSLENLFPCDQTEIYASKKISFIIDELIQTEVNYVNNLKKGMLNYGQLKDVEDLPEALSGETKQKMLLGNIKEILELHEKEILPLMLRNQRDLKGLFDEFAAHFEKNSFYCYVSFTMGKKSSMQLRQDNRLWLQTYQTQIKDKLGIDSFLVQPIQRLTRYPLLLQQFISEFYKSGISCKPVLTAVCKLETRMRRALDVVNQAEEIPNIEELNELDLQQLGNFRRATEFDAQHFPTRKKYRSKVFLFDRCLVCTEVRKKRLAYRQHYNWEHVELQRPLDSVSSNANKIINLLVKQEEGGSSVGSKREEYSFMAAEASVVKQWLQATHKIIEIARNEHARRNTFSLPMDLVLGVVLAIWLIWQYL
Protein: Penicillopepsin-1 (EC 3.4.23.20) (Acid protease) (Aspartic protease aspA) (Q01972)
Organism: Penicillium roqueforti
Function: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but can also activate trypsinogen and hydrolyze the B chain of insulin between positions 'Gly-20' and 'Glu-21'.
Subcellular location: Secreted {ECO:0000269|PubMed:9413440}.
Interaction partners:
Sequence:
MVVFSQVTVALTCFSAIASAAAVRQEPPQGFTVNQVQKAVPGTRTVNLPGLYANALVKYGATVPATVHAAAVSGSAITTPEADDVEYLTPVTIGSSTLNLDFDTGSADLWVFSSELTSSQQSGHDVYNVGSLGTKLSGASWSISYGDGSSASGDVYKDTVTVGGVKATGQAVEAAKKISSQFLQDKNNDGLLGMAFSSINTVSPTPQKTFFDTVKSSLGEPLFAVTLQGTGRPWHLRFGYIDSDKYTGTLAYADVDDSDGFWSFTADSYKIGTGAAGKSITGIADTGTTLLLLDSSIVTGLLQEGYPGSQNSSSAGGYIFPCSATLPDFTVTINGYDAVVPGKYINFAPVSTGSSSCYGGIQSNSGIGFSIFGDIFLKSQYVVFDSEGPRLGFAAQA
Protein: Meiotic recombination protein rec6 (P40385)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for formation of the rec12-mediated double-strand breaks (DSBs) that initiate meiotic recombination. May be involved primarily in the early steps of meiotic recombination (Probable).
Interaction partners:
- Meiotic recombination protein rec12
- Meiotic recombination protein rec14
- Meiotic recombination protein rec7
- Meiotic recombination protein rec15
- Meiotic recombination protein rec24
- Mei4-dependent protein 2
- Linear element protein rec10
- Linear element protein rec25
Sequence:
MHRVRSARDGIVLKYHFKEDWDETQNSPIDCIASSRLKFWKRLNFNIYLDPEVSNQNLKLLKTLTLHCDFQSPKKNLTMSKFKAMAVELIHEAFLKHIVSILSKECPLSFQPSYYSKMFNAMSNANIIAGSISRILTRESLDKSFEQSHFQLLMYKKCKLIYTRTLRKNEFDGIHKFPDLEDSKQKLQVADDEENKQYSESSLLDDSQLLCSSPPVDSTEEARTCNVEEDQDEILSVALVTTDTILSSDNFVNDMLSAAD
Protein: Hexosyltransferase (EC 2.4.1.-) (A1Z7G9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
- Beta-1,4-galactosyltransferase 7
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase I
- Xylosyltransferase oxt
- Hexosyltransferase
Sequence:
MRRLNNLVTFFTAITAFFFGSFLTKILSSVDQCPAHRSRIPHLEPHPNLFLMVLVLSAPHNADERNAMRRTWLANAGQSIAQPYLPEELIYLPTFNAQGHLQVELVAEQASRLRQYTNWQQSLLTEGPPRTKRLITVKHVFSIGTLDLSSSALAELEKEQNQNNDLLLLNRHHDTYKNLTAKLMQSLYILRRHYEFSYMLKVDDDTYVKLDSLVNTLVSYDRKLLRKRSEYRDHVLPQLYWGYFNGRSTIKTKGQWKESSYYLSKNYLPYALGGGYVLSRSLCDYIVNNSQLLSHYGSEDVSVGTWLAPLRHVYRWHDPRFDTSYAPRKCRSYHMVLHKRNGQMMRDIHDGELCSGIGSSILSDYYYDWTRTADKCCDSLVA
Protein: Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (EC 2.4.1.102) (EC 2.4.1.148) (EC 2.4.1.150) (C2GnT-mucin type) (C2GnT-M) (Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase) (Q5JCT0)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
Sequence:
MTSWQRLCWHYRLWTLGCYMLLAILALKLSLRLKCDFDAMDLDSEEFQSQYCRDLLYKTLKLPAKSSINCSGVIRGEQKAVTQALLNNLEIKKKQQLFTEADYLRMTADCEHFKTKRKFIQVPLSKEEASFPIAYSMVVHEKIENFERLLRAVYTPQNVYCVHMDQKSSEPFKQAVRAIVSCFPNVFIASKLVSVVYASWSRVQADLNCMEDLLQSPVPWKYLLNTCGTDFPIKTNAEMVKALKLLKGQNSMESEVPPPHKKSRWKYHYEVTDTLHMTSKRKTPPPNNLTMFTGNAYMVASRDFIEHVFSNSKARQLIEWVKDTYSPDEHLWATLQRASWMPGSDPLHRKFDLSDMRAIARLTKWYDHEGDIENGAPYTSCSGIHQRAVCVYGSGDLHWILQNHHLLANKFDPKVDDNVLQCLEEYLRHKAIYGTEL
Protein: Mismatch repair endonuclease PMS2 (EC 3.1.-.-) (DNA mismatch repair protein PMS2) (PMS1 protein homolog 2) (F1NQJ3)
Organism: Gallus gallus (Chicken)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Involved in B cell growth by positively regulating B cell proliferation and controlling replication efficiency. Controls cell cycle to prevent re-replication and defects in DNA damage-induced G2 checkpoint. Doesn't seem to counteract or control the immunoglobulin gene conversion (Ig GC) and to contribute to guanine/uracil mismatch repair. Possesses an ATPase activity, but in the absence of gross structural changes, ATP hydrolysis may not be necessary for proficient mismatch repair (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P54278}.
Interaction partners:
- DNA mismatch repair protein Msh6
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein
- DNA mismatch repair protein
- Uncharacterized protein.
- Fanconi anemia group J protein homolog
- Fanconi-associated nuclease
- DNA mismatch repair protein
- DNA repair protein complementing XP-A cells homolog
- HMG box domain-containing protein.
Sequence:
MEEAAPCSEPAKTIKRIDRESVHRICSGQVVLSLGTAVKELVENSLDAGATNIDVRLKDHGAELIEVSDNGGGVEEENFEGLTLKHYTSKIQDFSDLIHVETFGFRGEALSSLCALSDVTISTCHKSAKVGTRLVFDHNGKITQKAPYPRQQGTTVSIQQLFHTLPVRHKEFQRNIKKEYAKMVQILQAYCIISKGVRINCTNQVGQGKKSPVVSTTGGPNLKENIGAVFGKKQLQSLIPFVQLPPNEAVCEEYGLKSTDLPEKLYSITGFISRCDHGVGRSTTDRQFFFINQRPCDPAKVVKLVNEVYHLYNKHQYPFIVLNICVDSECVDINVTPDKRQILLQEEKLLLAILKTSLIEMFGSDVNKLNVNQNLLDIVGNVKAPPGDAEKPWVEMSHHSETENPSSEGKRVMTLSRLRESFSLHQTESYFQSPKKVKQRHSSSKQLSLDTILSTVRTQKAVLSEDSESCHEMKSKMPVPRKYLRKVDDIDSGFCSTSESDAGYNTPEAGSCVISESVNNPIEEEFCSSEEQHQNEYLKTVGHSEKSLECDIQVLGTEHKLNRVNDCNNQTNLPQEATNSLPRVRRFKNEADDFKAGIHPKVENTRNYMPCVDVLVEVKKKTVPLEFSMKALAERVRKIVQQQQKCTETQNYRRFRAKISPGENKVAEDELRKEISKEMFAKMEIIGQFNLGFIIAKLNSDLFIIDQHATDEKYNFEMLQQHTVLQGQKLIAPQNLNLTAVNETVLIENLEIFRKNGFDFVINENAPVTQRVKLISLPTSKNWTFGPQDIDELIFMLSDCPGVMCRPSRVRQMFASRACRKSVMIGTALNVQEMKKLVTHMGEIEHPWNCPHGRPTMRHIASLDLIASE
Protein: Xanthine phosphoribosyltransferase 1 (XPRT) (EC 2.4.2.-) (P47165)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May act as a xanthine phosphoribosyltransferase involved in the synthesis of purine nucleotides. Such activity is however unclear in vivo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Hypoxanthine-guanine phosphoribosyltransferase
- Phosphoribosylaminoimidazole carboxylase
- Purine nucleoside phosphorylase
- Adenine phosphoribosyltransferase 2
- mRNA-binding protein PUF3
- Uridine nucleosidase
Sequence:
MAENERMYISYNNIHKLCQGVAKHILARNERPDIIIAITGGGMIPARIIRSFLKTKGQKNIPIQAIGLSLYEDLGLDNSVETIGKEVIRTQWLDFGALNQHFDSLIGKKVLIVDEVDDTRTTLHYAVSELEKEIAEQQKVLNRMSEETVISIFVLHNKDKPKRAGLPDSMMNSGRYIAAQTVPDKWLCYPWDAEDIEEHTMLAKAQGHD
Protein: DNA ligase (EC 6.5.1.1) (Q8IES4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Proliferating cell nuclear antigen 1
- Flap endonuclease 1
- Endonuclease, putative
- Proliferating cell nuclear antigen 2
- DNA helicase
- Plasmodium RESA N-terminal domain-containing protein
- Replication factor C subunit 2, putative
- DNA-
- DNA helicase
- Exonuclease 1
Sequence:
MNFLILVVLIKMVVCKIINYVRSDYNFMLSFLRTRKIFSHKKIYFNFKVSKNITKNSSSNSYSDILKCFSFPRKGTNDKTKENETFEKGEVKEEEEEKDKNVKRKIINESSKNKRAKVKNENDVIKKGSLFNCVVREDEKVNDLSSPKFNPVHFNINDLYLSEKDKEKHKFKDSLLFTFLTNAFNQIEELKGSGTGSKKNVSIILSNIFRVLIYYSPNDLIPAVYITLNKVAPDYLNVEAGVGEALILKTMSEAYSRTESSIKKDLQQIEDLGIIAENCSCKMRTIFPLPRLTIQSVFHELKSIPNLIGSNSQQKKREVIKKLLVSAKTSEAKYIVRFLQQRLRIGVNSATVVQALSYAFILTRPSIPDDIIKRGKEINENLINGKLDGTNNLINKSNNKTEEWLTQSGDRNCIKEENLNDELLSKDDINKCENMDSLINEIRIRNEKINKPNIFYNLIEKVGDTRLLPLFFKELKNIYCEENNDIDIFECMEKSVKSALCELPNIEIIIQNLLNGDDMNTLSKKCTVKTGIPVQPMLAKPTKGVQEVLDRFNNVTFTCEYKYDGERAQIHYIDKDNIKIFSRNLETMTEKYPDVIQIIKDQIGENVKECIIDSEVVAYDIVNNKILPFQVLTTRKRKDVDIENIKVKVCLFPFDLICCNGIPVIKEPLAVRRKLLYSLLKSKDGVLSYATHSEMNNIEDIDMFLQDAIENNCEGLMVKTLVENASYEPSRRSLNWLKVKKDYVEGLSDSVDLVPIAGYYGKGKRSGVYGAFVLAAYNSETENFQTVCKAGTGFSDEILSTLYETLSEKIIPNKKSYYEVSDKLNPDVWFDAHYVWEVKAADLSLSPVHTAAIGIYADDKGIGLRFPRFLRLREDKNAEQATTTQQIVDFYEAQFSSNKNKNIDYNDDTESE
Protein: Heptosyltransferase family protein (Q72F07)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Heptosyltransferase family protein
- CgeB family protein
- ADP-heptose synthase, putative
- CgeB family protein
- Uncharacterized protein
- D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
- Potassium uptake protein TrkA, putative
- TPR domain protein
Sequence:
MRLVVINLTRFGDLLQTQPALAGLHAQGHETALVCLDNFAEAASLLYGVAHVAPLPGARLLAGLDDDWRRATADITDWCDDLTKSFRPDGVLNLTATLAGRLLARRLVPQGGPLLGFALDEHGFGLDADAWSTFLQAASRDRGCSPFNLVDVIRRVAGVGDQTPVFTLRCPDAERRAVVHRQLAEAAPEGCEGFVALQPGASEDRRRWPVASFAAVGDRLWREQRLCPVLVGSTAEQHLAEGYATAATAPFISLVGRTRLPDLAAALSCTRALVTNDTGTMHLAAGLGLPVLAIFLATAQPWDTGPYSDDACCLEPDMPCHPCPFGVPCPHDHACHDAIRPADVAALLLGRLTKGAWHSVPAKGARVWVARRDAHGFIDLASASAHGDAFASGHDDASAHGHDDASASGHEQETRTAWIREQRHFYRQFLDLKRPAATAGCPLPSLRAPDLPCALPQAFRHDCATVLGQASALLHLLGEQGLLLQRTSSDLAKQRFLTTCGRIHALFEQSPHFRALAHLWLSEMQTAGASLDTILQLASLYRALATAWHDHLSVATD
Protein: POU domain protein (A0A0A0MT46)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MLDCSDYVLDSRMNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSSLSSPSALNSPGIEGLSRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPTSLVATTPSLVTSSAATTLTVSPVLPLTSAAVTNLSVTGTSDTTSNNTATVISTAPPASSAVTSPSLSPSPSASASTSEASSASETSTTQTTSTPLSSPLGTSQVMVTASGLQTAAAAALQGAAQLPANASLAAMAAAAGLNPSLMAPSQFAAGGALLSLNPGTLSGALSPALMSNSTLATIQ
Protein: Uncharacterized protein DDB_G0286393 (Q54LV6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Aspartyl aminopeptidase
- Uncharacterized protein DDB_G0289357
- RBR-type E3 ubiquitin transferase
Sequence:
MDDDEFVFIESNPTQSTWVDVKKSQQQQQQQPQAPPQQQQQQILPVYRNLNPLVDENDGFTYQQQQLYLQQQQQFCQQQLLLEQQQQQQLLLKQQQQQLLLEQQQQQLLLKQQKQQLLLEQQLLLEQRQQQQQKVPIPIAQVPASTLVVESKQEEKIQEEQEVPVIVSIINSPPPPQEEEKPQLSKKEEPEWLKGKDKAPYISTSTSDVKYTSNVVSNKPYTTIKSSTSYSSVSGSGGSGIRRISLAELNGNSKPYTSSNATNKPFTTASKSTNSYSFSF
Protein: Gap junction beta-4 protein (Connexin-30.3) (Cx30.3) (Q02738)
Organism: Mus musculus (Mouse)
Function: Structural component of gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15692151}; Multi-pass membrane protein {ECO:0000305}. Cell junction, gap junction {ECO:0000269|PubMed:15692151}. Note=Colocalizes with GJB2 at gap junction plaques in the cochlea. {ECO:0000269|PubMed:15692151}.
Interaction partners:
- Gap junction beta-2 protein
- Gap junction beta-3 protein
- Gap junction delta-3 protein
- Gap junction gamma-1 protein
- Gap junction alpha-4 protein
- Gap junction alpha-3 protein
- Gap junction alpha-8 protein
- Gap junction alpha-5 protein
- Gap junction alpha-1 protein
- Gap junction epsilon-1 protein
Sequence:
MNWGFLQGILSGVNKYSTALGRIWLSVVFIFRVLVYVVAAEEVWDDDQKDFICNTKQPGCPNVCYDEFFPVSHVRLWALQLILVTCPSLLVVMHVAYREERERKHRLKHGPNAPALYSNLSKKRGGLWWTYLLSLIFKAAVDSGFLYIFHCIYKDYDMPRVVACSVTPCPHTVDCYIARPTEKKVFTYFMVVTAAICILLNLSEVVYLVGKRCMEVFRPRRRKASRRHQLPDTCPPYVISKGGHPQDESVILTKAGMATVDAGVYP
Protein: Protein FAM219A (Q8IW50)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMEEIDRFQVPTAHSEMQPLDPAAASISDGDCDAREGESVAMNYKPSPLQVKLEKQRELARKGSLKNGSMGSPVNQQPKKNNVMARTRLVVPNKGYSSLDQSPDEKPLVALDTDSDDDFDMSRYSSSGYSSAEQINQDLNIQLLKDGYRLDEIPDDEDLDLIPPKSVNPTCMCCQATSSTACHIQ
Protein: tRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (P0A873)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates guanosine-37 in various tRNAs.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Large ribosomal subunit protein bL19
- Small ribosomal subunit protein bS16
- Ribosome maturation factor RimM
- Large ribosomal subunit protein uL4
- Protein translocase subunit SecY
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein bS1
- Elongation factor G
Sequence:
MWIGIISLFPEMFRAITDYGVTGRAVKNGLLSIQSWSPRDFTHDRHRTVDDRPYGGGPGMLMMVQPLRDAIHAAKAAAGEGAKVIYLSPQGRKLDQAGVSELATNQKLILVCGRYEGIDERVIQTEIDEEWSIGDYVLSGGELPAMTLIDSVSRFIPGVLGHEASATEDSFAEGLLDCPHYTRPEVLEGMEVPPVLLSGNHAEIRRWRLKQSLGRTWLRRPELLENLALTEEQARLLAEFKTEHAQQQHKHDGMA
Protein: AT13664p (Q5U0T8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDEANKEDVKRASLSNSTVTIRPRLIYGLRSDVIGNIHFNLTKEVIYPVEGVLAFHDYVQNKQRFLRLPEDTRPEVISISSHRKLLAVVERHSKNGRYISIYELATLKKRRHLELPSNHRNAEIQQMIFTNDSRSVALITRPPEETLIMLVLDKTSTVIEGRATIPGSHGGAECIAGNPNDCNFMAVGGERTLLLMSKSERGFSISNNLKVKYRVTSMAFLSLDLLMIGTSDDQLILVENGEQKLAQKASDADTVDLMIDQEVFDRDKELQEQRFLPTQAVSLPDRRVLCMTAFPKGFAYIIFNRAFVFERVSKFKFERKTILTVPTNLYAEHMYQILNLAIDHKQETVIVTTSHCQIYVGILIVPETLKTKQLKFEPLGVLIHTGEIIAMSVCAWKPIIMTASRDQTIRIWNYETALVELVRKFQVDVNIVELSLTGQMAAIGFSDQLRITQIFMDDLNIVKTYNFPHCNAVRYSNFGHMMAAAYDNNIAITSVYKLDVLINLKGHNGIVLSVAWSRTDKFLISGGAEGAIYLWDIETGARLQEIVQKGTEYVTISCSTNDPLTIYAGTSIGTIREFQDSTLVREITIPSRTKGSVSDVCLARSDLIMFVADHEGNLFNMQLPFLEAGGGTFTNFRFFDGPVNKLRFSYDGTLLFAISNKGTLAIWAMDNIEGKVPYMDQDLMRSQEVLIPRSQLNDKIEQIANLELRLKQQAEEFQYQLSQNEIFDGQQLQEVHRSYCSALEELKELNNEIEARHTEEMNHITFQINSIREEHRIQLDTLATQYSERMLIEYQKFTNLRENMLELRESYEDKLKNSTGTLQDTVEALENNYKQQLNERKELIRDLMKEMQDKKAEFIEYCREVELENDRNMVSTQTEYENKLTTERNETQMWRGKAGVLQKKFESQSREIDNLLEEVEILKEEHHKSQRNIQKQMRNIEDLQKDIADRDYAINGKEKRIQDLLHKNQELDKYKQVLGHKIAELKAQIEPREFQINDKRKHIIEMEAELEGLNQNNVQLELQLKEMRDKYLSNVAELRTERHRAKASRECLHSICSDIYYVAGEINSAEALKKAVKELFRKHASDDELKRFVTLDAEVRDEFMRQRRQIENVLDRYKSVAEDKSVQKKYDKLFKENVILIEEIEKLNETNKMLRSKVKEDLRRSTKTIHK
Protein: AFG3-like protein spg-7 (EC 3.4.24.-) (Q9N3T5)
Organism: Caenorhabditis elegans
Function: Acts as a component of the m-AAA protease complex which is an ATP-dependent metalloprotease mediating degradation of non-assembled mitochondrial inner membrane proteins (By similarity). The complex is necessary for the assembly of mitochondrial respiratory chain and ATPase complexes (By similarity). Functions both in post-translational assembly and in the turnover of mistranslated or misfolded polypeptides. Plays a role in male tail tip morphogenesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P39925}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39925}.
Interaction partners:
- Mitochondrial prohibitin complex protein 1
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Lon protease homolog, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
- Chaperonin homolog Hsp-60, mitochondrial
- Heat shock protein hsp-6
- Stress activated transcription factor atfs-1
- ATP-dependent Clp protease proteolytic subunit 1, mitochondrial
- Mitochondrial prohibitin complex protein 2
- Probable voltage-dependent anion-selective channel
Sequence:
MWRLYRKTPKQLRNSVESCFKSVNSRQFSVSSFSAVAKDDKSVLKQQEVLHLLAKDQRFEERFFNQVQQTIRYFASKPNDLKKFFRKEASTDNKESSSSSDKKDSKGNKGEDNNPFNQFPGGWQQIAVSVGILLALYAFMDYQSYREISWKEFYSDFLEAGLVERLEVVDKRWVRIVSSSGKYAGQTCYFNIGSVDSFERSLGAAQHHLQYDADRQIPVLYKSEFNFKREIPNLISVAFPLLFGYYIYRMLKGGGAAGGAGRAGGGGLGGMFGGFGQSTARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDESSVIVIAATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIAARDANHEISNKHFEQAIERVVAGMEKKTQVLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYLPKEQYLYSKDQLLDRMCMTLGGRVAEEIFFGRITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSFETPAPGEMAFDKPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVGKRPFVEKNTYEEMVSGTGGLDENVELPKGLENWNKESEKKKKDEEKKKNDE