wanglab/gogpt-training-data huggingface dataset:
Protein: NirJ (P95416)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MLRISHYLRSLTEDAPTPRRAGGRRAPVVIWNLLRRCNLTCKHCYSTSADSDFRGELETAEILRGIDDLRAAGVRVLILSGGEPLMHPDLFEIAAHARQAGMFVALSSNGTLIDEGNIQRVAEARFDYVGISLDGLRETHDRFRQKQGSFDAALAAMRLCREADIRVGMRTTLTEENAAQLPALLDLMRELDVQKFYLSHLNYSGRGRRSRALDAHHRRTREALALLFERADQDIRQGRDSDFVTGNNDADAILLLDWLKRRRPQQLARLCELLLDWGGNASGEGIANIDNTGEVHPDSYWWHHSVGNIRHQRFADFWFERPDPLLLQLRQRPRPVVGRCSQCRWLDICNGNTRTRAWAGGELWGEDPGCYLSDQEIGLERIALHAV
Protein: DNA-binding protein creA (Carbon catabolite repressor A) (Q01981)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Transcription regulator component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Represses the transcription of the alcR, alcA and aldA genes by binding to a GC-rich region in their promoter. Also plays a role in response to carbon starvation and the control of extracellular proteases activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:18063396}.
Interaction partners:
- Xylanolytic transcriptional activator xlnR
- Catabolite repression protein creC
- Ubiquitin carboxyl-terminal hydrolase creB
- pH-response transcription factor pacC/RIM101
- HECT-type ubiquitin ligase-interacting protein creD
- Protein-methionine methyltransferase laeA
- Exo-1,4-beta-xylosidase xlnD
- Endo-1,4-beta-xylanase B
- E3 ubiquitin-protein ligase RSP5
- non-specific serine/threonine protein kinase
Sequence:
MPQPGSSVDFSNLLNPQNNTAIPAEVSNATASATMASGASLLPPMVKGARPAAEEARQDLPRPYKCPLCERAFHRLEHQTRHIRTHTGEKPHACQFPGCSKRFSRSDELTRHSRIHNNPNSRRGNKAQHLAAAAAAAAANQDGSAMANNAGSMMPPPSKPITRSAPVSQVGSPDISPPHSFSNYANHMRSNLSPYSRTSERASSGMDINLLATAASQVERDESFGFRSGQRSHHMYGPRHGSRGLPSLSAYAISHSMSRSHSHEDEDSYASHRVKRSRPNSPNSTAPSSPTFSHDSLSPTPDHTPLATPAHSPRLKPLSPSELHLPSIRHLSLHHTPALAPMEPQAEGPNYYNPNQPHVGPSISDIMSRPEGAQRKLPIPQVPKVAVQDMLNPSGFTSVSSSTANSVAGGDLAERF
Protein: AP-1 complex subunit gamma (Q7KVR7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MYPYYEQDWSVLPPENNRRFNPAFNMATIRQAFTEAVERVRMPTPTRLRDLIRQIRAARTAAEERAVVNKECAYIRSTFREEDSVWRCRNIAKLLYIHMLGYPAHFGQLECLKLTASTRFTDKRIGYLGAMLLLDERQDVHLLITNCLKNDLNSSTQFVVGLALCTLGAIASPEMARDLASEVERLMKSPNTYIRKKATLCAFRVIRRVPELMEIFLPATRSLLSEKNHGILITGVTLITEMCENSSDTLMHFKKIVPNLVRILKNLILGGYSPEHDVSGVSDPFLQVKILRLLRILGHNDPDASEAMNDILAQVATNTETSKNVGNTILYETVLSIMDIRSEGGLRVLAVNILGRFLLNSDKNIRYVALNTLLRTVHADTSAVQRHRTTILECLKDPDVSIRRRAMELSFALINAQNIRTMTKELLLFLEKADAEFKAQCSSGMILAAERYSPTTRWHLDTQLSVLIAAGNYVRDDVVSSTIQLVSSSPVPEQTYITNRFWESLQVANHCEDKQPLLQVAVWAIGEYGDLFMYGANEDEFERPTESDLIAVYYKFLTSAQVSTTSKQYALVSLAKLSTRLQQCVEEIQALITSFGSHLNVDLQQRGVEFTQLFGHYKHLRPPLLEKMPAMQISRISSQNGESGGGSFDDNSPDVIENGVEGGGGGGHSLIESNMNTLGDNTNILLDLLGSTDLSAGGAGDLVAATDLSNAVHKKNSRNANDVVAPVSNNQDLLDLLDLDLSAPSSTTTGAPAGGGGGGGIVALVGDNNQSSAANMNNMLGGLDLGGFGSGLDSSASIPTNGNDLASMLGGLGAPPAASPSLAASAPVGNLIDGHAGSLLADLNPTAASNNVVVPPQGPRLTALDKDGLLVQLVSVRGSDCMRIYMTTTNNSDNTLDQYLLQAAVQRSFQLQMLTPSGSVLPPGGVITQEMRVVATSNATLRMRLRIQYVLDGQQQVEQTEVSGFPEQQPAPAAAE
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (K7EIU8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSSMMVKDEYVHDFEGQPSLSTEGHSIQTIQHPPSNRASTETYSTPALLAPSESNATSTANFPNIPVASTTPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD
Protein: Peptidyl-prolyl cis-trans isomerase FKBP1B (PPIase FKBP1B) (EC 5.2.1.8) (12.6 kDa FK506-binding protein) (12.6 kDa FKBP) (FKBP-12.6) (FK506-binding protein 1B) (FKBP-1B) (Immunophilin FKBP12.6) (Rotamase) (Q9Z2I2)
Organism: Mus musculus (Mouse)
Function: Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Ryanodine receptor 2
- Ryanodine receptor 1
- Triadin
- Ryanodine receptor 3
- Calmodulin-like protein 3
- Calmodulin 5
- Calmodulin-4
- Calmodulin-1
- Calmodulin-like protein 4
- Aspartyl/asparaginyl beta-hydroxylase
Sequence:
MGVEIETISPGDGRTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLSLE
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (O61458)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
MVQMPPPPSNAPTSADACLSIVHSLMCHRQGGESEGFAKRAIESLVKKLKEKRDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARIWRWPDLHKNELKHVKYCAFAFDLKCDSVCVNPYHYERVVSPGIDLSGLSLQSGPSRLVKDEYSAGPLVGSMDIDGNDIGTIQHHPTQMVGPGGYGYPQGPSEYVGDANPMSAMFPTGRTIPKIEPQDGVAGSRGSWMVPPPPRLGQPPQQQQQQPQQQTPQPTQQQQAQSQAAAHSLPVPHGMPGMPGPMNPGPVMAPPPPPQQAQNPQGNGVHHTQANSPTDPASALAMQQQQQQQQQQQQQQQQQQQQSGGVPNGSVNAGGGAAAGGQYYGQPPPVSQMQGAGGGGTSVAPSVHAQQNGYVSQPGSAGSAPVGGGGVFGTAQPTPQQPQQPPTGVQANTGSAGAQAGAGGGAAGTWTGPNTLTYTQSMQPPDPRSLPGGFWNSSLSGDLGSPQQTPPQQQQQQQQPRLLSRQPPPEYWCSIAYFELDTQVGETFKVPSAKPNVIIDGYVDPSGGNRFCLGALSNVHRTEQSERARLHIGKGVQLDLRGEGDVWLRCLSDNSVFVQSYYLDREAGRTPGDAVHKIYPAACIKVFDVRQCHQQMHSLATNAQAAAAAQAAAVAGVANQQMGGGGRSMTAAAGIGVDDLRRLCILRLSFVKGWGPDYPRQSIKETPCWIEVHLHRALQLLDEVLHAMPIDGPRAAA
Protein: NAD kinase 1 (EC 2.7.1.23) (ATP-dependent NAD kinase) (Poly(P)-dependent NAD kinase) (PPNK) (O31612)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP, UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
Interaction partners:
- Nicotinate-nucleotide adenylyltransferase
- NH
- NAD-dependent protein deacetylase
- NAD kinase 2
- GTP pyrophosphokinase YjbM
- UPF0738 protein YjbL
- Uncharacterized RNA pseudouridine synthase YjbO
Sequence:
MKFAVSSKGDQVSDTLKSKIQAYLLDFDMELDENEPEIVISVGGDGTLLYAFHRYSDRLDKTAFVGVHTGHLGFYADWVPHEIEKLVLAIAKTPYHTVEYPLLEVIVTYHENEREERYLALNECTIKSIEGSLVADVEIKGQLFETFRGDGLCLSTPSGSTAYNKALGGAIIHPSIRAIQLAEMASINNRVFRTVGSPLLLPSHHDCMIKPRNEVDFQVTIDHLTLLHKDVKSIRCQVASEKVRFARFRPFPFWKRVQDSFIGKGE
Protein: Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49) (Q6FRR0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Malate dehydrogenase
- Malate dehydrogenase
- Pyruvate kinase 2
- Pyruvate carboxylase
- Pyruvate carboxylase
- Malate synthase
- Malate dehydrogenase
- Enolase 2
- Pyruvate kinase 1
- Enolase 1
Sequence:
MPSKSSVSGNSVEERIRSELGLSKEVTLIRRNAPAAVLYQDALKEKKTVISSAGALIAYSGEKTGRSPKDKRIVEEETSRDNVWWGPVNKPCSERTWAINRERAADYLRTRETLYVVDAFAGWDPKYRIKVRVVCARAYHALFMTNMLIRPTEEELANFGEPDFTVWNAGQFPANARTQDMTSKTTIEINFKAMEMVILGTEYAGEMKKGIFTVMFYLMPVHHNVLTLHSSCNQGIKNGDVTLFFGLSGTGKTTLSADPHRLLIGDDEHCWSDEGVFNIEGGCYAKCINLSREKEPEIFDAIRFGSVLENVIYDSESHEVDYDDSSITENTRCAYPIDFIPSAKIPCLAPAHPKNIILLTCDASGVLPPVSKLTPEQVMYHFISGYTSKMAGTEQGVTEPEPTFSSCFGQPFLSLHPMRYATMLAEKMHEHSANAWLINTGWTGSSYVSGGKRCALKYTRAILDAIHDGSLAKAEFESLPIFNLQVPKAVEGVPSELLNPARNWSEGEAKYQSAVSKLAGLFVENFKTYQDKATSDVLAAGPQL
Protein: Small ribosomal subunit protein uS9m (37S ribosomal protein S9, mitochondrial) (P38120)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS4m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL6m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS2m
Sequence:
MFSRLSLFRRAALAPAPMRMSFRTIYQKTEDELPRRIVPKLATFYSANPNHEDRINRLERLLRKYIKLPSQNNNEAQQTKAPWISFDEYALIGGGTKLKPTQYTQLLYMLNKLHNIDPQLTNDEITSELSQYYKKSSMLSNNIKIKTLDEFGRSIAVGKRKSSTAKVFVVRGTGEILVNGRQLNDYFLKMKDRESIMYPLQVIESVGKYNIFATTSGGGPTGQAESIMHAIAKALVVFNPLLKSRLHKAGVLTRDYRHVERKKPGKKKARKMPTWVKR
Protein: Pyrethroid hydrolase Ces2a (EC 3.1.1.88) (Carboxylic ester hydrolase) (EC 3.1.1.-) (Q8K3R0)
Organism: Rattus norvegicus (Rat)
Function: Carboxylesterases that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes permethrin faster than cypermethrin (By similarity). Hydrolyzes retinyl esters.
Subcellular location: Microsome {ECO:0000269|PubMed:12230550}.
Interaction partners:
Sequence:
MPLARLPGWLYVVACGLLLLLQHVHGQDSASPIRNTHTGQVRGSFVHVKDTKSGIHTFLGIPFAKPPVGPLRFAPPEDPEPWSGVRDATSQPAMCLQTDIMNLDGIKEMKLTVHPTPMSEDCLYLNIYTPAHAREGSNLPVMVWIHGGGLVLGSASMNDASTLAATEEIVIVSIQYRLGVLGFFSTGDQNARGNWGYLDQVAALRWVQQNIAYFGGNHGKVTIFGGSAGGTSVSSHVVSPMSKGLFHGAIMQSGVALLPDLISDKSEVVYKTVANLSGCEAPDSEALIRCLRAKSKQEILAINQVFKMIPGVVDGKFLPKHPQELLASGDFHPVPSIIGINTDECGWGIPVFLGLDHIIKKITRETLPTVLKSTAAQMMLPPECIDLIMEEYMGDTENPETLQEQFRHMLGDFMFVIPALQVAHFQRSQAPVYFYEFQHLPSFIKQVRPSHVKADHGDDILFVFGSYLWGMTFDLTEEEELLKRRVMKYWANFARTGNPNGEDLPHWPVLDHDEQYLQLNTQPAVGRALKARRLQFWTKTLPQKIQELKGSQSKHAEL
Protein: Nitrogen permease regulator 2 (P39923)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. Mediates inactivation of the TORC1 complex in response to amino acid starvation. Post-transcriptional regulator of nitrogen permeases. May be involved in putative NPR1-dependent phosphorylation of nitrogen permeases or in the processing and targeting of nitrogen permeases at the level of the endoplasmic reticulum.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:21454883}; Peripheral membrane protein {ECO:0000269|PubMed:21454883}.
Interaction partners:
- Restriction of telomere capping protein 1
- Nitrogen permease regulator 3
- Maintenance of telomere capping protein 5
- SEH-associated protein 4
- Nucleoporin SEH1
- Vacuolar membrane-associated protein IML1
- GTP-binding protein GTR1
- Protein transport protein SEC13
- GTP-binding protein GTR2
- Mitochondrial inner membrane protease subunit 1
Sequence:
MLSYFQGFVPIHTIFYSVFHPTEGSKIKYEFPPNNLKNHGINFNTFKNYIIPKPILCHKLITFKYGTYRIVCYPVTINSPIYARNFFSFNFVFVFPYDCETSPYEPAITRLGKMFKVLEEQNQLLSKSERDPVFFDLKVLENSTTTPSTAGPSSTPNPSSNTTPTHPTSEKDTKDMRSSRYSDLIKDLGLPQSAFSIQDLLMRIFQDLNNYSECLIPIDEGNAVDIKIFPLLRPPTTCVSLEDVPLSSVNLKKIIDVNWDPTMMSIVPYIDGLNSIAKISKLSNSDPGLVIECIRHLIYYKCVTLSDIFQFSNIYAPSSLIRNFLTDPLMASDCQSYVTFPEVSKISNLPLNKSLGSGDQDSPSFSVRRKSKSSSIPSNPDSRTTSFSSTSRVSQNSSLNSSFSSIYKDWRQSQTSCSSSNIHVINNRNRFLPTRSCLFDLYRSLSQGQTLKTWYESKYMILKENNIDIRRFITFGLEKRIIYRCYSFPVMINAGSREPKEMTPIITKDLVNNDKLLEKRNHNHLLSATGSRNTAQSGNLKPERPSKVSFEMQRVSSLATGKSTMPKLSDEEEGILEESIRNAETFDKICVLLSKPKLEVESYLNELGEFKVINS
Protein: Programmed cell death protein 1 (Protein PD-1) (mPD-1) (CD antigen CD279) (Q02242)
Organism: Mus musculus (Mouse)
Function: Inhibitory receptor on antigen activated T-cells that plays a critical role in induction and maintenance of immune tolerance to self. Delivers inhibitory signals upon binding to ligands, such as CD274/PDCD1L1 and CD273/PDCD1LG2. Following T-cell receptor (TCR) engagement, PDCD1 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation. Suppresses T-cell activation through the recruitment of PTPN11/SHP-2: following ligand-binding, PDCD1 is phosphorylated within the ITSM motif, leading to the recruitment of the protein tyrosine phosphatase PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules, such as ZAP70, PRKCQ/PKCtheta and CD247/CD3zeta. The PDCD1-mediated inhibitory pathway is exploited by tumors to attenuate anti-tumor immunity and facilitate tumor survival (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22641383, ECO:0000269|PubMed:30487606}; Single-pass type I membrane protein.
Interaction partners:
- Programmed cell death 1 ligand 1
- Programmed cell death 1 ligand 2
- T-lymphocyte activation antigen CD80
- T-lymphocyte activation antigen CD86
- Tyrosine-protein phosphatase non-receptor type 11
- Cytotoxic T-lymphocyte protein 4
- Galectin-9
- Tyrosine-protein phosphatase non-receptor type 6
- Lymphocyte activation gene 3 protein
- T-cell surface glycoprotein CD4
Sequence:
MWVRQVPWSFTWAVLQLSWQSGWLLEVPNGPWRSLTFYPAWLTVSEGANATFTCSLSNWSEDLMLNWNRLSPSNQTEKQAAFCNGLSQPVQDARFQIIQLPNRHDFHMNILDTRRNDSGIYLCGAISLHPKAKIEESPGAELVVTERILETSTRYPSPSPKPEGRFQGMVIGIMSALVGIPVLLLLAWALAVFCSTSMSEARGAGSKDDTLKEEPSAAPVPSVAYEELDFQGREKTPELPTACVHTEYATIVFTEGLGASAMGRRGSADGLQGPRPPRHEDGHCSWPL
Protein: Probable methionine--tRNA ligase, cytoplasmic (EC 6.1.1.10) (Methionyl-tRNA synthetase) (MetRS) (Q9UUF2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- tRNA-aminoacylation cofactor arc1
- Probable glutamate--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Putative proline--tRNA ligase C19C7.06
- Probable glutamine--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
- Putative leucine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Lysine--tRNA ligase, cytoplasmic
Sequence:
MATYKVQIPASFKTSYSFAESLKVSIAISAFSVKVPCEGAANCNSVRLVNSKEPEKYVSDANAIVSFLYWKQEEDLFNSFISSKLSILDWEALQFTPKAYTAKTKEDFAYLLSQLETIFKENEILNEFTPVEVALASDIYFCVLNGAPVREYPLLSAWYLKIEKQKPFVQALKLTFEKTLGQPAVTSTEKIPVSETTRNVNSQHLMRERVPGEKILPKSNERNILITSALPYVNNVPHLGNIVGSTLSADVFARYHRARNHNTLYICGTDEYGTATETKALEEGVSPKELCDKYHALHKEVYDWFEIDFDHFGRTTTPKQTGIAQHIFTKLYNNDYMAIDTMTQLYCEVHQGYLADRYVEGTCPKCGYDDARGDQCDGCGGLLNAFELIDPKCKLDRATPVKRETKHVFLSLDKLQPAVESWAMQSAVEGKWSNNGRSITESWLKEGLRPRCITRDLKWGTPVPLEEFKGKVLYVWFDATIGYISITANYTDEWEKWWRNPEQVKLYQFMGKDNVPFHTVIFPSSLLGTGEKWTMLHHINTTDYLNYETGKFSKSRGVGVFGNTAQDIGLSPSVWRYYLLSSRPETSDTMFTWKEFITRHNSELLANLGNFVNRTLKFTTAKYNGLVPHYLTDPSVGAGKLKADFVKDVNALLAKYNAALEASKLREGLRLAMEISARGNQYLQDNRIDNKCYLYERQKCADAIGYALNLIYLLAAIFYPYMPSTSTSIYKQLNAPAAAIPDTWELCLLPGHRIGEPEYLFTRIDESMEEEWRSKYGGNGSN
Protein: Kinesin-like protein KIN-14C (AtKIN14a) (Kinesin-like protein KatA) (Q07970)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Kinesin that supports microtubule movement in an ATP-dependent manner and has a minus-end directed polarity. Plays a crucial role in spindle morphogenesis in male meiosis. In mitosis, is required for normal microtubule accumulation at the spindle poles during prophase and may play a role in spindle assembly during prometaphase.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:8597656}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:8597656}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:8597656}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8597656}. Note=Colocalizes with microtubules during preprophase and cytokinesis. In M-phase, locates to the preprophase band. Present mainly in the midzone at metaphase and later during anaphase. Associated with the ends of the kinetochore fibers near the kinetochores. Detected on the phragmoplast by late cytokinesis. {ECO:0000269|PubMed:8597656}.
Interaction partners:
- Kinesin-like protein KIN-10A
- Serine/threonine-protein kinase Nek6
- Serine/threonine-protein kinase Nek5
- Microtubule-associated protein RP/EB family member 1B
- Microtubule-associated protein 70-4
- Kinesin-like protein KIN-5A
- microtubule-severing ATPase
- SUN domain-containing protein 1
- Kinesin-like protein KIN-12B
- Zinc finger protein WIP2
Sequence:
MASRNQNRPPRSPNAKKEGLGGISFDKRRKVETQGGTGRRQAFSAVNKQDVTMNSDVGSIEECGKVDFTKDEILALLSERAKAGKFDTKAKIEQMTDIIKRLKVCVKWFQQADETHVQEKENLKVSLESSEQKYNHKELEARTKEEELQATISKLEENVVSLHEKLAKEESSTQDAIECHRREKEARVAAEKVQASLGEELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNSKLQTDLETVRAALTRAEKEKSSILENLSTLRGHSKSLQDQLSSSRVLQDDAIKQKDSLLSEVTNLRNELQQVRDDRDRQVVQSQKLSEEIRKYQENVGKSSQELDILTAKSGSLEETCSLQKERLNMLEQQLAIANERQKMADASVSLTRTEFEEQKHLLCELQDRLADMEHQLCEGELLRKKLHNTILELKGNIRVFCRVRPLLPDDGGRHEATVIAYPTSTEAQGRGVDLVQSGNKHPFTFDKVFNHEASQEEVFFEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPEAPDQKGLIPRSLEQIFQASQSLGAQGWKYKMQVSMLEIYNETIRDLLSTNRTTSMDLVRADSGTSGKQYTITHDVNGHTHVSDLTIFDVCSVGKISSLLQQAAQSRSVGKTQMNEQSSRSHFVFTMRISGVNESTEQQVQGVLNLIDLAGSERLSKSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNISPDPTSAGESLCSLRFAARVNACEIGIPRRQTSTKLLDSRLSYG
Protein: Putative two-component response regulator-like APRR8 (Pseudo-response regulator 8) (O23100)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MENTEETERFSNDICVLLLDSDATCLANLSEMIRKCGYKVVATTRADDLPLIINNKDKKIDLVLAEFRLIEMNKYELLEKIRSICEIPVVVSGAHVKDAIVECLCRGAKLCLEKPLMENDFKILWQFTVSRQRNFRSQIDINPPEKNHSITHTQSLGAELKKNNNNSEVETEDLDKYKDELGQGNKRKERADTDTGEHTEKNNGSDLGDQKKPKLLFADDLQNETLEAVPNIEEANNERKAPTEIKKNGESSEKKSPELVCMEEELQKWSAESFIDLTASVENESQDPLESVGDSVGPHEIPLSPPESSNNNVAAQLQMPTHEALDEEVMQDGLSLSDLEVDLQEGHGSNKELFDKIFTDLAKELKP
Protein: Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Eukaryotic translation initiation factor 3 subunit 10) (Q9VN25)
Organism: Drosophila melanogaster (Fruit fly)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit J
Sequence:
MARYTQRPENALKRANEFIEVGKPLRALDTLQEVFRNKRWNYAYSETVIEPLMFKYLYLCVELKKSHIAKEGLFQYRNMFQLVNVNSLENVIRGYLKMAEEHTEAAQAQSSAAVAVLELDDLDNIATPESILMSAVCGEDAQDRSDRTILLPWVKFLWESYCQCLELLRVNTHCEALYHDIARMAFQFCLKYNRKSEFRRLCDKLRKHLEDICKSSNQTTGVSINKVETQQLCLDTRLYLLDSAIQMELWQEAYKAIEDIHGLMALSKKTPVPKTMANYYQKLAMVFSKAGNQLFHAAALLKLFQLTRELKKNLTKDDLQRMAAHVLLATLSIPLPSAHPEFDRFIEADKSPLEKAQKLAVLLGLPQPPTRVSLIREVVRLNVPQLVSEDFRNLYNWLEVDFNPLNLCKRIQSIVDFIENGPENALLTPYIQSLKDVTIMRLIRQISQVYESIKFQRLLQLASFCNIFELEKLLVESVRHNDMQIRIDHQKNSIYFGTDLTESQREYRPDGPALQSMPSEQIRSQLVNMSTVLTRAVSIVYPNRERDQRAKLRNQMVNHYHEIKDREHQRILQRQKIIEDRKEYIEKQNNAREEEEARRQEEESRKAKLAEQKRLEQEQEERERKRHQNEIQAIREKSLKEKVQQISQTAHGKKMLSKLDEEGIKKLDAEQIAKRESEELQREAKELQSKLKSQEKKIDYFERAKRLEEIPLFEKYLAEKQVKDKEFWEATEKTRIENAIAERKDAVAQQERLKRMYPDRDEFLEALKKERASLYVEKLKKFEAALEAERKKRLADRIIRRREERRQAFLREKEEERLRKEEEIRLAQAAEERAAAEARRLEREAEDEKRRAQYEKQRAKEEEAERKIKEDRDRLSRELASERERTEKDRDTWRPRGGDRPSASNGGSSEWRRAAPAASERNDRGGERIERGGERIERGGERLERGGERIERGGDRDRKDNEGADSSWRVRREPDSQRAAAPKDSGAPQSRDDKWRRGGERDRDFRIDGARRDRDDGPRRDRDDGPRRDRDDERGGFRRADGARRTDEPQRETGGNWRDAPRHADRETRRPAERRDRDVRETRGDQRGSAPKEAASGGVGGNWRTAPATREEKPAAKRDQAQEKENKAGDDGEWTSVKRR
Protein: Developmentally regulated GTP-binding protein, putative (Q38AS7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ZC3H15/TMA46 family C-terminal domain-containing protein
- RWD domain-containing protein
- 60S acidic ribosomal protein P0
- 40S ribosomal protein S3
- 40S ribosomal protein S3
- 60S ribosomal protein L2, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S13, putative
- Ribosomal protein S19, putative
- 40S ribosomal protein S15, putative
Sequence:
MSNLQKINDIEAEIARTQKNKATMAHLCQLKARLAQLKRELIASESKKGGAKGEGFDVQKTGDARIGFIGFPSVGKSTLLTKLTSTHSEVAAYEFTTLTCVPGVVSYRGAKLQMLDLPGIIEGAKDGKGRGRQVIAVARTCSLILIVLDIAKPLQHKLIIERELDGFGIRLNKKPPNIDIRKKDRGGISISSTCPLTHLDNETIKTILGEYRMSNADVMLRGDYTADELIDAIEGNRIYIPCIYVLNKIDQISIEELDIVSRIPHNCPISAHHSWNIDGLLECIWDHLNFIRLYTKPRGQVPDYDEPVILKKAPQPTVERFCLRLHRQMMKSFKHAWVWGASVKHQPQRVGKDHLLEDEDVVQVVKKV
Protein: Chaperone protein DNAJ, putative (Q57VQ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRTEGLRRALISDVAARWYVFQRRFLSTSTAHLVEEIRQALRVLSLSDSASDAEVRDRFQSLAKSNHPDVLQGGTEESSVAEDKMRRGVEAYKLLRRFTEAERHALLKQRVQQEEETERGRRVYEGVAGRKGEGSRATFEFNKFEQRRREMRNEAPPWKVDNHPPRNQRRSFLFYVLGGAATDARVSAAEILREYRRTGHLAGGRFRDCCAGSFGSRAPSGLFGANADEWARTRQRAERAQIVSAAFGRHIVAGVFAVTVFLLICMIFVAVKKHYAARGLYTNSESFSKRELR
Protein: Hydrogenase expression/formation protein, putative (Q72AS2)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Periplasmic [NiFe] hydrogenase large subunit
- cytochrome-c3 hydrogenase
- Periplasmic [NiFe] hydrogenase large subunit
- Periplasmic [NiFe] hydrogenase large subunit
- Periplasmic [NiFe] hydrogenase small subunit 2
- Periplasmic [NiFe] hydrogenase small subunit 1
- Pyridine nucleotide-disulfide oxidoreductase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Carbamoyltransferase
- Hydrogenase assembly chaperone hypC/hupF
Sequence:
MKKLLVLGIGNMLLTDDGVGVFAAQELMKETWPDNVNIMEAGTFTQDIFYLFEGYDALLVLDIIHTGAEPGTIYRLSEEDLVQKESQRLSIHDIDLIDSLRMAEMLGGKKPTMHVLGMEPFDYTTWNIGLSAPLSERYPAFLQLAREEIQAILASF