wanglab/gogpt-training-data huggingface dataset:
Protein: Early endosome antigen (F4ISU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT3g52230/F4F15_340
- 26S proteasome regulatory particle chain RPT6-like protein
- Expressed protein
- At1g68680
- Protein KINASE OF THE OUTER CHLOROPLAST MEMBRANE 1
- At3g49350
- At4g16450
- V-type proton ATPase subunit c3
- Tetratricopeptide repeat
- WPP domain-containing protein 1
Sequence:
MEEATQVTSSEVPVVKGDVDDLKTADISVKAVNGEVPKEEKEEEDGEFIKVEKEAFDAKDDAEKADHVPVEEQKEVIERSSSGSQRELHESQEKAKELELELERVAGELKRYESENTHLKDELLSAKEKLEETEKKHGDLEVVQKKQQEKIVEGEERHSSQLKSLEDALQSHDAKDKELTEVKEAFDALGIELESSRKKLIELEEGLKRSAEEAQKFEELHKQSASHADSESQKALEFSELLKSTKESAKEMEEKMASLQQEIKELNEKMSENEKVEAALKSSAGELAAVQEELALSKSRLLETEQKVSSTEALIDELTQELEQKKASESRFKEELSVLQDLDAQTKGLQAKLSEQEGINSKLAEELKEKELLESLSKDQEEKLRTANEKLAEVLKEKEALEANVAEVTSNVATVTEVCNELEEKLKTSDENFSKTDALLSQALSNNSELEQKLKSLEELHSEAGSAAAAATQKNLELEDVVRSSSQAAEEAKSQIKELETKFTAAEQKNAELEQQLNLLQLKSSDAERELKELSEKSSELQTAIEVAEEEKKQATTQMQEYKQKASELELSLTQSSARNSELEEDLRIALQKGAEHEDRANTTHQRSIELEGLCQSSQSKHEDAEGRLKDLELLLQTEKYRIQELEEQVSSLEKKHGETEADSKGYLGQVAELQSTLEAFQVKSSSLEAALNIATENEKELTENLNAVTSEKKKLEATVDEYSVKISESENLLESIRNELNVTQGKLESIENDLKAAGLQESEVMEKLKSAEESLEQKGREIDEATTKRMELEALHQSLSIDSEHRLQKAMEEFTSRDSEASSLTEKLRDLEGKIKSYEEQLAEASGKSSSLKEKLEQTLGRLAAAESVNEKLKQEFDQAQEKSLQSSSESELLAETNNQLKIKIQELEGLIGSGSVEKETALKRLEEAIERFNQKETESSDLVEKLKTHENQIEEYKKLAHEASGVADTRKVELEDALSKLKNLESTIEELGAKCQGLEKESGDLAEVNLKLNLELANHGSEANELQTKLSALEAEKEQTANELEASKTTIEDLTKQLTSEGEKLQSQISSHTEENNQVNAMFQSTKEELQSVIAKLEEQLTVESSKADTLVSEIEKLRAVAAEKSVLESHFEELEKTLSEVKAQLKENVENAATASVKVAELTSKLQEHEHIAGERDVLNEQVLQLQKELQAAQSSIDEQKQAHSQKQSELESALKKSQEEIEAKKKAVTEFESMVKDLEQKVQLADAKTKETEAMDVGVKSRDIDLSFSSPTKRKSKKKPEASLSSSSSSGNVTTPTQTASTSHLMTVKIVTGVALISVIIGIILGRKY
Protein: 26S proteasome regulatory subunit 6B homolog (26S protease subunit 6B homolog) (26S proteasome AAA-ATPase subunit RPT3) (Protein BMAA insensitive morphology 409) (Regulatory particle triple-A ATPase subunit 3) (Q9SEI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-1
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- Proteasome subunit beta type-2-B
- Proteasome subunit alpha type-5-A
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit RPN13
- 26S proteasome non-ATPase regulatory subunit 3 homolog A
Sequence:
MASAAVASMVLDPKASPALMDLSTADEEDLYGRLKSLERQLEFTDIQEEYVKDEQKNLKRELLRAQEEVKRIQSVPLVIGQFMEMVDQNNGIVGSTTGSNYYVRILSTINRELLKPSASVALHRHSNALVDVLPPEADSSISLLSQSEKPDVSYNDIGGCDIQKQEIREAVELPLTHHELYKQIGIDPPRGVLLYGPPGTGKTMLAKAVANHTTAAFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEVDAIATARFDAQTGADREVQRILMELLNQMDGFDQTVNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFQVCTSKMNLSDEVDLEDYVSRPDKISAAEIAAICQEAGMHAVRKNRYVILPKDFEKGYRANVKKPDTDFEFYK
Protein: RNA-binding protein, putative (Q586R7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RanBP2-type domain-containing protein
- Splicing factor TSR1
Sequence:
MQQYTLRVAGLADGTADDAVREFFTRFGEVTECSVAGTEATVSYKNQDDYAEALRMDGCEFDVGVTLKVEAVEKTTEDVPQADGAGAGSAEDAAGEVSNGANRDGLSDTGNTEESNKQKRFRDDYKVAVRHLPDDATEQQLRNMFQSAGTILDFFLEPRRRYAFVGFDSREAVEAALKMTGTELNGTIINVELKRTVSRESQLEMKVVVKNLPPDVTENSIRNFFAAVGEPVDIFIHERKMFAFVGFADESACAAAIQMDGTEMDGHRVQIERRQRQRCFKCNKEGHVATQCRGEPTCRTCGRPGHMARDCRMQPGSYDRNRGGNMGAMGRMGHAPPGGYYMGPMGGDRRGDVGRRPPYNDRRVGGEYDRRRPRSRSRSPSYERRHRRRSRSRSRSRTRSRSPKRFTRERERGRDRSRSPSRRRYPREGERPRVRDDRVRD
Protein: Stage 0 sporulation protein A homolog (Q46215)
Organism: Clostridium perfringens
Interaction partners:
Sequence:
MIKLHKKYKLKRRLLDMFSIALCEDNSLQREELKNNLSKVLDEIGVEYKLLTFETGEDLLREYPENLDMLFLDIQMGELTGMETARKVRKYDDKVEIIFITALWDYIQKGYEVRAFRYLIKPVKFKELQEQVTACVENILHKRYTYITIKDKNNVLKIRTEDILFLETFERKVIIHTNSQDYIVKMSMNKLEKELNNKGFFRCHTSYIVNLIKIEEIKKDYLLINKFTLPVSKHRMKNLKLRLTSLLGDLIC
Protein: MYB proto-oncogene, transcription factor (A0A8I5ZUL7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MCVHSYFCSIYSSDEDDEDIEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEDEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQEPSKASQTPVVSSFQKNNHLMGFAHASPPPTSQSSVNGEYPYYHIAEAQNISSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQALPTQNHTCSYPGWHSTSIVDQTRPHGDSAPVSCLGENHATPSLPADPGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHENSGLDTPTLPSTPLIGHKLTPCHRDQTVKTQKENSIFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKMLPQTPSHVVEDLQDVIKQESDESGIVAEFHENGPPLLKKIKQEVDSPTEKAGNFFCSNHWEETNLSTQLFAQASPVADAPNILTSSVLMTPVSEDEDNVLKAFTVPKNRPLVGPLQPCVGAWEPTPSCGKTEDQMTASGQARKYVNTFSARTLVM
Protein: Tubulin glycylase 3B (EC 6.3.2.-) (P0CAZ0)
Organism: Tetrahymena thermophila (strain SB210)
Function: Polyglycylase which modifies tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of tubulin. Polyglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:19531357}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19531357}. Note=Mainly present in oral cilia.
Interaction partners:
Sequence:
MFSIDIQGKSMSLCDPTSKIKQMQQQQQQLQQGTNNGIQKDQQLPNMIINGNSNSYLNNGSNLQQQAVIQQSNHKQSQIKYNSPLSHQQHHQFKIGHQNKLEYLRQQQAQKYNQIYQLDPQLQQQNQMFQQHQYMQNVQMQQQLLYQGNQEVFPPFNQIANGSAQNSILLQQYLSNNKGQTNNSNRENGGNFHSEQSPKSAAGSVVSGNGSNTQFAANILRNSNIIQQQNEFRFQQIQQTHQLLHSLVQQQPQPLSQQHSNQSSQSSNPQSQSPLPLSISSQQPVISMANYFNQPSQQSNSLFNGQQPTMFNSSENFQQKNILYSCVGNPNNPYNHHINNPYLQEKRYYKSSKLPKIKKENKPQQAFSDIRPSSREKSARFHLAASINTILNQNGSTSVNTQNNENMVQTLKGHSYSAVTEKSNIGQQEVNIPTTSKTQTLIKEHSLTNINSASKENNQVTLASNSNQTSKKAYENLMSAENDEEDKLKCIRYFRYNLGQLLHILGKKEIYFSNLNSKKPIKTFASITQQLGQKHMNLLSKNTINIINKVKKIVATKGKYKYRERFNFLHSAQLKSINYDVRKRLNQIQDKKVLSNTKSKDEEESSDDDETPVKSKSNNQNAVQQTDLAKWKKYNRLDPKTKVFIIKGGYGDLRKALQERGWVENPDYFSPCFDLKWTCKVQDIDYDNLQENQVVNHFDNNQTFTSKYGLARNLRTLIHSENIDVYKFFPRCFDLGDLQEFEDFIENFKVAKAESLVHRFKDMLKNGIESIDDKLELKIRLCNEVASRKFIDFYETVDFIFNYDVLPCVSPEEWEIISKDEFQLDNKKIEFYLERLRSHPTFKHLYYSNSQSQKQHMNKRKNSHRISVNHNHNDPIEEESAQSSTSLKQDSLQRFSSKSQELLDLCNQTLKKSSEKDPQHHLNGYRNIWIVKPNFLSRGRGIKCFNSLDKIMDYVVGKETQFVVQKYIENPLLINNKKFDMRQWAIVQDFCPPRIWFFEECYIRLCSVEHNIDDLNNRFVHLTNNIVQKYNKDAYADKDDLMMSQEQFAQYLKETEGRDVFYEEIQPKLKQMVIQSLKSCQDQVGARKNSMEFIGYDFMIDSNYQPWLIEINSSPSMEYSTSITEELVQRVLQDTTKVIVDYSMAKKGTKKNVDTGGFKLIYKGEKQTKNNKVLASYKK
Protein: SPTBN2 protein (Spectrin beta chain, non-erythrocytic 2) (A4QPE4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSTLSPTDFDSLEIQGQYSDINNRWDLPDSDWDNDSSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRVGDLYSDLRDGRNLLRLLEVLSGEILPKPTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLVWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLLDFESLKKCNAHYNLQNAFNLAEKELGLTKLLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGKRIGKVLDHAMEAERLVEKYESLASELLQWIEQTIVTLNDRQLANSLSGVQNQLQSFNSYRTVEKPPKFTEKGNLEVLLFTIQSKLRANNQKVYTPREGRLISDINKAWERLEKAEHERELALRTELIRQEKLEQLAARFDRKAAMRETWLSENQRLVSQDNFGLELAAVEAAVRKHEAIETDIVAYSGRVQAVDAVAAELAAERYHDIKRIAARQHNVARLWDFLRQMVAARRERLLLNLELQKVFQDLLYLMDWMEEMKGRLQSQDLGRHLAGVEDLLQLHELVEADIAVQAERVRAVSASALRFCNPGKEYRPCDPQLVSERVAKLTALEEREKERKRKREEEERRKQPPAPEPTASVPPGDLVGGQTASDTTWDGTQPRPPPSTQAPSVNGVCTDGEPSQPLLGQQRLEHSSFPEGPGPGSGDEANGPRGERQTRTRGPAPSAMPQSRSTESAHAATLPPRGPEPSAQEQMEGMLCRKQEMEAFGKKAANRSWQNVYCVLRRGSLGFYKDAKAASAGVPYHGEVPVSLARAQGSVAFDYRKRKHVFKLGLQDGKEYLFQAKDEAEMSSWLRVVNAAIATASSASGEPEEPVVPSTTRGMTRAMTMPPVSPVGAEGPVVLRSKDGREREREKRFSFFKKNK
Protein: Nuclease EXOG, mitochondrial (EC 3.1.30.-) (Endonuclease G-like 1) (Endo G-like 1) (Q8C163)
Organism: Mus musculus (Mouse)
Function: Endo/exonuclease with nicking activity towards supercoiled DNA, a preference for single-stranded DNA and 5'-3' exonuclease activity.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- Zinc phosphodiesterase ELAC protein 2
- DNA polymerase subunit gamma-1
- Flap endonuclease 1
Sequence:
MAAKSFASRLRDSRRFLNGFLAGAVVGAAGAGLTALQFFRRPDAESAKLARQPHESAEEAVLEQFGFPLAGTETRRYTNHALSYDQAKRVPRWVLEHISKDKIIGDADRKHCKFKPDPSVPSAFSALNEDYIGSGWSRGHMAPAGNNKFSSEAMAETFYLSNIVPQNFDNNSGYWNRIEMYCRELTERFEDVWIVSGPLTLPHTRNDGTKTVSYQVIGEDNVAVPSHLYKVILARRSPESTEPLALGAFVVPNKAIGFQSQLSEFQVSLHDLEKMSGLVFFPRLDRSRDIRNICSVDTCKLLGFQEFTLYLSTRKIDGARSVARLEKVLEALKSSGVEPDDYFLSRYEKKLEELKAKEQKDAQLEKQS
Protein: DnaJ homolog subfamily A member 3, mitochondrial (DnaJ protein Tid-1) (mTid-1) (Tumorous imaginal discs protein Tid56 homolog) (Q99M87)
Organism: Mus musculus (Mouse)
Function: Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity (By similarity). Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway.
Subcellular location: Mitochondrion matrix {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:19038220}. Postsynaptic cell membrane {ECO:0000269|PubMed:19038220}; Peripheral membrane protein {ECO:0000269|PubMed:19038220}. Note=Recruited to the postsynaptic cell membrane of the neuromuscular junction through interaction with MUSK.
Interaction partners:
- Stress-70 protein, mitochondrial
- Heat shock 70 kDa protein 1B
- Mitochondrial disaggregase
- 60 kDa heat shock protein, mitochondrial
- Endoplasmic reticulum chaperone BiP
- Heat shock cognate 71 kDa protein
- GrpE protein homolog 2, mitochondrial
- Heat shock 70 kDa protein 1A
- Lon protease homolog, mitochondrial
- GrpE protein homolog 1, mitochondrial
Sequence:
MAAWCSPRWLRVAVGTPRLPAAAGRGVQQPQGGVVATSLCRKLCVSAFGLSMGAHGPRALLTLRPGVRLTGTKSFPFVCTTSFHTSASLAKDDYYQILGVPRNASQKDIKKAYYQLAKKYHPDTNKDDPKAKEKFSQLAEAYEVLSDEVKRKQYDAYGSAGFDPGTSSSGQGYWRGGPSVDPEELFRKIFGEFSSSPFGDFQNVFDQPQEYIMELTFNQAAKGVNKEFTVNIMDTCERCDGKGNEPGTKVQHCHYCGGSGMETINTGPFVMRSTCRRCGGRGSIITNPCVVCRGAGQAKQKKRVTIPVPAGVEDGQTVRMPVGKREIFVTFRVQKSPVFRRDGADIHSDLFISIAQAILGGTAKAQGLYETINVTIPAGIQTDQKIRLTGKGIPRINSYGYGDHYIHIKIRVPKRLSSRQQNLILSYAEDETDVEGTVNGVTHTSTGGRTMDSSAGSKDRREAGEDNEGFLSKLKKIFTS
Protein: Rho guanine nucleotide exchange factor 28 (190 kDa guanine nucleotide exchange factor) (p190-RhoGEF) (p190RhoGEF) (Rho guanine nucleotide exchange factor) (Q8N1W1)
Organism: Homo sapiens (Human)
Function: Functions as a RHOA-specific guanine nucleotide exchange factor regulating signaling pathways downstream of integrins and growth factor receptors. Functions in axonal branching, synapse formation and dendritic morphogenesis. Functions also in focal adhesion formation, cell motility and B-lymphocytes activation. May regulate NEFL expression and aggregation and play a role in apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with the microtubule radial and cortical systems. {ECO:0000250}.
Interaction partners:
- Transforming protein RhoA
- Rho guanine nucleotide exchange factor 12
- Protein-tyrosine kinase 2-beta
- Rho guanine nucleotide exchange factor 1
- Focal adhesion kinase 1
- Guanine nucleotide-binding protein G
- Rho-related GTP-binding protein RhoC
- Neurofilament medium polypeptide
- Rho-related GTP-binding protein RhoB
- Neurofilament light polypeptide
Sequence:
MELSCSEAPLYGQMMIYAKFDKNVYLPEDAEFYFTYDGSHQRHVMIAERIEDNVLQSSVPGHGLQETVTVSVCLCSEGYSPVTMGSGSVTYVDNMACRLARLLVTQANRLTACSHQTLLTPFALTAGALPALDEELVLALTHLELPLEWTVLGSSSLEVSSHRESLLHLAMRWGLAKLSQFFLCLPGGVQALALPNEEGATPLDLALREGHSKLVEDVTNFQGRWSPSFSRVQLSEEASLHYIHSSETLTLTLNHTAEHLLEADIKLFRKYFWDRAFLVKAFEPEARPEERTAMPSSGAETEEEIKNSVSSRSAAEKEDIKRVKSLVVQHNEHEDQHSLDLDRSFDILKKSKPPSTLLAAGRLSDMLNGGDEVYANCMVIDQVGDLDISYINIEGITATTSPESRGCTLWPQSSKHTLPTETSPSVYPLSENVEGTAHTEAQQSFMSPSSSCASNLNLSFGWHGFEKEQSHLKKRSSSLDALDADSEGEGHSEPSHICYTPGSQSSSRTGIPSGDELDSFETNTEPDFNISRAESLPLSSNLQSKESLLSGVRSRSYSCSSPKISLGKTRLVRELTVCSSSEEQRAYSLSEPPRENRIQEEEWDKYIIPAKSESEKYKVSRTFSFLMNRMTSPRNKSKTKSKDAKDKEKLNRHQFAPGTFSGVLQCLVCDKTLLGKESLQCSNCNANVHKGCKDAAPACTKKFQEKYNKNKPQTILGNSSFRDIPQPGLSLHPSSSVPVGLPTGRRETVGQVHPLSRSVPGTTLESFRRSATSLESESDHNSCRSRSHSDELLQSMGSSPSTESFIMEDVVDSSLWSDLSSDAQEFEAESWSLVVDPSFCNRQEKDVIKRQDVIFELMQTEMHHIQTLFIMSEIFRKGMKEELQLDHSTVDKIFPCLDELLEIHRHFFYSMKERRQESCAGSDRNFVIDRIGDILVQQFSEENASKMKKIYGEFCCHHKEAVNLFKELQQNKKFQNFIKLRNSNLLARRRGIPECILLVTQRITKYPVLVERILQYTKERTEEHKDLRKALCLIKDMIATVDLKVNEYEKNQKWLEILNKIENKTYTKLKNGHVFRKQALMSEERTLLYDGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPSVISLQKLIAREVANEERGMFLISASSAGPEMYEIHTNSKEERNNWMRRIQQAVESCPEEKGGRTSESDEDKRKAEARVAKIQQCQEILTNQDQQICAYLEEKLHIYAELGELSGFEDVHLEPHLLIKPDPGEPPQAASLLAAALKEAESLQVAVKASQMGAVSQSCEDSCGDSVLADTLSSHDVPGSPTASLVTGGREGRGCSDVDPGIQGVVTDLAVSDAGEKVECRNFPGSSQSEIIQAIQNLTRLLYSLQAALTIQDSHIEIHRLVLQQQEGLSLGHSILRGGPLQDQKSRDADRQHEELANVHQLQHQLQQEQRRWLRRCEQQQRAQATRESWLQERERECQSQEELLLRSRGELDLQLQEYQHSLERLREGQRLVEREQARMRAQQSLLGHWKHGRQRSLPAVLLPGGPEVMELNRSESLCHENSFFINEALVQMSFNTFNKLNPSVIHQDATYPTTQSHSDLVRTSEHQVDLKVDPSQPSNVSHKLWTAAGSGHQILPFHESSKDSCKNDLDTSHTESPTPHDSNSHRPQLQAFITEAKLNLPTRTMTRQDGETGDGAKENIVYL
Protein: Probable serine/threonine-protein kinase At1g01540 (EC 2.7.11.1) (Q3EDL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein kinase superfamily protein
- Pyruvate, phosphate dikinase regulatory protein 1, chloroplastic
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase UCN
- Uncharacterized aarF domain-containing protein kinase At1g71810, chloroplastic
- AT3g24190/MUJ8_17
- Uncharacterized aarF domain-containing protein kinase At5g05200, chloroplastic
- Serine/threonine-protein kinase STN8, chloroplastic
- Protein KINASE OF THE OUTER CHLOROPLAST MEMBRANE 1
Sequence:
MSVYDAAFLNTELSKPTSIFGLRLWVVIGILLGSLIVIALFLLSLCLTSRRKNRKPRADFASAAIATPPISKEIKEIVPAQNQSVPAEIQVDIGKIEHRVVFSDRVSSGESRGTASASETASYSGSGNCGPEVSHLGWGRWYTLRELEAATNGLCEENVIGEGGYGIVYRGILTDGTKVAVKNLLNNRGQAEKEFKVEVEVIGRVRHKNLVRLLGYCVEGAYRMLVYDFVDNGNLEQWIHGDVGDVSPLTWDIRMNIILGMAKGLAYLHEGLEPKVVHRDIKSSNILLDRQWNAKVSDFGLAKLLGSESSYVTTRVMGTFGYVAPEYACTGMLNEKSDIYSFGILIMEIITGRNPVDYSRPQGETNLVDWLKSMVGNRRSEEVVDPKIPEPPSSKALKRVLLVALRCVDPDANKRPKMGHIIHMLEAEDLLYRDERRTTRDHGSRERQETAVVAAGSESGESGSRHHQQKQR
Protein: Flagellar protein FlgN (Q0P8F0)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Interaction partners:
- Flagellar hook-associated protein 1
- Uncharacterized protein
- TIGR02757 family protein
- Probable membrane transporter protein
Sequence:
MLKQRLDEVNAILAKLIALTEEDIENIKVAKHESVTPSVEEKNKLIAEFITAKKQLDVALVELNNSSTKGLSELLDDEDKQKLDLLKKNLQNLHSKNKEYAKFVLIVKDFLDGLVNKMFDINDGTNNAYGDKKTNPESIFKINV
Protein: Envelope glycoprotein UL130 (F5HCP3)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Plays a role in viral entry into host cells. Forms a pentameric complex at the surface of the viral envelope together with gH, gL, UL130 and UL131. This complex is required for entry in epithelial, endothelial and myeloid host cells. Mechanistically, engages host receptor(s) including neurophilin 2/NRP2 to mediate infection.
Subcellular location: Virion membrane {ECO:0000269|PubMed:23804643}. Note=Found as a pentameric complex at the surface of virion envelope. {ECO:0000269|PubMed:23804643}.
Interaction partners:
Sequence:
MLRLLLRHHFHCLLLCAVWATPCLASPWSTLTANQNPSPPWSKLTYSKPHDAATFYCPFLYPSPPRSPLQFSGFQRVSTGPECRNETLYLLYNREGQTLVERSSTWVKKVIWYLSGRNQTILQRMPRTASKPSDGNVQISVEDAKIFGAHMVPKQTKLLRFVVNDGTRYQMCVMKLESWAHVFRDYSVSFQVRLTFTEANNQTYTFCTHPNLIV
Protein: Uncharacterized protein C23H4.05c (O13948)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uba3-binding protein but1
- Uncharacterized but2-like protein C27D7.09c
- Uncharacterized RNA-binding protein C365.04c
- Uncharacterized protein C1604.06c
Sequence:
MLLHGLGRMNIIFICFPSLACLLTSRTPLCAPLFSHLDGMTPCPIDCGFAVGRSRGGGFGGKPESNSLHYDTMHKQHAMPFFIINPTEWKRNFCNTG
Protein: NF-kappa-B inhibitor-interacting Ras-like protein 2 (I-kappa-B-interacting Ras-like protein 2) (Kappa B-Ras protein 2) (KappaB-Ras2) (Q9CR56)
Organism: Mus musculus (Mouse)
Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- NF-kappa-B inhibitor alpha
Sequence:
MGKSCKVVVCGQASVGKTSILEQLLYGNHVVGSEMIETQEDIYVGSIETDRGVREQVRFYDTRGLRDGAELPKHCFSCTDGYVLVYSTDSRESFQRVELLKKEIDKSKDKKEVTIVVLGNKCDLQEQRRVDPDVAQHWAKSEKVKLWEVSVADRRSLLEPFIYLASKMTQPQSKSAFPLSRKNKGSGSLDG
Protein: DNA topoisomerase 3 (EC 5.6.2.1) (DNA topoisomerase III) (O61660)
Organism: Caenorhabditis elegans
Function: Component of the BTR double Holliday Junction dissolution complex, which is involved in homologous recombination during meiotic double strand break in the germline (Probable). Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:34252074}. Note=Localizes to nuclear foci throughout pachynema in meiotic prophase I during meiotic recombination (PubMed:34252074). Localization at nuclear foci is dependent on rmif-2 (PubMed:34252074). {ECO:0000269|PubMed:34252074}.
Interaction partners:
- RecQ-like DNA helicase blm-1
- RecQ-mediated genome instability protein 1
- Crossover junction endonuclease MUS81
- DNA repair endonuclease XPF
- RecQ-mediated genome instability protein 1 homolog
- Probable replication factor A 73 kDa subunit
- Exonuclease 1
- RPA_C domain-containing protein
- Replication protein A C-terminal domain-containing protein
- DNA replication ATP-dependent helicase/nuclease DNA2
Sequence:
MKRALFVAEKNDVAKGVAAILSNGTANRREGRSKFNKIYTLNTELFGQQTAISVTSVSGHMMNFQFHENMSNWQTASMVELFRAPVRHVVTPEMKLIEQTLREQAQRHDILVVWTDCDREGEAIGAEIVKVCRDSNRRLDIFRARFSEITKAAITRAARNLIRLDEKTVAAVDCRSELDLRIGSAFTRLQTLHLRNRFRDLLGQNDTSQVISYGSCQFPTLGFVTDRYKMIENFVSEPFWKLIVEHTRESHKVEFLWDRNRLFDRDTVDILHDECKETKEAHVEKVAKKPKSKWRPQALDTVELEKLGISKLRMSAKQTMQVAEKLYSKGFISYPRTETNKFPAGLNLTPLVQQQTQSNIWGDFANEVLQNGVNPRNGRKSDEAHPPIHPLKFTEKHQLQGDDWKVYELVVRHFLACVSQDAQGEETMVNLTVGTEKFHASGLRIRDMGYLKVYVYEKWGNRLLPTYTEGERFTDFELKIGDGKTQAPDFLTEADLISLMDKYGIGTDATHAEHIEKIKTREYIGVRPDGKLIPSFLGLALVDGYDDMGFAMSKPDLRANLEIGLKEICDGRRQKQEVLDEQIGKYRAIFVESERKIGVLSQSLQRYLDKNNQAGGGPGGPGGGGGPPRGPGGGGGGGPTGPPAPPKPPAKPRGRPPRKSISPAVKNGHDDPENDTIVTLSEVFGSMSNPKPARKPRAPRKSAAPKEQEEEEEVFCQCPEPMRAVTKVVQKEGPNKGKKFYTCSLPYTSSEKCNFFKWA
Protein: Cystathionine beta-synthase (EC 4.2.1.22) (Beta-thionase) (Serine sulfhydrase) (P35520)
Organism: Homo sapiens (Human)
Function: Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17087506, ECO:0000269|PubMed:23981774}. Nucleus {ECO:0000269|PubMed:17087506}.
Interaction partners:
Sequence:
MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLNFVAAQERDQK
Protein: Asparaginyl-tRNA synthetase (AsnRS) (NARS2) (EC 6.1.1.22) (Asparagine--tRNA ligase, mitochondrial) (Q8BGV0)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q96I59}. Mitochondrion {ECO:0000250|UniProtKB:Q96I59}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Glutamyl-tRNA
- Glutamyl-tRNA
- Tyrosine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Probable proline--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial
- Lysine--tRNA ligase
- Asparagine--tRNA ligase, cytoplasmic
Sequence:
MLGARRLLGALRLCSSVSCPRPRASAKMRVRDALRVQDARGECVTVQGWIRSVRSQKEVLFLHVNDGSSLESLQIVADSSFDSRELTFGSSVQVQGQLVKSQSKRQNVELKAEKIEVIGDCEAKAFPIKYKERHPLEYLRQYPHLRCRTNALGSILRVRSEATAAIHSYFKDNGFVHIHTPVLTSNDCEGAGELFQVEPSSKIKGPKESFFDVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMVEAEISFVESLQDLMQVMEELFKATTEMVLSHCPEDVELCHQFIAAGQKGRLEHMLKNNFLIISYTEAIEILKQASQNFAFTPKWGVDLQTEHEKYLVRHCGNIPVFVINYPSELKPFYMRENEDGPQNTVAAVDLLVPGVGELFGGSLREERYHVLEQRLARSGLTKAYQWYLDLRKFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFTHSCLL
Protein: 14-3-3-like protein GF14 psi (General regulatory factor 3) (Protein RARE COLD INDUCIBLE 1A) (P42644)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. Involved in the regulation of nutrient metabolism. Reciprocal negative transcription regulation of miR396. Negative regulator of constitutive freezing tolerance and cold acclimation by controlling cold-induced gene expression partially through an ethylene (ET)-dependent pathway; prevents ethylene (ET) biosynthesis, probably by binding 1-aminocyclopropane-1-carboxylate synthases (ACS) to reduce their stability, thus contributing to establish adequate ET levels under both standard and low-temperature conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25122152}. Nucleus {ECO:0000269|PubMed:25122152}. Note=Translocates from the cytosol to the nucleus when phosphorylated. {ECO:0000250|UniProtKB:P48349}.
Interaction partners:
- Protein BYPASS1-LIKE
- Pentatricopeptide repeat-containing protein At1g62910
- Growth-regulating factor 7
- Dual specificity phosphatase Cdc25
- Aspartate aminotransferase, mitochondrial
- Malate dehydrogenase 1, cytoplasmic
Sequence:
MSTREENVYMAKLAEQAERYEEMVEFMEKVAKTVDVEELSVEERNLLSVAYKNVIGARRASWRIISSIEQKEESKGNEDHVAIIKDYRGKIESELSKICDGILNVLEAHLIPSASPAESKVFYLKMKGDYHRYLAEFKAGAERKEAAESTLVAYKSASDIATAELAPTHPIRLGLALNFSVFYYEILNSPDRACSLAKQAFDDAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMTDEAGDEIKEASKPDGAE