wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription termination factor 1b, mitochondrial (Mitochondrial transcription termination factor 1b) (mTERF1b) (B9EJ57)
Organism: Mus musculus (Mouse)
Function: Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene; this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending and partial unwinding. Promotes base flipping. Transcription termination activity appears to be polarized with highest specificity for transcripts initiated on the light strand.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q99551}.
Interaction partners:
- Transcription termination factor 3, mitochondrial
- DNA-directed RNA polymerase, mitochondrial
- Dimethyladenosine transferase 2, mitochondrial
- Transcription termination factor 4, mitochondrial
Sequence:
MASRNIWCVRRNFLFDLRGWMLQYSAEVFLKSISFRTFSVECDSKDKESLEEEREDLLSNLVTMGVDIDMARRRQPGVFNKAVTNEQELKIFLLSKGASDKVIGSIISRYPRAITRTPESLSKRWDLWRKIMASDLEIVNILERSPESFFRSNNNLNLENNIKFLCSVGLTHKCLCRLLTNAPRTFSNSLNLNKQMVEFLQETGMSLGHNDPRDFVRKIISKNPSILIQSTKRVKTNIEFLQSTFNLNKQDLLLLICGPGARILDLSNDCTKKNYTNIRERLLSLGCSEEEVQRFVLSYLNMVFLSEKKFNDKIDCLIEEKISASQIIENPRILDSSINTLKTRIRELSHAGYDLSTSSIALLSWSQRRYEAKLKRLCG
Protein: Ubiquitin-conjugating enzyme E2 W (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme W) (N-terminal E2 ubiquitin-conjugating enzyme) (EC 2.3.2.25) (N-terminus-conjugating E2) (Ubiquitin carrier protein W) (Ubiquitin-protein ligase W) (Q8VDW4)
Organism: Mus musculus (Mouse)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:21229326}. Note=In the nucleus, colocalizes with FANCL.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 variant 2
- E3 ubiquitin-protein ligase FANCL
- Ubiquitin-conjugating enzyme E2 variant 1
- Ubiquitin-conjugating enzyme E2 J2
- Ubiquitin-conjugating enzyme E2 H
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin-conjugating enzyme E2 J1
- Ubiquitin-like modifier-activating enzyme 1
- Predicted gene 20431
- Ataxin-3
Sequence:
MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPIHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC
Protein: Bicarbonate transporter-like transmembrane domain-containing protein (Q55BP1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLVEKKNIQHSPINWKLDTRSKLDLEQSKDCLYFFEQESNEQQQQSLVDIVYFLYDNVINDFIKNKNKNQINNRDIFKTNIFNNDNKNSLKEYIKIEKYLILWCSLDNIKENAYCFYRLNNNNNNNENNNNNNKNNLEYLILIVGPTQIQQSKSSEEIAKSFSSAISYPSVQYQLHQARNKQEVIESFVTFLNNIENDNENQFERKLIPPIKNNNNYKEQNNESLKPLESVSNGLDHENYDNDDDDDDINDDTNINNKENSKLNFKYLINDIKYRYDFEIYKSDWKDGLKDWKSFQKTLSTTVFLFFAILLPSIAFGVLNYSNTEGLLGVSKTIIAQGIGGMIFALLSGQPMVILLSTAPLAIFIKITYSISIENGLDFYSLYSMIGLFNGFFLIIYSISGASRLMKYSSRFIEETFAIFITIAFLYDGIKPIVVLFIDNLYSCDNNCQLTNQTPVFTLLISLCTLWICFKLSNFNQTKYFNGVFRNLISDYALFLGVLISSAIRWTVFLPLEDEHFSHGLDDLLNTEIKMLPVWAYFLALALGFLLSLLYFVDQNISCSLATTPSHNLKKWSGVHLDLLIVAFINIVLSFLGLPWLHGALPHSSLHVRALATIESFTDTSTGETKEIFISVQETRASGFFSHLLIFICIFLVSNILIYIPIPVLYGVFFFLGVKATVGNQFWYRILLLITDNTFLPNSNMIRYCTKLEIHKFTTFQIICLLIFCFISFYPNPYLTIFFPLFLTILIPIKNYLLPIYFKKIIINILDN
Protein: NTF2-related export protein 2 (Protein p15-2) (Q9NPJ8)
Organism: Homo sapiens (Human)
Function: Regulator of protein export for NES-containing proteins. Also plays a role in mRNA nuclear export.
Subcellular location: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.
Interaction partners:
- Nuclear RNA export factor 3
- Nuclear RNA export factor 1
- Nuclear RNA export factor 2
- Nuclear RNA export factor 5
- Nuclear transport factor 2
- NTF2-related export protein 1
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup214
- Nuclear protein AMMECR1
- Potassium voltage-gated channel subfamily E regulatory beta subunit 5
Sequence:
MATSLDFKTYVDQACRAAEEFVNIYYETMDKRRRALTRLYLDKATLIWNGNAVSGLDALNNFFDTLPSSEFQVNMLDCQPVHEQATQSQTTVLVVTSGTVKFDGNKQHFFNQNFLLTAQSTPNNTVWKIASDCFRFQDWSSS
Protein: Altered inheritance of mitochondria protein 11 (Genetic interactor of prohibitins 8) (P87275)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- mRNA-binding protein PUF3
- Altered inheritance of mitochondria protein 18, mitochondrial
- Glutaredoxin-like protein YDR286C
Sequence:
MIEEKKELKKRRVLQMARFYGAAAFTLITMRLISRAIKVRKYVPSIFQQNYKLPPFSQRNEAMSALTYASAASIGTFSTLIFGFCWALDISTAREFVFKTREFMSLPQALETDTSMDEETSKLTKQLQDLLSSENNK
Protein: Cell wall integrity transcriptional regulator CAS5 (Caspofungin sensitivity protein 5) (Q5AMH6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor involved in the cell wall damage response. Acts with ADA2 to promote cell wall integrity. Required for expression of numerous cell wall biosynthesis inhibitor caspofungin-responsive genes. Plays a key role in adherence, hyphal development, and virulence.
Subcellular location: Nucleus {ECO:0000269|PubMed:28894103}. Cytoplasm {ECO:0000269|PubMed:28894103}. Note=Localizes to the cytoplasm under basal conditions and translocates to the nucleus under cell wall stress. {ECO:0000269|PubMed:28894103}.
Interaction partners:
Sequence:
MENYLLSSPTQLSQPYDDGTNSLLFMDNYELSQNLSQPLDQHLQSLQQQSQVQSQAPQQVQSLNQHQQLPQIQPFPTLVNNQQYAQETFQQLSQQHQQQQQQQQQFSPFQQSQLQQQFQYQYSQQQQQQHFQQPVTIEEEIVPASNNTNIQISKFFDDNKGDDEDIANSGNFNEFDHSRNISLDDTTITDLHRRENSINPPTGLPHSISSNTIYSYSSFESPQSHIQSQPSYSQGYHNQNSLSTPLRRNKSYSISSANFNQSPVNLATTAMNKIMKTPLRGHTRSRSKVDVNAAVTAAMNLGQATKSNSTSSYNSTLNPFYTPSQQLSSTDDDDISTPLLTPGTKLHTSKSTFFSPYNKDDLEDQDDDAVKQLRKAKSYTSLLRKKKREDMTPSKQNQQHQQQQQQQQQQQQSRQSGGGHIQNLSFPNSTSQPKIDLLAYDQNPMTSYPPMDKSILKNLNQSISPFNKPKLSPPPSNFPSISIDLTTIATNKSSSFSSSTTHRNYNENTPFNSANSTSGGLLPPMATFTVPTVIKEELQVHNLQEEEQEHQDEQMEIDSFESNEKNARPTLSTSSLVRSMKMANLEISNDQQMSSNEDENIVTEAVVKQEKNGPVVDDVNGTGTNSKKPRKKQKSKSKENCNKKGKVATGNGKDNDKNNECLVNKGNKTNNNDTSNDKLDNDNKNTNGNGNNDNDNDSEENNDNVDDADDDDDGTVTIPIPEDLNVTKVKVRNNRSKSNDKSDPKKKHKCPICESRFQRPEHVKRHLKSHSSEKPFECQMPNCGKRFNRKDNLKAHLKKIHGLVKGQEEFTRVLNENKEVS
Protein: Probable ATP-citrate synthase subunit 2 (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase 2) (Citrate cleavage enzyme subunit 2) (O13907)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA. Has a central role in de novo lipid synthesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable ATP-citrate synthase subunit 1
- Succinate--CoA ligase subunit alpha, mitochondrial
- Probable citrate synthase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Malate dehydrogenase, mitochondrial
- Aconitate hydratase, mitochondrial
- Pyruvate carboxylase
- Acetyl-CoA carboxylase
- 2-oxoglutarate dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase
Sequence:
MSAKSIREYDGKAVLAYWLNRSPSISKEEYKTVSATPAVQLAQIQFPLPTLVIPAESTTYREVVEDVFAKVEQEHPWVKETKLVAKPDQLIKRRGKSGLLKLNATWDEAKEWIRERAGKNQKVQHAVGYLTTFLVEPFVPHPPNTEYYININSVREGDWILFCNEGGVDVGDVDAKARKLLVPVRLSEFPSRATIASTLLSDIPVEQHESLVDFIIRLYSVYVDCQFTYLEINPLVVIPTAKGADVFYLDLAAKLDQTAEFECGAKWAVARAPESLGIKTSGEESGAINADHGPPMVFPAPFGRELSKEEAYVQGLDAKTGASLKLTILNAEGRVWNLVAGGGASVVYADAVAVNGAADELANYGEYSGAPTDGQTYEYAKTVLDLMTRGEPRADGKVLFIGGGIANFTSPAVTFRAIARALGDYKDKLHAHKVSIWVRRAGPNYQEGLRVIREAGKKFDLPLKVYGPECHISGIVPMGLGKAPVEAEWQMA
Protein: HTH-type transcriptional regulator HexR (Q88P32)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Involved in regulation of glucose metabolism. Transcriptional repressor of the gap-1 gene and of the edd-glk-gltR-2 and zwf-pgl-eda operons. Acts by binding directly to an inverted pseudopalindromic sequence in the promoter region.
Interaction partners:
- Glucokinase
- 2-dehydro-3-deoxy-phosphogluconate aldolase
- Glucose-6-phosphate 1-dehydrogenase
- Phosphogluconate dehydratase
- HTH-type transcriptional regulator PtxS
- Glucose-6-phosphate 1-dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
- Sodium/glutamate symporter
Sequence:
MRNLLEQIQGRLDELNKAERKVAEVILLNPQQATRFSIAALAQAAKVSEPTVNRFCRSFGVSGYPELKLQLAQSLASGAAYVSRAVEADDDPAAYTQKIFASAIASLDSACQQLDPQQVSRAVDMMIQARQIHFFGLGASAPVALDAQHKFFRFNLAVSAHADVLMQRMLASVAHTGDLFVIISYTGRTRELVEVARLARENGASVLGLTAAGSPLANACSLSLHIPLPEDTDIYMPMTSRIIQLTVLDVLATGMTLRRGVDFQPHLRKIKESLNASRYPIEDDDLN
Protein: Beta-secretase 2 (EC 3.4.23.45) (Zgc:103530) (Q5XJ89)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Seizure 6-like protein-like)
- ADP-ribosylation factor-binding protein GGA1
- Seizure-related 6 homolog
- Amyloid beta
Sequence:
MRLYGLLLLSLTFWKSHSVFKIPLNIFAGKFNASVQLDLRPLQKNEAAAKSGLSLASDPAGIVNFLDMINNLKGDSGRGYYMQMIIGTPGQTLNILVDTGSSNFAVAAAAHPYITHYFNRALSSTYQSTERAVAVKYTQGEWEGELGTDLITIPEGPSGAITINIAAILTSEGFFLPGINWQGILGLAYPLLARPDPSVEPFFNSVVRQTGIPDVFSLQMCGAGVPASTTGDPAGGSLIMGGVEPTLHRGPIWYTPVLEEWYYQVEVLKLEVGDQNLNLDCKEYNSDKAIVDSGTTLLRLPANVFTAVVDTIMQTSLIDDFSAGFFDGTKLACWMRGESPWRFFPKVSIYLRGTNTSQSFRITILPQVRIVP
Protein: Complement C8 alpha chain (A0A8I6ACZ6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MALRGNCTREGEPYRYRSLLQPSKFGGTICSGDIWDKANCDSPTPCLRQAQCGQDFQCRETGRCLKRHLVCNGDQDCLDGSDEDNCDDARVIEDDCRQYEPIPGSERAALGYNILTQEEGQSVYDAKYYGGQCETVYNGDWRRLQYDPTCERLYYGEDEKYFRKPYNFLKYHFEALADTLISSEFYDDANDLFSKIQRDKSQSNSVTFGISPAKSPITLDASVSWSDESSFMKELSKYNEKKYSFMRVSTKVQTAHFKMRRHNIVLDEGMMESLMELPEQFNYGMYSKFINDYGTHYITSGTMGGIYEYVLVLDKEKMRIHGITVEDVKKCIGGGVGLQFGEKIIGEGDLSGESCVMTGDGNQDKRKKDLAVEDIISRVQGGSSRWSTGLAHNSSAITYRSWGRSLKYNPVVIDFEMQPIYQLLQHTNLGPLETKRRNLRRALDQYLMEFNACRCGPCFNNGVPILEGTSCSCQCSMGRQGPACESMVLEAMEGAKADGRWSCWSSWSECRGGSRERRRQCNNPAPQNGGAPCLGKSLQTQAC
Protein: Sorting nexin-5 (B1H267)
Organism: Rattus norvegicus (Rat)
Function: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol lipids. Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde transport of lysosomal enzyme receptor IGF2R. May function as link between endosomal transport vesicles and dynactin. Plays a role in the internalization of EGFR after EGF stimulation. Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C and is retromer-independent. Together with PIP5K1C facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation. Plays a role in macropinocytosis (By similarity).
Subcellular location: Endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side. Cell membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Y5X3}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projection, phagocytic cup. Cell projection, ruffle. Note=Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2). Detected on macropinosomes. Targeted to membrane ruffles in response to EGFR stimulation (By similarity). {ECO:0000250|UniProtKB:Q9Y5X3}.
Interaction partners:
- Sorting nexin-2
- Sorting nexin-1
- Sorting nexin
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 29
- Sorting nexin
- Sorting nexin-3
- Stromal cell-derived factor 2-like 1
- Sorting nexin-27
Sequence:
MAAVPELLEQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLTETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFSGVKEVDDFFEQEKNFLINYYNRIKDSCAKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAETHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFKNN
Protein: C-X-C chemokine receptor type 2 (High affinity interleukin-8 receptor B) (C9JG19)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEDFNMESDSFEDFWKGEDLSNYSYSSTLPPFLLDAAPCEPESLEINKYFVVIIYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGIL
Protein: DUF2062 domain-containing protein (Q2YN05)
Organism: Brucella abortus (strain 2308)
Interaction partners:
- Holo-[acyl-carrier-protein] synthase
Sequence:
MFQRRYPPTRWERLRLYLWPRRSFSRSFRYGGKRILRITASPHAVAAGLAVGVFSAFTPFFGFHLIIAIVLAYFLAGNVAAAALGTTLANPLTLPFIWGSTFELGRFIMSGSVDSVPPVHLGHALETMRFEEVWTPLLKPMLFGSTILGAAFAVLVYFVTRYAVSVFRRRRLERLAEKHRLHRQRELQKA
Protein: DNAation factor-related protein 1, isoform B (A0A0B4KFQ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DNAation factor-related protein 4
- DNAation factor-related protein 2, isoform B
- DNAation factor-related protein 3, isoform A
Sequence:
METAANSGDSKKPFKVKDVTRNIKKAVCASSLEEIRSKVAEKFEKCDHLPTIHLDSDGTEIDDEEYFRTLDENTELVAVFPGEHWIDPTHYVTITTPHGNEAGTGNGELNGGGEGDTTDANNSESARIRQLVGQLQNNLCNVSVMNDADLDSLSNMDPNSLVDITGKEFMEQLKDAGRPLCAKRNAEDRLNLLKLLKAGAIFCSERYPEDAEAIDREIGRQLNEAESGQMSTTTTSNTRTIEVVQCDNQNTTITITVGEATTTCATASGAMGSSAAEAAANEANANPNRNPNANGDIXLPILGSLR
Protein: Probable 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) (Ketopantoate hydroxymethyltransferase) (Q09672)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Pantoate--beta-alanine ligase
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Dihydroxy-acid dehydratase, mitochondrial
- Probable 2-dehydropantoate 2-reductase
- Probable dihydrofolate synthetase
- Probable GTP cyclohydrolase-2
- Biotin synthase
- Riboflavin synthase
- 2,5-diamino-6-ribosylamino-4
- Folic acid synthesis protein fol1
Sequence:
MSLKQITISTLRQWKLANKKFACITAYDASFSRLFAEQGMPVMLVGDSLGMTAQGHSTTLPVSVEDIAYHTKSVRRGAPNRLLMADLPFMSYSTWEDACKNAATVMRAGANIVKIEGGGNWIFEIVQRLTERSVPVAGHLGLTPQSVNIFGGYKIQGREQSAAARLIENAQQLEKFGAQLLVLECIPESLAEQITKTISIPTIGIGAGKHTDGQILVMHDALGITGGRPPKFAKNFLSGAGDIRTAIQRYIYEVEQGLYPAEEHSFQ
Protein: 50S ribosomal protein L14, putative (Q580C1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- 50S ribosomal protein L17, putative
- 50S ribosomal protein L13, putative
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL3m
- Ribosomal protein L11, putative
- KOW domain-containing protein
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L5, putative
Sequence:
MFRFFSLRLAPAPSADAAAKLPAGKPANKSWFRHNLIIRRKASYRSRWGTGAEGYGTGVPFSDQVKLHCVDNTNCKHVRLISKATAERFAHCRVFPAVAHRVSVQRFKSGRGEVSRHRVKPGNIYWVCLLSRRQTNTRMSGLRTNFDRNTCILMNDQRVPLGTRVMYCAGRHVNHKYHLKAVVLANFFV
Protein: Proline-rich receptor-like protein kinase PERK1 (EC 2.7.11.1) (Proline-rich extensin-like receptor kinase 1) (AtPERK1) (Q9LV48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000305|PubMed:17644812}; Single-pass membrane protein {ECO:0000305|PubMed:17644812}.
Interaction partners:
- Serine/threonine-protein kinase KIPK2
- Serine/threonine-protein kinase KIPK1
Sequence:
MSTAPSPGTTPSPSPPSPPTNSTTTTPPPAASSPPPTTTPSSPPPSPSTNSTSPPPSSPLPPSLPPPSPPGSLTPPLPQPSPSAPITPSPPSPTTPSNPRSPPSPNQGPPNTPSGSTPRTPSNTKPSPPSDSSDGLSTGVVVGIAIGGVAILVILTLICLLCKKKRRRRHDDEAAYYVPPPPPSGPKAGGPYGGQQQYWQQQNASRPSDNHVVTSLPPPKPPSPPRKPPPPPPPPAFMSSSGGSDYSDLPVLPPPSPGLVLGFSKSTFTYEELSRATNGFSEANLLGQGGFGYVHKGILPSGKEVAVKQLKAGSGQGEREFQAEVEIISRVHHRHLVSLIGYCMAGVQRLLVYEFVPNNNLEFHLHGKGRPTMEWSTRLKIALGSAKGLSYLHEDCNPKIIHRDIKASNILIDFKFEAKVADFGLAKIASDTNTHVSTRVMGTFGYLAPEYAASGKLTEKSDVFSFGVVLLELITGRRPVDANNVYVDDSLVDWARPLLNRASEEGDFEGLADSKMGNEYDREEMARMVACAAACVRHSARRRPRMSQIVRALEGNVSLSDLNEGMRPGHSNVYSSYGGSTDYDTSQYNDDMIKFRKMALGTQEYGTTGEYSNPTSDYGLYPSGSSSEGQATREMEMGKIKKTGQGYSGPSL
Protein: Zinc finger protein 330 (Nucleolar autoantigen 36) (Nucleolar cysteine-rich protein) (Q9Y3S2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:10593942}. Nucleus, nucleolus {ECO:0000269|PubMed:10593942}. Chromosome, centromere {ECO:0000269|PubMed:10593942}. Note=Predominantly expressed in the nucleolus. In mitosis associated with centromeres and concentrated at the midbody in cytokinesis.
Interaction partners:
- Homeobox protein goosecoid
- Nucleolar transcription factor 1
Sequence:
MPKKKTGARKKAENRREREKQLRASRSTIDLAKHPCNASMECDKCQRRQKNRAFCYFCNSVQKLPICAQCGKTKCMMKSSDCVIKHAGVYSTGLAMVGAICDFCEAWVCHGRKCLSTHACACPLTDAECVECERGVWDHGGRIFSCSFCHNFLCEDDQFEHQASCQVLEAETFKCVSCNRLGQHSCLRCKACFCDDHTRSKVFKQEKGKQPPCPKCGHETQETKDLSMSTRSLKFGRQTGGEEGDGASGYDAYWKNLSSDKYGDTSYHDEEEDEYEAEDDEEEEDEGRKDSDTESSDLFTNLNLGRTYASGYAHYEEQEN
Protein: MLLT6 (Q8VHB4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKEMVGGCCVCSDERGWAENPLVYCDGHACSVAVHQACYGIVQVPTGPWFCRKCESQERAARVRCELCPHKDGALKRPDNGGWAHVVCALYIPEVQFANVLTMEPIVLQYVPHDRFNKTCYICEEQGRESKAASGACMTCNRHGCRQAFHVTCAQMAGLLCEEEVLEVDNVKYCGYCKYHFSKMKTSRHSSGGGGGAGGGSSGGGGGGSSSASGGGGGTGGGSGNSFLSGRRSRSASPSTQPEKHPTHHEKGQKKSRKDKERLKQKHKKRPESPPSVLAPAAVPTADKVSSATSSSHHEASTQETSESSRDSKGRKSSSHSLSHKDKKLGTGKGSSLQSSPDFAAFPKLEQPEEDKYPKPADPTPPAPPSPTAPEPPKADLFEQKVVFSGFGPIMRFTTTASSSSRARAPSPGDYKSPHITGAGASAGTHKRMPALSATLGPAEEAPETTLKEKKHKASKRSRHGPGRPKGSRGKEGASGPTASLPAAQLAGFTATAASPFSGGSLVSAGLGGLASRTFGPSGSLPSLSLESSLLGAGIYTSNKDSISHGGGMLRAVCSTPLSSSLPGPTGTSALPRLSRSPFTSTLASSSASISTAQVFSLAGSTFSLPSSHIFGTPMGTVNPLLTQAESSHTEPDLEDCSFRCHGTSPQESLSSMSPISSLPALFDQTSAPCAGGQLDSTAPGTTNMEQLLEKQGDGEAGVNIVEMLKALHALQKENQRLQEQILSLTAKKERLQVLNVQLSVPFPALPAALPATNGPIPGPYGLLPQAGSSDSLSVSKSPPGKNSLGLDNSLSTSSEDPHSGCPSRSSSSLSFHSTPPPLPLLQQSPATLPLALPGAPAPLPPQPQNGLGRAPGATGLGAMPMAEGLLGGLAGSGSLPLNGLLGGLNGAAAPNPAGLSQAGGAPRFNVAGCLNSLTEQQRHLLQQQEQQLQQLQQLLASPQLTPEHQTVVYQMIQQMQQKRELQRLQMAGGSQLPMASLLAGSSTPLLSAGTPGLLPTASAPPLLPAGALVAPSLGSNTSLMAAAAAAAAVAAAGGPPVLTAQTNPFLSLPGADASGNGPKGGTADKGASTSQEKG
Protein: C-C chemokine receptor type 7 (C-C CKR-7) (CC-CKR-7) (CCR-7) (BLR2) (CDw197) (Epstein-Barr virus-induced G-protein coupled receptor 1) (EBI1) (EBV-induced G-protein coupled receptor 1) (MIP-3 beta receptor) (CD antigen CD197) (P32248)
Organism: Homo sapiens (Human)
Function: Receptor for the MIP-3-beta chemokine. Probable mediator of EBV effects on B-lymphocytes or of normal lymphocyte functions.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Stromal cell-derived factor 1
- C-C motif chemokine 21
- C-C motif chemokine 19
- C-X-C motif chemokine 13
- C-C motif chemokine 4
- C-C motif chemokine 20
- C-C motif chemokine 25
- C-C motif chemokine 5
- C-C motif chemokine 22
- C-C motif chemokine 27
Sequence:
MDLGKPMKSVLVVALLVIFQVCLCQDEVTDDYIGDNTTVDYTLFESLCSKKDVRNFKAWFLPIMYSIICFVGLLGNGLVVLTYIYFKRLKTMTDTYLLNLAVADILFLLTLPFWAYSAAKSWVFGVHFCKLIFAIYKMSFFSGMLLLLCISIDRYVAIVQAVSAHRHRARVLLISKLSCVGIWILATVLSIPELLYSDLQRSSSEQAMRCSLITEHVEAFITIQVAQMVIGFLVPLLAMSFCYLVIIRTLLQARNFERNKAIKVIIAVVVVFIVFQLPYNGVVLAQTVANFNITSSTCELSKQLNIAYDVTYSLACVRCCVNPFLYAFIGVKFRNDLFKLFKDLGCLSQEQLRQWSSCRHIRRSSMSVEAETTTTFSP
Protein: ORMDL sphingolipid biosynthesis regulator 1 (A0A1B0GXE7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNVGVAHSEVNPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFFSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETPDQGKARLLTHWEQLDYGVQFTSSRKFFTISPIIL
Protein: Cyclin N-terminal domain-containing protein (Q38A58)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTATSGFDWLCDARRAFCAYGVDLIRTGSILVRTTPSVTYRASVLFQRFQAAAEEVRQKRGDYHSEEGFQRGAISRSGIEETCVMGIGLETCRQATYTIPSHVGTECSPGVLVLGDLFAPLDYCLYHFEDHDDIVYLAAACILVAAKVEDPSTRIRSIVSVFMRLNQRRRNEPVIELLQPPPERYENFKTRVREAEEIVLQTLGFQTFVECPFKYAIIFLGILVGNDPVDGGLVVTVGASPPQPPAAAGAANPTTPLVGSRPLQGSEAFSCPSAKKWLADAVCWLNDIPRWRELYAEEAYVLAVCALYWTRPPDVSGLPEEWTAAFGVESFKRDSVLSVYRENLDGALGSEKHKIEVLLTARHEKPDYPTMGQPARVANAEDEAASGGKPLLPPSDVSAVGTDPMPIQVKPTEPNAPIFIPDIVVGTAISAGPIIPPPSPSVVTPPSLAVLQSALSIPITLPPQQPISSNTTSAGGISCSGPLGLEEVLPGGGEEYNKSLPLEAVAPGIAELRPAEEEYQFEDFKEMQRRRRQKEEAELRQTKRRRSSSRRRRHRSDEKRRRRSDSHDRRRSDSRERRRRPRAPSPHKNRSGDRQHQHQHHHRQHPAASSQRPKSDRRDDRHRNDDYKRNDGKSQRRRR
Protein: Anaerobic ribonucleoside-triphosphate reductase-activating protein (EC 1.97.1.-) (Class III anaerobic ribonucleotide reductase small component) (P0A9N8)
Organism: Escherichia coli (strain K12)
Function: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
Subcellular location: Cytoplasm.
Interaction partners:
- Anaerobic ribonucleoside-triphosphate reductase
- Ribonucleoside-diphosphate reductase 1 subunit beta
- Ribonucleoside-diphosphate reductase 1 subunit alpha
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
- NADPH-dependent 7-cyano-7-deazaguanine reductase
- Glutaredoxin-like protein NrdH
- Protein NrdI
- Ribonucleoside-diphosphate reductase 2 subunit beta
Sequence:
MNYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGQPFTKAMEDQIINDLNDTRIKRQGISLSGGDPLHPQNVPDILKLVQRIRAECPGKDIWVWTGYKLDELNAAQMQVVDLINVLVDGKFVQDLKDPSLIWRGSSNQVVHHLR
Protein: Transport membrane protein (Q2F940)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPKMHLSFELLIEWNFAPETFLGEVRIRSVRILIGLGLTWFTRYWFSEESISPLAKPFLTLPLDSYFVRTQSTEAPPTYVATSSIACSYFVFPLISHQIWCFSIPSCYGEQRQKYNRFLHLSGSRFSLFLFLTPPRVVPNVWHFPYFVGATSTNSLMIKLQPKIYDYIMLTVRILFIPSVCSQVPVIVICLPEPRGLSVETFTSNRRFLMVFPLITAALSTPPDIWCQIVAPFLIYSIIEFAIFVALIVQVREEGWTIRMRGSIEKKEE