wanglab/gogpt-training-data huggingface dataset:
Protein: Proteasome subunit beta type-2 (EC 3.4.25.1) (Macropain subunit PUP1) (Multicatalytic endopeptidase complex subunit PUP1) (Proteasome component PUP1) (Proteinase YSCE subunit PUP1) (P25043)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- 26S proteasome regulatory subunit RPN12
- 26S proteasome regulatory subunit RPN6
- Proteasome subunit beta type-6
- Ubiquitin carboxyl-terminal hydrolase RPN11
- 26S proteasome regulatory subunit RPN10
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit RPN1
- 26S proteasome regulatory subunit RPN8
- 26S proteasome subunit RPT4
- Proteasome subunit alpha type-4
Sequence:
MAGLSFDNYQRNNFLAENSHTQPKATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQVDITA
Protein: Ras-related protein Rab-3A (EC 3.6.5.2) (P63011)
Organism: Mus musculus (Mouse)
Function: Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane. Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (By similarity). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (By similarity). Stimulates insulin secretion through interaction with RIMS2 isoform RIMS2 and RPH3AL effectors in pancreatic beta cells. Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9 (By similarity). Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1 (By similarity). Plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P63012}. Lysosome {ECO:0000250|UniProtKB:P20336}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P63012}. Cell projection, axon {ECO:0000269|PubMed:18849981}. Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Presynapse {ECO:0000269|PubMed:31651360}. Postsynapse {ECO:0000269|PubMed:31651360}. Note=Cycles between a vesicle-associated GTP-bound form and a cytosolic GDP-bound form. {ECO:0000250|UniProtKB:P63012}.
Interaction partners:
- Rabphilin-3A
- Regulating synaptic membrane exocytosis protein 1
- Synaptophysin
- Vesicle-associated membrane protein 2
- Protein unc-13 homolog B
- Synaptotagmin-1
- Synapsin-1
- DnaJ homolog subfamily C member 5
- Protein piccolo
- Syntaxin-binding protein 1
Sequence:
MASATDSRYGQKESSDQNFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEKMSESLDTADPAVTGAKQGPQLTDQQAPPHQDCAC
Protein: Heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) (AU-rich element RNA-binding protein 1) (Q9JJ54)
Organism: Rattus norvegicus (Rat)
Function: Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q14103}. Cytoplasm {ECO:0000250|UniProtKB:Q14103}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally. {ECO:0000250|UniProtKB:Q14103}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein Q
- Heterogeneous nuclear ribonucleoprotein A3
- Far upstream element-binding protein 2
- Transportin-1
- Heterogeneous nuclear ribonucleoprotein U
- ELAV-like protein 1
- Polyadenylate-binding protein-interacting protein 1
- Heterogeneous nuclear ribonucleoprotein K
- Polypyrimidine tract-binding protein 1
- DNA
Sequence:
MSEEQFGGDGAAAAATAAVGGSAGEQEGAMVAAAQGAAAAAGSGSGGGSAPGGTEGGSTEAEGAKIDASKNEEDEGHSNSSPRHTEAATAQREEWKMFIGGLSWDTTKKDLKDYFSKFGDVVDCTLKLDPITGRSRGFGFVLFKESESVDKVMDQKEHKLNGKVIDPKRAKAMKTKEPVKKIFVGGLSPDTPEEKIREYFGGFGEVESIELPMDNKTNKRRGFCFITFKEEEPVKKIMEKKYHNVGLSKCEIKVAMSKEQYQQQQQWGSRGGFAGRARGRGGGPSQNWNQGYSNYWNQGYGSYGYNSQGYGGYGGYDYTGYNSYYGYGDYSNQQSGYGKVSRRGGHQNSYKPY
Protein: Uncharacterized protein Rv1424c (P9WLX7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MTVVPGAPSRPASAVSRPSYRQCVQASAQTSARRYSFPSYRRPPAEKLVFPVLLGILTLLLSACQTASASGYNEPRGYDRATLKLVFSMDLGMCLNRFTYDSKLAPSRPQVVACDSREARIRNDGFHANAPSCMRIDYELITQNHRAYYCLKYLVRVGYCYPAVTTPGKPPSVLLYAPSACDESLPSPRVATALVPGTRSANREFSRFVVTEIKSLGAGGRCDSASVSLQPPEEIEGPAIPPASSQLVCVAPK
Protein: Protein sprint (SH2 poly-proline-containing Ras-interactor protein) (Q8MQW8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Potential Ras effector protein. May function as a guanine nucleotide exchange (GEF), by exchanging bound GDP for free GTP (By similarity).
Interaction partners:
- Ras-related protein Rab5
Sequence:
MVNAVMDAIALLSSLASDLDIMLNDLRSAPSHAATATATATTTATVATATATTTANRQQQHHNHHNQQQMQSRQLHAHHWQSINNNKNNNISNKNNNNNNNNNNNINNNNNNNNHSAHPPCLIDIKLKSSRSAATKITHTTTANQLQQQQRRRVAPKPLPRPPRRTRPTGQKEVGPSEEDGDTDASDLANMTSPLSASAAATRINGLSPEVKKVQRLPLWNARNGNGSTTTHCHPTGVSVQRRLPIQSHQQRILNQRFHHQRMHHGTSEPIPSGVATPSSLDSASVDGGKSHTGNNNNINNNHNGQQSQKSQQQAGLAAKLNVLAQSNLNNNNTTNQPGSMTPASNRTGLDSNQNQKQNLNADSRRSSSVDPDADADDVVDAAHGGAFEDDMQALLPKCSRRSRDELSQSRTSLVSSSEGGILAEGETSSEDDEEEPVEAEDEGEESSRDSSDNSPPCDLGLMERLLVTHPMWFLPGIQRSGAVHLLQGKEEGTFIVRGSSQPNTMAVSVRLPQDTGPYIEHYLIQSHDNVLSLESSRFTFGSIPSLIAHYAQCCDELPVQLMLPRVLREANNRKKLSSLALLGQEFWSYVSSPALLGPLTPSVAPSKDQQLLDAKSPLSLTETSGLGTATFFSDTVSKPPPTGAPPLPGGGLFSPTGSGQLLGFFSQAGTPSDTTNSSLSSFTTSGGQHMQLLSPNSVDSVILTMSPVDNPGHYLPGSTGAPMAPLCPSVVDQQLSTFKVAQTAPEVDQVRPQRPKPPNTLNLKPPAPPLRWSKPHSPDQNGSANGNFTVTTTVTFSMENGGGGGSGPTVGNGNGKFVEVTTPAASNPFNALLNGQASTFQTFAKRLSPEGECKDTLSSQGSSSNDSRWPPPARKLLTSPMTPLTPSGGSSSSGGKSRKSRAGKESQHYKESDILESPPMQYCASALSDKISDYEDVWSHDPSDRASLLTSFRPALDTVGGVMNRRPDLLAETPSTPTPTQQSHLTPCEEETTATPNESSSQSLLQFSGDVPARSRAGLLLPNLSGQVPPVAMTKSMTAAEDDGGDTTPTAEGQANGASRSKQGSPFYAEPADALRQAGLTSAATAILRRQHRSQMLHASQRHSEPLKAGFGGSGNGAMLQPSDLEKLAGSLDELKPKPKVSQQQQQSQQQQQPTKRARNRIDHWQLDSSWEFMAKQDTGSHAGGDYDTAAIDWQEKENSLGRDSRADGQGKKRTLTIHQIIANRLPDLNLPELVRCSTPPQTAALQPHVLGQDKAGVGCDGSQKSFQSQIGCRLSSYDNVFCQNSFGGIDSAQSDDGTIFSEPWDSSQWDTFLPHDDATINSDTIHLSKCRPALSEDDTIVEELQSTKDGSNGSCNQDTLKANRNGAGHHKLNNGNGNGKANNRPKVATILRNPSMRDREVLCHPRNKMSIQSSGPGDSLRAYTLQLAQDPSSTFARNIENFICCTKESREAAPQVVMRNMRQFMSGMKNYLVKHGEGKFHAELETARARLKSDEFLNLDAMLETVMHQLVVLPLREHLYGIFVDHYQRSEDIQLLAQNVRYACEREAADFGIRPTVTPPSQAALRLIANLLWRLQEAELPLDKLELFLCVISTVFDATGCPRGQQLGADDFLPVLVYVVAKCGFVGAEIEAEFMWGLLQPTLLNGEPGYYLTALCSAVQVLKTFMASEGESGSGSLDWRSSCLPACSSVLRVIIPDECNGSLQTRTLPVRPHTTTREVCRIIAHKARITNPQDYALFKLVDGEETLLTDAECPQDARLAAKGKHCMLAYKRIDAKIAWPTAQLAGH
Protein: Gibberellin 20-oxidase-like protein (EC 1.14.11.-) (F4KBY0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of root hair growth.
Interaction partners:
- 2-oxoglutarate
Sequence:
MSLELPVFDISKPLSESSLTSLQDACKEWGFFYVTNHGVSRDMYKKLRRFSTGVFELEDEEKMKMGASNYTPRFIASPFFESLRVSGPDFYASAKSSVDAFSDQATDEEFSGLMKEYGEKMTKLCEKIMKAILSSFGDDLHHKYYESEFGNCHGYFRINNYTIPSDQEDDHHNGDEQDLIEGLGMHTDMSCITIVDQDDIGGLQVRTRDGIGLMDINPKDEALVVNVGDLLHAWTNGRLRSSQHRVILKRRGFVGNRFSLAFFWCFDDGKVVFAPDEVVGGCEGMRVFRSFKCGDYLRFRESNEKGKFEKVGDTVEDFARIEDRR
Protein: Mite group 2 allergen-like Ixo r 2 (Der-p2 allergen-like protein) (A1EA99)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Binds human IgE in vitro, and may neutralize IgE antibodies present in blood from repeatedly tick-bitten people. Does not have antimicrobial activity against E.coli or M.luteus.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MFRYLVFLLIVGAVSCQRRKAVYKPCGGSGKLISVEVEPCDSDPCVFKKGTDVKVHVTMVADQDSDTATLDARVKVFGFQMPVPGIETDLCKGTVECPVIKGRKYSVTAIFPVPSLMSLKTEVTFKVIGDKGLSVCGQSDIVIE
Protein: L-cysteine desulfhydrase Cds1 (EC 4.4.1.1) (O69652)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A cysteine desulfhydrase that generates hydrogen sulfide, H(2)S. The H(2)S produced by this enzyme stimulates respiration in M.tuberculosis, mediated primarily via cytochrome bd with a lesser contribution from cytochrome bc1/aa3. H(2)S modulates the balance between respiration and glycolysis, and also contributes to redox homeostasis. Probably eliminates toxic levels of Cys (which can induce oxidative stress).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Serine acetyltransferase
- Cystathionine gamma-synthase
- O-succinylhomoserine sulfhydrylase
- Conserved protein
- Sulfite reductase [ferredoxin]
- S-sulfocysteine synthase
- O-acetylserine sulfhydrylase
- Phosphoserine aminotransferase
- cysteine-S-conjugate beta-lyase
- Putative cystathionine beta-lyase
Sequence:
MSGGACIAVRSLSRSWTDNAIRLIEADARRSADTHLLRYPLPAAWCTDVDVELYLKDETTHITGSLKHRLARSLFLYALCNGWINENTTVVEASSGSTAVSEAYFAALLGLPFIAVMPAATSASKIALIESQGGRCHFVQNSSQVYAEAERVAKETGGHYLDQFTNAERATDWRGNNNIAESIYVQMREEKHPTPEWIVVGAGTGGTSATIGRYIRYRRHATRLCVVDPENSAFFPAYSEGRYDIVMPTSSRIEGIGRPRVEPSFLPGVVDRMVAVPDAASIAAARHVSAVLGRRVGPSTGTNLWGAFGLLAEMVKQGRSGSVVTLLADSGDRYADTYFSDEWVSAQGLDPAGPAAALVEFERSCRWT
Protein: JNK-interacting protein (JIP) (JNK MAP kinase scaffold protein) (Uncoordinated protein 16) (P34609)
Organism: Caenorhabditis elegans
Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of synaptic vesicle transport, through interactions with the JNK-signaling components and motor proteins. Binds specific components of the JNK signaling pathway namely jnk-1, jkk-1 and sek-1. Associates with components of the motor protein, kinesin-1. Pre-assembled unc-16 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location. Regulates the retrograde transport of autophagosomes from the neurites to the cell body of AIY interneurons.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026}. Note=Diffusely localized throughout cell body but intensely localized in regions adjacent to nucleus and at presumptive tips of neural processes.
Interaction partners:
- Kinesin light chain
- ADP-ribosylation factor 6
- Dynein light intermediate chain
- Kinesin heavy chain
- PID domain-containing protein
- Kinesin light chain
- Dynactin subunit 1
- Putative RNA-binding protein
- RRM domain-containing protein
- Kinesin-like protein unc-104
Sequence:
MACNLSPVNEMADSITSSTPSEIVYGGPGSPDEHRTMSDKVQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLEEREVEQKLEFDRLHERYNTLLRTHVDHMERTKYLMGSEKFELMQNMPLPNMQLRNKMGMAASVDASSIRGVSDLISAHMTQSTTMDVNLANHITNEDWQDEFSSDIEPSPRDIPQSSADALTSPITTKEPTPKREAASPKQSEEEEADETTSVDPKENNDLLGADLTDDESDWNGLGLIPRRHRPNEMLDDDDTSDDGSLGMGREVENLIKENSELLDMKNALNIVKNDLINQVDELNSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLKQKLMEKENEQEEDDVPMAMRKRFTRSEMQRVLMDRNAYKEKLMELEESIKWTEMQRAKKMQQQQQNVNQKKSGGIWEFFSSLLGDSVTPPASSRGNRASSSRGKMTRSVEYIDPDMISERRAAERREQYKLVREHVKKEDGRIEAYGWSLPNVEAEVSSVPIPVCCRPLLDNEPSLKIWCATGVVLRGGRDERGQWIVGDPIYFAPASMKKTKTSNHRPELEDEIKRARNLDARESELDEWQSSSLVWVVSSNQGKSLIAVLDANNPNNIIETFPACDSHLLCIQAVSGVMEGEPEMNEEQSKKYLSGGGKIKDLPEGLDGTDLGACEWVELRKMEDSEDGVPTYCSNDMKPSPKRTRDFSISEVAPVDSSAPVKEDPLPPPANRPGGRAALPPHIRDAMSKYDGVSGQMSGALPTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPDAVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSATSSVRSLCLVSTNIWATYKNCVVVLDAESLQIVKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVDIEPYVTKMLGTSKLDFSYMRTTALLVSNRRLWIGTGTGVIISVPFSGQLEKKIETKDSKRPAGPGGLVRVYGATSENATNDEKTNDDFIPYCNLAHAQLSFHGHKDSVKFFLGVPGASKNGEDESAEVTLRRMLIMSGGDGYIDFRIGEENEPELTGQSIRPRDMSHLIIWEVDAELPILSK
Protein: Transmembrane protein 220 (Q6QAJ8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAPALWRACNGLMAAFFALAALVQVNDPDAEVWVVVYTIPAVLTLLVGLNPEVTGNVIWKSISAIHILFCTVWAVGLASYLLHRTQQNILHEEEGRELSGLVIITAWIILCHSSSKNPVGGRIQLAIAIVITLFPFISWVYIYINKEMRSSWPTHCKTVI
Protein: ADP-ribosylation factor GTPase-activating protein AGD12 (ARF GAP AGD12) (Protein ARF-GAP DOMAIN 12) (AtAGD12) (Zinc- and calcium-binding protein) (AtZAC) (Q9FVJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTPase-activating protein (GAP) for ADP ribosylation factor (ARF). Binds phosphatidylinositol 3-monophosohate (PI-3-P) and anionic phospholipids.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:11202441}. Cell membrane {ECO:0000269|PubMed:11202441}.
Interaction partners:
- Protein AGENET DOMAIN
- ADP-ribosylation factor GTPase-activating protein
Sequence:
MSYSGAGLGKPGSGKRRIRDLLTQSDNRVCADCGAPDPKWASANIGVFICLKCCGVHRSLGSHISKVLSVTLDEWSDEEVDSMIEIGGNASANSIYEAFIPEGSSKPGPDASHDQRMRFIRSKYEHQEFLKPSLRITSVRGSSTKTPAFLSSSLSKKIVDSFRTNSSSQQPQLEGMVEFIGLLKVTIKKGTNMAIRDMMSSDPYVVLTLGQQKAQSTVVKSNLNPVWNEELMLSVPHNYGSVKLQVFDYDTFSADDIMGEAEIDIQPLITSAMAFGDPEMFGDMQIGKWLKSHDNALIEDSIINIADGKVKQEVQIKLQNVESGELELEMEWLPLEQ
Protein: Obg-like ATPase 1 (J3KQ32)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03167}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03167}. Nucleus, nucleolus {ECO:0000256|HAMAP-Rule:MF_03167}. Note=Predominantly cytoplasmic, shuttles between the nucleus and the cytoplasm. {ECO:0000256|HAMAP-Rule:MF_03167}.
Interaction partners:
Sequence:
MSRTFSAKGGRDLVEGPQYLMPPKKGGDGIKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQYHKPASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAVRGGDKKLKPEYDIMCKVKSWVIDQKKPVRFYHDWNDKEIEVLNKHLFLTSKPMVYLVNLSEKDYIRKKNKWLIKIKEWVDKYDPGALVIPFSGALELKLQELSAEERQKYLEANMTQSALPKIIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYEDFKEEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFNTPQQPKKK
Protein: [NU+] prion formation protein 1 (Q08972)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in the mRNA export process (By similarity). Forms the [NU+] prion and induces [PSI+] prion formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS13A
- Large ribosomal subunit protein uL5B
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL30A
Sequence:
MPPKKFKDLNSFLDDQPKDPNLVASPFGGYFKNPAADAGSNNASKKSSYQQQRNWKQGGNYQQGGYQSYNSNYNNYNNYNNYNNYNNYNNYNKYNGQGYQKSTYKQSAVTPNQSGTPTPSASTTSLTSLNEKLSNLELTPISQFLSKIPECQSITDCKNQIKLIIEEFGKEGNSTGEKIEEWKIVDVLSKFIKPKNPSLVRESAMLIISNIAQFFSGKPPQEAYLLPFFNVALDCISDKENTVKRAAQHAIDSLLNCFPMEALTCFVLPTILDYLSSGAKWQAKMAALSVVDRIREDSANDLLELTFKDAVPVLTDVATDFKPELAKQGYKTLLDYVSILDNLDLSPRYKLIVDTLQDPSKVPESVKSLSSVTFVAEVTEPSLSLLVPILNRSLNLSSSSQEQLRQTVIVVENLTRLVNNRNEIESFIPLLLPGIQKVVDTASLPEVRELAEKALNVLKEDDEADKENKFSGRLTLEEGRDFLLDHLKDIKADDSCFVKPYMNDETVIKYMSKILTVDSNVNDWKRLEDFLTAVFGGSDSQREFVKQDFIHNLRALFYQEKERADEDEGIEIVNTDFSLAYGSRMLLNKTNLRLLKGHRYGLCGRNGAGKSTLMRAIANGQLDGFPDKDTLRTCFVEHKLQGEEGDLDLVSFIALDEELQSTSREEIAAALESVGFDEERRAQTVGSLSGGWKMKLELARAMLQKADILLLDEPTNHLDVSNVKWLEEYLLEHTDITSLIVSHDSGFLDTVCTDIIHYENKKLAYYKGNLAAFVEQKPEAKSYYTLTDSNAQMRFPPPGILTGVKSNTRAVAKMTDVTFSYPGAQKPSLSHVSCSLSLSSRVACLGPNGAGKSTLIKLLTGELVPNEGKVEKHPNLRIGYIAQHALQHVNEHKEKTANQYLQWRYQFGDDREVLLKESRKISEDEKEMMTKEIDIDDGRGKRAIEAIVGRQKLKKSFQYEVKWKYWKPKYNSWVPKDVLVEHGFEKLVQKFDDHEASREGLGYRELIPSVITKHFEDVGLDSEIANHTPLGSLSGGQLVKVVIAGAMWNNPHLLVLDEPTNYLDRDSLGALAVAIRDWSGGVVMISHNNEFVGALCPEQWIVENGKMVQKGSAQVDQSKFEDGGNADAVGLKASNLAKPSVDDDDSPANIKVKQRKKRLTRNEKKLQAERRRLRYIEWLSSPKGTPKPVDTDDEED
Protein: Uridylate kinase (UK) (EC 2.7.4.14) (ATP:UMP phosphotransferase) (Deoxycytidylate kinase) (CK) (dCMP kinase) (Suppressor of cdc8 protein) (Uridine monophosphate kinase) (UMP kinase) (UMPK) (P15700)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP, AMP, GMP, dGMP and dTMP. ATP and dATP are the best phosphate donors, but can also use GTP, dGTP, dCTP, and dTTP to some degree.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:1333436, ECO:0000269|PubMed:8391780}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:1333436, ECO:0000269|PubMed:8391780}. Note=Predominantly cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:8391780}.
Interaction partners:
- Thymidylate kinase
- Nucleoside diphosphate kinase
- Uridine kinase
- Orotidine 5'-phosphate decarboxylase
- Ribonucleoside-diphosphate reductase large chain 1
- Ribonucleoside-diphosphate reductase large chain 2
- Uracil phosphoribosyltransferase
- Putative uridine kinase DAS2
- Ribonucleoside-diphosphate reductase small chain 1
- Ribonucleoside-diphosphate reductase small chain 2
Sequence:
MTAATTSQPAFSPDQVSVIFVLGGPGAGKGTQCEKLVKDYSFVHLSAGDLLRAEQGRAGSQYGELIKNCIKEGQIVPQEITLALLRNAISDNVKANKHKFLIDGFPRKMDQAISFERDIVESKFILFFDCPEDIMLERLLERGKTSGRSDDNIESIKKRFNTFKETSMPVIEYFETKSKVVRVRCDRSVEDVYKDVQDAIRDSL
Protein: Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) (Q9W3J5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
- Tyrosine--tRNA ligase
- Probable phenylalanine--tRNA ligase, mitochondrial
- Bifunctional glutamate/proline--tRNA ligase
- Lysine--tRNA ligase
- histidine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Glycine--tRNA ligase
- Tryptophan--tRNA ligase, cytoplasmic
Sequence:
MHPDLTERILQHLETTDKADTLDLAALFAEDHQKIVGSLKSIQAHGELVTAETVTHKSLGLTDEGRAVVENGSHEALVYDLVPPEGIAQAALMAAGGANAKVGFSKAMSHGWILVDKSVTPPLVRRKVDTITDVVRNQLQQVALGKGDQLPAKEVADFKKRKLLQETTTKSFVLARGPEFATTLTKLETDLTVEMLANGLWDQLKFKAYNFDALGAPPTRGHLHPLLKVRTEFRQIFLEMGFSEMPTNNYVESSFWNFDALYQPQQHPARDAHDTFFVNHPAKSHKFPQDYLERVKKVHSVGGYGSKGYGYDWKLEEAQKNLLRTHTTAVSARMLYKLANQEGGFKAAKYFSIDKVFRNETLDATHLAEFHQVEGVIADVGLTLGDLIGTLYEFFRKLGITQLEFKPAYNPYTEPSMEIFCYHPGLAKWIEVGNSGVFRPEMLLPMGLPENVNVIAWGLSLERPTMIKYGINNIRDLVGPKVDLKMVEEGPICRLDHA
Protein: Choline/ethanolamine transporter FLVCR1 (Feline leukemia virus subgroup C receptor-related protein 1) (Feline leukemia virus subgroup C receptor) (Heme transporter FLVCR1) (Major facilitator superfamily domain containing 7B) (Mfsd7b) (B2RXV4)
Organism: Mus musculus (Mouse)
Function: Heme transporter that exports cytoplasmic heme. It can also export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. Does not export bilirubin. Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity. Heme export provides protection from heme or ferrous iron toxicities in liver, brain, sensory neurons and during erythtopoiesis, a process in which heme synthesis intensifies. Causes susceptibility to FeLV-C in vitro.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:23187127}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane {ECO:0000269|PubMed:23187127}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with HADHA. {ECO:0000269|PubMed:23187127}.
Interaction partners:
- Hemopexin
- Heme transporter HRG1
- ATP-binding cassette sub-family B member 10, mitochondrial
- Proton-coupled folate transporter
Sequence:
MARPDDEVGPAVAPGHPLGKGYLPVPKGAPDGEARLVPQNGPEALNGGPGLGPLIAGAQGGPQALIAAEEETQARLLPAGDGEDVPCPACPPRTALSPRRFVVLLIFSLYSLVNAFQWIQYSSISNVFEDFYEVSPLHINWLSMVYMVAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWVKCGSVQRHLFWVTMLGQILCSVAQVFILGLPSPVASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPALGTQNSTGLLAHTQNNTDLLAHNINTMFYGTAFISTFLFFLTIIAFKEKPPLPPSQAQAVLRDSPPEEYSYKSSIWNLCRNIPFVLLLVSYGIMTGAFYSISTLLNQIILTYYVGEEVNAGRIGLTLVVAGMVGSILCGLWLDYTKTYKQTTLIVYVLSFIGMLIFTFTLNLGYIIVVFFTGGILGFFMTGYLPLGFEFAVEITYPESEGMSSGLLNTAAQILGIFFTLAQGKITTDYNSPEAGNIFLCAWMFVGIILTALIKSDLRRHNINTGLTNIDVKAVPVDSRVDPKPKVMVSIQSESSL
Protein: E3 ubiquitin-protein ligase ZFP91 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase ZFP91) (Zinc finger protein 757) (Zinc finger protein 91 homolog) (Zfp-91) (Q96JP5)
Organism: Homo sapiens (Human)
Function: Atypical E3 ubiquitin-protein ligase that mediates 'Lys-63'-linked ubiquitination of MAP3K14/NIK, leading to stabilize and activate MAP3K14/NIK. It thereby acts as an activator of the non-canonical NF-kappa-B2/NFKB2 pathway. May also play an important role in cell proliferation and/or anti-apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:12738986}.
Interaction partners:
- Protein cereblon
- Ciliary neurotrophic factor
Sequence:
MPGETEEPRPPEQQDQEGGEAAKAAPEEPQQRPPEAVAAAPAGTTSSRVLRGGRDRGRAAAAAAAAAVSRRRKAEYPRRRRSSPSARPPDVPGQQPQAAKSPSPVQGKKSPRLLCIEKVTTDKDPKEEKEEEDDSALPQEVSIAASRPSRGWRSSRTSVSRHRDTENTRSSRSKTGSLQLICKSEPNTDQLDYDVGEEHQSPGGISSEEEEEEEEEMLISEEEIPFKDDPRDETYKPHLERETPKPRRKSGKVKEEKEKKEIKVEVEVEVKEEENEIREDEEPPRKRGRRRKDDKSPRLPKRRKKPPIQYVRCEMEGCGTVLAHPRYLQHHIKYQHLLKKKYVCPHPSCGRLFRLQKQLLRHAKHHTDQRDYICEYCARAFKSSHNLAVHRMIHTGEKPLQCEICGFTCRQKASLNWHMKKHDADSFYQFSCNICGKKFEKKDSVVAHKAKSHPEVLIAEALAANAGALITSTDILGTNPESLTQPSDGQGLPLLPEPLGNSTSGECLLLEAEGMSKSYCSGTERVSLMADGKIFVGSGSSGGTEGLVMNSDILGATTEVLIEDSDSAGP