wanglab/gogpt-training-data huggingface dataset:
Protein: Rho guanine nucleotide exchange factor 9 (Collybistin) (Rac/Cdc42 guanine nucleotide exchange factor 9) (A0A1B0GV84)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MANRELAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFVRLWVNQEDEVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMSTERHYIKHLKDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNNDDPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQASVLDWEGEDILDRSSELIYTGEMAWIYQPYGRNQQRVFFLFDHQMVLCKKDLIRRDILYYKGRIDMDKYEVVDIEDGRDDDFNVSMKNAFKLHNKETEEIHLFFAKKLEEKIRWLRAFREERKMVQEDEKIGFEISENQKRQAAMTVRKVPKQKGVNSARSVPPSYPPPQDPLNHGQYLVPDGIAQSQVFEFTEPKRSQSPFWQNFSRCLGSIDRSMEGFKTEPT
Protein: Clathrin heavy chain (Q38B01)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR002290}. Membrane, coated pit {ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR002290}.
Interaction partners:
- AP-1 complex subunit gamma
- AP complex subunit beta
- Clathrin coat assembly protein, putative
- AP complex subunit beta
- AP-4 complex subunit epsilon
- AP complex subunit sigma
- Coatomer subunit alpha
- AP complex subunit sigma
- AP complex subunit sigma
- Mu-adaptin 4, putative
Sequence:
MDNPLTSAEVFQLNSVSGGLRPGTISFKTLTLQSDKYVCIRDVQPDGQTSLVIVDLGKRESMRNSIRDAESAIMNPMAKILALRSGRNLQIFDVDAANRLKVVVFNEDVVYWCWIDARTVGIVSNTAVYHWSLDTAADAPPQLVFSRAPEFDASFQVLSYQTDEQKKWLMLCGVMRTAEGMVGKTQLFSVENNSGRVLDGHSGTFISTNTPTDPRSCNLMCLAWNNPSTGGKILIMELPTGSKTDLTVQRRMIDVPFAQGDFPVATHVSPRHKLLTVVTSRGSVVLMDLFTGVVIKTHQLPNNTIFCGTPYTKTGGILCVNNAGSVFHVSPNDNTIVPFVKNQLQNADLALRIAGSANLGGVDDLYRVQLDNQLRAGNIEEAVRTCLRAPNNALRGPDILSRFQLMPPIPGQQPAISTYFKVAVAETTLNAHESAELARAVIPKGGVDYVKQQYAADKLTASEELGDLMSAADPELAIKIYHKAEAHAKVVGVLLQRNETQKAVEYCKRAGFTPNWRVILNNAIHVNPQGAVGLAQVLHRDMGDAPVVDPIEVVDMFVTAQHIQQATEFVLEVLRDNTGENTKDLQTKLLEINLKHSHPSVAEKIFARGVCVHFDAMLLAPLCERASLPQRAIECYVMAQRMDPGIDNLANIRRCFSNAQVLSPDWVIEFFGKLSPGDSMKCLEDLLANHHQNFKIIVQVATKYNEALGADKLINVFLERKLFDILYYYLGAVVPYTRDPEVHFRYIEAAAEVGQVQELERMTRESPCYDPERTKNYLKNKKMTNLWPLINVCDQHNFVDELIRYLIDTNNEALIEQYVQRRNPLKTPAVVGALIDCNVQEDFIKNILNSVGTMCPIAELVDVAEERSRLRLIGPWLEARLAEKKTDTALHNAIAKLLVISGNLPEKFIEENDYYDPVVMGKYCEDRDPNLSYLVYRKAKMSTELVEITSKNGMWKQLARYLVKQQDPALWASVLTESSINRDRLVEAVQQTALPESEVTEEVSTTVKAFMDAELTEELTSILDQIVVRGRFRKNRYLENLLIMSAVRASKAKVMEYVTTLDSYDAKEIAGIATAAELHEEAMTVYDKFEMRMEAATVLLRDLKDLPRGRLYAQRCNLPAVWTVLGEYLLAAGEVREAIEVLIRAKNPNYVDAVTAAAERSNQFGDLVKYLNMARQESTSNDNKIESVLLLTYARTGRLSELEELLQNTHNVQIQPVADKCFEDGYYDSARLLYSMSMNFHKLALTLVRMNNLAEAVDAAQKAQSRSTWDAVNHACIEANDVRLAAICAVPLVLQVESLQDVVNRYEAYGLYDELFAVLKSASTNSGAHMGIFTEMGLQLAKYKPEKLLEHVHMYSKKINAHKLISVCEEYHHWLALRVLHVGNEDWLAAAKTMMCHFADAFDHDVFKDVASHLGASDFVYNAISFYVNTCPQNLCDFLTSMFKVLDPDRVLREVKNVAPIHLILPYLESAQPRNSRLINDALNDLYVEEENFVALRNSVENYNNFDSVELSARLEKMELFEFRKIALFLHRRHKAFDHALAVAKENKLFQEAIDTAVESADPKVVEELLDFFAVERPDSFVSCLYACYDYLSPDVVLEKAWLNNRINIAMPYLIQAIHDFTQRVSRLEKGANDGMQPSKDGSRRGGVPGYAGGNDPLMIQAGPAQPMGVPMHNVNIHPQPGYGGVPGQGYAGGMGNPNMMPY
Protein: Monoterpene synthase like 1, chloroplastic (PcTPS-mono1) (EC 4.2.3.-) (R9QMY7)
Organism: Pinus contorta (Shore pine) (Lodgepole pine)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MDLISVLPSTSKSCVCMHKPLSSSTHKLKPFCRTIRILGMPRPRKSVLMASSMSMSVNTLVSDDDIQRRTGGYHSNLWNDDVIQFLSTPYGELAYRERGERLIDEVRDIFSSMSLEDGEFSDLIQRLWMVDNVERLGIDRHFKNEIKSALDYVYSYWSEKGIGCGTKSIITNLNSTALGFRTLPLHGYPVSADVLKHFRNQIGQFVSCPSETEEDIRSMVNLYRASLIAFPGEEVMEEAESFSEKYLKETLQKIPDCSLSREIGDVLEHGWHTNLPRFEARNYIDVFGQDTKNMESNRKTEKLLELAKLEFNIFQSIQKTELESLLRWWNDSGSPQITFTRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITVLDDMYDLFGTVEELKLFTAAIKRWDPSATDCLPQYMKGIYMMVYNTVNEMSAEAQKAQGRDTLNYARQAWEVYLDSYMQEAKWIATGYLPTFEEYLENGKVSSGHRVSALQPMLTMDIPFPPHILKEVDFPSNLNDLACAILRLRGDTRCYQEDRARGEETSCISCYMIDNPGATEEDALNHLNVMISGVIKELNWELLKPDSSVPISSKKINFDITRAFHYGYKYRDGYSVSSVETKSLVMRTLLEPVPL
Protein: Protein RecA (Recombinase A) [Cleaved into: Endonuclease PI-MtuI (EC 3.1.-.-) (Mtu RecA intein)] (P9WHJ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Regulatory protein RecX
- LexA repressor
- DNA polymerase I
- DNA repair protein RadA
- DNA-directed RNA polymerase subunit beta
- DNA polymerase IV 1
- DNA topoisomerase 1
- 5'-3' exonuclease
- Crossover junction endodeoxyribonuclease RuvC
- ATP-dependent DNA helicase UvrD1
Sequence:
MTQTPDREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNKCLAEGTRIFDPVTGTTHRIEDVVDGRKPIHVVAAAKDGTLHARPVVSWFDQGTRDVIGLRIAGGAIVWATPDHKVLTEYGWRAAGELRKGDRVAQPRRFDGFGDSAPIPADHARLLGYLIGDGRDGWVGGKTPINFINVQRALIDDVTRIAATLGCAAHPQGRISLAIAHRPGERNGVADLCQQAGIYGKLAWEKTIPNWFFEPDIAADIVGNLLFGLFESDGWVSREQTGALRVGYTTTSEQLAHQIHWLLLRFGVGSTVRDYDPTQKRPSIVNGRRIQSKRQVFEVRISGMDNVTAFAESVPMWGPRGAALIQAIPEATQGRRRGSQATYLAAEMTDAVLNYLDERGVTAQEAAAMIGVASGDPRGGMKQVLGASRLRRDRVQALADALDDKFLHDMLAEELRYSVIREVLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEGEQLGQGKENARNFLVENADVADEIEKKIKEKLGIGAVVTDDPSNDGVLPAPVDF
Protein: Mitochondrial ribosomal protein L48, isoform A (Mitochondrial ribosomal protein L48, isoform B) (RE01048p) (Q9VQ35)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein mL51
- Large ribosomal subunit protein mL49
- Small ribosomal subunit protein mS40
- GH07821p
- Large ribosomal subunit protein mL40
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein mL42
- Large ribosomal subunit protein uL30m
- Large ribosomal subunit protein mL45
Sequence:
MLRRILPSVRLALQVPKATTTAVRSTSGSVYEPDYLESLKPKFPQYESLNVQIKGYDYPQLESYQRFLHGLAEYLDLDVSDCYALPPQKTTVQRLRPNSTVIESEYKLTTYERNLQLNNVDAPVYPQFLRLAQAALPEGVSLQVQEYTDDCEERRYVPDKELLDLKDELERMGGPTTTRKK
Protein: Trace amine-associated receptor 13d (Q5QNQ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDLSSQEYDPSQFCFPAVNNSCLKGTHHVSTQTVVYLILASAMTVTILGNSVVIISIAHFKQLQTTTNILVMSLALADLLLGLVVMPFSMIRSVDGCWYYGETFCMLHSSFDLFLTSVSIFHLIFIAVDRHQAVCFPLQYPTMITIPVAWVMVMISWSMAALYSYGLVYSKANMEGLDEYIQSMYCVGGCTLYFNALWSVLDTLITFFLPCSVMIGLYARIFVVAKKHARIINEANQNEIDGTFKSSRRSEQKAAKTLGIVVGAFIMCWLPFFINSLMDPYINFSTPVALFEAFVWLGYINSTMNPIIYGFFYPWFRKTLYLIITRRIFEPNSSDINIFTL
Protein: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMN/NaMN adenylyltransferase 2) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 2) (NMN adenylyltransferase 2) (Nicotinate-nucleotide adenylyltransferase 2) (NaMN adenylyltransferase 2) (Q0HA29)
Organism: Rattus norvegicus (Rat)
Function: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons (By similarity). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Also acts as an activator of ADP-ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16 (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8BNJ3}; Lipid-anchor {ECO:0000250|UniProtKB:Q8BNJ3}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8BNJ3}; Lipid-anchor {ECO:0000250|UniProtKB:Q8BNJ3}. Cytoplasm {ECO:0000250|UniProtKB:Q9BZQ4}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BNJ3}. Note=Delivered to axons with Golgi-derived cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q8BNJ3}.
Interaction partners:
- Nicotinate phosphoribosyltransferase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Glutamine-dependent NAD
- Nicotinamide phosphoribosyltransferase
- NAD kinase
- Nicotinamide riboside kinase 1
- NAD-dependent protein deacetylase
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- NAD-dependent protein deacetylase sirtuin-1
- 5'-nucleotidase
Sequence:
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQHENTQPIYQNSNVPTKPTAAKILGKVGESLGRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADADRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG
Protein: Early growth response protein 1 (EGR-1) (AT225) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor ETR103) (Transcription factor Zif268) (Zinc finger protein 225) (Zinc finger protein Krox-24) (P18146)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (By similarity). Binds double-stranded target DNA, irrespective of the cytosine methylation status. Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Activates expression of p53/TP53 and TGFB1, and thereby helps prevent tumor formation. Required for normal progress through mitosis and normal proliferation of hepatocytes after partial hepatectomy. Mediates responses to ischemia and hypoxia; regulates the expression of proteins such as IL1B and CXCL2 that are involved in inflammatory processes and development of tissue damage after ischemia. Regulates biosynthesis of luteinizing hormone (LHB) in the pituitary (By similarity). Regulates the amplitude of the expression rhythms of clock genes: BMAL1, PER2 and NR1D1 in the liver via the activation of PER1 (clock repressor) transcription. Regulates the rhythmic expression of core-clock gene BMAL1 in the suprachiasmatic nucleus (SCN) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:20363028}. Cytoplasm {ECO:0000269|PubMed:20363028}.
Interaction partners:
- Protein c-Fos
- NGFI-A-binding protein 1
- NGFI-A-binding protein 2
- Transcription factor Jun
- Protein FosB
- E3 SUMO-protein ligase EGR2
- Transcription factor JunB
- Cellular tumor antigen p53
- Mitogen-activated protein kinase 3
- Transcription factor JunD
Sequence:
MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGAPEGSGSNSSSSSSGGGGGGGGGSNSSSSSSTFNPQADTGEQPYEHLTAESFPDISLNNEKVLVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPASSSSAPSPAASSASASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPAAKGGFQVPMIPDYLFPQQQGDLGLGTPDQKPFQGLESRTQQPSLTPLSTIKAFATQSGSQDLKALNTSYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASSATSSLSSYPSPVATSYPSPVTTSYPSPATTSYPSPVPTSFSSPGSSTYPSPVHSGFPSPSVATTYSSVPPAFPAQVSSFPSSAVTNSFSASTGLSDMTATFSPRTIEIC
Protein: Probable LRR receptor-like serine/threonine-protein kinase At5g63710 (EC 2.7.11.1) (Q8W4S5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Mitochondrial arginine transporter BAC1
Sequence:
MAHSGNGESFHDPLRGFIQRNCFRWNNQKLILQCFMALAFVGITSSTTQPDIEGGALLQLRDSLNDSSNRLKWTRDFVSPCYSWSYVTCRGQSVVALNLASSGFTGTLSPAITKLKFLVTLELQNNSLSGALPDSLGNMVNLQTLNLSVNSFSGSIPASWSQLSNLKHLDLSSNNLTGSIPTQFFSIPTFDFSGTQLICGKSLNQPCSSSSRLPVTSSKKKLRDITLTASCVASIILFLGAMVMYHHHRVRRTKYDIFFDVAGEDDRKISFGQLKRFSLREIQLATDSFNESNLIGQGGFGKVYRGLLPDKTKVAVKRLADYFSPGGEAAFQREIQLISVAVHKNLLRLIGFCTTSSERILVYPYMENLSVAYRLRDLKAGEEGLDWPTRKRVAFGSAHGLEYLHEHCNPKIIHRDLKAANILLDNNFEPVLGDFGLAKLVDTSLTHVTTQVRGTMGHIAPEYLCTGKSSEKTDVFGYGITLLELVTGQRAIDFSRLEEEENILLLDHIKKLLREQRLRDIVDSNLTTYDSKEVETIVQVALLCTQGSPEDRPAMSEVVKMLQGTGGLAEKWTEWEQLEEVRNKEALLLPTLPATWDEEETTVDQESIRLSTAR
Protein: Peroxisomal adenine nucleotide carrier 1 (AtPNC1) (Q9MA90)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Peroxisomal adenine nucleotide transporter catalyzing the counterexchange of ATP with AMP. ATP is needed by reactions that generate acyl-CoA for peroxisomal fatty acid beta-oxidation during postgerminative growth. Required for the beta-oxidation reactions involved in auxin biosynthesis and for the conversion of seed-reserved triacylglycerols into sucrose that is necessary for growth before the onset of photosynthesis.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:19073762, ECO:0000269|PubMed:19073763}; Multi-pass membrane protein {ECO:0000269|PubMed:19073762, ECO:0000269|PubMed:19073763}.
Interaction partners:
- ABC transporter D family member 1
- Peroxisome biogenesis protein 19-1
- Peroxisome biogenesis protein 19-2
- Enoyl-CoA delta isomerase 1, peroxisomal
- ADP,ATP carrier protein 1, mitochondrial
- Phospholipase A1-IIgamma
- Dihydropyrimidinase
- Mitochondrial adenine nucleotide transporter ADNT1
- Peroxisomal 2,4-dienoyl-CoA reductase [
- Peroxisome biogenesis protein 16
Sequence:
MGVDLESVSEATSGAIGSLLSTTILYPLDTCKSKFQAEVRARGQQKYRYLSDVMWEAISKGQVFSLYQGLGTKNFQSFISQFIYFYSYSYFKRVHSERTGSKSIGTKANLLIAAAAGACTSVLIQPLDTASSRMQTSEFGESKGLWKTLTEGSWADAFDGLGISLLLTSNPAIQYTVFDQLKQHLLKQKNAKAENGSSPVVLSAFMAFVLGAVSKSVATVLTYPAIRCKVMIQAADESKENETKKPRRRTRKTIPGVVYAIWRKEGMLGFFKGLQAQILKTVLSSALLLMIKEKITATTWILILAIRRTLFLTNTKGKLRSP
Protein: GH02377p (Q95SS9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMAGIVLRMAFLIQVPFPRSCTRNLLSFPIALLSPLLYLSTFCACSNLIPAALIDVHKDALDLSHLRGKEQVGFWTQLSVLLRRHLRSMSRDMFAVQMRLVMHVVVALLLGVVYWQIGGDAQKIVSNVSCLFFCDTLRVRRQCHALDPAVHAGLGGVHQGVLQRMVLPGSLLSVQGPGRSAPAADLSHNVHQHRLLHDGSATGIPTICHVLGPVRDDRLHWPLHRGDRRLPVHHAVGHIPGAQCHHSVPPVLRLLYSAERALLVSAPHLRRVLLQVHLRGSDASHLWIRSRGTGVLCHKQLLLLQNGGAVPQGLPDGGQ
Protein: Uncharacterized protein (A0A453YY93)
Organism: Anopheles gambiae (African malaria mosquito)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDRIVLVALVAGCLLVAVAAQADYIQQEQCVTASNRAGYCTTKAECPDQEQLDLRAATCSDATHYCCPDRSEQLPSRNRPKLLTQCDSNRGYCVKGDACSVRTFRLRSNRCPAYEEVCCPKNAFPEEFHATQVAKHDLSMGATTSTTSTTATTTTTTTTTTTTTTTTTTPNPVGESDQILEIQASTTPVSATTANSLGTSLDAQSIEGTGASEPTKLPIPLRPITPDQQTVESSGVNNTTDSIEKSAKPTTNTSDAQLELTSSSESNDLVTSIIDTALVDDNSLQETDTTTIPVIPPNAADPPPTPALTAQFTPESFSYQDCGQLNLNGVVQRTINEDFRAEYGEFPWMVALFQLPEQRYCCNGALIDPKAILTTAHCVTNCGGRAANIMVRFGEWNMSSTHEMAIPREDIGVKSVHQHPRYSPSALLNNIAVLELAHPVQYQATIQPVCLPSANQPLRAMENMIATGWGRVMEENAPPTQILKRLDLQRMEPSICREALRRVRRPYPFILDSSFVCSTTNHGDQERPCDGDAGAPVVVELPGTTNRYYLHGLVSWGYGCHQKQIPYTVLTKVVHFREWIDRIVLGFKKKVKKGHSKQRE
Protein: 5-cytosine rRNA methyltransferase nsun-4 (EC 2.1.1.-) (5-cytosine tRNA methyltransferase nsun-4) (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 4) (RNA cytosine C(5)-methyltransferase nsun-4) (rRNA cytosine C(5)-methyltransferase nsun-4) (tRNA cytosine C(5)-methyltransferase nsun-4) (Q95XR2)
Organism: Caenorhabditis elegans
Function: Mitochondrial methyltransferase which methylates cytosine to 5-methylcytosine (m5C) in rRNAs and tRNAs at multiple sites. May play a role in the translation of leucine and proline codons (Probable).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96CB9}.
Interaction partners:
- Mitochondrial transcription termination factor family protein
- GTPase Era, mitochondrial
- G domain-containing protein
- Nucleolar complex protein 2 homolog
- Ribosome biogenesis protein BRX1 homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Nucleolar GTP-binding protein 1
- Probable rRNA-processing protein EBP2 homolog
- 26S rRNA
- 26S rRNA
Sequence:
MSCLRQSSQSFYFTQIRWKTVKFKTKIAKTKPLKTPSAQALDHFDFYYGPLFGKKWPSIRLGLLSPNRYLAVMNTMSRNWQAHDEILSDMGAKDLLASIRGKAEDQAIETKRKSVEEKANRETQKVKHEISNPSTSTNTEDSEPDEAIFRSAAGLGEFRASAGELSSGSLQMGLGQSNQNKNVEITGFEGEGVRIPKRDHFFYYPQALHVRSFDRAVLLDFPAPMKDEVGVPSYWLLDGGSLLPVLALGLQKDDSLLDMCAAPGGKSLLAALSNLPSKIVCNDFKLARLGQLKRALMTYVPEDSETIDKFVLKRKDASDVKTWDEFEAYDKVLVDVPCSTDRLSVSTDDGNLFSTGSTQQRLDLPVLQTKILVNALRSVKVGGSVVYSTCTLSPSQNEAVVENAVAVVRNDFGIVTVEESLHQLVSHMTSSGLYRFHDTPLGALVVPFLPSNFGPMYICKLTRLQ
Protein: U6 snRNA-associated Sm-like protein LSm5 (P62322)
Organism: Mus musculus (Mouse)
Function: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y4Y9}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm3
- U6 snRNA-associated Sm-like protein LSm1
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein F
Sequence:
MAANATTNPSQLLPLELVDKCIGSRIHIVMKSDKEIVGTLLGFDDFVNMVLEDVTEFEITPEGRRITKLDQILLNGNNITMLVPGGEGPEV
Protein: ATP synthase F(1) complex subunit gamma, mitochondrial (ATP synthase F1 subunit gamma) (F-ATPase gamma subunit) (P05631)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:1827992, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Peripheral membrane protein {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Matrix side {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:95168}.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
Sequence:
MFSRAGVAGLSAWTVQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTHSDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFSLDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD
Protein: Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 (EC 2.4.1.-) (Forssman glycolipid synthase-like protein) (Q8N5D6)
Organism: Homo sapiens (Human)
Function: Has lost the ability to synthesize Forssman glycolipid antigen (FORS1/FG). Might have acquired an alternative function in glycosphingolipid metabolism, but it remains to be established. It appears to have drifted more slowly than confirmed pseudogenes in the glycosyltransferase 6 family, suggesting that it has remained under evolutionary pressure.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
- Beta-1,3-galactosyltransferase 5
- Alpha-N-acetylgalactosaminidase
- Beta-hexosaminidase subunit alpha
- Beta-hexosaminidase subunit beta
Sequence:
MHRRRLALGLGFCLLAGTSLSVLWVYLENWLPVSYVPYYLPCPEIFNMKLHYKREKPLQPVVWSQYPQPKLLEHRPTQLLTLTPWLAPIVSEGTFNPELLQHIYQPLNLTIGVTVFAVGKYTHFIQSFLESAEEFFMRGYRVHYYIFTDNPAAVPGVPLGPHRLLSSIPIQGHSHWEETSMRRMETISQHIAKRAHREVDYLFCLDVDMVFRNPWGPETLGDLVAAIHPSYYAVPRQQFPYERRRVSTAFVADSEGDFYYGGAVFGGQVARVYEFTRGCHMAILADKANGIMAAWREESHLNRHFISNKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKDISCLRS
Protein: Endoplasmic reticulum junction formation protein lunapark (ER junction formation factor lunapark) (O94414)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in tubular endoplasmic reticulum network formation and maintenance.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Note=Localizes to three-way ER tubule junctions. {ECO:0000250}.
Interaction partners:
- Reticulon-like protein 1
- Lap-Emerin-Man domain protein 2
Sequence:
MGWFFQKKKEFDFGGELDRLEMKLEEAQYNIDNIQSQKKKILFRYTVCSLAIYTIGMAVWASRSSILFQHPLFSKLFRISLYILGVFSLYMFRWAIAWFCEKRLSRARMNLHKLNAEKRKILDALKSRKEYFETQALLEKYGEQPTLAQKKLSNAAAAKSVPGSSSSSSDPMHPQHWYDRVLEGLVGANENSENNREALICSHCFHHNGLASYGEKASDVRYVCLFCKAWNGPPIDKSLPSSEMDSNLQTNPSSISKGKKNNSNNTTQKGPNIISSPQVINASSPVRKAGKKKSKKALPTSPLSSSSPDASYNSVSDSFHTVAASVPESLTPTK
Protein: ER lumen protein-retaining receptor B (Q8VWI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Determines the specificity of the luminal endoplasmic reticulum protein retention system. Required for the retro-transport of calreticulin-3 (CRT3) from the Golgi to the ER. Specifically required for elongation factor Tu receptor (EFR) function in response to the pathogen-associated molecular pattern (PAMP) elf18.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:19717464}; Multi-pass membrane protein {ECO:0000269|PubMed:19717464}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:19717464}; Multi-pass membrane protein {ECO:0000305|PubMed:19717464}.
Interaction partners:
- At3g27230
- Stromal cell-derived factor 2-like protein
- Tetratricopeptide repeat
- MIF4G domain-containing protein
- Uncharacterized protein AT4g35690
- Protein involved in starch initiation 1
- Probable diphthine methyl ester synthase
- Pentatricopeptide repeat
- F-box protein At1g70590
- At4g12840
Sequence:
MNIFRLAGDMTHLASVLVLLLKIHTIKSCAGVSLKTQELYAIVFATRYLDIFTSFVSLYNTSMKLVFLGSSFSIVWYMKYHKAVHRTYDREQDTFRHWFLVLPCFLLALLIHEKFTFLEVLWTSSLYLEAVAILPQLVLLQRTRNIDNLTGQYIFLLGGYRGLYILNWIYRYFTEPHFVHWITWIAGFVQTLLYADFFYYYFLSWKNNKKLQLPA