wanglab/gogpt-training-data huggingface dataset:
Protein: Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (EC 6.2.1.4) (GTP-specific succinyl-CoA synthetase subunit beta) (G-SCS) (GTPSCS) (Succinyl-CoA synthetase beta-G chain) (SCS-betaG) (Q9Z2I8)
Organism: Mus musculus (Mouse)
Function: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03221}.
Interaction partners:
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Methylmalonyl-CoA mutase, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
Sequence:
MASPVAIAAQAGKLLRERALRPLLAVRSQAGHLTPRRWLNLQEYQSKKLMSEHGVRVQRFFVANTAKEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPKVVGELAQQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSHNGPVIVGSPQGGVDIEEVAASSPELIFKEQIDIFEGIKDSQAQRMAENLGFLGSLKNQAADQITKLYHLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAARYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYEAFKLLTSDPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQNILKSSGLPITSAVDLEDAAKKAVASVAKK
Protein: LPS-assembly lipoprotein LptE (Q8ZQZ7)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01186}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01186}.
Interaction partners:
- LPS-assembly protein LptD
- Lipopolysaccharide export system protein LptC
- Lipopolysaccharide export system protein LptA
- Leucine--tRNA ligase
- DNA polymerase III subunit delta
- Outer membrane protein assembly factor BamC
- Outer membrane protein assembly factor BamA
- Nicotinate-nucleotide adenylyltransferase
- Outer membrane protein assembly factor BamD
- Outer-membrane lipoprotein LolB
Sequence:
MRYLVTLLLSLAVLVTAGCGWHLRSTTQVPASMKTMILDSGDPNGPLSRAVRNQLRLNNVNLLDKDTTRKDVPSLRLGTVTILQDTASVFQDGQTAEYQMVMTVNASVLIPGHDIYPISTKVYRSFFDNPQMALAKDNEQAMIVQEMYDKAAEQLIRKLTSVRAADIQATKEEATADNETAAPASTPARVSTTLSN
Protein: ST14 transmembrane serine protease matriptase (A0A8I6AEJ8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MGNNRGRKAGGGSQDFGAGLKYNSRLENMNGFEEGVEFLPVNNAKQVEKRGPRRWVVMVAVVFSFLLLSLMAGLLVWHFHYRNVRIQKVFNGHLRITNENFLDAYENSTSTEFISLASQVKEALKLMYSEVPVLGPYHKKSTVTAFSEGSVIAYYWSEFSIPPHLEEEVDRAMAVERVVTLPPRARALKSFVLTSVVAFPIDPRMLQRTQDNSCSFALHARGRTVTRFTTPGFPNSPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPHAVVRLCGTFSPSYNLTFLSSQNVFLVTLITNTDRRHPGFEATFFQLPKMSSCGGLLSEAQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNIPVGSCTKDYVEINGEKFCGERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEYLSYDSNDRCNATHQFMCKNQFCKPLFWVCDSVNDCGDGSDEEGCSCPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDEASCDNVNAVSCTKYTYRCQNGLCLNKGNPECDGKKDCSDGSDEKNCDCGLRSFTKQARVVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDETIFKYSDHTMWTAFLGLLDQSKRSASGVQEHKLKRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQTTCEELLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWIKEQTGV
Protein: Afadin (Afadin adherens junction formation factor) (Protein Af-6) (O35889)
Organism: Rattus norvegicus (Rat)
Function: Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:9334353}. Note=Not found at cell-matrix AJs. {ECO:0000269|PubMed:9334353}.
Interaction partners:
- Tight junction protein ZO-1
- Tight junction protein 2
- Nectin-3
- Occludin
- Junctional adhesion molecule A
- Nectin-1
- Vinculin
- GTP-binding protein
- PDZ domain containing 11
- Protein jagged-1
Sequence:
MSAGGRDEERRKLADIIHHWNANRLDLFEISQPTEDLEFHGVMRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGERRLDIDEKPLVVQLNWNKDDREGRFVLKNENDAIPAKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKEERPSQGDDSENSRLAAEVYKDMPETSFTRTISNPEVVMKRRRQQKLEKRMQEFRSSDGRPDSGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAESLEKYGLEKENPKDYCIARVMLPPGAQHSDERGAKEIILDDDECPLQIFREWPSDKGILVFQLKRRPPDYIPKKMKKHVEGKPLKGKDRADGSGYGSALPPEKLPYLVELSPGRRNHFAYYSYHTYEDGSDSRDKPKLYRLQLSVTEVGTEKFDDNSIQLFGPGIQPHHCDLTNMDGVVTVTPRSMDAETYVDGQRISETTMLQSGMRLQFGTSHVFKFVDPIQDHVLSKRSVDGGLMVKGPRHKPGAVQETTFELGGDIHSGTALPASRSTTRLDSDRVSSASSTAERGMVKPMIRLDQEQDYRRRESRTQDAAGPELMLPASIEFRESSEDSFLSAIINYTNSSTVHFKLSPTYVLYMACRYVLSSQHRPDISPTERTHKAIAVVNKMVSMMEGVIQEVDQVDQKQKNIAGALAFWMANASELLNFIKQDRDLSRITLDAQDVLAHLVQMAFKYLVHCLQSELNNYMPAFLDDPEENSLQRPKIDDVLHTLTGAMSLLRRCRVNAALTIQLFSQLFHFINMWLFNRLVTDPDSGLCSHYWGAIIRQQLGHIEAWAEKQGLELAADCHLSRIVQATTLLTMDKYVPDDIPNINSTCFKLNSLQLQALLQNYHCAPDEPFIPTDLIENVVAVAENTADELARSDGRDVQLEEDPDLQLPFLLPEDGYSCDVVRNIPNGLQEFLDPLCQRGFCRLVPHTRSPGTWTIYFEGADYESHLMRENTELTQPLRKEPEVITVTLKKQNGMGLSIVAAKGAGQDKLGIYVKSVVKGGAADVDGRLAAGDQLLSVDGRSLVGLSQERAAELMTRTSSVVTLEVAKQGAIYHGLATLLNQPSPMMQRISDRRGSGKPRPKSEGFELYNNSAQNGSPESPQMPWTEYSEPKKLPGDDRLMKNRADHRSSPNVANQPPSPGGKSPYTSGTAAKITSVSTGNLCTEEQTPPPRPEAYPIPTQTYTREYFTFPASKSQDRMAPVQNQWPNYEEKPHMHTESDHASIAIQRVTRSQEELREEKVYQLERHRVESGMDRKCDSDMWINQSSSVESSTSSQEHLNHSSKSVTPASTLTKSGPGRWKTPAAVLPTPVAVSQPIRTDLPPPPPPPPAHYTSDFDGISMDLPLPPPPANQAAPQSAQVAAAERKKREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQSLNPASFSPLATQAKPEKPSTLQRPQETVIRELQPQQQPRTIERRDLQYITISKEELSSGDSLSPDPWKRDAREKLEKQQQMHIVDMLSKEIHELQNKGDRTAEESDRLRKLMLEWQFQKRLQESKQKDEDDDEEEDDDVDTMLIMQRLEAERRARLQDEERRRQQQLEEMRKREVEDRVRQEEDGRHQEEERVKRDAEEKRRQEEGYYSRLEAERRRQHEEAARRLLEPEEPGLSRPPLPQDYEPPSQSSAPSAPPPPPQRNASYLKTQVLSPDSLFTAKFVAYDDDDEEENYVPAGPNSYSGSAGTTAGTYDAPRDTREKLSRSQDADLPGSSGAPENLTFRERQRLFSQGQDVSDKVKASRKLTELENELNTK
Protein: Heterogeneous nuclear ribonucleoprotein R (Q566E4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein U
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein M
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 3
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein Q
- Heterogeneous nuclear ribonucleoprotein H
Sequence:
MANQVNGNAVQLKEEEEPMDTSSVTHTEHYKTLVEAGLPQKVAERLDEIFQTGLVAYVDLDERAIDALREFNEEGALSVLQQFKESDLSHVQNKSAFLCGVMKTYRQREKQGSKVQESTKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGVQPGIGTEVFVGKIPRDLYEDELVPLFEKAGPIWDLRLMMDPLSGQNRGYAFITFCGKEAAQEAVKLCDSYEIRPGKHLGVCISVANNRLFVGSIPKNKTKENILEEFSKVTEGLVDVILYHQPDDKKKNRGFCFLEYEDHKSAAQARRRLMSGKVKVWGNVVTVEWADPVEEPDPEVMAKVKVLFVRNLATTVTEEILEKSFSEFGKLERVKKLKDYAFVHFEDRGAAVKAMDEMNGKEIEGEEIEIVLAKPPDKKRKERQAARQASRSTAYEDYYYHPPPRMPPPMRGRGRGGRGGYGYPPDYYGYEDYYDDYYGYDYHDYRGGYEDPYYGYDDGYAVRGRGGGRGGRGAPPPPRGRGAPPPRGRAGYSQRGAPLGPPRGSRGGRGGPAQQQRGRGSRGARGNRGGNVGGKRKADGYNQPDSKRRQTNNQQNWGSQPIAQQPLQQGGDYSGNYGYNNDNQEFYQDTYGQQWK
Protein: 3',5'-cyclic-AMP phosphodiesterase (EC 3.1.4.53) (Q3TAQ1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKEQGGTVSGAASSRGGGDSAMASLQPLQPNYLSVCLFPEESYQKLAMETLEELDWCLDQLETIQTYRSVSEMASNKVRTPLSLTTTGAPGSSLSVDLVEVRQHFLCSYLATTVS
Protein: PH domain-containing protein DDB_G0274775 (Q86IV4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSEPELKVSVSQLAPSDREGWLTKQGGSIRTWRRRWFVLKGKKLFYFKSKGDIEATGLIELEQNSFVKEEKDKDKKKKYMFTVGTSKRVFYIFAETETDMKQWMESIKRNLDGEGGMKSGGNDIVSSPKINSEPTPKVNQNGSAPEKSSLSSPRSKISNAKSIIPFLREEESKVLEFWQIWSESIPPQSDLQSGTAIEFHVATSIDMQKLTWRTAGPQNIFIQKMVDFFWNVGAPESEIDRLNDVGAIINPVKIGSWIDMSDKGGMDGGWYFPVDIPLKLAIEASDAGEPTRKLSEWAESNEVVNCYSIGRDMGAAPPRQTETRFKLPGPDFIAQLNLAVDAFKTFEFPPIPSNALEILYQSSNTLEAGGLCLSVITSSEGFVRLGLLIPKPTRDVVGQLCEIGQANRERISKFETALGGCGPAFVEFQYLQKGFGYTVYKEGFDIVFHYMVGEDQSE
Protein: Wh11p (A0A1D8PHF8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Hsp12p
- Meiotic sister chromatid recombination protein 1
- Op4p
- Csh1p
- White-opaque regulator 1
- Csp37p
- Asr2p
- Asr1p
- Glyoxalase 3
Sequence:
MSDLGRKDIGDKIESKLTPDSQKSTPEQFKDKVTDSLDSAAGKATSENDKSFVQKASDAIFGDSK
Protein: Optic atrophy 3 protein homolog (Q1L9A2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May play some role in mitochondrial processes.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Transmembrane protein 126A
- Mitochondrial outer membrane protein SLC25A46
- Mitochondrial inner membrane m-AAA protease component paraplegin
Sequence:
MVVGAFPIAKLLYLGVRQLSKPVANRIKAGARRSEFFKNYICLPPAQAYHWIEMRTKMRIMGFRGSTIKPLNEDAAAELGAELLGEAIIFVIGGGCMVLEYSRQAANSRRKEEELAQSITSLQTQLGELALTTETLDAQIREVNRLLLSLPAAPSSK
Protein: Galactoside alpha-(1,2)-fucosyltransferase 2 (Alpha(1,2)FT 2) (Fucosyltransferase 2) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2) (GDP-fucose: beta-galactoside alpha1,2-fucosyltransferase) (MFUT-II) (Secretory blood group protein 2) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2) (EC 2.4.1.344) (Q9JL27)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
Interaction partners:
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Beta-1,3-galactosyltransferase 5
- Alpha-
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- Beta-1,3-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Beta-1,4-galactosyltransferase 1
Sequence:
MASAQVPFSFPLAHFLIFVFVTSTIIHLQQRIVKLQTLSEKELQAVQMSSPNAARTDMQQSAKLQGIFTINSIGRLGNQMGEYATLFALARMNGRLAFIPESMHNALAPIFRISLPVLHSDTARRIPWQNYHLNDWMEERYRHIPGQYVRFTGYPCSWTFYHHLRPEILKEFTLHDHVREEAQAFLRGLRVNGSQPSTFVGVHVRRGDYVHVMPKVWKGVVADRGYLEKALDRFRARYSSPVFVVTSNGMAWCRENINTSLGDVVFAGNGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLAGGDTIYLANYTLPDSPFLKIFKPAAAFLPEWMGIPADLSPLLKH
Protein: MALT1 paracaspase (K7EP42)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGEKGCTVTELSDFLQAMEHTEVLQLLSPPGIKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPNGNTSELIFNAVHVKDAGFYVCRVNNNFTFEFSQWSQLDVCDIPES
Protein: Uncharacterized protein (Q4GZ55)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKFLVVDGDWPVTPYTLTRSELVSHSVEEADGGSEGGQLIIHGHTLVALCQQQLHTSVVRVRAAPDLSTLGLTILHESLSDSTGNIRLVTPKSLTRQVFAVDDLLVHGRLIVFTSRWESLASAAIVGVKSDRREEHELTRRTKSRPEETKNSGRGNHDTSVSRPSVFSGRNRTALHKFTCAETYFQSIPPATVHDLDLLNNLIQAGTIRLDPRVEVYLCTVCGFLPRQTFTTSCCGAIMCGACTPLISTSSVMPSVMSERYVCIACKELPFTSHTAHVSRDAEVMKLVRELRVLHHPQLASAASATSSHGMAEKSHASLPFLLHSMGIMPAKRDVGGAAAPVLGSVFPNP
Protein: Probable galactinol--sucrose galactosyltransferase 4 (EC 2.4.1.82) (Raffinose synthase 4) (Q9SYJ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transglycosidase operating by a ping-pong reaction mechanism. Involved in the synthesis of raffinose, a major soluble carbohydrate in seeds, roots and tubers (By similarity).
Interaction partners:
- Alpha-galactosidase 2
- Alpha-galactosidase 1
- Alpha-galactosidase 3
- Beta-fructofuranosidase, insoluble isoenzyme CWINV3
- Beta-fructofuranosidase, insoluble isoenzyme CWINV5
- Acid beta-fructofuranosidase 3, vacuolar
- Beta-fructofuranosidase, insoluble isoenzyme CWINV4
- Beta-fructofuranosidase, insoluble isoenzyme CWINV6
- Beta-fructofuranosidase, insoluble isoenzyme CWINV2
- Acid beta-fructofuranosidase 4, vacuolar
Sequence:
MAPLHESLSSINDVIESKPLFVPITKPILQPNSFNLSEGSLCAKDSTPILFDVPQNVTFTPFSSHSISTDAPLPILLRVQANAHKGGFLGFTKESPSDRLTNSLGRFEDREFLSLFRFKMWWSTAWIGKSGSDLQAETQWVMLKIPEIDSYVAIIPTIEGAFRASLTPGEKGNVLICAESGSTKVKESSFKSIAYIHICDNPYNLMKEAFSALRVHMNTFKLLEEKKLPKIVDKFGWCTWDACYLTVDPATIWTGVKEFEDGGVCPKFVIIDDGWQSINFDGDELDKDAENLVLGGEQMTARLTSFKECKKFRNYKGGSFITSDASHFNPLKPKMLIYKATERIQAIILRRKLVKESGEQDLTELDEKIKILSEELNAMFDEVEKEESLGSDDVSGSGMAAFTKDLRLRFKSLDDIYVWHALCGAWNGVRPETMMDLKAKVAPFELSPSLGATMADLAVDKVVEAGIGLVHPSKAHEFYDSMHSYLASVGVTGAKIDVFQTLESLAEEHGGRVELAKAYYDGLTESMIKNFNGTDVIASMQQCNEFFFLATKQISIGRVGDDFWWQDPYGDPQGVYWLQGVHMIHCSYNSIWMGQMIQPDWDMFQSDHVCAEYHAASRAICGGPVYLSDHLGKASHNFDLIKKLAFFDGTIPRCVHYALPTRDSLFKNPLFDKESILKIFNFNKFGGVIGTFNCQGAGWSPEEHRFKGYKECYTTVSGTVHVSDIEWDQNPEAAGSQVTYTGDYLVYKQQSEEILFMNSKSEAMKITLEPSAFDLLSFVPVTELVSSGVRFAPLGLINMFNCVGTVQDMKVTGDNSIRVDVKGEGRFMAYSSSAPVKCYLNDKEAEFKWEEETGKLSFFVPWVEESGGISHLSFTF
Protein: KAT8 regulatory NSL complex subunit 2 (NSL complex protein NSL2) (Non-specific lethal 2 homolog) (Q9VAF4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSFSPNQLRQCARFTGTPCTPDKEHQLREQIHSELVKIKYCANPTYECSLMRIEGYEYCIRHILRDPRSNFRQCSHVYSNGRKCINAVAKYDNKKELILTTLCFEHNRQTQLQKTHMNVGRIRSRVETNETLLHSLSSHINVEDIKPEVKKIERDDDEIDVVSPHVTPFVTQDHRNSIGHVVESSRKRRRILDYASDSSSNDADPPCLRNTAQDIEFYESDHESIDSEDDDPLKHAGVFTRAEAVKIAETKLIKLQGLYREQISYLQNVLRQRRRKYLHDIRRERELYCSIHDQLKDTPHERKLYEQLKALNSYHRRQGVEAVLYKKLKEKRARDALYAAKSSSNPKCVFTEGGVKCGERTLPCCKHCRKHILEDKRQVLFRACGVERSGVVCQEPVASILEDSSCVLHLTVAPAKRQYIQKKCESETEEEETQSTSLISTIKKEEEDPSDKLYTSQALNVTTAHGEDNKGDVKPREYAPNRS
Protein: Oleosin L (Allergen Ses i 5) (Oleosin 15 kDa) (allergen Ses i 5.0101) (Q9XHP2)
Organism: Sesamum indicum (Oriental sesame) (Sesamum orientale)
Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Subcellular location: Lipid droplet {ECO:0000255|RuleBase:RU000540, ECO:0000269|PubMed:12450125, ECO:0000269|PubMed:16436145}. Membrane {ECO:0000255|RuleBase:RU000540}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU000540}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}.
Interaction partners:
Sequence:
MAEHYGQQQQTRAPHLQLQPRAQRVVKAATAVTAGGSLLVLSGLTLAGTVIALTIATPLLVIFSPVLVPAVITIFLLGAGFLASGGFGVAALSVLSWIYRYLTGKHPPGADQLESAKTKLASKAREMKDRAEQFSQQPVAGSQTS
Protein: tRNA 2'-phosphotransferase 1 (mTPT1) (EC 2.7.1.160) (Q8K3A2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Interaction partners:
- RNA-splicing ligase RtcB homolog
- tRNA-splicing endonuclease subunit Sen34
- ADP-ribosylhydrolase ARH3
- Protein mono-ADP-ribosyltransferase PARP10
- ADP-ribose glycohydrolase MACROD1
Sequence:
MNAPGGRRKEGRRTHRPREQDRNVQLSKALSYALRHGALKLGLPMRADGFVPLQALLQLPQFHSFSIEDVQLVVNTNEKQRFTLQPGEPSTGLLIRANQGHSLQVPELELTPLETPQALPLTLVHGTFWKHWPSILLKGLSRQGRTHIHLASGLPGDPGVISGIRPNCEVAVFIDGPLALTDGIPFFCSANGVILTPGNAEGFLLPKYFKEALQLRPTRKPLSLAGDKETETQSGPKLSSRGGRRKIQQ
Protein: Transcription factor MYBC1 (O22210)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that acts as a negative regulator of freezing tolerance via a CBF-independent pathway.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20331973}.
Interaction partners:
- UPF0496 protein At3g28290
- Myb domain protein 110
Sequence:
MREDNPNWFLRWEEELPSPEELIPISQTLITPHLALAFQIGSPNHHLGSKRTTAIYHQKLQSSTTPTTPTPTPPPMMMNSDFGGGDSTDLGSGSIGGEPARTLKRPRLVWTPQLHKRFVDAVGHLGIKNAVPKTIMQLMSVEGLTRENVASHLQKYRLYLRRMQGGNGNGITGGHVIVSDSATDRLFASSPVPAHFLSPDYLMPPLEHSYMGKHVITQQNQVVRNLRYEDSEYGHGSMKMLKLFPAGN
Protein: Phosphatidylinositol-specific phospholipase C X domain-containing protein (Q5AZ98)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MKFSQILTGLAGASSLCSALAASTSAPYGLNQGQKIRHNSATAAAAVCSADDATYSSESMPAGEYTDWGALGLDDVTSGRQYITIVNLTPHRFKLDSTHSYQMDMFDWGDIPPGRARQNIAHYSTRLTANPVDTGGEAYYSIVGTSKKFEIRATTHVPHMYWRRTVIDLSDMGLGQREYLDPRAEVPVTLVITGSDSYGFMASLTHGSGNWMKQMYRVIKDRPLQHLVMPGTHDSGMSTISGKIVSIGSEANTQTQGLNIYDQLRVGARWFDLRIMSVHQSDPSSYEFWVAHVNDETADVPVGNTGESLADIINEVNRFTSENPGEIIFLKLRYLIGIKRLPGGAIRWNTAIANKFFSELKKINNRCPNLDTTTKFQRQKASYFMDQNDGKGCVLFLLDGSNIPSGVPSSSPSDGIYPASAMTVNDHWSNLATTQPVAEDQIAVWSAINRVSPFTNDQFLISQWLVSADALQTTALTIQNIAIMPTNPALYWAGVNAMSPTKWPNVLLVDYIGVVITDQFAWNQLSAELYTLAIGLNLYMLSENCDVSGQRSPLLPPVAEASKTLAVKSALQKIAPSWNGIIFANGTIIDKPPRNLHYGRMELLKNGTVFGNGTVLEKDVPNPYLYSVLA
Protein: ATP synthase subunit C lysine N-methyltransferase (EC 2.1.1.-) (Protein N-lysine methyltransferase FAM173B) (hFAM173B) (Q6P4H8)
Organism: Homo sapiens (Human)
Function: Mitochondrial protein-lysine N-methyltransferase that trimethylates ATP synthase subunit C, ATP5MC1 and ATP5MC2. Trimethylation is required for proper incorporation of the C subunit into the ATP synthase complex and mitochondrial respiration. Promotes chronic pain. Involved in persistent inflammatory and neuropathic pain: methyltransferase activity in the mitochondria of sensory neurons promotes chronic pain via a pathway that depends on the production of reactive oxygen species (ROS) and on the engagement of spinal cord microglia.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:30530489, ECO:0000305|PubMed:29444090}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to mitochondrial cristae. {ECO:0000269|PubMed:29444090}.
Interaction partners:
- Carboxymethylenebutenolidase homolog
Sequence:
MEGGGGIPLETLKEESQSRHVLPASFEVNSLQKSNWGFLLTGLVGGTLVAVYAVATPFVTPALRKVCLPFVPATTKQIENVVKMLRCRRGSLVDIGSGDGRIVIAAAKKGFTAVGYELNPWLVWYSRYRAWREGVHGSAKFYISDLWKVTFSQYSNVVIFGVPQMMLQLEKKLERELEDDARVIACRFPFPHWTPDHVTGEGIDTVWAYDASTFRGREKRPCTSMHFQLPIQA
Protein: Nuclear transition protein 2 (TP-2) (TP2) (P29258)
Organism: Sus scrofa (Pig)
Function: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P11101}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11101}. Chromosome {ECO:0000250|UniProtKB:P11101}. Note=Loaded onto the nucleosomes of condensing spermatids (By similarity). Nuclear import is mediated by IPO4. Nucleolar localization requires the protein to be phosphorylated (By similarity). {ECO:0000250|UniProtKB:P11101, ECO:0000250|UniProtKB:P11378}.
Interaction partners:
- Protamine-2
- Spermatid nuclear transition protein 1
- G protein-coupled receptor 149
Sequence:
MDTKTQSLPNAHTQPHSNSGPQSHACNQCSCSHHCQNCSQSCDRSQSCSRSRSSSQSPTGHRSLPGHQSQSLSPSPSPRHRKRAMHSHRCPSRPGTRSCSHSKKRKNVEGKANKRKGIKRSQQVYKTKRRSSGRKYN
Protein: Small ribosomal subunit protein mS40 (28S ribosomal protein S18-2, mitochondrial) (MRP-S18-2) (28S ribosomal protein S18b, mitochondrial) (MRP-S18-b) (Mrps18-b) (S18mt-b) (Q767K8)
Organism: Sus scrofa (Pig)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25837512}.
Interaction partners:
- Mitochondrial ribosomal protein S22
- Death associated protein 3.
- Small ribosomal subunit protein mS26
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein mS31
- Mitochondrial ribosomal protein S34
- 28S ribosomal protein S28, mitochondrial
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS9m
Sequence:
MAASILNVLLRRLPGVSPFRGAYGVQVLLQTLCTKAPPEDDSLPQVPISPYKDEPWKYLDSEEYQNRYGSRPVWADYRRNHKGGIPPQRTRKMCIRGNKVAGNPCPICRDQKLHVDFRNVKLLEQFVCAHTGIIFHAPYTGVCMKQHKKLTQAIQKARDHGLLRYHIPQVEPRDLDFSTTHGAVSSTPPAPTLVSGDPWYPWYSWKQPPERELSRLRRLYQGRLREESGPPPELMPEVPLTAPAEASSTEPGAPQSAL
Protein: Dimethylsulfoniopropionate lyase 1 (DMSP lyase 1) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 1) (P0DN21)
Organism: Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi)
Function: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle. Constitutes by far the most highly expressed Alma gene in CCMP373 strain.
Interaction partners:
Sequence:
MGNCTSHPHHEPQVHFDTVDGMATVKAFAGIRQVTMGVLRIDYEYQTNLGDILDPRSFDFRIISATAEGLTFAKAKAGDKLDATGKELLERAVRQLIDNGADFIVGDCGFLVYWQVMVRDYAQDYAQKKYGRKCPVMMSSLVLALPLLATIPSGGQIGILTASEKSLQAVQKKLPIVIEDHQKEDGGQRSRSVPAAEDPSGIMINFSDPRFKVVGLDEVKDFKHALDAQGADAVNDRRDIAVQIAAYCQKVQEKNPQIAAWLIECTEAGGFAWAIKVGTGLPVWDPITLGRFLSLGFTANVPNVALTLGQHGENPLDPSATTAGKGRCTGEEPGQIHALGAEFQAIREGTL
Protein: Proline/serine-rich protein C17A5.10 (O13772)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in assembly and disassembly of the actin cytoskeleton.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein hob1
- Hsp70 nucleotide exchange factor fes1
- Chromatin structure-remodeling complex subunit sfh1
Sequence:
MTDDSVPPPSYEEVLRQEGVIDSPNSSNGQTSTSAGHPSSSSSTLPNYAASSLNSRPVSSSGSGNAYSQAPYPPARPTSQRPNSWQPGNASTMYASPPPSSNYNTAKPPYQTSQFYARPQSSYAPPPSGRPRISYPYPPGYMCYKCHNTGYKDSGRPCGRCARRFGRSYDVQFSRPPPGALVVYPGDPRIPGRVCGNCKGSGQLDFIFFTEICPVCNGVGKIPY