wanglab/gogpt-training-data huggingface dataset:
Protein: Sterol esterase 2 (EC 3.1.1.13) (Steryl ester hydrolase 2) (Q07950)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mediates the hydrolysis of steryl esters. Required for mobilization of steryl ester, thereby playing a central role in lipid metabolism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15632184, ECO:0000269|PubMed:15713625}; Single-pass type II membrane protein {ECO:0000269|PubMed:15632184, ECO:0000269|PubMed:15713625}.
Interaction partners:
- Triacylglycerol lipase 5
- Triacylglycerol lipase 3
- Triacylglycerol lipase 4
- Sterol O-acyltransferase 2
- Phospholipid:diacylglycerol acyltransferase
- Monoglyceride lipase
- Diacylglycerol O-acyltransferase 1
Sequence:
MVNKVVDEVQRLVSAIILTSFMTGLFILSLWKNYVTVHFQHKNDPRDTRSSRTKIQPNDKKKKRPARHSRPLSISSTTPLDLQRDQENNIEYDRTVTSKLSMTSNASLSENGDGNANIKMETNVNQAPYAAENPFQNIALAEDTKLVPDLKYYYKEYGIDIEEFEVETDDGFIIDLWHFKSRLNDGVEEVKREPILLLHGLLQSCGAFASSGRKSLAYFLYESGFDVWLGNNRCGLNAKWNMKKLGNDHSKKWDWDMHQMVQYDLKALINYVLDSTGYAKLSLVAHSQGTTQGFMGLVNGEKLYASDFKLVDKLENFVALAPAVYPGPLLDEKAFVRLMAKGIDSPWYFGRRSFIPLMMTMRKLMVGTKIFSFLSYIMFNYLFDWNDVLWDRVLRDRNFLFSPVHISVKLMQWWLSPLPNKLSFKKGAEKIFPDKKTWFPIAKNDDDSGNNLDNNKLHLNPKRQNSEEFPHIIMFIPKQDRLVDGERLINHFINHEANAVYKIWYIDEYSHLDVLWAHDVIDRIGKPMIENLRFPNAR
Protein: Myosin VIIA (A0A8J8XYU9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVILQKGDYVWMDLKSGQEFDVPIGAMVKLCESGQIQVVDDEGNEHWISPQNATHIKPMHPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSSEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEILKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASHLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPSQEVTNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHRLNANYVPPKNSHETQFGINHFAGIVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFVKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQDDLQGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERDKAITDRVILLQKVIRGFKDRSNFLRLKSAATLIQRHWRGHHCRKNYELIRLGFLRLQALHRSRKLHKQYRLARQRIIKFQARCRAYLVRRAFRHRLWAVITVQAYARGMIARRLHRRLRVEYWRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLQQMERARHEPINHSDMVDKMFGFLGTSSGLPGQEGQAPSGFEDLERGRREMVEEDVDAALPLPDEDEEDLSEYKFAKFAATYFQGTTTHSYTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPKYHTAMSDGSEKIPVMTKIYETLGKKTYKRELQALQGEGEAQLSEGQKKTSVKHKLVHLTLKKKSKLTEEVTKRLHDGESMVQGNSMLEDRPTSNLEKLHFIIGNGILRPALRDEIYCQISKQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPPGYAPYCEERLRRTFVNGTRTQPPSWLELQATKSKKPIMLPVTFMDGTTKTLLADSATTAKELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQERNAPWRLFFRKEVFTPWHNPSEDNVATNLIYQQVVRGVKFGEYRCEKEDDLAELASQQYFVDYGSEMILERLLSLVPTYIPDREITPLKNLEKWAQLAIAAHKKGIYAQRRTDAQKVKQDVVNYARFKWPLLFSRFYEAYKFSGPPLPKSDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSRECRVLLSLGCSDLGCASCHSGRAGLTPAGPCSPCWSCRGAKLMAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKRSKYVVALQDNPNPAGEESGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDCVYVMPTVTLPPREIVALVTMTPDQRQDVVRLLQLRTAEPEVRTKPYTLEEFSYDYFRSPPKHTLSRVMVSKARGKDRLWSHTREPLKQALLKKIVGSEELSQEACMSFIAVLKYMGDYPSKRTRSVNELTDQIFEWAVKAEPLKDEAYVQILKQLTDNHIRYSEEKGWELLWLCTGLFPPSNILLPHVQRFLQSRKHCPLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQHKTTQIFHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISVPENDFFFDFVRHLTDWIKKARPIKDGIVPSLTYQVFFMKKLWTTTVPGKDPMADSIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFFEVKQTTEPNFPEILLIAINKYGISLIDPRTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKMDDLLTSYISQMLTAMSKQRNSRSGR
Protein: tRNA methyltransferase 10 homolog C (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221) (Q3UFY8)
Organism: Mus musculus (Mouse)
Function: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends. Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. In addition to tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L0Y3}.
Interaction partners:
- Mitochondrial ribonuclease P catalytic subunit
- 3-hydroxyacyl-CoA dehydrogenase type-2
- tRNA
- tRNA
- tRNA
- Ribosome production factor 1
- tRNA
- Zinc phosphodiesterase ELAC protein 2
- Ribonuclease P protein subunit p30
- Ribonuclease P protein subunit p38
Sequence:
MNVTVRFLRPFARCLVPYTFHRKRSHLYSGVLQRYMSSKAPSLSCHNKDSASPPEQLELDGWKATMKSSIQEDGVSEVSDKDEDSLASTRELIEMWRLLGKEVPEHITEEDLKTLMECASKSAKKKYLRYLYGKEKAKKAKQVKKEMKAEAREEAKRARLLETTAEEQQQDFMFLRLWDRQINIALGWKGVQAMQFGQPLVFDMAYDNYMKPSELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDSAYHRELVKRYREKWDKLLLTATEKSPVDLFPKDSIIYLTADSPNVMTTFKHDKIYIIGSFVDKNTQTGTSLAKAKRLNIATECLPLDKYLQWEIGNKNLTLDQMIRILLCLKNTGNWEEALKFVPRRKHTGYLEVSEQSQELVRKLKKTKTLNSFRKGSLNVRTWKR
Protein: Calcium-binding EF-hand family protein (EF-Hand containing protein-like) (Putative EF-hand containing protein) (Q9T0I9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Calcium-binding EF hand family protein
- PHD finger family protein
- Calcium-binding EF-hand family protein
- Probable serine/threonine-protein kinase PBL16
- ATP synthase E chain
- ATP synthase E chain
- Protein MANNAN SYNTHESIS-RELATED 1
- Protein MANNAN SYNTHESIS-RELATED 2
- Probable protein phosphatase 2C 58
- Probable calcium-binding protein CML21
Sequence:
MDLKSNNHQQQQQVLDGSDIVELVENEKVFDKFVEQKFQQLDQDEDGKLSVTELQPAVADIGAALGLPAQGTSPDSDHIYSEVLNEFTHGSQEKVSKTEFKEVLSDILLGMAAGLKRDPIVILRMDGEDLSEFVHGPGYEIESISVFSELSSSKDASLRDCIVKALQSLSVDHGMPPSNDPWVMSNIVEPIVDSCLDEEDKREKSASQERFLEAFKRVVESVAQRLNEQPVIVAHSENTFDGSGIRRLLSNKFEFDKALNVAMETIPKDRQGKVSKGYLRAVLDTVAPSATLPPIGAVSQMDNMIMEALKMVNGDDGNVVKEEEFKKTMAEILGSIMLQLEGSPISVSSNSVVHEPLTSATFLPSTSTDTEEPSN
Protein: Pleckstrin homology domain-containing family B member 1 (PH domain-containing family B member 1) (Evectin-1) (PH domain-containing protein in retina 1) (PHRET1) (Pleckstrin homology domain retinal protein 1) (Q9UF11)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000269|PubMed:10585447}. Cytoplasm {ECO:0000250|UniProtKB:Q9QYE9}. Note=Localizes to the apical juxta-nuclear Golgi region of the cytoplasm (By similarity). Membrane-associated (PubMed:10585447). Highly expressed in the outer segments of photoreceptor cells, both in rods and cones (PubMed:10585447). {ECO:0000250|UniProtKB:Q9QYE9, ECO:0000269|PubMed:10585447}.
Interaction partners:
Sequence:
MSPAAPVPPDSALESPFEEMALVRGGWLWRQSSILRRWKRNWFALWLDGTLGYYHDETAQDEEDRVLIHFNVRDIKIGPECHDVQPPEGRSRDGLLTVNLREGGRLHLCAETKDDALAWKTALLEANSTPAPAGATVPPRSRRVCSKVRCVTRSWSPCKVERRIWVRVYSPYQDYYEVVPPNAHEATYVRSYYGPPYAGPGVTHVIVREDPCYSAGAPLAMGMLAGAATGAALGSLMWSPCWF
Protein: Inactive tyrosine-protein kinase 7 (Colon carcinoma kinase 4) (CCK-4) (Protein-tyrosine kinase 7) (Pseudo tyrosine kinase receptor 7) (Tyrosine-protein kinase-like 7) (Q13308)
Organism: Homo sapiens (Human)
Function: Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis.
Subcellular location: Membrane {ECO:0000269|PubMed:20837484}; Single-pass type I membrane protein {ECO:0000269|PubMed:20837484}. Cell junction {ECO:0000269|PubMed:20837484}. Note=Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells.
Interaction partners:
- Protein Wnt-5a
- Cholecystokinin receptor type A
- Gastrin/cholecystokinin type B receptor
- Cholecystokinin
- Vang-like protein 2
- Vang-like protein 1
- Segment polarity protein dishevelled homolog DVL-1
- Protein Wnt-3a
- Periostin
- Low-density lipoprotein receptor-related protein 6
Sequence:
MGAARGSPARPRRLPLLSVLLLPLLGGTQTAIVFIKQPSSQDALQGRRALLRCEVEAPGPVHVYWLLDGAPVQDTERRFAQGSSLSFAAVDRLQDSGTFQCVARDDVTGEEARSANASFNIKWIEAGPVVLKHPASEAEIQPQTQVTLRCHIDGHPRPTYQWFRDGTPLSDGQSNHTVSSKERNLTLRPAGPEHSGLYSCCAHSAFGQACSSQNFTLSIADESFARVVLAPQDVVVARYEEAMFHCQFSAQPPPSLQWLFEDETPITNRSRPPHLRRATVFANGSLLLTQVRPRNAGIYRCIGQGQRGPPIILEATLHLAEIEDMPLFEPRVFTAGSEERVTCLPPKGLPEPSVWWEHAGVRLPTHGRVYQKGHELVLANIAESDAGVYTCHAANLAGQRRQDVNITVATVPSWLKKPQDSQLEEGKPGYLDCLTQATPKPTVVWYRNQMLISEDSRFEVFKNGTLRINSVEVYDGTWYRCMSSTPAGSIEAQARVQVLEKLKFTPPPQPQQCMEFDKEATVPCSATGREKPTIKWERADGSSLPEWVTDNAGTLHFARVTRDDAGNYTCIASNGPQGQIRAHVQLTVAVFITFKVEPERTTVYQGHTALLQCEAQGDPKPLIQWKGKDRILDPTKLGPRMHIFQNGSLVIHDVAPEDSGRYTCIAGNSCNIKHTEAPLYVVDKPVPEESEGPGSPPPYKMIQTIGLSVGAAVAYIIAVLGLMFYCKKRCKAKRLQKQPEGEEPEMECLNGGPLQNGQPSAEIQEEVALTSLGSGPAATNKRHSTSDKMHFPRSSLQPITTLGKSEFGEVFLAKAQGLEEGVAETLVLVKSLQSKDEQQQLDFRRELEMFGKLNHANVVRLLGLCREAEPHYMVLEYVDLGDLKQFLRISKSKDEKLKSQPLSTKQKVALCTQVALGMEHLSNNRFVHKDLAARNCLVSAQRQVKVSALGLSKDVYNSEYYHFRQAWVPLRWMSPEAILEGDFSTKSDVWAFGVLMWEVFTHGEMPHGGQADDEVLADLQAGKARLPQPEGCPSKLYRLMQRCWALSPKDRPSFSEIASALGDSTVDSKP
Protein: Lethal (3) neo38, isoform B (Lethal (3) neo38, isoform C) (Lethal (3) neo38, isoform K) (RE64859p) (Q7KSP5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMNFSAFGGPFSGIHQFAAKFDAQTPGAFGTPPAAAANAAAAAAAAGTDNHVQRYQTNGNHFNQNVPNVSAANNMQYGQNISIPYSQPQGDLNFLNAAAAADHKGKIHPKIERDREEVLNQQILQNVNQSWQTLANTANTVDYSSHLLSATLPISIQHFLKYSETIKKESTGDVLKNGTNLASLALGGVALTPSNNGANGGHHNGLVGMDHGGHMTNMTDANGAALTNGASNGVNGNANGTVTNGGAGAVSSSGSVGTTNASGGTGTASGKKTKKKKPPKEKKPRPKPGEIRETKALDGSTLYCCPECQMAYPDRSLIEQHVISHAVERRFVCDICNAALKRKDHLTRHKLSHIPDRPHVCNICMKSFKRKEQLTLHIVIHSGEKKHVCIECGKGFYRKDHLRKHTRSHIARRVKSEVSAQNVNGSAGGGGGGGGGNSAQSNALHGS
Protein: Transcriptional repressor NrdR (P9WIZ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Interaction partners:
- LexA repressor
- Cobalamin biosynthesis protein CobN
- Cell wall hydrolase ChiZ
- RecBCD enzyme subunit RecD
- Riboflavin biosynthesis protein RibD
- Peroxynitrite isomerase 1
- Phosphoribosyltransferase
Sequence:
MHCPFCRHPDSRVIDSRETDEGQAIRRRRSCPECGRRFTTVETAVLAVVKRSGVTEPFSREKVISGVRRACQGRQVDDDALNLLAQQVEDSVRAAGSPEIPSHDVGLAILGPLRELDEVAYLRFASVYRSFSSADDFAREIEALRAHRNLSAHS
Protein: Pyrokinin 2 receptor 2, isoform A (Pyrokinin 2 receptor 2, isoform B) (Q9VFW6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protein hugin
- Cardio acceleratory peptide 2b
Sequence:
MAVKMLPTNSSGVLATDLQLFHNEKFLLNLTQVLNISADNLTSLLQGLEPEELLPTVTPMTPLSLLATLSVGYALIFIAGVLGNLITCIVISRNNFMHTATNFYLFNLAISDMILLCSGMPQDLYNLWHPDNYPFSDSICILESVLSETAANATVLTITAFTVERYIAICHPFRQHTMSKLSRAVKFIFAIWIAALLLALPQAIQFSVVMQGMGTSCTMKNDFFAHVFAVSGFLFFGGPMTAICVLYVLIGVKLKRSRLLQALPRRCYDVNRGISAQTRVIRMLVAVAVAFFICWAPFHAQRLMAVYGSTSGIESQWFNDVFSILDYTSGVLYFLSTCINPLLYNIMSHKFREAFKVTLARHFGLGGKNQGRGLPHTYSALRRNQTGSLRLHTTDSVRTTMTSMATTTTGLNGSANGSGNGTTTGQSVRLNRVSLDSVQMQGQNRSRQDLFDNPRRMLQTQISQLSSVGDAHSLLEEDLQFPGEPLQRQPTMCSIDELTDDLAISRSRLKLTRITRPPGGVTGGVAGGSTTGAAGSGGVSGDESSGKVRKAKVKVLKSSSPFKGLRTKFNWRARRKGSHKPHEKGATVNGGDTEERAAF
Protein: PvdE (Pyoverdine export ABC transporter PvdE) (Q5DIW1)
Organism: Pseudomonas aeruginosa
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTNPKRGAIRELLALLRPFRAIVAVSIALGMAGGLAITLLLASINNALHSENGLGQGVLLSFGGLCLLALVSSIVSDIGTSYVGQHIIAKLRKELGEKVLSAPIEQIERYRTHRLIPVLTHDIDTISDFSFSFTPLAIALTITFGCLGYLAYLSVPMFLLTVVAIVIGTAAQYLARSRGFKGFYAARDLEDELQKHYTAIASGAKELRIHRPRRYRMHTGRISETANNIRDLHISSINIFILAKTFGSMLFFVVIGLALTLQAYWPSSNPAAITGFVMVLLYMKGPLEQVVTILPIVSRAQVAFQRVAELSERFSSPEPHLLLSEQEAPDKTVDSLELRDVRYSPPAVEGSEPFHLGPINLRIAQGDIVFIVGENGCGKTTLIKLLLGLYRPQSGEILLNGEPVSAETRDDYRQLFSTIFADYYLFDDLVQGKQASLQNATQYLQRLEIAHKVSVMDGNFSTTDLSTGQRKRLALINAWLEERPVLVFDEWAADQDPAFRRVFYTELLPDLKRQGKTIIVISHDDRYFEMADQLIRLSAGKVVKETETA
Protein: Flavin carrier protein 1 (Bypass of PAM1 protein 1) (FAD transporter 1) (Heme utilization factor 1) (TRP-like ion channel protein FLC1) (Q08967)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be responsible for the transport of FAD into the endoplasmic reticulum lumen, where it is required for oxidative protein folding.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16717099}; Multi-pass membrane protein {ECO:0000269|PubMed:16717099}.
Interaction partners:
- Sphingolipid long chain base-responsive protein LSP1
- Ribosome biogenesis protein ERB1
- Mannan endo-1,6-alpha-mannosidase DFG5
- Flavin carrier protein 2
Sequence:
MQVLVTLWCLICTCLVLPVAAKKRTLTASSLVTCMENSQLSANSFDVSFSPDDRSLHYDLDMTTQIDSYIYAYVDVYAYGFKIITENFDVCSMGWKQFCPVHPGNIQIDSIEYIAQKYVKMIPGIAYQVPDIDAYVRLNIYNNVSENLACIQVFFSNGKTVSQIGVKWVTAVIAGIGLLTSAVLSTFGNSTAASHISANTMSLFLYFQSVAVVAMQHVDSVPPIAAAWSENLAWSMGLIRITFMQKIFRWYVEATGGSASLYLTATTMSVLTQRGLDYLKNTSVYKRAENVLYGNSNTLIFRGIKRMGYRMKIENTAIVCTGFTFFVLCGYFLAGFIMACKYSIELCIRCGWMRSDRFYQFRKNWRSVLKGSLLRYIYIGFTQLTILSFWEFTERDSAGVIVIACLFIVLSCGLMAWAAYRTIFFASKSVEMYNNPAALLYGDEYVLNKYGFFYTMFNAKHYWWNALLTTYILVKALFVGFAQASGKTQALAIFIIDLAYFVAIIRYKPYLDRPTNIVNIFICTVTLVNSFLFMFFSNLFNQKYAVSAIMGWVFFIMNAAFSLLLLLMILAFTTIILFSKNPDSRFKPAKDDRASFQKHAIPHEGALNKSVANELMALGNVAKDHTENWEYELKSQEGKSEDNLFGVEYDDEKTGTNSENAESSSKETTRPTFSEKVLRSLSIKRNKSKLGSFKRSAPDKITQQEVSPDRASSSPNSKSYPGVSHTRQESEANNGLINAYEDEQFSLMEPSILEDAASSTQMHAMPARDLSLSSVANAQDVTKKANILDPDYL
Protein: Complement component C8 gamma chain (P07360)
Organism: Homo sapiens (Human)
Function: C8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol.
Subcellular location: Secreted.
Interaction partners:
- Complement component C8 alpha chain
- Complement component C8 beta chain
- Complement C5
- Complement component C7
- Complement component C6
- Complement component C9
- Lipocalin-1
- Prostaglandin-H2 D-isomerase
- Glycodelin
- Complement C1r subcomponent
Sequence:
MLPPGTATLLTLLLAAGSLGQKPQRPRRPASPISTIQPKANFDAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHVAPQGTAMAVSTFRKLDGICWQVRQLYGDTGVLGRFLLQARDARGAVHVVVAETDYQSFAVLYLERAGQLSVKLYARSLPVSDSVLSGFEQRVQEAHLTEDQIFYFPKYGFCEAADQFHVLDEVRR
Protein: Tyrosine-protein phosphatase non-receptor type (EC 3.1.3.48) (A8K3N4)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MPTTIEREFEELDTQRRWQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCIKGDSSIQKRWKELSKEDLSPAFDHSPNKIMTEKYNGNRIGLEEEKLTGDRCTGLSSKMQDTMEENSESALRKRIREDRKATTAQKVQQMKQRLNENERKRKRPRLTDT
Protein: Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial (EC 2.3.1.-) (Protein LIPID X D2) (AtLpxD2) (F4JIP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21709257}.
Interaction partners:
- Probable lipid-A-disaccharide synthase, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 3, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 5, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 2, mitochondrial
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 1, mitochondrial
- Probable tetraacyldisaccharide 4'-kinase, mitochondrial
- Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial
- Is a member of the PF|00364 Biotin-requiring enzymes family
- At5g19070
Sequence:
MAATLWRLYSKSICNSLQGIILNKPFIQKQLLLSSRTRSLSFSSDSQFGSATAEVCSNTGLKTGGGIIVKEGFLRWENGGGTCHSSAQIYSSALVEFGAVVHEKAVLGAEVHVGSGTVIGPSVDIGPSTRIGYNVSISNCSIGDSCVIHNGVCIGQDGFGFYVDEHGNMVKKPQTLNVKIGNRVEIGANTCIDRGSWRETVIEDDTKIDNLVQIGHNVIIGKCCLLCGQVGIAGSVTIGDYVALGGRAAVRDHVSIVSKVRLAANSCVTRNITEPGDFGGFPAVPIHEWRKQIVRAQIANKREI
Protein: LD09246p1 (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform C) (Uncharacterized protein, isoform D) (Uncharacterized protein, isoform E) (Q9V4F3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein, isoform A
- FI18814p1
Sequence:
MAAQVTPKISTCINSKGSIQKKNQAQHHDMSEQSKVNESTLPLSDDPRTLQLALELSLVGFNDNQNCYAQPAQPLPMPLSARSDFEIGTINSTLPIPSAPNCLLLPNAGAVSSEDRSKKSQNMTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVNKAKREILSAADHFSLIRASRKPVSDSQNNGMVGSTTSSGGGAVPRMSGPPCMPGQVTIQVRVPYRVVGLVVGPKGATIKHIQQETQTYIVTPSREKEPIFEVTGLPDNVDTARKQIEAHIALRTGSGSGSGDAITMQSSDSVDTKEYASLPSLTQILNDDLNSEILSSIYKNSVPSTQEYANNSMKTVVNVSNSVKLVQGHHTGNCFQKSEFAEMEMTANITAADILDKRLPGNEVSVPLAKANVANIVFRTTSSKTLSFCPPTSTSASFHSNCNANILTRSCSSASSTTSTKSTNNSANTPPEILNIWKSISDSIDVDEGIGDSPSIWNQPANIIPTAHCSPTISISPTDSLLGMGEHSANQQNLNHAKEPIMPNLPQKIKGIQVQSNADNFLTHRECFVCNENTVTTALVPCGHNMFCMECANHICLSMDAVCPVCNSIVYHAMRILG
Protein: M-phase phosphoprotein 9 (Q99550)
Organism: Homo sapiens (Human)
Function: Negatively regulates cilia formation by recruiting the CP110-CEP97 complex (a negative regulator of ciliogenesis) at the distal end of the mother centriole in ciliary cells. At the beginning of cilia formation, MPHOSPH9 undergoes TTBK2-mediated phosphorylation and degradation via the ubiquitin-proteasome system and removes itself and the CP110-CEP97 complex from the distal end of the mother centriole, which subsequently promotes cilia formation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:30375385}. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30375385}. Note=Localizes to the distal and proximal end of centriole pairs in duplicated centrosomes. In ciliated cells, localizes to the distal and proximal end of daughter centriole and proximal of the mother centriole but not in the distal end of the mother centriole (PubMed:21399614). Recruited by KIF24 to the distal end of mother centriole where it forms a ring-like structure (PubMed:30375385). {ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:30375385}.
Interaction partners:
- G2/mitotic-specific cyclin-B1
- DNA repair protein RAD51 homolog 1
Sequence:
MEEFDLVKTLHKTSSSVGSDENSLHSLGLNLNTDRSSPHLSTNGVSSFSGKTRPSVIQGTVEVLTSLMQELQNSGKTDSELWKNCETRWLQLFNLVEKQCQEQIVAQQEQFHNQIQHIQEEIKNLVKLQTSSASLASCEGNSSNKQVSSESQMGFFSLSSERNESVIHYPESTEPEIQQEMSTSQPDCNVDSCSVSSGYGTFCISELNLYKSKDPKEFMEHIDVPKGQYVAPAVPAESLVDGVKNENFYIQTPEECHVSLKEDVSISPGEFEHNFLGENKVSEVYSGKTNSNAITSWAQKLKQNQPKRAHVEDGGSRSKQGNEQSKKTPIEKSDFAAATHPRAFYLSKPDETPNAWMSDSGTGLTYWKLEEKDMHHSLPETLEKTFISLSSTDVSPNQSNTSNEMKLPSLKDIYYKKQRENKQLPERNLTSASNPNHPPEVLTLDPTLHMKPKQQISGIQPHGLPNALDDRISFSPDSVLEPSMSSPSDIDSFSQASNVTSQLPGFPKYPSHTKASPVDSWKNQTFQNESRTSSTFPSVYTITSNDISVNTVDEENTVMVASASVSQSQLPGTANSVPECISLTSLEDPVILSKIRQNLKEKHARHIADLRAYYESEINSLKQKLEAKEISGVEDWKITNQILVDRCGQLDSALHEATSRVRTLENKNNLLEIEVNDLRERFSAASSASKILQERIEEMRTSSKEKDNTIIRLKSRLQDLEEAFENAYKLSDDKEAQLKQENKMFQDLLGEYESLGKEHRRVKDALNTTENKLLDAYTQISDLKRMISKLEAQVKQVEHENMLSLRHNSRIHVRPSRANTLATSDVSRRKWLIPGAEYSIFTGQPLDTQDSNVDNQLEETCSLGHRSPLEKDSSPGSSSTSLLIKKQRETSDTPIMRALKELDEGKIFKNWGTQTEKEDTSNINPRQTETSVNASRSPEKCAQQRQKRLNSASQRSSSLPPSNRKSSTPTKREIMLTPVTVAYSPKRSPKENLSPGFSHLLSKNESSPIRFDILLDDLDTVPVSTLQRTNPRKQLQFLPLDDSEEKTYSEKATDNHVNHSSCPEPVPNGVKKVSVRTAWEKNKSVSYEQCKPVSVTPQGNDFEYTAKIRTLAETERFFDELTKEKDQIEAALSRMPSPGGRITLQTRLNQEALEDRLERINRELGSVRMTLKKFHVLRTSANL
Protein: Methylated-thiol--corrinoid protein MtsB (Methylthiol:coenzyme M methyltransferase 30 kDa subunit) (Q48925)
Organism: Methanosarcina barkeri
Function: Harbors a corrinoid prosthetic group and acts as a methyl group carrier in methanogenesis from methylated-thiols.
Interaction partners:
Sequence:
MIRHIDLAVQNILEMKEKEPAKFKRLIDEGIMIGLGVDLEDGNKEVTTVDQIKNQNRPKDPEYASVAEAVIEGNNAETVKLISALLEKGKDPTDLVLNALMPGIQTVCELYDIGESYVPEILLANEALMKGVELCQKKKGEVPSQGKVVSLVIVGDLHDIGKNIVAAILRANGFEVIDLGRDVTVEAAVEAVKSTKANLVTGTTLMSTTKGGLKALANALEPEGVPLACGGAAVDRRFVDTFGNSVYGRTPLDAVKIAKEICEGKSWEEARNELY
Protein: DNA repair protein XRCC1 (X-ray repair cross-complementing protein 1) (O54935)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity. Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P18887}. Chromosome {ECO:0000250|UniProtKB:P18887}. Note=Moves from the nucleoli to the global nuclear chromatin upon DNA damage. Recruited to DNA damage sites fowwing interaction with poly-ADP-ribose chains. {ECO:0000250|UniProtKB:P18887}.
Interaction partners:
Sequence:
MPEISLRHVVSGSSQDSTHCAENLLKADTYRKWRAATAGEKTISVVLQLEKEEQIHSIDIGNDGSAFVEVLVTRSAGGGGATAIEQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPYGLSFVRFHSPPDKDEAETPSQKGTVTKLGQFRVKEEDDGASSLKPGALFFSRINKTSSASARGPAGPSYAAATLQASNATSSASSVSKALGSSCKPQESPKGKRKLDLNLEDRRPASKPSAGPPTLKRPKLTVPSRSPAAAAASTPAQKAAPGKPREGTEPRGARAGPQELGKILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTPDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCYRLRRRLPSRRYLMAGLGSSSEDEEDDSPGESGEDEAPKLSRKRPQAKAKTQAAGPSSPQRPPTPKETKSPSPEPQDNSDTEGEQSEGQDNGAEDSGDTEDELRRVAEQREQRQPPAPGENGEDPYAGSTDENTDNEASTEADLPIPELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSERVQFVITAQEWDPIFEEALMENPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA