wanglab/gogpt-training-data huggingface dataset:
Protein: Glial cell line-derived neurotrophic family receptor-like, isoform E (A0A0B4K7J4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
- Ret oncogene, isoform A
- Unc-13, isoform E
- Dipeptidase
- Sidestep II, isoform A
Sequence:
MTRFRIKNLKILSCCLSLWVVLFGGALHLAQGSEFPERECCDLTTTSTVGPLPMPPAALPTDKSLSSATTALETDLAIGRSGSTIKGVVAILNCILARQLCFEDPSCSAILEIIPRVCGPIPVSCSTVTVTKCQAALRTLQAFQFFRPTCLCKEPGMDPDCNHFRDFLFDHPCGFVLKKAEKDPYPIDALPTCNHALSVCQQERKCLKLFEDFKTHCKVRDNKCKMENRDACHDSWTNLRLSPMFGCICPNNHMKKRCDRIFNIVNHNPCVDRLIFFPNGLPKLKQPRPKAKPRPKPKPKSKPKPRQRHHGMNGTELMTNNIEYHDEPNGLSDPEDEANETVDEDPGGHGDEDEDEEDDDYDDRIRAEIYSNYPHYLHPPSWGINNPLVLASHSPHTLDDDDDVVVEVVANKKPPPVTLHHHNDELDHDVVVVVDAGPHSHSHPHSHTFYSHGDQSSTTGSGLPGPAPTIPSPPNTGTKMHKTAPLGDLVAGSDITHRTYTGPSMDERVRILGMDEKLHQRIFNDNLALIDTPLIAMGSGSGSGTVTTSVSGYGLGMGMGLSGSFNYLGSMHGVPSYPFNISGFHQRHMAAAAADNEPFDIIDTGLGYGGNGNAGVYYQSGQDVEVDLSTEIIKQHFQSTCHTALDTCREDPSCSSSLQPMLTHCELHRCNRNACMSSLQAFYKGPHEDLNLDIAFCLCKKTSSQQNGNGNRHDMCMIAQEKLHPVCAQRPPDNSNPASSNGIYYHPPPACHVVADSCKEDRECRLKLEYYEQACAVDSVTKKCAGRPSGCRTAMIGILGTMLRTTCACQGTDPQHLYQCVGWRRLLWMNPCVVEAQKDFHMKRLAELGFLTTTTTTTTTTTTTTTTTTTRAPPPPPPPTTTTTTTTSMQPRQTPRKPATHIFKDVITAKEKSEPTSVEHNYLDPPDSIPLPSVNVESGGNGGNDDYHNGNGNGHGNGNGNGRRKNGGKGRGGSVDFDDPVIFVDPRETTEFVGISITEPVTTTTTTMATTTTTQPPRNCVVQRPRQSDQLIREGSSKRIYSLDDVECSELCSCGESLILTCHALCVPFAPCRTALAFYSHASPAYQAFRGRCLCYSGRFICMKPPLGEYILPGGIFLLLGYSAADEALLRPHTNLGVQDAVRALQQYVTTYIDNQTQCTLTLFNMTEENIIIAARLPHDGKLKDIELLRKEKDECTAILKTISHQINSEHSELQSHRLLSIFKMSEVEVVWPESTSAAARSGHGPGQFAGCDRLLYAAMLALAYLSSWTTLRMSDVAT
Protein: CD5 antigen-like (Apoptosis inhibitor expressed by macrophages) (mAIM) (Apoptosis inhibitory 6) (SP-alpha) (Q9QWK4)
Organism: Mus musculus (Mouse)
Function: Secreted protein that acts as a key regulator of lipid synthesis: mainly expressed by macrophages in lymphoid and inflamed tissues and regulates mechanisms in inflammatory responses, such as infection or atherosclerosis. Able to inhibit lipid droplet size in adipocytes. Following incorporation into mature adipocytes via CD36-mediated endocytosis, associates with cytosolic FASN, inhibiting fatty acid synthase activity and leading to lipolysis, the degradation of triacylglycerols into glycerol and free fatty acids (FFA). CD5L-induced lipolysis occurs with progression of obesity: participates in obesity-associated inflammation following recruitment of inflammatory macrophages into adipose tissues, a cause of insulin resistance and obesity-related metabolic disease. Regulation of intracellular lipids mediated by CD5L has a direct effect on transcription regulation mediated by nuclear receptors ROR-gamma (RORC). Acts as a key regulator of metabolic switch in T-helper Th17 cells. Regulates the expression of pro-inflammatory genes in Th17 cells by altering the lipid content and limiting synthesis of cholesterol ligand of RORC, the master transcription factor of Th17-cell differentiation. CD5L is mainly present in non-pathogenic Th17 cells, where it decreases the content of polyunsaturated fatty acyls (PUFA), affecting two metabolic proteins MSMO1 and CYP51A1, which synthesize ligands of RORC, limiting RORC activity and expression of pro-inflammatory genes. Participates in obesity-associated autoimmunity via its association with IgM, interfering with the binding of IgM to Fcalpha/mu receptor and enhancing the development of long-lived plasma cells that produce high-affinity IgG autoantibodies. Also acts as an inhibitor of apoptosis in macrophages: promotes macrophage survival from the apoptotic effects of oxidized lipids in case of atherosclerosis. Involved in early response to microbial infection against various pathogens by acting as a pattern recognition receptor and by promoting autophagy (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:20519120, ECO:0000269|PubMed:23236605, ECO:0000269|PubMed:9892623}. Cytoplasm {ECO:0000269|PubMed:20519120}. Note=Secreted by macrophages and circulates in the blood (PubMed:20519120). Transported in the cytoplasm via CD36-mediated endocytosis (PubMed:20519120). {ECO:0000269|PubMed:20519120}.
Interaction partners:
- C-type lectin domain family 4 member F
Sequence:
MAPLFNLMLAILSIFVGSCFSESPTKVQLVGGAHRCEGRVEVEHNGQWGTVCDDGWDRRDVAVVCRELNCGAVIQTPRGASYQPPASEQRVLIQGVDCNGTEDTLAQCELNYDVFDCSHEEDAGAQCENPDSDLLFIPEDVRLVDGPGHCQGRVEVLHQSQWSTVCKAGWNLQVSKVVCRQLGCGRALLTYGSCNKNTQGKGPIWMGKMSCSGQEANLRSCLLSRLENNCTHGEDTWMECEDPFELKLVGGDTPCSGRLEVLHKGSWGSVCDDNWGEKEDQVVCKQLGCGKSLHPSPKTRKIYGPGAGRIWLDDVNCSGKEQSLEFCRHRLWGYHDCTHKEDVEVICTDFDV
Protein: Kinesin like protein 67a (P91945)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MPSEQHTNIKVAVRVRPYNVRELEQKQRSIIKVMDRSALLFDPDEEDDEFFFQGAKQPYRDITKRMNKKLTMEFDRVFDIDNSNQDLFEECTAPLVDAVLNGYNCSVFVYGATGAGKTFTMLGSEAHPGLTYLTMQDLFDKIQAQSDVRKFDVGVSYLEVYNEHVMNLLTKSGPLKLREDNNGVVVSGLCLTPIYSAEELLRMLMLGNSHRTQHPTDANAESSRSHAIFQVHIRITERKTDTKRTVKLSMIDLAGSERAASTKGIGVRFKEGASINKSLLALGNCINKLADGLKHIPYRDSNLTRILKDSLGGNCRTLMVANVSMSSLTYEDTYNTLKYASRAKKIRTTLKQNVLKSKMPTEFYVKKIDEVVAENERLKERNKALEAKATQLERAGNSGFDPLELKTWYSKIDAVYAAARQLQEHVLGMRSKIKNINYRQTLKKELEEFRKLMCVDQRVCQEDFRRFANYMSTLTSQMEKYKEELPSWLSKMEIAYQDLESLKREVNKSKAYQILIVYVKYKDLELQLTKQNIFNNHVNAINQELVENLDLMRKSFRTACEVLNQTYDRLEDGQKLTPEIEAVFERLLRKMRFADSEANTKMAEMNPLVVPMALRSSGQEEEEPTCSLTASAKKRQRQAAQSDDDLHLSMEDFDSQDTESDSEELHRTFKRPRNLNETQVLGPCSSSSSSSTSSSSSARKALTATVTKQRNVQQRLVSDLISDQNVRGGNEKIKKALLKSNHFTAQGLQRTLAAASLAKENVKYNANYVRKSPRALMAKALAGTSTLARKPLGSASKEPPLVKFNRAASFRLKK
Protein: 60S ribosomal protein-like (Q57X71)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L17, putative
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S5, putative
- Small ribosomal subunit protein uS5
- 50S ribosomal protein L17, putative
- Large ribosomal subunit protein uL5
- 60S ribosomal protein L35, putative
- 40S ribosomal protein S13, putative
- 60S ribosomal protein L5, putative
Sequence:
MRRVLCGVSVRCGALSSRFCSGGKADKPKLEELAATYSQLTLKELSDLQRLVFKKLGHSDDFYEKALLRGLGGGGGGGAAVAFPVAAAAGAAPSGASATEAEPPKTEKKKVEKTSFDVKLEKYAPDIKVKLIKELRSVTNLSIADAKNAIEKCPGLVQTNMRKEDAEKLKGLFEKLGATVQLL
Protein: Testican-3 (SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3) (Q9BQ16)
Organism: Homo sapiens (Human)
Function: May participate in diverse steps of neurogenesis. Inhibits the processing of pro-matrix metalloproteinase 2 (MMP-2) by MT1-MMP and MT3-MMP. May interfere with tumor invasion.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Matrix metalloproteinase-16
- Matrix metalloproteinase-14
Sequence:
MLKVSAVLCVCAAAWCSQSLAAAAAVAAAGGRSDGGNFLDDKQWLTTISQYDKEVGQWNKFRDEVEDDYFRTWSPGKPFDQALDPAKDPCLKMKCSRHKVCIAQDSQTAVCISHRRLTHRMKEAGVDHRQWRGPILSTCKQCPVVYPSPVCGSDGHTYSFQCKLEYQACVLGKQISVKCEGHCPCPSDKPTSTSRNVKRACSDLEFREVANRLRDWFKALHESGSQNKKTKTLLRPERSRFDTSILPICKDSLGWMFNRLDTNYDLLLDQSELRSIYLDKNEQCTKAFFNSCDTYKDSLISNNEWCYCFQRQQDPPCQTELSNIQKRQGVKKLLGQYIPLCDEDGYYKPTQCHGSVGQCWCVDRYGNEVMGSRINGVADCAIDFEISGDFASGDFHEWTDDEDDEDDIMNDEDEIEDDDEDEGDDDDGGDDHDVYI
Protein: Uncharacterized protein (Q57Y57)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGCGDSRVRASAQPQHQSHPQSVDVQDCGPNKLLVERDKEQEHEESSPVGLEPPCVQQPIAADSANSNPGPHREEEAKEANAVSPPEAPVHFNRDSEVPTELVTTVPSGVAPGGGGREVPERVNGPEIVDRKGGHDTEVRSKEPKINGTAVALGPRDKEKDVDAGDCEAEGGMSTNAETPALTEDTPATSNCGERNGSSTVPLERLRLPVRKKQPSRCLVHVLEGDTVSVSVSSTSTGYVSFTSLISAYGSSGHIRKKSTLRPGDLSLVTLSPLSSAANTPRSSGEGLKAAAGAEELSGQAMRGLNSSRIWRFRRLKIMPCGDTSLLLKGRRRRRKGSRATCGTQSTHNRSGVLTPTQASFSALGAVANCGRRGINAVDPRNHVVHISR
Protein: Galactose-1-phosphate uridylyltransferase (Gal-1-P uridylyltransferase) (EC 2.7.7.12) (UDP-glucose--hexose-1-phosphate uridylyltransferase) (P08431)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Galactose transporter
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Galactokinase
- Bifunctional protein GAL10
- Protein GAL3
- UTP--glucose-1-phosphate uridylyltransferase
- Galactose/lactose metabolism regulatory protein GAL80
- Regulatory protein GAL4
- Phosphoglucomutase 2
- Phosphoglucomutase 1
Sequence:
MTAEEFDFSSHSHRRYNPLTDSWILVSPHRAKRPWLGQQEAAYKPTAPLYDPKCYLCPGNKRATGNLNPRYESTYIFPNDYAAVRLDQPILPQNDSNEDNLKNRLLKVQSVRGNCFVICFSPNHNLTIPQMKQSDLVHIVNSWQALTDDLSREARENHKPFKYVQIFENKGTAMGCSNLHPHGQAWCLESIPSEVSQELKSFDKYKREHNTDLFADYVKLESREKSRVVVENESFIVVVPYWAIWPFETLVISKKKLASISQFNQMVKEDLASILKQLTIKYDNLFETSFPYSMGIHQAPLNATGDELSNSWFHMHFYPPLLRSATVRKFLVGFELLGEPQRDLTSEQAAEKLRNLDGQIHYLQRL
Protein: Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin) (Q8SXM2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03022}. Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles. {ECO:0000256|HAMAP-Rule:MF_03022}.
Interaction partners:
Sequence:
MALPRKLISKIYDIKAHDSRVTSLDLGETGRVLVTGGEDRNVNLWAIGQNECFMSLTGHNRSIDCVRFAYKDNFVYSADDIGIIRRWDLNSQKIYSTLNGHMKSVRTLDFNPSGEYVVSGSNDTTVRLWDVQNENNCIKVCRGHMSHVNSVKFSPDGLWIASAGLEGSILIWDIRKSKQIMEFIADPPVTAITCVQFHPFEFLLAAGRVDGTVSIYDLEHQQLVSQTTHFYGQAIRCITFSDNGECLFVGSSSGISVIGWEPDRELDHIKSTWSSLADMKVVNNKLICGCHEIDTVSINTISLDRVIPFYQPPNSLPNFKHNSTNRKSFTRGNQKFRLSVGGAKPAQVQEEHEGDKSGLSSPNYSLEVVNEAVLESAETSPMSSLPPVHLASMAGPSADLAPHHVVYGGAIDSALRQGKYSRVPDNMASYGSSYGAIDTRLMSLNEPSSLHKPDIYNLYPLDKNEEADVQQLEFNLNDSNPPILNNYDNYEMAEDFPVNQNLNYITNNYKPVPATSTINASSKSIKKTTTTTLHKRTTNNMAGAKQTSTGIFGGSKLSQVSSVSSMELHKLDDNMVLKKSSSSNVVNKNKRPMGSAQSQFSKENNQQKNINVEIITKPPMRSRTTLDMRTSHQAKTQEKQIHQQQPMNNRIIMDDHDFDMLSRSHEAVLQELSNRQSSLDLLRHATRSHDVLGALRQARSCGKSIFIDLLGAILEKPSSWNLDFCMFVLPEIYELLQSQHKFHFTRACDTLRIILSNFLPTIQENLDSWAANGLGVDVTREDRQRKCAECQRWLLQIKNLPESTHFGSTLSQLQNIIIF
Protein: Alpha terpineol synthase, chloroplastic (EC 4.2.3.111) ((-)-sabinene synthase, chloroplastic) (EC 4.2.3.109) (1,8-cineole synthase, chloroplastic) (EC 4.2.3.108) (Myrcene synthase, chloroplastic) (EC 4.2.3.15) (Terpene synthase 1,8cin) (PcTPS-1,8cin) (Terpene synthase alphaterp) (PcTPS-alphaterp) (R9QMZ0)
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. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to alpha-terpineol and, to a lower extent, to 1,8-cineole, myrcene and (-)-sabinene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MALLSVAPLQKPLTSCSPFSTTMPTLGVCTPRKVVTPSIIMCSTTAVSDAGAKRRIANHHSNLWGDDFIHSLSTHYEAPSYRERAERLIKEVKEMFTEIEDGLSITPLSDLLSRLSMVDSIERLGIDRHFKMEIKSALDYVHSYWSEKGIGCGRESGVTDLNSTALGLRTLRLHGYPVSSSVLEQFKDEKGQFATSSIQTDGGEIRSIFNLFRASLVAFPNEKVMEDAQIFSTIYLKEYLEKIPLSSLSRQIEYVMEYGWHTNLPRLEARHYMDVFGYNEMPWMSYGNTEKLLELAKLEFNIFHSIQQRELKHISRWWKDSGFSQMNFVRHRHVEYYTLASCFAIDPQHSAFRVSFAKMCHLVTVLDDIYDTFGTMEELQLFTAAVKRWDPSATDSLPEYMKRVYTVLYETVNEMAQVAKKSQGRDTINYARHAWEAYLDSYMKEAEWISTGCLPTFEEYYENGKISFGYRISMLQPILSMDIPFPHHILQEIDYPSRFSSLAAGILRLKGDTRCYQADSARGEEASCISCYMKENPGLTEEDVVNHIHGMVDDLIKELNWELLKPDCNVPISSKKHAFDICRAVHHGYKYRDGYSVATNEIKDLVMITVLEPVPL
Protein: IscR (Q9HXI7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Iron-sulfur cluster assembly scaffold protein IscU
- Co-chaperone protein HscB homolog
- Cysteine desulfurase IscS
- 2Fe-2S ferredoxin
- Chaperone protein HscA homolog
- Uncharacterized protein PA3808
- Fe/S biogenesis protein NfuA
- Iron-binding protein IscA
- Iron-sulfur cluster insertion protein ErpA
- cysteine desulfurase
Sequence:
MRLTTKGRYAVTAMLDLALHAQQGPVSLADISERQGISLSYLEQLFAKLRRGNLVTSVRGPGGGYQLSRHMSGIHVAQVIDAVNESVDATRCQGQGDCHSGDTCLTHHLWCDLSLQIHEFLSGISLADLVSRQEVQEVALRQDERRCSGKTPRLDKIEASAID
Protein: Gamma-crystallin A (Gamma-A-crystallin) (Gamma-crystallin 1-1) (P10065)
Organism: Rattus norvegicus (Rat)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A chain
- Filensin
Sequence:
MGKITFYEDRGFQGRCYECSSDCPNLQTYFSRCNSIRVDSGCWMLYERPNYQGYQYFLRRGDYPDYQQWMGFSDSIRSCRSIPYTSSHRIRLYERDDYRGLVSELTEDCSCIHDRFRLNEIYSMHVLEGSWVLYEMPNYRGRQYLLRPGDYRRYHDWGAMDAKVGSLRRVMDLY
Protein: Kallistatin (Kallikrein inhibitor) (Peptidase inhibitor 4) (PI-4) (Serpin A4) (P29622)
Organism: Homo sapiens (Human)
Function: Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein.
Subcellular location: Secreted.
Interaction partners:
- Kallikrein-1
- Kallikrein-2
- Elafin
- Kallikrein-4
- Low-density lipoprotein receptor-related protein 6
- Azurocidin
Sequence:
MHLIDYLLLLLVGLLALSHGQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIFFSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHGLETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRGKIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQEHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKRNFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKATLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDPTKP
Protein: Rifin (Q8I0G7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLLYSKILLFALALNILLTSYYAHNKNKIYIKSHTPTTRSRLLSECDLYMSSNDNDPDMKSVKENFDRQTSQRFEEYDERMKDKRQKRKEQRDKNIDEIIKKDRMDKSLAEKVEKCCLICGCGLGGVAAGIGIIGGITISELKKAAMATAIVSAKEAGMAAAKAEGAAAGKEFVIAGLKRMGISTLGGKDLGTYFATTDYTNFKTIARVINSEYQTDSCLIGGSGAEKPICTWVRAKEGAARVIQGKQFSTQETIKTGVENIVSNAETVAGEASKKATEDVIKSSIAAVDAKYVICQNAIIASVVAILVIVLVMIIIYLILRYRRKKKMTKKLQYTKLLNQ
Protein: Ferredoxin reductase (P95034)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable reductase
- Uncharacterized NAD-dependent oxidoreductase Rv0687
- Nitrite reductase small subunit
- Rubredoxin
- Rubredoxin
- Uncharacterized protein Rv2633c
- Putative Rieske 2Fe-2S iron-sulfur protein Rv3818
- Glutamate synthase large chain
Sequence:
MNAHVTSREGVNEFDDGIVIVGGGLAAARTAEQLRRAGYSGRLTIVSDEVHLPYDRPPLSKEVLRSEVDDVALKPREFYDEKDIALRLGSAAVSLDTGEQTVTLADGTVLGYDELVIATGLVPRRIPSLPDLDGIRVLRSFDESMALRKHASAARHAVVVGAGFIGCEVAASLRGLGVDVVLVEPQPAPLASVLGEQIGQLVTRLHRDEGVDVRTGVTVAEVRGKGHVDAVVLTDGTELPADLVVVGIGSTPATEWLEGSGVEVDNGVICDKAGRTSAPNVWALGDVASWRDPMGHQARVEHWSNVADQARVVVPAMLGTDVPTGVVVPYFWSDQYDVKIQCLGEPHATDVVHLVEDDGRKFLAYYERDGVLVGVVGGGMAGKVMKVRGKIAAGAPIAEVLDQTQA
Protein: General transcription and DNA repair factor IIH subunit tfb1 (TFIIH subunit tfb1) (RNA polymerase II transcription factor B 73 kDa subunit) (RNA polymerase II transcription factor B p73 subunit) (RNA polymerase II transcription factor B subunit 1) (O13745)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- General transcription and DNA repair factor IIH subunit tfb2
- General transcription and DNA repair factor IIH subunit tfb4
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription and DNA repair factor IIH subunit ssl1
- RNA polymerase II transcription factor B subunit 3
- Transcription initiation factor IIE subunit alpha
- Cyclin mcs2
- Transcription initiation factor IIE subunit beta
- DNA repair protein rad13
Sequence:
MGDRVEALAIFRKKQGVLSIDSRLKWTGEGKTTPSVDIAFDAISNLQTTPASNPKVMIRVFIVVKEGEDPTSLVFHFTGTPNARENCDMITNELRNAIQRQREGSQSKPQGANVDRVNSTNLEKDIDLQESLLTNNPDLLQTFKEAVMKGHLSNEQFWSTRLHLLRAHAVERSQQRGPYNVLSTIKPKTVDNQMKVSLTGQQIHDMFEQHPLLRKVYDKHVPPLAEGEFWSRFFLSKLCKKLRGDRITPMDPSDDIMDKYLKDNEEVTKVSDEPIASHLFDLEGNDQNANVIAELRPDITMRIDKEALPFMKNINQLSERLLEKSLGNSKRFNNENEETYLKESGFHDLEEEASDSKVVLKIKGQDQLLENNFVPSKNQVGLEPLPSLEALQHLYQEDSISLNHIEHDSDSLAEAAMQLTQSMREKHEFETHGTASNLPIDIKNEIVLCHTVTIEFLHQFWNALLNTTFPDKKAMAPLQNALLNSKKRVEAIASQAQEQNVDPKLVYELVSCTLTSIDTSISEYQRRMSYPPA
Protein: SUZ12 polycomb repressive complex 2 subunit (A0A8I6AIG5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAAVAAAVASGGKSGGGGCGGGGGYSASSSSAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSQNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVSEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPVAKPLATRNSESLHQENKPGSVKPAQTIAVKETLTTEMQTRKEKDTSNETRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLESEDGEVEQQRTYSSGHNRLYFHSDTCLPLRPQEMEVDSEDEKDPEWLREKTITQIEEFSDVNEGEKEVMKLWNLHVMKHGFIADNQMNHACMLFVENYGQKIIKKNLCRNFMLHLVSMHDFNLISIMSIDKAVTKLREMQQKLEKGESAAPANEDIAEEQNGTANGFSETNSKEKALETDGVSGVPKQSKKQKL
Protein: Casein kinase I isoform alpha (CKI-alpha) (EC 2.7.11.1) (CK1) (P97633)
Organism: Rattus norvegicus (Rat)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates (By similarity). Can phosphorylate a large number of proteins (By similarity). Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45' (By similarity). May phosphorylate PER1 and PER2 (By similarity). May play a role in segregating chromosomes during mitosis. May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration (By similarity). Acts as an inhibitor of NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P48729}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P48729}. Nucleus speckle {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8BK63}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8BK63}. Note=Localizes to the centrosome in interphase cells, and to kinetochore fibers during mitosis. Also recruited to the keratin cytoskeleton. {ECO:0000250|UniProtKB:P48729}.
Interaction partners:
- Glycogen synthase kinase-3 beta
- Catenin beta-1
- Adenomatous polyposis coli protein
- Axin-2
- Protein cereblon
- APC membrane recruitment protein 1
- Splicing factor 3B subunit 1
- Beta-adrenergic receptor kinase 1
- Beta-transducin repeat containing E3 ubiquitin protein ligase
- GLI family zinc finger 3
Sequence:
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQGKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF
Protein: Acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (Ergosterol biosynthesis protein 10) (Q9UQW6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). Erg10 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase eg10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hcs1 (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- Probable acetyl-coenzyme A synthetase
- Probable citrate synthase, mitochondrial
- Secretory component protein psh3
- Acetyl-CoA hydrolase
- Mevalonate kinase
- Acetyl-CoA carboxylase
- Uncharacterized protein C14C4.04
- Uncharacterized protein C18G6.12c
- Small ribosomal subunit protein mS47
Sequence:
MVNTEVYIVSAVRTPMGSFGGSFASLPATKLGSIAIKGALERVNIKPSDVDEVFMGNVVSANLGQNPARQCALGAGLPRSIVCTTVNKVCASGMKATILGAQTIMTGNAEIVVAGGTESMSNAPYYAPKNRFGAKYGNVELVDGLLRDGLSDAYDGLPMGNAAELCAEEHSIDRASQDAFAISSYKRAQNAQATKAFEQEIVPVEVPVGRGKPNKLVTEDEEPKNLNEDKLKSVRAVFKSNGTVTAANASTLNDGASALVLMSAAKVKELGLKPLAKIIGWGEAAQDPERFTTSPSLAIPKALKHAGIEASQVDYYEINEAFSVVAVANTKILGLDPERVNINGGGVAMGHPLGSSGSRIICTLAYILAQKDAKIGVAAVCNGGGGASSIVIERV
Protein: LIM/homeobox protein Lhx3 (G3V8E3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MLLEAELDCHREQPGAPGAAALCTFSRTPEIPMCAGCDQHILDRFILKALDRHWHSKCLKCSDCHVPLAERCFSRGESVYCKDDFFKRFGTKCAACQLGIPPTQVVRRAQDFVYHLHCFACVVCKRQLATGDEFYLMEDSRLVCKADYETAKQREAEATAKRPRTTITAKQLETLKSAYNTSPKPARHVREQLSSETGLDMRVVQVWFQNRRAKEKRLKKDAGRQRWGQYFRNMKRSRGSSKSDKDSIQEGQDSDAEVSFTDEPSMADMGTANGLYSSLGEPAPALGRPVGGLGSFTLEHGGLAGPEQFRELRPGSPYGIPPSPAAPQSLPGPQPLLSSLVYPDTNLGLVPSGPPGGPPPMRVLAGNGPSSDLSTESSGGYPDFPASPASWLDEVDHAQF
Protein: RAB11A, member RAS oncogene family (H3BSC1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEAAFQTILTEIYRIVSQKQMSDRRENDMSPSNNVVPIHVPPTTENKPKVQCCQNI
Protein: Solute carrier family 25 member 3 (Phosphate carrier protein, mitochondrial) (Phosphate transport protein) (F8VVM2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MFSSVAHLARANPFNTPHLQLVHDGLGDLRSSSPGPTGQPRRPRNLAAAAVEEYSCEFGSAKYYALCGFGGVLSCGLTHTAVVPLDLVKCRMQVDPQKYKGIFNGFSVTLKEDGVRGLAKGWAPTFLGYSMQGLCKFGFYEVFKVLYSNMLGEENTYLWRTSLYLAASASAEFFADIALAPMEAAKVRIQTQPGYANTLRDAAPKMYKEEGLKAFYKGVAPLWMRQIPYTMMKFACFERTVEALYKFVVPKPRSECSKPEQLVVTFVAGYIGVWKGLFARIIMIGTLTALQWFIYDSVKVYFRLPRPPPPEMPESLKKKLGLTQ
Protein: At1g21010 (Poly polymerase) (Q7XJ58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F3H9.15 protein
- Uncharacterized protein At5g17350
- At3g03280
- 6,7-dimethyl-8-ribityllumazine synthase
- Basic-leucine zipper transcription factor K
- Emb|CAB85509.1
- 6,7-dimethyl-8-ribityllumazine synthase
- At3g10120
- At1g71015
- D-ribose-binding periplasmic protein
Sequence:
MGICVSFRREDSNSSPTVKIVTVNGDLREYNVPVIASQVLEAESAAAYSSSSSSRPSSYFICDSDSLYYDDFIPAIKSEEPLQADQIYFVLPISKRQSRLTASDMAALAVKASVAIQNSVKKESRRRKKVRISPVMMLTGSNDSVNGNGSETTVKKGRPFVSKTAPVKASSGINRSGSVRNLRRYTSKRAKLAVRSFRLKLSTIYEGSVV