wanglab/gogpt-training-data huggingface dataset:
Protein: Forkhead box protein O (dFOXO) (Protein FKHR) (Q95V55)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription factor involved in the regulation of the insulin signaling pathway. Consistently activates both the downstream target Thor\d4EBP and the feedback control target InR. Involved in negative regulation of the cell cycle, modulating cell growth and proliferation. In response to cellular stresses, such as nutrient deprivation or increased levels of reactive oxygen species, foxo is activated and inhibits growth through the action of target genes such as Thor. Foxo activated in the adult fat body can regulate lifespan in adults; an insulin peptide itself may function as one secondary messenger of insulin-regulated aging. Also regulates Lip4, homolog of human acid lipases, thereby acting as a key modulator of lipid metabolism by insulin signaling and integrates insulin responses to glucose and lipid homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12893776, ECO:0000269|PubMed:15175753}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:12893776, ECO:0000269|PubMed:15175753}. Note=When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. {ECO:0000269|PubMed:12893776, ECO:0000269|PubMed:15175753}.
Interaction partners:
- NAD-dependent histone deacetylase sirtuin-1
- RAC serine/threonine-protein kinase
- histone acetyltransferase
- Insulin-like receptor
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- non-specific serine/threonine protein kinase
- Stress-activated protein kinase JNK
- 14-3-3 protein zeta
- Serine/threonine-protein kinase STK11
- phosphatidylinositol 3-kinase
Sequence:
MMDGYAQEWPRLTHTDNGLAMDQLGGDLPLDVGFEPQTRARSNTWPCPRPENFVEPTDELDSTKASNQQLAPGDSQQAIQNANAAKKNSSRRNAWGNLSYADLITHAIGSATDKRLTLSQIYEWMVQNVPYFKDKGDSNSSAGWKNSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTGTMADELTLCNQQQQGFSAASGLPSQPPPPPYQPPQHQQAQQQQQQQSPYALNGPASGYNTLQPQSQCLLHRSLNCSCMHNARDGLSPNSVTTTMSPAYPNSEPSSDSLNTYSNVVLDGPADTAALMVQQQQQQQQQQQLSASLEGQCLEVLNNEAQPIDEFNLENFPVGNLECNVEELLQQEMSYGGLLDINIPLATVNTNLVNSSSGPLSISNISNLSNISSNSGSSLSLNQLQAQLQQQQQQQQAQQQQQAQQQQQQHQQHQQQLLLNNNNNSSSSLELATQTATTNLNARVQYSQPSVVTSPPSWVH
Protein: Cyclin-dependent kinase 4 inhibitor B (p14-INK4b) (p15-INK4b) (P55271)
Organism: Mus musculus (Mouse)
Function: Interacts strongly with CDK4 and CDK6. Potent inhibitor. Potential effector of TGF-beta induced cell cycle arrest (By similarity).
Interaction partners:
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 6
- G1/S-specific cyclin-D1
- Myc proto-oncogene protein
- G1/S-specific cyclin-D2
- G1/S-specific cyclin-D3
- Tumor suppressor ARF
- E3 ubiquitin-protein ligase Mdm2
- Cellular tumor antigen p53
- Cyclin-dependent kinase inhibitor 1
Sequence:
MLGGSSDAGLATAAARGQVETVRQLLEAGADPNALNRFGRRPIQVMMMGSAQVAELLLLHGAEPNCADPATLTRPVHDAAREGFLDTLVVLHRAGARLDVCDAWGRLPVDLAEEQGHRDIARYLHAATGD
Protein: Crystaline entomocidal protoxin (R4I3J1)
Organism: Bacillus thuringiensis
Interaction partners:
Sequence:
MATINELYPVPYNVLAHPIKEVDDPYSWSNLLKGIQEGWEEWGKTGQKKLFEDHLTIAWNLYKTGKLDYFALTKASISLIGFIPGAEAAVPFINMFVDFVWPKLFGANTEGKDQQLFNAIMDAVNKMVDNKFLRYNLSTLNKTIEGLQGNLGLFQNPIQVAICQGSTPERVIFDQNCTPCNPNQPCKDDLDRVASRFDTANSQFTQHLPEFKNPWSDENSTQEFKRTSVELTLPLYTTVATLHLLLYKGYIEFMTKWNFHNAQYLNNLKVELQQLIHSYSETVRTSFLQFLPTLNNRSKSSVNAYNGYVRNMTVNCLDIAATWPTFDTHNYHQGRKLDLTRIILSDTAGPIKEYTTGDKTSGPQHSNITPNNILDTPSPTYQHSFVSVDSIVYSRKELQQLDIATYSTNNSNNCHPYGLRLSYTDGSRYDYGDNQPDFTTSNNNYCHNSYTAPITLVNARHLYNAKGSLQNVESLVVSTVNGGSGSCICDAWINYLRPPQTSKNESRPDQKINVLYPITETVNKGTGGNLGVISAYVPMELVPENVIGDVNADTKLPLTQLKGFPFEKYGSEYNNRGISLVREWINGNNAVKLSNSQSVGIQITNQTKQKYEIRCRYASKGDNNVYFNVDLSENPFRNSISFGSTESSVVGVQGENGKYILKSITTVEIPAGSFYVHITNQGSSDLFLDRIEFVPKIQFQFCDNNNLHCDCNNPVDTDCTFCCVCTSLTDCDCNNPRGLDCTLCCQVENQLPSFVTLTDLQNITTQVNALVASSEHDTLATDVSDYEIEEVVLKVDALSGEVFGKEKKALRKLVNHTKRLSKARNLLIGGNFDNLDAWYRGRNVVNVSDHELFKSDHVLLPPPTLYSSYMFQKVEESKLKANTRYTVSGFIAHAEDLEIVVSRYGQEVKKVVQVPYGEAFPLTSRGAICCPPRSTCNGKPADPHFFSYSIDVGTLDVEANPGIELGLRIVERTGMARVSNLEIREDRPLKKNELRNVQRAARNWRTAYDQERAEVTALIQPVLNQINALYENEDWNRAIRSGVSYHDLEAIVLPTLPKLNHWFMSDMLGEQGSILAQFQEALDRAYTQLEESTILHNGHFTTDAANWTIEGDAHHAILEDGRRVLRLPDWSSSVSQTIEIENFDPDKEYQLVFHAQGEGTVSLQHGEEGEYVETHPHKSANFTTSHRQGVTFETNKVTVEITSEDGEFLVDHIALVEAPLPTDDQSSDGNTTSNTNSNTSMNNNQ
Protein: ATP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.93) (ATP-dependent NAD(P)HX dehydratase) (Carbohydrate kinase domain-containing protein) (NAD(P)HX dehydratase) (Q9CZ42)
Organism: Mus musculus (Mouse)
Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03157, ECO:0000269|PubMed:18614015}.
Interaction partners:
- NAD
Sequence:
MAVHACGAAAAVVALLSAAIALQWSPLYAVLQRALSLHTAHATKDMENLFQLVRNIVPALTSKKHKGQDGRIGIVGGCQEYTGAPYFAGISALKVGADLTHVFCAREAAPVIKSYSPELIVHPVLDSSNAVEEVEKWLPRLHALVVGPGLGRDDLLLNNVRGILESTKARDIPVVIDADGLWLVAQQPALIHSYHKAILTPNHVEFSRLWEAVLSSPMDSNDLKGSTLKLSQALGNITVVQKGEQDLISNGQQVLVCNQEGSSRRCGGQGDLLSGSLGVMVHWALRAGPEKTNGSSPLLVAAWGACTLTRECNRQAFQKYGRSTTTTDMITEVGTAFSRLFTT
Protein: Replication factor C subunit 1 (D3ZFT1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR036578}.
Interaction partners:
- Replication factor C subunit 3
- Replication factor C subunit 4
- Replication factor C subunit 5
- Replication factor C subunit 2
- Proliferating cell nuclear antigen
- Flap endonuclease 1
- ATPase family AAA domain-containing protein 5
- Replication protein A subunit
- DNA polymerase alpha subunit B
- DNA polymerase epsilon catalytic subunit
Sequence:
MDIRKFFGVISSGKKPVNETVKKNEKTKPSEGTVKGKKGVKEAKVNNPCKEDASRPKQHNKKKRIIYDSDSESEETVQVKNAKKKSEKLPVSCKPGKISRKDPVTYISETDEDDDFLCKKAASKSKENGVSTNSYLGASNVKKNEENTKTKSKPLSPIKLTPTSVLDYFGTESVQRSGKKMVASKKKELDLCLSCLIFFGIQSSQTPDDSRLNDEAIAKQLQLDEDAELERQLHEDEEFARTLALLDEEPKTKKARKDSEEGESFSPAKAELSKAAKQKSPANAEHFSIGRKTYSPAKYGKGRGSEGTKQPCRSAHQKEACSSLKASSKLALMKAQEENSYKETELLAAKRESAIEPKGEKTTPRKTKGSPTKRESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAAALGTKILDEDGLLDLIRTMPGKKSKYEIAAEAEMKKEKSKLERTPQKNDQGKRKLSPTKRELEPKKSKLTPLKHSPRKAVKEEERVCPRGLDAKEPHGSHSASREECLLWVDKYKPTSLKNIIGQQGDQSCANKLLRWLRNWHKSSPEEKKHAKFGKVASKDDGSSFKAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKNSLKAIVAESLNNTSIKGFYTSGASPSVSARHALIMDEVDGMAGNEDRGGIQELIGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKSAMLSIAFKEGLKIPPPAMNEIILGANQDVRQVLHNLSMWCAQSKVLTYDQAKADSQRAKKDIRLGPFDVTRKVFAAGEETAHMSLMDKSDLFFHDYSIAPLFVQENYLHVKPVAAGGDMKKHLMLLSRAADSICDGDLVDNQIRSKQNWSLLPTQAIYASVVPGELMRGYMSQFPSFPSWLGKHSSTGKHDRTVQDLSLHMSLRTYSSKRTVNMDYLSHIRDALVRPLTSQGVEGVQRVVTLMDTYYLVKEDFDNIMEVSSWGGKPSTFSKLDPKVKAAFTRAYNKEAHLTPYSLQVVKASRPSIGPALDSEYNEESQEDATQSDEKEQDALETDAMIKQKKTRSSKPSKSEKEKESKKGKGKNSKK
Protein: Sister chromatid cohesion 1 protein 4 (AtRAD21-3) (AtRAD21.3) (Q8W1Y0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in sister chromatid and centromere cohesion during mitosis.
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000305}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein SCC2
- Wings apart-like protein 1
- Wings apart-like protein 2
- Structural maintenance of chromosomes protein 1
- Protein CHROMOSOME TRANSMISSION FIDELITY 7
- Structural maintenance of chromosomes protein 4
- Sister-chromatid cohesion protein 3
- Structural maintenance of chromosomes protein 5
- Binding protein.
Sequence:
MFYSQFILAKKGPLGTIWIAAHLERKLRKNQVADTDIGVSVDSILFPEAPIALRLSSHLLLGVVRIYSRKVNYLFDDCSEALLKVKQAFRSAAVDLPPEESTAPYHSITLPETFDLDDFELPDNEIFQGNYVDHHVSTKEQITLQDTMDGVVYSTSQFGLDERFGDGDTSQAALDLDEAVFQDKDVIGSDDEGVPGIDHNAYLDAAAPGIKDSMEGVSEAMPMDFNEEQVEDLAMNNEFIEDAQAPQTPGLVEVPNSSSVREQMACDDHMDVEDLNAEEGIKSSGELNANEMPKRGEDLSSEYNAPESAVTPVEVDKSQIDENVNTQNEPEEERAEHVHVTSPCCSHITTEMEDPGQVMNEAGANVVPDKPDAVPPLETPGEENRDHFAIATEVNQETDSSLQGDEQAYSRPDGQLNNAHETDEQLGNLTGFTDSDFPPPEKVLAVPNRQGDGNDFMVESTPDKEDPGTCNDDAGNNNITGKKRTFTESTLTAESLNSVESVGLIQSKRTADSVPDDDDLLSSILVGKSSFLKMRPTPVLEPATTKRLRSAPRSTATKRKVLMDDPMVLHGDIIRQQLTNTEDIRRVRKKAPCTVPEIVMLQRQALEDGLFKEPIFTGMSVELVSLHTEPYDLRGIMIIENDDRHASVGAVEDNECSVTAVEENKTEESSDPQAHPNDCEEQPGTAHTHPQEEQTINQQEELKDDNELAEKSDLEVLKEGNGAADEVNLVVIDDVSQIPSEEKLDRVEDLQVEESHENHDGEGGQDVCADPNEKSCTDVIEIAEGDTDINPIFNEMDLKVEDELPHEDEKTDASAEVSELGRDDQTPCDNTVGSTETGCLEAGDLSNMALENCNEPLVEANSDGLNPETESYNKYEPHNEMSNEEASMQNALDGEHTSRDGLMGDNDEMDTMENAHDTGFLNVDDDEVDEDHEEDDIQYDDETRLLENSGWSSRTRAVAKYLQTLFDKETENGKNVLVADKLLAGKTRKEASRMFFETLVLKTRDYIQVEQGKPYESIIIKPRPKLTKSIF
Protein: Uncharacterized protein (Q57UX6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRCVLFTLYVITSSFLTIGGTMKDKNKCTFRYFEVLPIDHEPEYQNGYVCDICFMEYSEGPFFHCSKSGKDVCLRCGGKMGLTPFTALVSKVMRPTVYWSESESSRAIALCYQIHRDILGCHFIDGANLLISTRDDLPSYFIDSNSCIEKSIVLSRSDIERRFPWAGEVAEVMGVNAVSFHETSACNDQSRLCFLSSFRVEGAFIEFRFSDGFCELVHCENGTIVAIRDSAVLSCFLMGLPVRWGRSLPKAASSVLEWYLKGGQR
Protein: Dystrobrevin beta (DTN-B) (Beta-dystrobrevin) (P84060)
Organism: Rattus norvegicus (Rat)
Function: Scaffolding protein that assembles DMD and SNTA1 molecules to the basal membrane of kidney cells and liver sinusoids. May function as a repressor of the SYN1 promoter through the binding of repressor element-1 (RE-1), in turn regulates SYN1 expression and may be involved in cell proliferation regulation during the early phase of neural differentiation. May be required for proper maturation and function of a subset of inhibitory synapses.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O70585}. Postsynaptic density {ECO:0000269|PubMed:10545507}. Cell projection, dendrite {ECO:0000250|UniProtKB:O70585}. Basal cell membrane {ECO:0000250|UniProtKB:O70585}. Postsynapse {ECO:0000250|UniProtKB:O70585}. Nucleus {ECO:0000250|UniProtKB:O70585}. Note=Localized at inhibitory synapses on the dendrites of cerebellar Purkinje cells. {ECO:0000250|UniProtKB:O70585}.
Interaction partners:
- Dystrophin
- Beta-2-syntrophin
- Syntrophin, gamma 1
- Alpha-1-syntrophin
- Radial spoke head 3
- Protein phosphatase 1 regulatory subunit 21
- Beta-1-syntrophin
- Dysbindin
- Dystroglycan 1
- Utrophin
Sequence:
MIEEGGNKRKTMAEKRQLFIEMRAQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHATEISVSRLETVISSIYYQLNKRLPSTHQINVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTMMADPPPQCLVWLPLMHRLAHVENVFHPVECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKELSSWKSPAKKLSHAISKSLGCVPSREPPHPVFPEQPEKPLDLAHIVPPRPLTNMNDTMVSHMSSGVPTPTKRLQYGQDMPNLLADEHALIASYVARLQHCTRVLDSPSRLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKAQATGSPHTSPTHGGGRSMPMPVRSTSAGSTPTHGPQDSLSGVGGDVQEAFAQGTRRNLRNDLLVAADSITNTMSSLVKELHSGETQRFPLVSSSPSCPLPCPTIPTHSPSFHATFPSRNTRDLHPVPPSHMVSLY
Protein: Receptor-like cytosolic serine/threonine-protein kinase RBK1 (EC 2.7.11.1) (Protein ROP BINDING PROTEIN KINASES 1) (Q8H1D6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18088316}. Endomembrane system {ECO:0000269|PubMed:18088316}; Peripheral membrane protein {ECO:0000269|PubMed:18088316}. Nucleus {ECO:0000269|PubMed:18088316}.
Interaction partners:
- Rac-like GTP-binding protein ARAC5
- Rac-like GTP-binding protein ARAC3
- Probable E3 ubiquitin-protein ligase ARI1
Sequence:
MAVEDNKNSESKNHQEVELHRNDLGLEDSSSPRGVLGMVSDSDNSSSSCSSCSSDDKSSSTSSPFSNTTKTVSSSHHGLQWNKMIESIKKKSMRRFSVIPLLASYELTRKNLRRKQPKLTPSESAFTCEAFFMAKPSWRNFTYEELAVATDYFNPENMIGKGGHAEVYKGVLINGETVAIKKLMSHAKEEEERVSDFLSELGIIAHVNHPNAARLRGFSSDRGLHFVLEYAPYGSLASMLFGSEECLEWKIRYKVALGIADGLSYLHNACPRRIIHRDIKASNILLNHDYEAQISDFGLAKWLPENWPHHVVFPIEGTFGYLAPEYFMHGIVDEKIDVFAFGVLLLEIITSRRAVDTASRQSIVAWAKPFLEKNSMEDIVDPRLGNMFNPTEMQRVMLTASMCVHHIAAMRPDMTRLVQLLRGEDGPAELQQKAGERTMSVNACDLQDHTSSSYLNELRRHRQLLME
Protein: Acetylcholine receptor subunit alpha-type unc-38 (Uncoordinated protein 38) (Q23022)
Organism: Caenorhabditis elegans
Function: Alpha subunit of nicotinic acetylcholine receptor (nAChR). Probably acts in cholinergic motoneurons to regulate presynaptic neurotransmitter release, thereby ensuring normal level of excitation of cholinergic motoneurons during locomotion. Involved in nAChR sensitivity to nicotine.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:15990870}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15990870}; Multi-pass membrane protein {ECO:0000255}. Note=Co-localizes with unc-29 and lev-1 and partially with acr-12 and acr-8 at nerve cord synapses. {ECO:0000269|PubMed:15990870}.
Interaction partners:
- Acetylcholine receptor subunit beta-type unc-29
- Acetylcholine receptor subunit beta-type lev-1
- Acetylcholine receptor subunit alpha-type unc-63
- AcetylCholine Receptor
- Protein unc-50
- Acetylcholine receptor subunit beta-type acr-3
- Resistance to inhibitors of cholinesterase protein 3
- AcetylCholine Receptor
- AcetylCholine Receptor
- Ig-like domain-containing protein
Sequence:
MRSFWLFLLLLLFCISFIKLTEGNEDAKRLYDDLMVNYNRHRRPSTSPNKPLTIKLKLRLSQIIDVHEIDQIMTCSVWLKQTWIDRKLSWDPVNYGGVNVLYVPYEMIWVPDIVLYNNADSNYNITISTKATLHYTGEVTWEPPAIFKSMCQIDVRWFPFDEQQCHLKFGSWTFSENLLSVELNEPSLRYEEEIDEKGIIDNVTVAEDGIDLSDYYPSVEWDIMSRVAKRRAKNYPSCCPQSAYIDVTYYLQLRRKPLFYTVNLVFPCVGISFLTILVFYLPSDSGEKVTLCISILVALTIFFLLLTEIIPATSITLPLIGKYLLFTMVMVTLSVVVTVISLNLHFRTPTTHLMPNWVKKVFLKWLPKLLFMRRPIDDYEEKFDDKKKPKDGKIALSVHAHRVSNVGNNIRNATIDDTIQKMYYSPPVVKAFENICFIAELLKKKDRDDKIDEDWKYVAMVLDRLFLLIFSIACFVGTVIILLRAPTLYDTRQPIDLQYRPANLSANPISF
Protein: D-galactonate transporter (D-galactonate/H(+) symporter) (P0AA76)
Organism: Escherichia coli (strain K12)
Function: Involved in D-galactonate metabolism. Catalyzes the proton-dependent uptake of galactonate into the cell.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:31083648}; Multi-pass membrane protein {ECO:0000269|PubMed:31083648}.
Interaction partners:
- 2-dehydro-3-deoxygalactonokinase
- Galactonate operon transcriptional repressor
- D-galactonate dehydratase
- 2-dehydro-3-deoxy-6-phosphogalactonate aldolase
- Uncharacterized protein YjiH
Sequence:
MDIPVNAAKPGRRRYLTLVMIFITVVICYVDRANLAVASAHIQEEFGITKAEMGYVFSAFAWLYTLCQIPGGWFLDRVGSRVTYFIAIFGWSVATLFQGFATGLMSLIGLRAITGIFEAPAFPTNNRMVTSWFPEHERASAVGFYTSGQFVGLAFLTPLLIWIQEMLSWHWVFIVTGGIGIIWSLIWFKVYQPPRLTKGISKAELDYIRDGGGLVDGDAPVKKEARQPLTAKDWKLVFHRKLIGVYLGQFAVASTLWFFLTWFPNYLTQEKGITALKAGFMTTVPFLAAFVGVLLSGWVADLLVRKGFSLGFARKTPIICGLLISTCIMGANYTNDPMMIMCLMALAFFGNGFASITWSLVSSLAPMRLIGLTGGVFNFAGGLGGITVPLVVGYLAQGYGFAPALVYISAVALIGALSYILLVGDVKRVG
Protein: Dve protein (O77289)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MDFQSAMETFAEAWVAANAGQQSQALALTRAVNAAAVVASANAKSPNASSSASASLADLAVKKEHSISPPHSVVSVGVGVAGEDQHRRSSLQGVQEKLTQLQMQQQHHQQQQQQQQQQQQQQHHHHQQQAQQAGTGVGSGELAGRRSSEGTPPTAHPPTNSEGQALSSSTASSSQNATPKSDRERERERERDRDREERVERGSISCLPPAALGMAVGVQQAQHQEKLLSHPALDSRREFDVSKVNPKSLPLHCVVESVHSLHASLTIDTRQPWKRRPNIETDSYVIIAAXTPWSEIVQTALQRLGYSQEVANTARGSLIIKHWKPIPLEQISDNPAVPVSDIVGELTSVITLRIVILRPKTSPFGEIKDKLLKLLVLQSHAVLRSTGCPLDEVTLSQICRSSHQNTYALPGGEISDELRRKFDQWWSNQLSPQATAMTPKMLPFMTGPSAVPVPVAVPGEMDFPVGTAMAAAAAAAAHLAAAGGAAGGNPLGSMGSRESLLLANEAAHHAGAGQAPGPGHHGSMLVHPMHASMHHHHHHGGGGGHGPPYPNQKTRMRTSFDPEMELPKLQKWFADNPHPSRQQIQTYVVQLNALESRRGRKPLDVNNVVYWFKNARAAQKRAEMRGGSLGSAISALGHAAMNGYLSQHAPLGQNSSSSAGSQPMSMGNLSMSHDYLKSPLSLKSEDIDTMSQHSDDMDEEQSRPNTPQLPLSLTTHERHRSSPLMDEDEDEAGEQQQPQEAKSDGMNGSVKDEERQEKSRDELQDNEKENSNGEDRHLDADAQMEASSNLNNNHNNSSLHIEQEVGSTPKRSTPKEEDDDLDMDEDEEDNENDASHLDEFRSPSPDLAGGVVPHKDQLPFPMVPNSMFSQSFMYMSHYIPAFGQAAAGHPHHHAAAAAAAAGIQPNALMGGGGLNLSSISNEERRKRNRTFIDPVTEVPKLEQWFAMNTHPSHNLILKYTEDLNTMPYRQKFPRLESKNVQFWFKNRRAKCKRLKMSLYDSNQCAQLGGLGSFVPKYEERD
Protein: SUMO-conjugating enzyme SCE1 (EC 2.3.2.-) (Protein EMBRYO DEFECTIVE 1637) (Protein hus5 homolog) (SUMO-conjugating enzyme 1) (AtSCE1) (Q42551)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: SUMO-conjugating enzyme that accepts the SUMO proteins from the E1 SUMO-activating heterodimer SAE1/SAE2 and catalyzes its covalent attachment to other proteins with the E3 SUMO ligases SIZ1 and MMS21. Associates with SIZ1 for sumoylation of the transcription factor GTE3.
Interaction partners:
- Small ubiquitin-related modifier 5
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier 1
- SUMO-activating enzyme subunit 2
- Small ubiquitin-related modifier 3
- E3 SUMO-protein ligase MMS21
- Putative small ubiquitin-related modifier 6
- Putative small ubiquitin-related modifier 4
- E4 SUMO-protein ligase PIAL2
- Putative small ubiquitin-related modifier 8
Sequence:
MASGIARGRLAEERKSWRKNHPHGFVAKPETGQDGTVNLMVWHCTIPGKAGTDWEGGFFPLTMHFSEDYPSKPPKCKFPQGFFHPNVYPSGTVCLSILNEDYGWRPAITVKQILVGIQDLLDTPNPADPAQTDGYHLFCQDPVEYKKRVKLQSKQYPALV
Protein: Protein phosphatase 2C-related protein (Q54PX6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSTTNTDMIDSSSDIKDETITHNNDTVDTTKATEITADKNLEVSIDKNKENKNTADDNKEKEKEKENINNNNNNDTTNNNNSNNNNNNTPPKESNNTTTTTKSEESSSDDTYNSGTGDAPSTPQVAHQTIQPQQAQSTHFTTEPSSKTRSVRDFGVSFEKNARYRRTMEDEHVIIDCFGGDANQGYFAIYDGHGGRGAVEFTAKTLHVNLLDEINKSPEGDILELFRNSYLLTDKQMNESEIQFSGTTSITALIRKNPVDGEKYLYVANAGDARAVVCHNKVAERLSYDHKGSDPEEVKRIDAAGGFVCNGRVNGILAVTRSLGDHSMKDHVIGDPYKRSIKLDSGHTHLILACDGLWDVTSDQDAVDLILNETEAQKMSDKLLLHALKKGSTDNISIIVVIL
Protein: Cleavage stimulation factor subunit 2 tau variant (CF-1 64 kDa subunit tau variant) (Cleavage stimulation factor 64 kDa subunit tau variant) (CSTF 64 kDa subunit tau variant) (TauCstF-64) (Q8C7E9)
Organism: Mus musculus (Mouse)
Function: May play a significant role in AAUAAA-independent mRNA polyadenylation in germ cells. Directly involved in the binding to pre-mRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:14681198}.
Interaction partners:
- Cleavage stimulation factor subunit 1
- Cleavage stimulation factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 3
- Symplekin
- pre-mRNA 3' end processing protein WDR33
- Pre-mRNA cleavage complex 2 protein Pcf11
- Cleavage and polyadenylation specificity factor subunit 4
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Sequence:
MSSLAVRDPAMDRSLRSVFVGNIPYEATEEQLKDIFSEVGSVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGPAAPIIDSPYGDPIDPEDAPESITRAVASLPPEQMFELMKQMKLCVQNSHQEARNMLLQNPQLAYALLQAQVVMRIMDPEIALKILHRKIHVTPLIPGKSQPVSGPGPGGPGPSGPGGPGPGPAPGLCPGPNVMLNQQNPPAPQPQHLPRRPVKDIPPLMQTSIQGGIPAPGPIPAAVPGPGPGSLTPGGAMQPQVGMPVVGPVPLERGQMQISDPRPPMPRGPMPSGGIPPRGLLGDAPNDPRGGTLLSVTGEVEPRGYMGPPHQGPPMHHGHDNRGPASHDMRGGPLAADPRMLIGEPRGPMIDQRGLPMDGRGGRESRGMETRPMETEVLEPRGMERRMETCAMETRGMDARGLEMRGPGPSSRGPMTGGIQGPGPINMGAGGPQGPRQVPNIAGVGNPGGTMQGAGIQGGGMQGAGMQGGGMQGAGMQGGGMQGAGMQAGMQGASMQGGMQGAGMQGASKQGGGQPSSFSPGQSQVTPQDQEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAS
Protein: Flagellum-adhesion glycoprotein (Q581C1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGGRTESREALAALVAALLLLLGFVSPVIGDQTVGTKVIVNLFNSCINCSSGQADGINGTGRLFKAVGGFFKNKSFPLLLCDVGGGGSTVRLVNKTGIYTVAGNLAKRGDEVGPLEVARFNHPTSVVGVNNDIYVADRDNDCMKRIDADGMVTKFAANEVDKPSSIIYHEQDGAPVLFISDTGNSRIMYSQISVSNNVTAKLVGGFQPGVMQISKKRNFMYVVKETSWIAAVDLNSLSDSDGNKKSWDIANMSCLDYVDALMLTEDENELYYYGEPNGESHIMSLELNSSETGLLCPKKVMEWMHGPIVSLVKVNGCEYYAITETAVYAVREKCYSPTPLPPVTPTPTPGSPPRSTAVAAFRASSFPMGNDRLMHALYSWIIKDVEVAFRTEDFYAVFLPPGEINVPGGTNVSTWTNLTAMMNLENTILITNYRGPPGMSKGRAQKRLFSSPWTWTRMFLEEVSQQEQWSHLLPLCMVKCVDDCQHITLAESVCGDDSRLSRCDGVCLGGIVSSALLGAVAIVLLFLMVVSPYNVKFAFVRLPAFE
Protein: E3 ubiquitin-protein ligase TRIM11 (EC 2.3.2.27) (Protein BIA1) (RING finger protein 92) (Tripartite motif-containing protein 11) (Q96F44)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16904669, ECO:0000269|PubMed:18248090}. Nucleus {ECO:0000269|PubMed:16904669}.
Interaction partners:
- Interferon-inducible protein AIM2
- T-cell receptor-associated transmembrane adapter 1
- Ubiquitin-conjugating enzyme E2 N
- Mediator of RNA polymerase II transcription subunit 15
- Gamma-butyrobetaine dioxygenase
- Pleckstrin homology domain-containing family F member 1
Sequence:
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ