wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane E3 ubiquitin-protein ligase FLY1 (EC 2.3.2.27) (Protein FLYING SAUCER 1) (RING-type E3 ubiquitin transferase FLY1) (Q5PP23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that regulates the degree of methylesterification of pectin in seed mucilage. May be involved in the recycling of pectin methylesterase enzymes in the endomembrane system of seed coat epidermal cells. Possesses E3 ubiquitin-protein ligase activity in vitro when associated with the E1 enzyme UBA1 and the E2 enzyme UBC8. May be involved in xylem development.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:23482858}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pectinesterase inhibitor 6
- Beta-galactosidase 6
- COBRA-like protein 2
- Peroxidase 36
- UDP-rhamnose/UDP-galactose transporter 2
- Subtilisin-like protease SBT1.7
- Probable galacturonosyltransferase-like 5
- Cellulose synthase A catalytic subunit 5
- Probable pectinesterase/pectinesterase inhibitor 58
- O-fucosyltransferase 7
Sequence:
MKKREHLGLGFFEWQIILWLSIWLAISQQALGLRPIREKPRSWSDEWLFGRKQEAEVGPFSAWNITGTYRGTWKFLNSLNSSSKFQDFQKENGNSVVELVAVPTKITGVHYVQGVVVFHDVFDNEQNVGGAQINLEGVYIWPFRQLRLVANSGKESDSGQEDNNLLSNPYHLLGIFSSQVFQESPRDRLLKRKLSPVNEMEKHCNIEIAAQVSRVASSENNGDKNYYHMEGLMESPGVGDDGDCFSPLLLNATSVNVEVYYNKAVNYTLMVTFVSFLQVLLLIRQMEHGNTQSGAAKVSIVMIGQQAIMDAYLCLLHLTAGILVESLFNAFATAAFFKFVVFSIFEMRYLLAIWKATRPSNSGEGWETMRRELSFLYSRFYGILLGGILIMYQFHNYMQPILLLMYSFWIPQIVANVVRDSRKPLHPYYILGMTATRLAIPLYVFGCPHNFMRVEPNKVWCICLCTFMGLQAVILLLQHYFGSRCFVPRQMLPEKYNYHRRFNRDVSRTTDCVICMTAIDLRQHTSDCMVTPCEHFFHSGCLQRWMDIKMECPTCRRSLPPA
Protein: Large ribosomal subunit protein eL34 (60S ribosomal protein L34) (Q8SYG0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVQRLTLRRRLSYNTRSNKRRIVRTPGGRLVYQYVKKNPTVPRCGQCKEKLHGITASRPSERPRMSKRLKTVSRTYGGVLCHSCLRERIVRAFLIEEQKIVKALKSQREALVKPVKKVVEKKPVKAAAKKPAGKAAGKPGAKVAGKKPAPKGAPKGVVKSKK
Protein: Transcription factor JunB (Transcription factor AP-1 subunit JunB) (Q5U079)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCTKMEQPFYHDDSYTATGYGRAPGGLSLHDYKLLKPSLAVNLADPYRSLKAPGARGPGPEGGGGGSYFSGQGSDTGASLKLASSELERLIVPNSNGVITTTPTPPGQYFYPRGGGSGGGAGGAGGGVTEEQEGFADGFVKALDDLHKMNHVTPPNVSLGATGGPPAGPGGVYAGPEPPPVYTNLSSYSPASASSGGAGAAVGTGSSYPTTTISYLPHAPPFAGGHPAQLGLGRGASTFKEEPQTVPEARSRDATPPVSPINMEDQERIKVERKRLRNRLAATKCRKRKLERIARLEDKVKTLKAENAGLSSTAGLLREQVAQLKQKVMTHVSNGCQLLLGVKGHAF
Protein: Doublecortin domain-containing protein 2 (Q5DU00)
Organism: Mus musculus (Mouse)
Function: Protein that plays a role in the inhibition of canonical Wnt signaling pathway (By similarity). May be involved in neuronal migration during development of the cerebral neocortex (By similarity). Involved in the control of ciliogenesis and ciliary length (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q9UHG0}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UHG0}. Cell projection, kinocilium {ECO:0000250|UniProtKB:D3ZR10}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:D3ZR10}. Note=Localizes to the ciliary axoneme and to mitotic spindle fibers in a cell-cycle-dependent manner. {ECO:0000250|UniProtKB:Q9UHG0}.
Interaction partners:
- Dyslexia-associated protein KIAA0319 homolog
- Dynein axonemal assembly factor 4
Sequence:
MNGPSSRSSHLSQPVVKSVLVYRNGDPFFAGRRVVIHEKKVSSFDVFLKEVTGGVQAPFGAVRNIYTPRTGHRIRKLDQIESGGNYVAGGPEAFKKLNYLDIGEIKKRPMEAVNTEVKPVIHSRINVSARFRKSLHEPCTIFLIANGDLISPASRLLIPKKALNQWDHVLQMVTEKITLRSGAVHRLYTLEGKLVESGAELENGQFYVAVGRDKFKRLPYSELLFDKSAMRRPYGQKASSLPPMVGSRKSKGSGNYRQSKSTIGSSDNSSPQPLKRKGKKDSNSEKPTKVKQSVKSKTSHQAIPDNGEGIFKAGAERSETRGAAEVQEDEDTQVEVPVDQRPAEIVDEEEDGEKTSKDANQKEDFSAMNGETEDRGGSKAAGTSEQEEGIPDHGEKKSSPSRVNGGTDEENGEELDQVAEELQPTEDEKGKAEGDNSGQDEAGLDAQRPPRPEVTVTSPQENEENEANKASSAVA
Protein: Low-affinity gluconate transporter (Gluconate permease) (Gnt-I system) (P0AC96)
Organism: Escherichia coli (strain K12)
Function: Part of the gluconate utilization system Gnt-I; low-affinity intake of gluconate.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Thermoresistant gluconokinase
- Thermosensitive gluconokinase
- HTH-type transcriptional regulator GntR
Sequence:
MTTLTLVLTAVGSVLLLLFLVMKARMHAFLALMVVSMGAGLFSGMPLDKIAATMEKGMGGTLGFLAVVVALGAMFGKILHETGAVDQIAVKMLKSFGHSRAHYAIGLAGLVCALPLFFEVAIVLLISVAFSMARHTGTNLVKLVIPLFAGVAAAAAFLVPGPAPMLLASQMNADFGWMILIGLCAAIPGMIIAGPLWGNFISRYVELHIPDDISEPHLGEGKMPSFGFSLSLILLPLVLVGLKTIAARFVPEGSTAYEWFEFIGHPFTAILVACLVAIYGLAMRQGMPKDKVMEICGHALQPAGIILLVIGAGGVFKQVLVDSGVGPALGEALTGMGLPIAITCFVLAAAVRIIQGSATVACLTAVGLVMPVIEQLNYSGAQMAALSICIAGGSIVVSHVNDAGFWLFGKFTGATEAETLKTWTMMETILGTVGAIVGMIAFQLLS
Protein: Cell division control protein 14 (P36589)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the septation initiation network (SIN) required for cytokinesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10775265, ECO:0000269|PubMed:11384993}. Note=Localizes to the SPB prior to cytokinesis and leaves once septation is complete.
Interaction partners:
- Tyrosine-protein phosphatase CDC14 homolog
- Serine/threonine-protein kinase sid1
- Serine/threonine-protein kinase sid2
- Cell division control protein 7
- Septation initiation network scaffold protein cdc11
- Septum-promoting GTP-binding protein 1
- Cell division control protein 16
- Maintenance of ploidy protein mob1
- Cell division control protein 15
- Anillin-related medial ring protein mid1
Sequence:
MEDLLNNAKQHLCMRNPKLIRIGLRQVESIVYHVAKPSHDDKIPREIFLKLQDSPLYNSTTPCIYALDSLLEYQQNEEAYEKNFQFIQKLIDDLLHVIEGLVLIHPKSQTLFEDKATLRLFIHLLQPSQPSMLQVAAMKTLVCIMADRPLAIRLFEQINGLQQICVVFKHKQTSQDTRFQILEFFYFYLSPEPYSIDVIAYRKTRTEKQAYLSKYLSNVQGLRDDLDKFQPFGKLDETFD
Protein: Epididymal-specific lipocalin-8 (Epididymal 17 kDa lipocalin) (EP17) (mEP17) (Q924P3)
Organism: Mus musculus (Mouse)
Function: May play a role in male fertility. May act as a retinoid carrier protein within the epididymis.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Epididymal-specific lipocalin-9
- Cystatin-11
- LCN6 isoform alpha
- Epididymal secretory glutathione peroxidase
- Cystatin-12
- Epididymal-specific lipocalin-10
- Epididymal-specific lipocalin-12
- Disintegrin and metalloproteinase domain-containing protein 7
- Vomeronasal secretory protein 1
- Epididymal protein Me9
Sequence:
MEARLLSNVCGFFLVFLLQAESTRVELVPEKIAGFWKEVAVASDQKLVLKAQRRVEGLFLTFSGGNVTVKAVYNSSGSCVTESSLGSERDTVGEFAFPGNREIHVLDTDYERYTILKLTLLWQGRNFHVLKYFTRSLENEDEPGFWLFREMTADQGLYMLARHGRCAELLKEGLV
Protein: Translation initiation factor IF-2 (Q9HV55)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS4
- Ribosome-binding factor A
- Large ribosomal subunit protein uL3
Sequence:
MTQVTVKELAQVVDTPVERLLLQMRDAGLPHTSAEQVVTDSEKQALLTHLKGSHGDRASEPRKITLQRKTTTTLKVGGSKTVSVEVRKKKTYVKRSPDEIEAERQRELEEQRAAEEAERLKAEEAAARQRAEEEARKAEEAARAKAAQEAAATAGAEPAVVADVAVAEPVAKPAAVEERKKEEPRRVPKRDEDDDRRDRKHTQHRPSVKEKEKVPAPRVAPRSTDEESDGYRRGGRGGKSKLKKRNQHGFQNPTGPIVREVNIGETITVAELAAQMSVKGAEVVKFMFKMGSPVTINQVLDQETAQLVAEELGHKVKLVSENALEEQLAESLKFEGEAVTRAPVVTVMGHVDHGKTSLLDYIRRAKVAAGEAGGITQHIGAYHVETERGMVTFLDTPGHAAFTAMRARGAQATDIVILVVAADDGVMPQTQEAVQHAKAAGVPIVVAVNKIDKPEANPDNIKNGLAALDVIPEEWGGDAPFVPVSAKLGTGVDELLEAVLLQAEVLELKATPSAPGRGVVVESRLDKGRGPVATVLVQDGTLRQGDMVLVGINYGRVRAMLDENGKPIKEAGPSIPVEILGLDGTPDAGDEMTVVADEKKAREVALFRQGKFREVKLARAHAGKLENIFENMGQEEKKTLNIVLKADVRGSLEALQGSLSGLGNDEVQVRVVGGGVGGITESDANLALASNAVLFGFNVRADAGARKIVEAEGLDMRYYNVIYDIIEDVKKALTGMLGSDLRENILGIAEVRDVFRSPKFGAIAGCMVTEGMVHRNRPIRVLRDDVVIFEGELESLRRFKDDVAEVRAGMECGIGVKSYNDVKVGDKIEVFEKVEVARSL
Protein: CDK4/6 kinase (Q94877)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSYVRQLKRQKMSQAKKFGDGDPFNYQELNIIGEGAYGTVYRARDVITGNIVALKKVRISLNENGVPMSTLREISLLKQLNASNHANIVKLYEVCQFLERDGQLLILLAFEHVEQDLSDLIDRLPKSGMSPPTIQRLSRELLTGVDFLHSHRIIHRDLKPQNLLVSSQGHLKIADFGLAKTYGSEMKLTSVVVTLWYRAPEVLLAQPYNSTVDIWSAACIIFEMFNRRALFPGTSEKNQLDRIFELTGRPTEQQWPQTISVALEHFPQRHPKRPKDFCPHLCKYADDLLNKMLSYDLHLRPSALACLEHDYFQQEPL
Protein: Rifin (Q8IK40)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLNYTKILLFFFPLNILVTSYHGNNNNKTYVTSHIPTNTSRLLSEKDLQSSIYDNDPDMKSVKENFDRQTSQRFEEYEERMIPQRQKYNEQRDKDIQKIILKDKMEKSLEEKVEKGCLRCGFGLGGVAAGVGIFGSIAVNELKKAAIAKAVVVAKEAAEKAGAAAAAEAGKNAVIAGLEEMGISTLRGNVFETLFTANTYPNASEIALAINEQYNPSSCILPIGGSGPSETFCTWVKVKSDAAPKIPGKVSSTYEVIETAVKSIVTDAKTVAETAAKKATEEAIKASTDAVESAYAACQTAIIASVVAILVIVLVMMIIYLILRYRRKKKMNKKLQYTKLLNQ
Protein: Negative regulator of flagellin synthesis (Anti-sigma-28 factor) (P0AEM4)
Organism: Escherichia coli (strain K12)
Function: Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA.
Interaction partners:
- Flagella synthesis protein FlgN
- RNA polymerase sigma factor FliA
- Flagellar secretion chaperone FliS
- Flagella basal body P-ring formation protein FlgA
- Flagellar hook-associated protein 2
- Flagellar hook-associated protein 1
- Flagellin
- Flagellar basal body rod protein FlgB
- Flagellar hook protein FlgE
- Flagellar hook-associated protein 3
Sequence:
MSIDRTSPLKPVSTVQPRETTDAPVTNSRAAKTTASTSTSVTLSDAQAKLMQPGSSDINLERVEALKLAIRNGELKMDTGKIADALINEAQQDLQSN
Protein: Alaserpin (Serpin-1) (P14754)
Organism: Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Function: Inhibits elastase.
Subcellular location: Secreted, extracellular space.
Interaction partners:
Sequence:
MKIIMCIFGLAALAMAGETDLQKILRESNDQFTAQMFSEVVKANPGQNVVLSAFSVLPPLGQLALASVGESHDELLRALALPNDNVTKDVFADLNRGVRAVKGVDLKMASKIYVAKGLELNDDFAAVSRDVFGSEVQNVDFVKSVEAAGAINKWVEDQTNNRIKNLVDPDALDETTRSVLVNAIYFKGSWKDKFVKERTMDRDFHVSKDKTIKVPTMIGKKDVRYADVPELDAKMIEMSYEGDQASMIIILPNQVDGITALEQKLKDPKALSRAEERLYNTEVEIYLPKFKIETTTDLKEVLSNMNIKKLFTPGAARLENLLKTKESLYVDAAIQKAFIEVNEEGAEAAAANAFGIVPASLILYPEVHIDRPFYFELKIDGIPMFNGKVIEP
Protein: Condensin complex subunit 2 (Chromosome-associated protein H) (AtCAP-H) (Non-SMC condensin I complex subunit H) (Protein EMBRYO DEFECTIVE 2795) (Q564K3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity). Essential protein.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15883832}. Chromosome {ECO:0000269|PubMed:15883832}. Note=Localized at mitotic chromosomes from pro-metaphase to telophase. During interphase, mainly found in cytoplasm.
Interaction partners:
- Structural maintenance of chromosomes protein 4
- Condensin-1 complex subunit CAP-D2
- Structural maintenance of chromosomes protein 2-1
- ARM repeat superfamily protein
- Structural maintenance of chromosomes protein 2-2
- Structural maintenance of chromosomes protein
- Condensin-2 complex subunit H2
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1
Sequence:
MDESLTPNPKQKPASTTTRIQAPTSPFFLGSNDDRLEREQARAARAAASRRRSVIFARGSQPETESDPCFDKQQILELFQNCIKLASENKINQKNTWELNLIDHLCEIIKVEDENNTETNFQKASCTLEAGVKIYSMRVDSVHSEAYKVLGGITRAGHDDGGDHEDAAGAVENATNQKKQPEKKISPLSTLEPSFDALNVKKFDVAFAVDPLYHQTSAQFDEGGAKGLLLNNLGVYGGCQVLFDSQEIPGKLVSSANKHDKSETIDLSFVKECVEQMVLNMRKKDEIVPSLRAIINQFDEENQRPSDTFSCGQQTTESFDISHGNDASYADDDEGYENFGTSFDYEGQSGDVDENFGPNEAEPIYSNFHEEVEPASLQDMDSDDRLENVDDYLFLSLGISSKQNSWAGPDHWKYRKTKGPDVQPASEIKSSPPAKKTRKKKQAEPELDFAKALEEEMPDIFAPPKNPKTLLLPASRTPCQTKLPEDCHYQPENLIKLFLLPNVMCLGRRRRKNSGETSRQQPDDYEHGESWGNDNVYDDDDGPFDDNENDQSDAEDTNTLISQPRQVNKIDVQYDKASKQVDVQVLKETLWECLQESHQPPIQDEEHQQEPPESRSFKVLLASFPDDCQAAERTQDISPHLCFICLLHLANEHNLSLIGSQNLDDLTIHLA
Protein: Ribonuclease VapC43 (RNase VapC43) (EC 3.1.-.-) (Toxin VapC43) (P9WF55)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB43.
Interaction partners:
- Antitoxin VapB43
- Putative antitoxin VapB7
- Ribonuclease VapC7
- Ribonuclease VapC4
Sequence:
MLCVDVNVLVYAHRADLREHADYRGLLERLANDDEPLGLPDSVLAGFIRVVTNRRVFTEPTSPQDAWQAVDALLAAPAAMRLRPGERHWMAFRQLASDVDANGNDIADAHLAAYALENNATWLSADRGFARFRRLRWRHPLDGQTHL
Protein: SEC14 like lipid binding 2 (SEC14-like 2 (S. cerevisiae), isoform CRA_c) (cDNA FLJ34083 fis, clone FCBBF3004409, highly similar to SEC14-like protein 2) (B3KRD8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLRKVIQQYLSGGMCGYDLDGCPVWYDIIGPLDAKGLLFSASKQDLLRTKMRECELLLQECAHQTTKLGRKVETITIIYDCEGLGLKHLWKPAVEAYGEFLCMFEENYPETLKRLFVVKAPKLFPVAYNLIKPFLSEDTRKKIMVLGANWKEVLLKHISPDQVPVEYGGTMTDPDGNPKCKSKINYGGDIPRKYYVRDQVKQQYEHSVQISRGSSHQVEYEILFPGCVLRWQFMSDGADVGFGIFLKTKMGERQRAGEMTEVLPNQRYNSHLVPEDGTLTCSDPGIYVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK
Protein: Netrin-B (Q24568)
Organism: Drosophila melanogaster (Fruit fly)
Function: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either fra or unc-5 receptors will lead to axon attraction or repulsion, respectively. While short-range repulsion requires both fra and unc-5 receptors, long-range repulsion only requires unc-5.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29513217}. Note=Expressed in the perinuclear region of the oldest most anterior lamina neurons at 24 hours after puparium formation. {ECO:0000269|PubMed:29513217}.
Interaction partners:
- FI24025p1
- Netrin receptor unc-5
- Uncharacterized protein
- Roundabout 1, isoform A
- Down syndrome cell adhesion molecule 1, isoform BX
- MIP08606p
- Roundabout 2, isoform B
- Protein slit
- LP22668p
- receptor protein-tyrosine kinase
Sequence:
MVRATGTRMGLLLPIILALAIGSSAAGISSNDPCYFEGKPRKCLPSFVNAAYGNPVQASSVCGAQQPERYCELLRDGNAGECRSCEQQRYGPAALTDLNNPSNVTCWRSGAVNVPHDPDSAPPDNVTLTLSLGKKYELTYISLSFCPRSPRPDSLAIFKSSDFGQTWQPFQFYSSQCQKFYGRPDRAKISKFNEQEARCINSQHDTGGAAQRFAFNTLEGRPSANDLDSSLVLQDWVTATDIRVVFHRLELPPQLLKVKNANAFSDEMGGSREEDEDDDADLELDGEQDEYDYNLQDNDSADAGYDEYEEPKKHLELDDDHLHLDYASDGESVVKRQGKHKGSAYEKHYQSKLAATTPPQQPPKVTPPGKVTPPSTAAPSAAASAVTLPISQHYAVSDFAVGGRCKCNGHASECVATVSSGSGTALSDQDDGQDEDTPSAPSLANHFGRSTQMSAKLTMTCACKHNTAGPECERCKPFYFDRPWGRATDNDANECKMCQCNGHARRCRFNLELYKLSGRVSGGVCYNCQHDTTGRYCHYCREGYYRDATKPPNHRKVCKRCDCHPVGSTGKTCNHLSGQCPCKEGVTGLTCNRCARGYQQTRSHVAPCIKVPTNANMIQAESAGGGGGGGTGDYKDGGGSQVEEMKKYCGKCKASPKKLNLNKFCMEDYAILAKVIGHDRASQDISTEKFSIERQNEIYKYEINIQTIFKRNPMSGTTSSLLGRGNMMLLVPRKSIECQCPKIKLNKSYLILGRDSEAAPGYLAIGPSSVVLEWKDEWSLRMKRFQRRARKCS
Protein: TraO protein (Q46704)
Organism: Escherichia coli
Interaction partners:
Sequence:
MKKLLLSAVVLSVLGGAATNVMALEVGRNSPYDYRIKSVVYNPVNVVKIDAVAGVATHIVVAPDETYITHAFGDSESRTFAHKMNHFFVKPKQAMSDTNLVIVTDKRTYNIVLHFIGEETKKNADGTVSKSFIETPWAVRHAVLQLTYEYPFEQQEKAKSAADKKRITQKLKQTAFAGAKNYQYVMSEQPEMRSIQPVHVWDNYRFTRFEFPANAELPQVYMISASGKETLPNSHVVGENRNIIEVETVAKEWRIRLGDKVVGVRNNNFAPGRGAVATGTASPDVRRVQIGEDN
Protein: KLF transcription factor 1 (A0A8I5ZPH7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
NPFSHPECCSCRGCFRARYPVPTIQAVRSLPQWWRSEETQDLGPGPPNPTEPSFHVSLKSEDPPGEDDERDVTCAWDPDLFLTNFSGPEPPSTPRTCALAPSGGPVAQFAPPESLSAYAGGPGLVTGPLGSEEHAGWAHPTPRPPTPEPFVAPVLAPGLAPKAQPAFSESRAVSAGGFFPRAGLAVPAAPSAPYGLLSGYPALYPAPQYQGHFQLFRGLAAPSAGPTAPPSFLNCLGPGAVGTELGATAIAGDAGLSPGAAPPKRSRRTLAQKRQAAHTCGHEGCGKSYTKSSHLKAHLRTHTGEKPYACSWDGCNWRFARSDELTRHYRKHTGHRPFCCGLCPRAFSRSDHLALHMKRHL
Protein: NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) (P00388)
Organism: Rattus norvegicus (Rat)
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
Interaction partners:
- Cytochrome b5
- Cytochrome b5 type B
- Heme oxygenase 1
- Cytochrome P450 3A1
- Cytochrome P450 2B1
- Cytochrome P450 3A
- Cytochrome P450 1A1
- Lanosterol 14-alpha demethylase
- FAD synthase
- Cytochrome P450 2E1
Sequence:
MGDSHEDTSATMPEAVAEEVSLFSTTDMVLFSLIVGVLTYWFIFRKKKEEIPEFSKIQTTAPPVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEESSIRQYELVVHEDMDVAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEAKSGRVNKGVATSWLRAKEPAGENGGRALVPMFVRKSQFRLPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS
Protein: Pyruvate kinase (PK) (EC 2.7.1.40) (Q07637)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Interaction partners:
Sequence:
MNKRVKIVSTLGPAVEIRGGKKFGESGYWGESLDVEASAKNIAALIEEGANVFRFNFSHGDHPEQGARMATVHRAEEIAGHKVGFLLDTKGPEMRTELFADGADAISVVTGDKFRVATKQGLKSTPELIALNVAGGLDIFDDVEIGQTILIDDGKLGLSLTGKDAATREFEVEAQNDGVIGKQKGVNIPNTKIPFPALAERDDADIRFGLSQPGGINFIAISFVRTANDVKEVRRICEETGNPHVQLLAKIENQQGIENLDEIIEAADGIMIARGDMGIEVPFEMVPVYQKLIISKVNKAGKIVVTATNMLESMTYNPRATRSEISDVFNAVIDGTDATMLSGESANGKYPRESVRTMATVNKNAQTMLKEYGRLHPERYDKSTVTEVVAASVKNAAEAMDIKLIVALTESGNTARLISKHRPNADILAITFDEKVERGLMINWGVIPTMTEKPSSTDDMFEVAEKVALASGLVESGDNIIIVAGVPVGTGRTNTMRIRTVK
Protein: PHO85 cyclin-2 (Cyclin HCS26 homolog) (G1/S-specific cyclin PCL2) (P25693)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: G1/S-specific cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Essential for the control of the cell cycle at the G1/S (start) transition. Together with cyclin PCL1, positively controls degradation of sphingoid long chain base kinase LCB4. The PCL2-PHO85 cyclin-CDK holoenzyme phosphorylates LCB4, which is required for its ubiquitination and degradation. PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14688790}. Nucleus {ECO:0000269|PubMed:14688790}. Note=Localizes to sites of polarized growth, namely the incipient bud site, the bud tip and the bud neck.
Interaction partners:
- Cyclin-dependent protein kinase PHO85
- PHO85 cyclin-1
- PHO85 cyclin CLG1
- PHO85 cyclin-9
- PHO85 cyclin-5
- Cyclin-dependent kinase 1
- G1/S-specific cyclin CLN1
- Transcriptional factor SWI5
- G1/S-specific cyclin CLN2
- PHO85 cyclin-6
Sequence:
MSNYEALLKFNRKAVSKEMVQYLASTTASIIKIKKTNSMIDIALPAPPLTKFINRLIKHSNVQTPTLMATSVYLAKLRSIIPSNVYGIETTRHRIFLGCLILAAKTLNDSSPLNKHWAEYTDGLLILREVNTIERELLEYFDWDVTISTDDLITCLSPFLKPIKEEQLYKSQRDCRTLKNFSAQEKDIVNKTSISHSRSSSNMSIPSLASTSTLSTLESRRSNLSNYSNRIRTLPELHESNNISDKFSPRTYNIDSKHDNKENRPIPTIKPFNFSKARPVILKTGLNKQIIKEDTKVKKSNWSNYFKS
Protein: Elongation factor 1-alpha 2 (EF-1-alpha-2) (EC 3.6.5.-) (Eukaryotic elongation factor 1 A-2) (eEF1A-2) (Statin-S1) (P62631)
Organism: Mus musculus (Mouse)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q05639}.
Interaction partners:
- Elongation factor 1-beta
- Elongation factor 1-gamma
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran, testis-specific isoform
- Heat shock factor protein 1
- Small ribosomal subunit protein uS5
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Elongation factor 1-alpha 1
Sequence:
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWKVERKEGNASGVSLLEALDTILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNVCGDSKADPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKKSGGAGKVTKSAQKAQKAGK
Protein: Lysophospholipase 1 (EC 3.1.1.5) (Phospholipase B 1) (P39105)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase B and lysophospholipase activities. It also displays transacylase activity. Substrate preference is phosphatidylserine > phosphatidylinositol >> phosphatidylcholine > phosphatidylethanolamine. The substrate specificity is pH- and ion-dependent. In contrast with activities observed at optimum pH 3.5, the order of substrate preference at pH 5.5 is phosphatidylcholine = phosphatidylethanolamine >> phosphatidylinositol. Degrades predominantly phosphatidylcholine and to some extent phosphatidylinositol in vivo.
Subcellular location: Cell membrane {ECO:0000305|PubMed:10383953, ECO:0000305|PubMed:10497163}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:10383953, ECO:0000305|PubMed:10497163}.
Interaction partners:
- Lysophospholipase NTE1
- Lysophospholipase 2
- Lysophospholipid acyltransferase
- Triacylglycerol lipase 5
- Triacylglycerol lipase 4
- Glycerophosphocholine phosphodiesterase GDE1
- Lysophospholipase 3
- Ceramide synthase LAC1
- Superoxide dismutase
- Orotate phosphoribosyltransferase 1
Sequence:
MKLQSLLVSAAVLTSLTENVNAWSPNNSYVPANVTCDDDINLVREASGLSDNETEWLKKRDAYTKEALHSFLNRATSNFSDTSLLSTLFGSNSSNMPKIAVACSGGGYRAMLSGAGMLAAMDNRTDGANEHGLGGLLQGATYLAGLSGGNWLTSTLAWNNWTSVQAIVDNTTESNSIWDISHSILTPDGINIFKTGSRWDDISDDVQDKKDAGFNISLADVWGRALAYNFWPSLHRGGVGYTWSTLREADVFKNGEMPFPITVADGRYPGTTVINLNATLFEFNPFEMGSWDPTLNAFTDVKYLGTNVTNGKPVNKGQCIAGFDNTGFITATSSTLFNQFLLRLNSTDLPSFIANLATDFLEDLSDNSDDIAIYAPNPFKEANFLQKNATSSIIESEYLFLVDGGEDNQNIPLVPLLQKERELDVIFALDNSADTDDYWPDGASLVNTYQRQFGSQGLNLSFPYVPDVNTFVNLGLNKKPTFFGCDARNLTDLEYIPPLIVYIPNSRHSFNGNQSTFKMSYSDSERLGMIKNGFEAATMGNFTDDSDFLGCVGCAIIRRKQQNLNATLPSECSQCFTNYCWNGTIDSRSVSGVGNDDYSSSASLSASAAAASASASASASASASASGSSTHKKNAGNALVNYSNLNTNTFIGVLSVISAVFGLI
Protein: Testis-enriched HMG-box-containing protein 2, isoform A (Q9VCZ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDYGARPKKPMSAFMLWMNSTGRKNIRAEHPDFSVQEVSVKGGEMWRAMADEHKIVWQESASKAMAEYKEKLEKWNAFKEHQTESFPHIYEAPLSSRFSKTNQRPTLFVYDSKDEAMAPICRTCFSKAKCFH
Protein: Lactoylglutathione lyase (EC 4.4.1.5) (Glyoxalase I) (Q8IIM5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- hydroxyacylglutathione hydrolase
- hydroxyacylglutathione hydrolase
- Glyoxalase I-like protein GILP
- NADH-cytochrome b5 reductase, putative
- FAD-dependent monooxygenase, putative
Sequence:
MAQEISNLVKKYNVTWQQTMLRIYDPKETVEFYEKNFGMINIHTYHFNEYNFSLYFLITPPYDEEERKKLPEPNTKESEKYLWNLNTVCLELTYNHNSQEKLSNGNNENDRGFGHIAFNCNDVIEQCDNLFKKNVKFHKLPHETKMKTIGFALDPNNYWIEIVKRSNQVKWKNYKNITNFSQTMIRVKNPEKSLYFYIHILGMKLIHVKHCSDFSLYFLKSNYACAENNKEMIEDQSNKNTNEIYDFNSLKNSYQTDEDYENFKQSWEPVLELTHNHGTEDDDNFSYHNGNTEPRGFGHIGFLVNDLENYCKELETLNVTFKKKVTEGLMKNIAFIYDPDNYVIELIQRDTSFIAK