wanglab/gogpt-training-data huggingface dataset:
Protein: Retinoblastoma-like protein A (Q54FX2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters (By similarity). Plays a dual role, regulating cell-cycle progression and transcriptional events leading to terminal differentiation. In the absence of a G1 phase, functions in late G2 controlling the expression of both S-phase and mitotic genes. Controls stalk/spore preference by suppressing the DIF response in cells destined for the spore pathway. DIF is a chlorinated hydroxyphenone made by cells of spore pathway that promotes stalk differentiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q08999}.
Interaction partners:
- Transcription factor E2F/dimerisation partner family protein
- Transcription factor E2F/dimerisation partner family protein
- RmlC-like cupin family protein
- Probable histone-binding protein rbbD
- Cyclin-dependent kinase 1
- G2/mitotic-specific cyclin-B
- Anaphase-promoting complex subunit cdh1
- NuA4 complex subunit EAF3 homolog
- Type-1 histone deacetylase 1
- Tesmin/TSO1-like, CXC domain-containing protein
Sequence:
MMAHNKNDLTNINTKTTAPTTTTTEQQPEQQQQQPEQQQQEKQNNNNNNNNNNNNNNNINNNENNENNNNDIINNKINLLDELVAAAELKGRYTQIQLEELKSKLDRTSSALNVDQDTIKLAWCLLENMQLVSVDTSEQFQKQIVACSLFICGNKKFSSLLYNLNQPSSSSFQPDNNSKIKGRKIRKTNNSKNKNNDSNEEEEETTTDTEEEEEEDTLLNENNNSINKNSSNNNELLVSIRSCINESGGDSQFLQNSVFLSQLLKHFEGEIKLSQFFDTLRSFISNLRLGNAFEEQGRQLEQSFNTLNNLYRKYEQIFFTLFHPTENYILKTTQQHNYNNNSNNNNNNNNNNNNNNNNNRTNEDYLLSIGWLIFLFCKNKLFTKDSPDFVQSLHLLLCIINFIYVNTSISELKKIPQGVQIIDTATGDILLYLAKSIPCNLDDLSNVNQNIFSTYSNLLINNSILKLFDNNNNNNNNNNNNNNNSDGIKSIFNNSSIIKDNYNSLNKSYELYYYANGDIDERLFYSFDHDIYVLNNNNNNQNNNNNNNNHNNNYYNNNNNNNNNNNNNNHLNYQYSSLLPPSTPTTPSRYGSSSSSGGGGGGNLRKNIYGTPSKSLSAGNLGSVIPQTPISLTLTLESWLKVEIQNYRDPNPSLNLINILKSADQPQQTSEVDKMIERVSSLTNNTDSLFSIGGIDDHQQQQQQQQEVKQRRKNMAIQLYYCLLEKLIKFEQNTSSNINVLLNHEDFHKSLLSNSFEIIAYVYKMEGLYFPHFINVFKLHPFSYLRLIDLVLKVDADLPKLLAQHFSQIEEKILEKYVWSNNSTVFSTIKSHDFQNIFNSNGVGAAITTHLRPTQVFSTPTKNQNNNPFRNQQLINTNIPNTPTKKNPFIQNFIKKVSTLIIAKCRKLIHAMGLSSDYVVQIYQVMIKILIDETLLFKNREIDVLLICSIYAICKVNSKNITFKAIIDKSCISAKVYKEVYIGNDENNNNNNNNNNNNNNNNNNNNNNINNNNNNNENNNNNNNPVKGDIILFYNKIFLTKMDPYIHEVFSKYQQQQQHQYQQPLQNLPPPLLNQNSPKKWNPLFHTPTKNQNNNPYNSNNNTPNKFSSSIPLSPQKGVNYNSSFSVNSMVTISPMKQHTPISSSYTYIVAKSPSKELFQINQCLNKKKNDEMVPPPPTTPSSINNNNNNNNNNNNNNNNNNNNNSNDNNNNNNNNNNNNNNNNSNNNSNNNNNTEKKMVGKRLLFDYEESPSTPSSSSSPTILNNNKKNNNNNKSENVDDPGNNSPSSSPLSSSSSSSSSSSSGGRKRLKS
Protein: DJ576K7.1 (FK506 binding protein 12-rapamycin associated protein 1) (Q96QW8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
EIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGD
Protein: Protein STD1 (Glucose repression modulator MSN3) (Suppressor of Tbp deletion protein 1) (Suppressor of fluoride sensitivity 3) (Q02794)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in modulation of glucose-regulated gene expression. Together with MTH1, represses the hexose transporter (HXT) genes in conditions of low glucose. Stimulates the SNF1 kinase by an interaction with the catalytic domain that antagonizes autoinhibition and promotes an active conformation of the kinase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10373505}; Peripheral membrane protein {ECO:0000269|PubMed:10373505}. Nucleus {ECO:0000269|PubMed:10373505}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Glucose transport transcription regulator RGT1
- Low glucose sensor SNF3
- High glucose sensor RGT2
- Carbon catabolite-derepressing protein kinase
- Casein kinase I homolog 1
- General transcriptional corepressor CYC8
- Low-affinity glucose transporter HXT1
- Low-affinity glucose transporter HXT3
- Plasma membrane ATPase 1
Sequence:
MFVSPPPATARNQVLGKRKSKRHDENPKNVQPNADTEMTNSVPSIGFNSNLPHNNQEINTPNHYNLSSNSGNVRSNNNFVTTPPEYADRARIEIIKRLLPTAGTKPMEVNSNTAENANIQHINTPDSQSFVSDHSSSYESSIFSQPSTALTDITTGSSLIDTKTPKFVTEVTLEDALPKTFYDMYSPEVLMSDPANILYNGRPKFTKRELLDWDLNDIRSLLIVEQLRPEWGSQLPTVVTSGINLPQFRLQLLPLSSSDEFIIATLVNSDLYIEANLDRNFKLTSAKYTVASARKRHEEMTGSKEPIMRLSKPEWRNIIENYLLNVAVEAQCRYDFKQKRSEYKRWKLLNSNLKRPDMPPPSLIPHGFKIHDCTNSGSLLKKALMKNLQLKNYKNDAKTLGAGTQKNVVNKVSLTSEERAAIWFQCQTQVYQRLGLDWKPDGMS
Protein: Carnosine dipeptidase 2, isoform A (EC 3.4.13.-) (RE11562p) (Q8MT58)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Histidine decarboxylase
- Carnosine N-methyltransferase unmet
- (S)-3-amino-2-methylpropionate transaminase (GABA aminotransferase) (Gamma-amino-N-butyrate transaminase) (L-AIBAT)
- Uncharacterized protein, isoform B
- aldehyde dehydrogenase
- Beta-ureidopropionase
- Aldehyde dehydrogenase type III, isoform Q
- Glutamate decarboxylase
- aldehyde dehydrogenase
- Black, isoform A
Sequence:
MPELSSELQKFFAFVDGKKEDYIGALKTVVGIQSVSAWPEKRGEIGRMVEWTADRLRSLGAETELADVGQQTLPNGQIIPLPKVLLGTLGKDPSKKTVLVYGHLDVQPALKEDGWNTNPFELTEVDGKLFGRGASDDKGPVLCWIHAIEAYQKLNIALPVNVKFVFEGMEESGSEGLDDLLLERKDNFLADVDFVCISDNYWLGKKRPCLTYGLRGLAYFQVEVECSSKDLHSGVFGGTVHEAMPDLCHLLSILVDKDTNILVPGVDRDVAPQIKNEQSIYENIDFEVSEYKKDIGVEQLPHNGDKTRLLQARWRYPSLSVHGIEGAFYEPGAKTVIPKKVIGKFSIRLVPNQDPKHIEECVVKYLNDKWAERGSPNKMKVTMLSAGKPWTEDPNHPHYEAAKRAIKHVFNVEPDMTREGGSIPVTLTLQEATGKNVILVPVGACDDGAHSQNEKIDIYNYIEGTKLLGAYLHEVGKL
Protein: ATP-sensitive inward rectifier potassium channel 1a.1 isoform X2 (Potassium inwardly rectifying channel subfamily J member 1a, tandem duplicate 1) (Q1L8I4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 1b
- Barttin
- Solute carrier family 12 member 1.
- Ammonium transporter Rh type C-like 2
Sequence:
MTRSLREWFKEYMSERRGRKNRLVTKDGRCNIEFGNVMHRNRFAYVLDFWTTFVETRWRFILLYFVASFTLSWFIFGLIWYWLARNNGDLLWQNPPPGHKPCAFSVNDMTYAFLFSLETQSTIGFGNIYVTDQCPGGVALIVIQTIIGLFINIFWCGIVMTKISLPKKRAKTITFSESAVICPKKGTLCLQIRVANLRKTLMIGSQIYGKLLRTTVTGGETVILDQVSIDFMVDAGKDNLFFVCPLTLYHIIDKSSPFFNMAVDTMHQQDFELVVFLDGMAESTSSACQVRTSYIPQEIMWGYDFLPIISRSKEGRYRVDFSNFAKVVPVPTAHCTHCYHNEPGNHLHLKGIDNKGFEVIDIEPPNGTKM
Protein: U6 snRNA-associated Sm-like protein LSm4 (A0A8I6APJ0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365049}.
Interaction partners:
Sequence:
MRGHTLPLSLLKTAQNHPMLVELKNGETYNGHLVSCDNWMNINLREVICTSRDGDKFWRMPECYIRGSTIKYLRIPDEIIDMVREEAAKGRGRGGPQQQKQQKGRGMGGAGRGRVTMRGGRQASSEQSQPELSPGRWVRRPPGAFA
Protein: Threonine--tRNA ligase, mitochondrial (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase-like 1) (Q9BW92)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Leucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase 2, cytoplasmic
- Valine--tRNA ligase
- Alanine--tRNA ligase, mitochondrial
- Threonine--tRNA ligase 1, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Isoleucine--tRNA ligase, mitochondrial
- Asparagine--tRNA ligase, cytoplasmic
Sequence:
MALYQRWRCLRLQGLQACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASMAQKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEYGFYHDFFLGKERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLSNSSSLWRSSGAPETLQRVSGISFPTTELLRVWEAWREEAELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDRPPSSQSDDSTRHITDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGQAGALERPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTRVPNAEEIF
Protein: Perilipin-5 (Lipid storage droplet protein 5) (M0R7Z9)
Organism: Rattus norvegicus (Rat)
Function: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648}. Cytoplasm {ECO:0000250|UniProtKB:Q8BVZ1}. Mitochondrion {ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648}. Note=Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm. {ECO:0000250|UniProtKB:Q8BVZ1}.
Interaction partners:
- Patatin-like phospholipase domain-containing protein 2
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Perilipin-1
- Perilipin
- Hormone-sensitive lipase
- Lipid transferase CIDEC
Sequence:
MDQRGKDTTLALHSRMSGDQTAQDPGSSLGELDQHNVVKRVVALPLVRATCTAVSGAYNSAKDRHPLLGSACRFAEHCVCSVATCALDHAQPLLEHLQPKLATVNDLACRGLDKLEEKLPFLQQPSDTVVTSAKDAVAKSVTGVVDLAQRGRRWSGELRRSVSQAMDTVLRRSVSQAMDTVLGKSEELVDHFLPMTEAELVALATESQGPEVGSVEEQRQKQGYFVRLGSLSARLRHLAYQHSLGKLRESKHRTQEMLAQLQKTLELIQHMQSRASPTPTFHHPKVQELCGDWSPCLENGYRHSQVELETLALSRSLTLELQSAVDALAGCVRGLPPSAQAKVAEVQRSVDALQATFADAHCLGDVAPTALAEGQDSVAQAHACVDEFLDLVLRAMPLAWLVGPFAPILVERSEPLINLATCVDEVVGDPDPRWAHMDWPAQQRAWEAEPADPGGQEAEPPLGQVKHTMMPELDF
Protein: DISCO interacting protein 1, isoform F (Q9W5S7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSVGQRVAFLSTHWTSPLQAANVQEQQSSPVALYPTSASPVAVQSPQDAFLAVQSPGAPAPVQLANSSDQQNNPDADAIASKLPMPVIIKEEPISVNDEPSVDNIEDNTSASTSASGIGGKIPFKKIFQKRKKSSERTRDKKLRQNRQLRKSMLPKNALMALNEVKGVTISDFTIDSNTDGGFTAVVTVNSNQYEGKGTSKMTAKNAACEKAWRDFIIAKMTPKPPRIHQVEMGSEPMDINEDEADAPDDDLPMLNLASFAIYKLFAEWEREGYVVPEMHPSANAAQQAGGDAGTPVPPVPKEPKKPPVRTELPSGWETMHPATILCIMRPGLNYVDYGSSGDKTNGMQHLGIMVDNQEFHANGRSKKIARRNVAVKVCNSLFGTNFTYSDTT
Protein: Uroporphyrinogen-III synthase (UROIIIS) (UROS) (EC 4.2.1.75) (Hydroxymethylbilane hydrolyase [cyclizing]) (Uroporphyrinogen-III cosynthase) (P87214)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Interaction partners:
- Porphobilinogen deaminase
- Uroporphyrinogen decarboxylase
- Probable uroporphyrinogen-III C-methyltransferase
- Delta-aminolevulinic acid dehydratase
- Ferrochelatase, mitochondrial
- Siroheme biosynthesis protein met8
- Probable oxygen-dependent coproporphyrinogen-III oxidase
- Protoheme IX farnesyltransferase, mitochondrial
- Lipoyl synthase, mitochondrial
- Protoporphyrinogen oxidase
Sequence:
MKTALLLKTKSQPFDPYVEAFEKYGRDTAFIPVLRHKRVHEEQLRDKLKNVRKTYCGLIVTSQRVSETLDEALKQEDETERQKILMETPIFTVGPATDDSIRRLGFQQTHGKDCGRGEVLADLIEEWYTTTKQHKPLLFLVGEKHRDIIQRKLGDDRVDSLIVYATQELENTETQIKDTIRKHPTIDWIVAFSPTSICSLLNTFELKIATIGPTTGDYLKKLGTQPNVVSPAPNPESLASSIVAFDEENSS
Protein: Myomesin-3 (Myomesin family member 3) (A2ABU4)
Organism: Mus musculus (Mouse)
Function: May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle.
Subcellular location: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:18177667}.
Interaction partners:
Sequence:
MTLPHSPGSAGEPQASQTVQVHRLEHRQEEEQKEERQHSLQMGSSVQRRTYRSSEEEQQFSSEDYALAAALALTASSELSWEAKLRRQTTTVELEERGQRRVGFGNDLERMELAFLRTQRLLRQRRDWKALRQRTEEKVREAKELIELCSGRGPWFWIPLRSHAVWEHTTVLLTCTVQGSPPFQVTWYKNDIRIDPRLFPAGKYRITNNYGLLTLEIMRCTVEDSATYTVLVKNAYGQASSFAKVLIRNYLGKDAGFDSEIFKRSMFGPSAEFTSVLKPIFAQEKEPFSLTCLFSDDVLEAEQRIQWYRDGRLLRSSTRRQILYADRQASVKVSCAYKEDEGFYTIRVSSPFGPQEQSAYVFIRDAAAEKPGAPGSPLNVRCLNVHRDCLTLTWVPPSDTRGSTITGYSIEMCQGDSEEWMPCLKAPGGTCRCPIQGLVEGQSYQFRVRAISKAGTSLPSKASEAVVTGDYDAVHKSTEIPYDLGSKITISKNDFEDAVTIPSAPTNVHASEIREAYAVLSWEEPRPRGRAPLTYTLEKSVIGSGTWEAISTETPIKSPRFALLDLEKGKSYVFRVRALNQYGMSDPSEPSEPVALKGKPATLPPPAQVQAFRNTQTSVSLAWEPVDGGSELLGYYIYSREAGASEWQTVNNKPIQDTKFTVPGLRTGKEYDFCIRSVSEAGVGESSAATQPVRVKQALATPSAPYDFALLNCGKNEMVIGWKPPKRRGGGKILGYFMDQHDSVESDWHPVNRQPIPSRVCKVTNLHEGHFYEFRARAVNWAGIGELSAPSSLFECKEWTMPEPGPPYDVRVSEVQATSVMLQWEPPLYIGAGPVTGYHVSFQEKGSEEWKPVTPDATSDTHLRVSDLQPGKQYMFRVQAMNSAGLGQPSVPTDPVLLEDKPDAQEIEVGVDDEGQIYLAFEAPEAPDFPEFQWSKDYQGPPDPQRVEVEDEISKSKVILKEPDLQDLGIYSVVVPDADEDTSASHTLTEEELNKLKKLSHEIRNPVIKLISGWNVEILEQGEVRLWLEVEKLSPAAELHLIFNEKEIFSSPNRKINFDREKGLVEVIIQQLSEDDKGSYTAQLQDGKAKNQITLALVDDEFDKLLRKADAKRRDWKRKQGPYFQEPLTWKVTDDCQVLLSCKVTNTKKESRFQWFFQKKEAPHGQYNPPTGDGSLSIEGFSKENQGVYRAVVSDERGEDDTVLDLTGEALDAVLTELGRIGALSATPLKIQGTEEGIRLFSKVKYYNVDYMKTAWFHKDKRLESGDRVRAGTTLDEIWLHILDPKDSDKGKYTLEITAGKEVRQLSADLSGQAFDDALAEHQRLKALAVIEKNRAKVVRGLPDVATIMEDKTLCLTCVISGDPSPEISWLKNDQPISFFDRYHMEVKGTEVTVTIDKVTSEDSGRYGIFVKNKYGSETGQVTISVFKHGEEPKELKKK
Protein: Anaphase-promoting complex subunit 11 (EC 6.3.2.-) (Q12157)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably catalytic subunit of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. APC11 is required to recruit the ubiquitin-conjugating enzyme E2 to the APC/C.
Interaction partners:
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit SWM1
- Anaphase-promoting complex subunit DOC1
- Anaphase-promoting complex subunit 9
- Anaphase-promoting complex subunit MND2
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit CDC27
Sequence:
MKVKINEVHSVFAWSWHIPSTSDEDAANNDPIGNDEDEDVCGICRASYNGTCPSCKFPGDQCPLVIGLCHHNFHDHCIYRWLDTPTSKGLCPMCRQTFQLQKGLAINDAHVQKFVEIVSRRREEMIEEGVAEEFVDFDEPIRQNTDNPIGRQQVDTILDEDFLLR
Protein: CRAL-TRIO domain-containing protein C23B6.04c (Q9UU99)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cell membrane {ECO:0000269|PubMed:10759889}; Peripheral membrane protein {ECO:0000269|PubMed:10759889}. Note=Cell periphery.
Interaction partners:
- Probable pyridoxamine 5'-phosphate oxidase
Sequence:
MKDSEHHHHGHNGFSKFLHKLGFGKSKGKSHKSNTSSIHERENTAAKGPASNVRPARPNVSTSSTSNEVRKSVPVGNPTVHTKTGSSSSPASKMRNTVNLQHIQAANQKTRNAEGERKVAQRRVQSDKAEANDAAMSSSAPTVDVSEGNSAAEPKITPDDSDTPRLNVDMNDKINVDEAAAKSDSKLNVDQINSTTESEKRVEKVNPNIANNPLKSPDAVAYSSETVSDEKQPTEHPVSANVPAKSEKAVCDENTKISLTNTEHYKFHSLRGDVEVVVGDLERDGRDTSLGDASVNEAAKETDVDSSRFISDEKAVTEDAMKTEHASNAPLTDERHFQFHSSEGDIEGIVGTMQRQRQSVSSYDTIVPSQFYKQKVVQNSPPSLLSTDNKIPESGSDHPSSQDNSSKASLVENSQTQSSTPRKPLPTTTSPKVNPEPHSESISDTRPSTPRKVPPSTVPKMNPKLQGGNSVTAPSTPSKVLPAMSPKVAPKFQGGRSSTAPSTPNKVLPAASAKAAPKLQEKAASFDIPNKSTIISTKSTVASPIKANENSPALKSKASFEFPKELDPDGTWNAPIPYPDANCPMAPTYRNLTSEQEEMYEEVLKYCLELKEIPVASNSSKKTDLIELERLWLTRECILRYLRATKWHVSNAKKRIVDTLVWRRHFGVNNMDPDEIQEENATGKQVLLGYDKDGRPCLYLYPARQNTKTSPLQIRHLVFSLECAIDLMPPGVETLALLINFKSSSNRSNPSVGQGKEVLNILQTHYCERLGRALVINIPWAVWGFFKLISPFIDPITREKLKFNEPLDRYVPKDQLDSNFGGSLHFEYHHEKYWPQLVELCKSRRLGILEKWRKMGSKIGTSEWDLKGGEEYVELMQQYVRPSLTNRSSSPTVTPTVNTDRQPKTLTNSADELSPQKRRVENPKPVVKDEGPVSIVEDEESTPVVTKKEDSIPVAQSTKADAGLDAENDLLPKSGSGVSETPAFSHARDVSTASFSDAVSFITADSIE
Protein: cAMP-dependent protein kinase, catalytic subunit-like (EC 2.7.11.11) (Q7JP68)
Organism: Caenorhabditis elegans
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- PH domain-containing protein
- C2 domain-containing protein
- Probable 3',5'-cyclic-AMP phosphodiesterase pde-4
- Thioredoxin domain-containing protein
Sequence:
MVILSHHKRSPPLLMRLFRICRFFRRLMSSSTSSVESVEDESCSNECSASFTFDTNNNSRGNNQVNELAEETHMKLSITPTRESFSLSQLERIITIGKGTFGRVELARDKITGAHYALKVLNIRRVVDMRQTQHVHNEKRVLLQLKHPFIVKMYASEKDSNHLYMIMEFVPGGEMFSYLRASRSFSNSMARFYASEIVCALEYIHSLGIVYRDLKPENLMLSKEGHIKMADFGFAKELRDRTYTICGTPDYLAPESLARTGHNKGVDWWALGILIYEMMVGKPPFRGKTTSEIYDAIIEHKLKFPRSFNLAAKDLVKKLLEVDRTQRIGCMKNGTQDVKDHKWFEKVNWDDTLHLRVEPPIVPTLYHPGDTGNFDDYEEDTTGGPLCSQRDRDLFAEW
Protein: Trihelix transcription factor GT-2 (Trihelix DNA-binding protein GT-2) (Q39117)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that binds specific DNA sequence.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Alcohol dehydrogenase transcription factor Myb/SANT-like family protein
- Nuclear transcription factor Y subunit B-8
- 1-aminocyclopropane-1-carboxylate oxidase homolog 1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Myb family transcription factor APL
- Protein BIG GRAIN 1-like A
Sequence:
MSGNSEGLLESSGGGVGGSVEEEKDMKMEETGEGAGSGGNRWPRPETLALLRIRSEMDKAFRDSTLKAPLWEEISRKMMELGYKRSSKKCKEKFENVYKYHKRTKEGRTGKSEGKTYRFFEELEAFETLSSYQPEPESQPAKSSAVITNAPATSSLIPWISSSNPSTEKSSSPLKHHHQVSVQPITTNPTFLAKQPSSTTPFPFYSSNNTTTVSQPPISNDLMNNVSSLNLFSSSTSSSTASDEEEDHHQVKSSRKKRKYWKGLFTKLTKELMEKQEKMQKRFLETLEYREKERISREEAWRVQEIGRINREHETLIHERSNAAAKDAAIISFLHKISGGQPQQPQQHNHKPSQRKQYQSDHSITFESKEPRAVLLDTTIKMGNYDNNHSVSPSSSRWPKTEVEALIRIRKNLEANYQENGTKGPLWEEISAGMRRLGYNRSAKRCKEKWENINKYFKKVKESNKKRPLDSKTCPYFHQLEALYNERNKSGAMPLPLPLMVTPQRQLLLSQETQTEFETDQREKVGDKEDEEEGESEEDEYDEEEEGEGDNETSEFEIVLNKTSSPMDINNNLFT
Protein: Centrosomal protein 75 kDa (Q54RJ3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MISNIQKQNQIKQQQQLQIISNENFNNNQYLLRSSHAGIVMIGGIDFDRINVGKKRIVKFTLANTNSTPFVVTDLYLQQSIKPIILMNDTMKQQQQQQYYQEPIFSIVSTNNNNSNSNNSNSNSNSSNRFPISIPPNMDFESSISFTPLHPGNFTALLSIASEDEGIQQISLHGQGDIPSAPTQIIYTDNQVPIVIDTPKKLEYNSLDFNQLTKTNNSNARSTSFTSNRNNTLSTSWPLFFDCDINNDLTNTNFMIKTQNGITNYNNNNNNNNNNNNSNFPKNVYITPPPPPKNNNNSSNPSCIKKTVTFRDNSEDNNNNNNNNNNNNNNNNNNNNNNNNNNNTNENYLNNENSEKGNNGNIGNIGNIGNNNKKVTTTVLQKKFTNDTNERKFYYNSGKNQPSVVYNKIQLIENKISDLSRQIDSNHNINHIPFDINSNQPIFRAYPSNNKFISKRPQNHHFNQPQQQQQQQQQQQQQQQQHFYIHPNNNNPPQPKLYQPTQNRQQPQNNNKHQEQQQQQEQQNEQEKQNQEFYQYIHNEDSPQQQHQQQQQQQSNNFNNNNPKNVKPKPIIQNTKPINHNSKDDVFDDDDDDSRVLSEEDKDMLRLMEKTPLPKGQTPAAFKNFLQPDVYSFSPSINRFNQTPFKTRNDIF
Protein: Uncharacterized protein (Q384F1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MALLSLDVIVRLRSRHEEGGDYGSPVTQEKLRAIEFVVRNMKSTAPWPPPAASDGKPLAMPSEEAYGALAPSVFYYAPLGGRFSKEFREALRRGITRLLTELVLRQLVNMRQEKITGARSSGNTSGIESFVSFRGGCHNREVAYVHWSPGLLSLLLSAVDTSELRFDASLPLGSTLVPFTREMKAPTVQQSTGTELLGSHGLHGSINYKSGGNDHVHKYENLVCQLHAEMQRMEVIQQSLHDERTADRLADFLYHFHLKPAEQMREAGGDALKLQRYRDALDCYCKALSTVQKGLLVPYRHALRPPPSLEDRVEGTMEEDILDEATAFALVASSPSAKRERTFLAPANRYFNTLLQLDILEATDGEGKEICGMRSDSLLFGCRAVFPRARPLFHVWYMLHRHAVVAVANAAHTLLLLQAAQTPSFNSVMPESETCVTELSSKELRHRQARAGRWCGRALGMLQCINVWLGDCFKNPAAEGAAPTREWIWVQSMRFKILLRRARLMQLVGTFEEWNRAVEATDEQLRVLQAQSDLSCCASEVQGILDDVRERLGQERSLLQRNHDRGSGLVLRL
Protein: Potassium voltage-gated channel subfamily E member 2 (MinK-related peptide 1) (Minimum potassium ion channel-related peptide 1) (Potassium channel subunit beta MiRP1) (Q9D808)
Organism: Mus musculus (Mouse)
Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with HCN1 and HCN2 and increase potassium current (By similarity). Interacts with KCNQ1; forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P63161, ECO:0000250|UniProtKB:Q9Y6J6}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:24595108}; Single-pass membrane protein {ECO:0000255}. Note=Colocalizes with KCNB1 at the plasma membrane. Localizes at the apical membrane of the choroid plexus epithelium. {ECO:0000250|UniProtKB:P63161, ECO:0000269|PubMed:24595108}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 1
- Voltage-gated inwardly rectifying potassium channel KCNH2
- Potassium voltage-gated channel subfamily E member 3
- Sodium channel protein type 5 subunit alpha
- Potassium voltage-gated channel subfamily E member 4
- A-type voltage-gated potassium channel KCND2
- A-kinase anchor protein 9
- Potassium voltage-gated channel subfamily A member 5
- Potassium voltage-gated channel subfamily E regulatory beta subunit 5
- A-type voltage-gated potassium channel KCND3
Sequence:
MATLANLTQTLEDAFKKIFITYMDSWRRNTTAEEQALQARVDAENFYYVILYLMVMIGMFSFIVVAILVSTVKSKRREHSQHPYHQYIVEDWQEKYKSQILHLEDSKATIHENMGATGFTVSP