wanglab/gogpt-training-data huggingface dataset:
Protein: Replication factor C subunit 1 (Replication factor C1) (O60182)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 1 is essential for cell cycle progression. It may associate with components of the DNA replication machinery and serve to enhance the efficiency of DNA replication.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Replication factor C subunit 3
- Replication factor C subunit 2
- Replication factor C subunit 5
- Replication factor C subunit 4
- Proliferating cell nuclear antigen
- Replication factor A protein 1
- Telomere length regulation protein elg1
- Checkpoint protein rad17
- Flap endonuclease 1
- N-acetyltransferase eso1
Sequence:
MSNSDIRSFFGGGNAQKKPKVSPTPTSPKPKRSLKKKRIVLSDDEDGTIENSKVPASKSKVQKRNESEDISHSLPSIVHEDDKLVGSDGVSTTPDEYFEQQSTRSRSKPRIISNKETTTSKDVVHPVKTENFANDLDTTSDSKPVVHQTRATRKPAQPKAEKSTTSKSKSHTTTATTHTSRSSKSKGLPRFSDEVSQALKNVPLIDVDSMGVMAPGTFYERAATTQTPGSKPVPEGNSDCLSGISFVITGILETLTRQEATDLIKQYGGKVTGAPSVRTDFILLGENAGPRKVETIKQHKIPAINEDGLFYLITHLPASGGTGAAAQAAQQKKEQEEKKILETVARMDDSNKKESQPSQIWTSKYAPTSLKDICGNKGVVQKLQKWLQDYHKNRKSNFNKPGPDGLGLYKAVLLSGPPGIGKTTAAHLVAKLEGYDVLELNASDTRSKRLLDEQLFGVTDSQSLAGYFGTKANPVDMAKSRLVLIMDEIDGMSSGDRGGVGQLNMIIKKSMIPIICICNDRAHPKLRPLDRTTFDLRFRRPDANSMRSRIMSIAYREGLKLSPQAVDQLVQGTQSDMRQIINLLSTYKLSCSEMTPQNSQAVIKNSEKHIVMKPWDICSRYLHGGMFHPSSKSTINDKLELYFNDHEFSYLMVQENYLNTTPDRIRQEPPKMSHLKHLELISSAANSFSDSDLVDSMIHGPQQHWSLMPTHALMSCVRPASFVAGSGSRQIRFTNWLGNNSKTNKLYRMLREIQVHMRLKVSANKLDLRQHYIPILYESLPVKLSTGHSDVVPEIIELMDEYYLNREDFDSITELVLPADAGEKLMKTIPTAAKSAFTRKYNSSSHPIAFFGSSDVLPMKGSAQREVPDVEDAIEAEDEMLEEASDSEAANEEDIDLSKDKFISVPKKPKKRTKAKAEASSSSSTSRRSRKKTA
Protein: Ferrochelatase (EC 4.98.1.1) (Heme synthase) (Protoheme ferro-lyase) (P23871)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen IX dehydrogenase [quinone]
- Oxygen-dependent coproporphyrinogen-III oxidase
- Bacterioferritin
- Delta-aminolevulinic acid dehydratase
- Glutamyl-tRNA reductase
- Protoheme IX farnesyltransferase
- Uroporphyrinogen-III synthase
- Glutamate-1-semialdehyde 2,1-aminomutase
- Porphobilinogen deaminase
Sequence:
MRQTKTGILLANLGTPDAPTPEAVKRYLKQFLSDRRVVDTSRLLWWPLLRGVILPLRSPRVAKLYASVWMEGGSPLMVYSRQQQQALAQRLPEMPVALGMSYGSPSLESAVDELLAEHVDHIVVLPLYPQFSCSTVGAVWDELARILARKRSIPGISFIRDYADNHDYINALANSVRASFAKHGEPDLLLLSYHGIPQRYADEGDDYPQRCRTTTRELASALGMAPEKVMMTFQSRFGREPWLMPYTDETLKMLGEKGVGHIQVMCPGFAADCLETLEEIAEQNREVFLGAGGKKYEYIPALNATPEHIEMMANLVAAYR
Protein: Putative tyrosine-protein phosphatase OCA1 (EC 3.1.3.48) (Oxidant-induced cell-cycle arrest protein 1) (P50946)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Putative tyrosine-protein phosphatase required for protection against superoxide stress. Involved in cell-cycle delay in response to linoleic acid hydroperoxide (LoaOOH).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Tyrosine-protein phosphatase-like protein OCA2
- Inositol diphosphatase SIW14
- Protein OCA4
- Oxidant-induced cell-cycle arrest protein 5
- GTP-binding protein YPT1
Sequence:
MTSKVGEYEDVPEDESRLTEENVSVPEEEVEDEDEEEDDDDDHIYINEETESGREKVLVSHAPQERIVPPLNFCPVERYLYRSGQPSPVNFPFLLNLKLKTIIWLSNEEPQDTLLEFCDTHRINLQFAAINPDAGEDDNPWDGLTEHSIINVLQTIVTQENYPLLVCCGMGRHRTGTVIGCLRRIMGWNLASVSEEYRRFTGSRGGRILVELLIEAFDTNLVKIDKNKAPSWLLTALE
Protein: Large ribosomal subunit protein uL13C (60S ribosomal protein L16-C) (O43004)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- mRNA export factor elf1
- Elongation factor 3
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL10
Sequence:
MSEFQKLVIIDAKGHLMGRLASTVAKQLLAGQKVVVVRCEELNISGHFFRNKLKYLAYLRKACRYNPSRGAFHFRAPSRIFTKAVRGMLPHKTTRGNIALKNLQALEGIPPPFDKQKRLVVPAALRVLRLKPSRKYCTIGRLSSEVGWKYKNIVSKLEERRKIKSAAFYQAKSANQKHINVAKTKSSVNEKLAVFGY
Protein: High Incidence of Males (Increased X chromosome loss) (O17724)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSRIRSNNDNIIILTDEQRKTVGRIAGRSQNRNTSKKIADGPYFLPRYRIRDNAERSVGARFKSLPQKEQDEVVNEAFSNLREYLKKREPFYAKLRKANSKYSSKPKEREKSVDSNDEADRRNKGNKKTQKNASKNCQIEKSSNNSGILKKSGSGISVASKPKKSVAFAPGVYEDLSTDDDLEFLNSVIVNSDRPTSQCDNPARRMCGRPPTKHRDTEQSQEITGSKKQKIFPTPHEKPAWWSFRIPKKRAQ
Protein: Protein NONRESPONDING TO OXYLIPINS 2, mitochondrial (Q6NNL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for mitochondrial morphology, functionality and distribution. Contributes to 9-lipoxygenase (9-LOX)-derived oxylipin synthesis, but not to brassinosteroids (BRs) signaling. Required for waving-inducing oxylipin 9-hydroxyoctadecatrienoic acid and derivatives (e.g. 9-HOT, 2-HOE, 13-HOT, 13-HOD, 13-KOD, 12,13-KHOD, 9-HOT, 9-HOD, 9-KOT, 9-KOD and 9,10-KHOE)-mediated root development regulation, including callose deposition, root waving and lateral roots formation. Involved in basal plant defense toward pathogenic bacteria (e.g. Pseudomonas syringae pv tomato), both in compatible (e.g. Pst DC3000) and incompatible (e.g. Pst DC3000 avrRPM1) interactions, as well as against obligate biotrophic pathogenic fungi (e.g. Golovinomyces cichoracearum), probably via the promotion of callose deposition in the cell wall. Confers sensitivity to the herbicide isoxaben, an herbicide inhibiting cellulose synthesis and altering the cell wall.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23370715}.
Interaction partners:
Sequence:
MASRCRSLSKPAFSAFRSAMNKPSIRPKSASSFIGVPPSPGFSRPIGQLGSLQSLLPLYSAVASARLTSCLGIDSQNSRSLAQGMLCSANPGV
Protein: Copine-9 (Copine IX) (Q8IYJ1)
Organism: Homo sapiens (Human)
Function: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes (By similarity). Plays a role in dendrite formation by melanocytes.
Interaction partners:
Sequence:
MSLGGASERSVPATKIEITVSCRNLLDLDTFSKSDPMVVLYTQSRASQEWREFGRTEVIDNTLNPDFVRKFVLDYFFEEKQNLRFDVYNVDSKTNISKPKDFLGQAFLALGEVIGGQGSRVERTLTGVPGKKCGTILLTAEELSNCRDIATMQLCANKLDKKDFFGKSDPFLVFYRSNEDGTFTICHKTEVVKNTLNPVWQPFSIPVRALCNGDYDRTVKIDVYDWDRDGSHDFIGEFTTSYRELSKAQNQFTVYEVLNPRKKCKKKKYVNSGTVTLLSFSVDSEFTFVDYIKGGTQLNFTVAIDFTASNGNPLQPTSLHYMSPYQLSAYAMALKAVGEIIQDYDSDKLFPAYGFGAKLPPEGRISHQFPLNNNDEDPNCAGIEGVLESYFQSLRTVQLYGPTYFAPVINQVARAAAKISDGSQYYVLLIITDGVISDMTQTKEAIVSASSLPMSIIIVGVGPAMFEAMEELDGDDVRVSSRGRYAERDIVQFVPFRDYVDRSGNQVLSMARLAKDVLAEIPEQLLSYMRTRDIQPRPPPPANPSPIPAPEQP
Protein: Histone H3-like centromeric protein A (Centromere protein A) (CENP-A) (O35216)
Organism: Mus musculus (Mouse)
Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P49450}. Chromosome, centromere {ECO:0000250|UniProtKB:P49450}. Note=Localizes exclusively to sites of kinetochore assembly in centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constriction but encompassing only one third of the constriction width and height. Phosphorylation at Ser-62 during early mitosis abolishes association with chromatin and centromeres and results in dispersed nuclear location. {ECO:0000250|UniProtKB:P49450}.
Interaction partners:
- Holliday junction recognition protein
- Centromere protein N
- Centromere protein H
- Centromere protein T
- Centromere protein M
- Centromere protein C
- Centromere protein U
- Aurora kinase B
- Cyclin-dependent kinase 1
- Centromere protein K
Sequence:
MGPRRKPQTPRRRPSSPAPGPSRQSSSVGSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRVTLFPKDIQLTRRIRGFEGGLP
Protein: ATP-binding cassette, sub-family A (ABC1), member 1A (Phospholipid-transporting ATPase ABCA1a) (B8A446)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Nuclear receptor subfamily 1, group H, member 3
- Zgc:172302 protein.
- ATP-binding cassette, sub-family A
- Apolipoprotein Eb
- Sterol regulatory element-binding protein 2
- Apolipoprotein A-Ia
- Retinoic acid receptor RXR-alpha-A
- Cholesteryl ester transfer protein
- Platelet glycoprotein 4
- Palmitoyltransferase ZDHHC8B
Sequence:
MAVSTQLGLLLWKNFTYRRRQTIQLLVEIIWPLFIFFILISVRLYYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGETPGVVGNFNDSIISRLFTDAKKILLYSQQDKSFEGFKGLVRALRKLQRNTEGFKLKDFLHDNETLSAFLEKNATLPKHAVRQIVEANVNLEKVLIKGFGVHLTDLCNSTSLEEFVTIADKDVSQLTQNIICQSPADWLNNAEQHFLSNLDFLKPIRKDVKSDPKIIKDVSIATDSLLESLGALAVELASMKSWRDMRNEILYLTGNSTQSPNHMYQAVSRIVCGHPEGGGLKIKSLNWFEDNNYKALFGNNGNDSDSEPASVYDNSSTPYCNNLMKGLESSPISRMIWRALKPLLMGKILYTPDTPATQRIIHEVNKTFQELGVLRDLGGMWEEMRPKIWNFMENSEEMDLVRTLLQNNASARFFNAKLSGTEWRVEDVSRFLSKSSEDTRPHGTAYTWREVFNETDQAIQTISRFMECVNLDKLEPVANEERLVNKSMRLLDDRKFWAGIVFPDMQSNTSDLPLNVNYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDLRYIWGGFTYLQDVIEHGIIRALTGSKEKTGVYIQQMPYPCYVDDIFLRVMSRSMPLFMTLAWMYSVAIIIKGVVYEKEARLKETMRIMGLDNGILWLSWFISSLIPLLISAALLVLILKMGNLLPYSDPGVIYLFLSSFAVVTIMQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQNYVGFGAKIVVSLLSPVAFGFGCEYFALFEEQGVGIQWSNLLSSPMQEDSYNLTTSICLMLFDSVLYAVMTWYIEAVFPGQYGIPRPWYFPFTKSYWCGEKCGWTTSVPSNRKENAEAVCIEEEPAHIDPGVYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKTQLGTGYYLTLVKKDFDLSASSCRTSSSTVSYSKGSLKKDDSVSESSSDAGLGSDHESETTTIDISLISNVIFKHVPTARLVEDLGHEITYVLPYESAKDGAFVELFHEIDDRLTDLSISSYGISDTTLEEIFLKVAEDCGVDAETSDGTLPARRNRRHAFGDHQSCLKPFTEDDFDFNDSEGDPESRETDWLDGADGKGSYQVKGWSLKRQQFVALLWKRLLYARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLALEPSMYEEQFTFISNDAPEDRHTNRLLDALKDSPAYTDQCTDGKNTASRSCPIKDGEWLVPEVTESIEAIFLNGNWSMENPSPLCECSCEGRKKMLPECPPGAGGLPPPQIKVTHDETLQNLSGRNISDYLVKTYAQIIGKSLKNKLWVNEFRYGGFSLGARNTQALPPGDELTDAISHIRSRFSLESGTAADRFLGSLSTFIRGLDTNNNVKIWFNNKGWHSIGSFLNVMNNAVLRANLPPGLDRSKFGINAFNHPLNLTKEQLSHVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVNKAKHMQFISGVQPFLYWLANFVWDMCNYIVPATLVIIIFVCFQQEAYVSSTNLPVLALLLLLYGWSITPLMYPASFFFKIPSTAYVVLTSVNILIGINGSVSTFVLELFGSNEIGGINDILKNVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFRSPLAWDMVGKNLFAMAIEGVIFFSITVLIQYRFCIKARSLSTKLKPIGEEDEDVARERQRILGGGGQTDILELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKFGDGYTIILRVAGADPRLEPVMEFIERELPGSTLKEKHRNMLQYQLSSSLTSLARIFNILSKNKEQLHIEDYSVSQTTLDQVFVNFAKDQSDEDHLKDISMNKNDAVVDISKLNAFLTDEKAKETVV
Protein: Mitochondrial fission factor (Q4KM98)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in mitochondrial and peroxisomal fission (By similarity). Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (By similarity). May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q6PCP5}; Single-pass type IV membrane protein {ECO:0000255}. Peroxisome {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:23792689}.
Interaction partners:
Sequence:
MAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQGFQDGVPNASVIMQVPERIVVTGNNEDISFSRPADLDLIQSTPFKPLALKTPPRVLTLSERPLDFLDLERPPPTPQSEEIRAVGRLKRERSMSENAVRQNGQLVRNDSMYGISSLDAAVEGASEDMSVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR
Protein: fructose-bisphosphate aldolase (EC 4.1.2.13) (Q6UV40)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
TNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSSLAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGT
Protein: Leucine-rich repeat protein kinase family protein (F4IB69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MERHCVLVATFLLMLHIVHAQDQIGFISVDCGLAPRESPYNEAKTGLTYTSDDGLVNVGKPGRIAKEFEPLADKPTLTLRYFPEGVRNCYNLNVTSDTNYLIKATFVYGNYDGLNVGPNFDLYFGPNLWTTVCLIKTGISIPFINVLELRPMKKNMYVTQGESLNYLFRVYISNSSTRIRFPDDVYDRKWYPYFDNSWTQVTTTLDVNTSLTYELPQSVMAKAATPIKANDTLNITWTVEPPTTKFYSYMHFAELQTLRANDAREFNVTMNGIYTYGPYSPKPLKTETIYDKIPEQCDGGACLLQVVKTLKSTLPPLLNAIEAFTVIDFPQMETNGDDVDAIKNVQDTYGISRISWQGDPCVPKLFLWDGLNCNNSDNSTSPIITSLDLSSSGLTGSITQAIQNLTNLQELDLSDNNLTGEIPDFLGDIKSLLVINLSGNNLSGSVPPSLLQKKGMKLNVEGNPHLLCTADSCVKKGEDGHKKKSVIVPVVASIASIAVLIGALVLFFILRKKKSPKVEGPPPSYMQASDGRSPRSSEPAIVTKNRRFTYSQVAIMTNNFQRILGKGGFGMVYHGFVNGTEQVAVKILSHSSSQGYKEFKAEVELLLRVHHKNLVGLVGYCDEGENMALIYEYMANGDLKEHMSGTRNRFTLNWGTRLKIVVESAQGLEYLHNGCKPPMVHRDVKTTNILLNEHFQAKLADFGLSRSFPIEGETHVSTVVAGTPGYLDPEYYKTNWLTEKSDVYSFGIVLLELITNRPVIDKSREKPHIAEWVGVMLTKGDINSIMDPNLNEDYDSGSVWKAVELAMSCLNPSSARRPTMSQVVIELNECIASENSRGGASRDMDSKSSIEVSLTFDTELSPTAR
Protein: At2g21080 (Ras guanine nucleotide exchange factor K) (Q8L726)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Dual specificity phosphatase Cdc25
- Origin of replication complex subunit 2
- Cyclin-dependent kinases regulatory subunit 1
- Cyclin-dependent kinases regulatory subunit 2
- Retinoblastoma-related protein 1
- Cell division control protein 6 homolog B
- Cell division control protein 6 homolog
- Wee1-like protein kinase
- F10B6.17
- Anaphase-promoting complex subunit 1
Sequence:
MNPGEDEYFLLHLPNLSNTPLQPSKSLPSDDLRNFRLLLKWCALDHSSSCGKAVSYMMFVVFTLLVPLISCLFIKTPRNRPSAVMDANSFNVLVQFPESGLAVIGFLTLICFFRIYSLTKLLFLDDSTLVRLGYSRELDKALRYLAYILVPSFLVELVHKSIFFYSAEVSFPFIKSSCAALNFVMFFLVLFSWVYRTGVFLLVCILFRLTCELQILRFRGLHKLFDRCGSDTIEDVCKEHVRIKKQLSATSHRYRFFIITAFVVISTSQFVALLLVLASKSEKSFLSSGDLVVCSAVQLSGFFLCLLGAARITHRAQGVVCIATRWHMALTCASEAVSPESDTDSSDNIYINVSPSLDLSSFFQARQALVEYLRHNNKGITLYGYALDRGLLHTLFAFEFSLVMWILSKVVVLS
Protein: DNA nucleotidylexotransferase (EC 2.7.7.31) (E9PT58)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR000817}.
Interaction partners:
- Caspase-3
- V
Sequence:
MDPLQAVHLGPRKKRPRQTGASGASTPHDIRFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSEFELLDISWLIECMGAGKPVEMAGRHQLVVRRNPSLSPVPGSQTVPPPPMQKISQYACQRRTTLNNHNQLFTDAFDILAENYEFRENEVSCLPFMRAASVLKSLSFPIVSMKDIEGIPCLGDKVKCVIEGIIEDGESSEVKAVLNDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIKSDKSLRFTHMQKAGFLYYEDLVSCVNRAEAEAVSMLVKEAVVAFLPDALVTMTGGFRRGKMTGHDVDFLITSPEATEEEEQQLLHKVTNFWRQQGLLLYCDIIESTFEKFKLPSRKVDALDHFQKCFLILKLHRGLVRSEESGQQEGKDWKAIRVDLVMCPYERRAFALLGWTGSRQFERDLRRYATHERKMMLDNHALYDKTKRVFLEAESEEEIFAHLGLDYIEPWERNA
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (Q96D47)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367045}.
Interaction partners:
Sequence:
LLSADVDIKELAVETKNFSGAELEGLVRAAQSTAMNRHIKASTKVEVDMEKAESLQVTRGDFLASLENDIKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEGASPLDFD
Protein: LD12230p (Q8SZS8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
ELRNEKDDVCFRRKRARAFDVPGAREPESKRPKEFQSTPIDVRKYPETNRNPFKTAAKDAAKDDARKMMTKKDDTTKVVSKDVERGVKSKEDNKMATNKDDDKKSSSKDDAWKSRTREDAKKSVQRSKSPRPEHSKTTDRKSTAQARRPDPHRSRSPKHNSRRDHHRNQESSSRHAKRRSQSASPSKIQLPREKANAIITLTDDETNDQRSKSPVPVTVKLVTESQPAEKVVSNRRDAALETNANSSKESKVETKDITQPTNGLIAEPCIPKHEIIPGLSLINPESADFSKNEIKLDPVILQDRTEDSGHQLLNKEPIPKVVVLEKCKNILAEDCPADEQPLDKFKDGKESEETQAKLDKKEPFAVETAVETPSKEESNDNIVLSKNTTSQADVCSQHDENDEAEIREPMDQVNSVVESDLGVRIIEDIRLPKMANIDHFAVKVDNHGEAPAAVTDSALNQENLATQDQKICAEMKDPTIFTTSDETPIKSATILYAKPDSTKLDHSDEHDEVILETAIDMLKKEQDAASTAESTYPKLRIAEDAIEMALEQLHQQSPDETVVTSTSNRAPQTPKSLITILTQTPKQADPLRSQTKSKTVSPMATPKKTATEKTPVKKRKVNMDSSPQVPAHDVTIDETLGACSLQDESSTVTKRCSLGHTDYQYEQIKDEVILRVKRRGRRRKPTPMEIPTTAADKPI
Protein: Required for meiotic nuclear division protein 1 homolog (Q9NWS8)
Organism: Homo sapiens (Human)
Function: Required for mitochondrial translation, possibly by coordinating the assembly or maintenance of the mitochondrial ribosome.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23022098, ECO:0000269|PubMed:23022099, ECO:0000269|PubMed:25604853}. Note=May be localized in mitochondrial RNA granules (PubMed:25604853). {ECO:0000269|PubMed:25604853}.
Interaction partners:
- Zinc finger and BTB domain-containing protein 2
- Damage-control phosphatase ARMT1
- Coiled-coil domain-containing protein 170
- tRNA
Sequence:
MPATLLRAVARSHHILSKAHQCRRIGHLMLKPLKEFENTTCSTLTIRQSLDLFLPDKTASGLNKSQILEMNQKKSDTSMLSPLNAARCQDEKAHLPTMKSFGTHRRVTHKPNLLGSKWFIKILKRHFSSVSTETFVPKQDFPQVKRPLKASRTRQPSRTNLPVLSVNEDLMHCTAFATADEYHLGNLSQDLASHGYVEVTSLPRDAANILVMGVENSAKEGDPGTIFFFREGAAVFWNVKDKTMKHVMKVLEKHEIQPYEIALVHWENEELNYIKIEGQSKLHRGEIKLNSELDLDDAILEKFAFSNALCLSVKLAIWEASLDKFIESIQSIPEALKAGKKVKLSHEEVMQKIGELFALRHRINLSSDFLITPDFYWDRENLEGLYDKTCQFLSIGRRVKVMNEKLQHCMELTDLMRNHLNEKRALRLEWMIVILITIEVMFELGRVFF
Protein: Claudin-4 (Clostridium perfringens enterotoxin receptor) (CPE-R) (CPE-receptor) (Williams-Beuren syndrome chromosomal region 8 protein) (O14493)
Organism: Homo sapiens (Human)
Function: Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney. Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:O35054}. Cell membrane {ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tight junction protein 1
- Occludin
- Claudin-12
- Claudin-7
- Claudin-1
- Tight junction protein ZO-3
- Junctional adhesion molecule A
- Claudin-8
- Tight junction protein 2
- Claudin-3
Sequence:
MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV
Protein: Interactor of constitutive active ROPs 1 (ROP-interactive partner 1) (Q8LE98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a scaffold, mediating interaction of ROPs with different proteins. Required for primary and adventitious root maintenance, but not for their formation. Promotes the stabilization of ARAC11 on the plasma membrane of the pollen tube initiation site but not the activation of ARAC11. Regulates directionality of polar auxin transport, and is required for the formation of a stable auxin maximum and tip localized auxin gradient during embryogenesis, organogenesis, and meristem activity. Involved in exocytosis and in the recycling of PIN proteins back to the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17493810, ECO:0000269|PubMed:20098722}; Peripheral membrane protein. Nucleus {ECO:0000269|PubMed:19825600}. Note=The localization of the ICR1-ROP complexes at the plasma membrane depend on the lipid modifications of the ROPs (PubMed:17493810). Localized in the nuclei in mature pollen, then shifts to the site of germination and stays at the apical cortex of growing pollen tubes (PubMed:19825600). {ECO:0000269|PubMed:17493810, ECO:0000269|PubMed:19825600}.
Interaction partners:
- Rac-like GTP-binding protein ARAC11
- CRIB domain-containing protein RIC4
- CRIB domain-containing protein RIC3
- Exocyst complex component SEC8
- Rac-like GTP-binding protein ARAC4
- Exocyst complex component SEC3A
- Exocyst complex component SEC6
- Rac-like GTP-binding protein ARAC3
- Filament-like plant protein 2
- Pollen receptor-like kinase 2
Sequence:
MPRPRVSELSQRQAPRLRSSSSTSDSNHSNRLITTDQSFKPGVDRKSPRSGGPNSDPLGQKKLGGRISDLESQLGQAQEELRLLKEQLANAEAVKKQAQDELHKKSKKPNPLARVEESATEAERIDRDEIPGDVQKETDVFEVPVEKIAVEEEELRSGNDEAEKLVAKEDEIKMLKARLYDMEKEHESLGKENESLKNQLSDSASEISNVKANEDEMVSKVSRIGEELEESRAKTAHLKEKLESMEEAKDALEAEMKKLRVQTEQWRKAADAAAAVLSGEFEMNGRDRSGSTEKYYAGGFFDPSAGFMDPPGMADDYDDGLGSGKRKSSGMKMFGELWRKKGQK
Protein: Mediator of RNA polymerase II transcription subunit 21 (Mediator complex subunit 21) (RNAPII complex component SRB7) (Suppressor of RNA polymerase B 7) (P47822)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 6
Sequence:
MTDRLTQLQICLDQMTEQFCATLNYIDKNHGFERLTVNEPQMSDKHATVVPPEEFSNTIDELSTDIILKTRQINKLIDSLPGVDVSAEEQLRKIDMLQKKLVEVEDEKIEAIKKKEKLLRHVDSLIEDFVDGIANSKKST