wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor BTF3 (Q9U9Q7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNAEKLKKLQAQVRIGGKGTPRRKKKIVHSTPATDDKKLQSSLKKLSVNTIPGIEEVNIIKNDGTVIHFNNPKAQASLPTNTFAITGHGENKTITEMVPGILTQLGPQDINQLKKLATEIASKNGAGGVAGSSAADAGDDDVPDLVENFEEVAIADTKEEKSGEVAASA
Protein: Probable hypoxanthine oxidase XdhD (EC 1.-.-.-) (Q46814)
Organism: Escherichia coli (strain K12)
Function: Probably has no xanthine dehydrogenase activity; however deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage.
Interaction partners:
- Uncharacterized protein YgfM
- Putative oxidoreductase YgfK
- Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA
- Aldehyde oxidoreductase FAD-binding subunit PaoB
- Putative xanthine dehydrogenase FAD-binding subunit XdhB
- Molybdenum cofactor cytidylyltransferase
- Putative aminohydrolase SsnA
- Uncharacterized protein YqeB
- Molybdenum cofactor insertion chaperone PaoD
- Putative dimethyl sulfoxide reductase chain YnfE
Sequence:
MIIHFTLNGAPQELTVNPGENVQKLLFNMGMHSVRNSDDGFGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGKWNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQVIELAVARKNNPQATIDIAPTFRDDLEVIGKHYPKTDAAKMVQAKPCYVEDRVTADACVIKMLRSPHAHALITHLDVSKAEALPGVVHVITHLNCPDIYYTPGGQSAPEPSPLDRRMFGKKMRHVGDRVAAVVAESEEIALEALKLIDVEYEVLKPVMSIDEAMAEDAPVVHDEPVVYVAGAPDTLEDDNSHAAQRGEHMIINFPIGSRPRKNIAASIHGHIGDMDKGFADADVIIERTYNSTQAQQCPTETHICFTRMDGDRLVIHASTQVPWHLRRQVARLVGMKQHKVHVIKERVGGGFGSKQDILLEEVCAWATCVTGRPVLFRYTREEEFIANTSRHVAKVTVKLGAKKDGRLTAVKMDFRANTGPYGNHSLTVPCNGPALSLPLYPCDNVDFQVTTYYSNICPNGAYQGYGAPKGNFAITMALAELAEQLQIDQLEIIERNRVHEGQELKILGAIGEGKAPTSVPSAASCALEEILRQGREMIQWSSPKPQNGDWHIGRGVAIIMQKSGIPDIDQANCMIKLESDGTFIVHSGGADIGTGLDTVVTKLAAEVLHCPPQDVHVISGDTDHALFDKGAYASSGTCFSGNAARLAAENLREKILFHGAQMLGEPVADVQLATPGVVRGKKGEVSFGDIAHKGETGTGFGSLVGTGSYITPDFAFPYGANFAEVAVNTRTGEIRLDKFYALLDCGTPVNPELALGQIYGATLRAIGHSMSEEIIYDAEGHPLTRDLRSYGAPKIGDIPRDFRAVLVPSDDKVGPFGAKSISEIGVNGAAPAIATAIHDACGIWLREWHFTPEKILTALEKI
Protein: Beta sliding clamp (Beta clamp) (Sliding clamp) (Beta-clamp processivity factor) (DNA polymerase III beta sliding clamp subunit) (DNA polymerase III subunit beta) (P05649)
Organism: Bacillus subtilis (strain 168)
Function: Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
Subcellular location: Cytoplasm, nucleoid {ECO:0000269|PubMed:19737352, ECO:0000269|PubMed:21170359}. Note=Localizes in tight foci to the chromosomal replication center at mid-cell (PubMed:19737352, PubMed:21170359). When replication is blocked most foci are also lost (PubMed:19737352). Positioning does not rely on the C-terminus of SSB (ssbA) (PubMed:21170359). During sporulation colocalizes with SirA (PubMed:25041308). {ECO:0000269|PubMed:19737352, ECO:0000269|PubMed:21170359, ECO:0000269|PubMed:25041308}.
Interaction partners:
- DNA polymerase III PolC-type
- DNA polymerase III subunit tau
- Chromosomal replication initiator protein DnaA
- DNA polymerase III subunit delta'
- DNA polymerase III subunit delta
- DNA polymerase I
- DNA mismatch repair protein MutL
- DNA replication and repair protein RecF
- DNA polymerase III subunit alpha
- DNA mismatch repair protein MutS
Sequence:
MKFTIQKDRLVESVQDVLKAVSSRTTIPILTGIKIVASDDGVSFTGSDSDISIESFIPKEEGDKEIVTIEQPGSIVLQARFFSEIVKKLPMATVEIEVQNQYLTIIRSGKAEFNLNGLDADEYPHLPQIEEHHAIQIPTDLLKNLIRQTVFAVSTSETRPILTGVNWKVEQSELLCTATDSHRLALRKAKLDIPEDRSYNVVIPGKSLTELSKILDDNQELVDIVITETQVLFKAKNVLFFSRLLDGNYPDTTSLIPQDSKTEIIVNTKEFLQAIDRASLLAREGRNNVVKLSAKPAESIEISSNSPEIGKVVEAIVADQIEGEELNISFSPKYMLDALKVLEGAEIRVSFTGAMRPFLIRTPNDETIVQLILPVRTY
Protein: EAL domain-containing protein (Q9HUF2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Diguanylate cyclase
- EAL domain-containing protein
- histidine kinase
- Cyclic di-GMP phosphodiesterase PA2567
- Sensory/regulatory protein RpfC
- histidine kinase
- FimX
- histidine kinase
- Biofilm dispersion protein BdlA
- Diguanylate cyclase
Sequence:
MKSHPDAASRSAAEVVTQLPVPSRLGLLRFERLNEPSWALLFLDPACERQLGLPATTLCALLDAPYASLMEPEARHRLHEQIQQQLVKRPHYQVSYKLHTPNGVLTMLEFGEAFQQHGRQLLHGYLMVEERAESAERSEQLLDLESQNLRLKASLDLYQRSQDDHLQHLLRSRTQQNLIVRLARHRYLSSDPLLEAAQLITQAACEAYGTARAGIWRLLDDQRLEAVTVYRRDLDQYEKPQSIDASRYPAYLEAVHSGRAIDAHNAQRDPRTQELYKDYLRPLGVNALLDATIRIGGEVVGVLCLEHAGENRMWQSDEIAFAGELADQYAQVLMNHERRNVSSALHLFQRAVEQSASAFLLIDRDGVVEYVNPSFTSITQYSADEVRNRRLSELPALENLSELLFDARSALTQQNSWQGEFRSRRKNHEPYWGQLSLSKVYDDLGELTHYIGIYEDITQNKLAQQHIEKLAYRDNLTGLANRHYFIGALEERLESSGDRPLSLLLVDIDNFKRINDSLGHQTGDKLLVSLARRLRSCLGDGATLARFASNEFAVLLDDTAVEKGESIAAQVLHMLDKPLFVDNQLINITGSIGLASAPQHGCDPQTLMKYAGLALHKAKANGKHQVQVFTEALTAEASYKLFVESNLRRALAQNELAVHYQPKLCLRSGQLLGLEALLRWQHPEKGMIRPDRFISVAEETGLIVPIGKWVIREACRQARELAEAGLGELQIAINLSPKQFTDPDLVGSIAAILHEENIPASQLELELTESLLLDATDDTRQQLERLKSLGLTLAMDDFGTGYSSLSYLKKFPIDVIKIDRSFIKDIPDSQDDMEITSAVIAMAHNLKLKVVAEGVESAEQLAFLRRNRCDIGQGYLFDRPIPSDLLNTSLLRYPCRTLH
Protein: Peptidoglycan recognition protein L1 (M9PNV5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MSGAQGVEDSMISPMEPHWKWCLTLLVVLVSAHTDTKVTSSQHMDDFIRVLEQVEYRNPGLQPVNVLRGLRRAAGLRDEFMQHFLGTIREDSTSEAPVMDSNLSDFIGRAVHHQVTERGREEGVVLTADGTTVAMSPVLLGIEAGLVSKTRCQVRGLYPLTLARNLGLSFQRFHSSLLSHRLGPDGCWDDVTSPQVFTLSDKPSLATDALVNGGMDGVILGMEVSAQSQRPLKLSSLLRTYYCHHLEVEGLDTAPRLISRLRRENFRELARPPLLQRQVVRSLVLQRRLIDHSTMLSQEKEELTAVVREGIKEFVHKYMDCPAIIPRCQWGAAPYRGTPTPLSLPLSFMYIHHTYQPGQPCLTFQQCSADMRSMQRFHQDDRGWDDIGYSFVAGSDGYLYRGRGWHWQGAHTKGYNSKGYGVSFIGDYTSRLPSQQTMELVRDRLASCAVGGGRLVGNFTLYGHRQLVKTSCPGDALYSEITGWEHFGEVQN
Protein: Importin subunit beta-5 (114 kDa karyopherin) (Karyopherin subunit beta-5) (Karyopherin-114) (Q10297)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of TATA-binding protein (TBP) and of histones H2A and H2B (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15116432}.
Interaction partners:
- Probable importin subunit beta-4
- Importin subunit beta-2
- Importin subunit beta-3
- Importin subunit beta-1
- Importin beta-like protein kap113
- Histone H2B-alpha
- Importin-alpha re-exporter
- TATA-box-binding protein
- Histone H2A.Z-specific chaperone chz1
- Histone H2A.Z
Sequence:
MVESKIIKLLEQVQSADPNSRIQAELGLRDLEKYHDFAAKLTDIASSGASVPLRQGSLIYLQRYIVHHWSPLFEQFQDGPIPDENVKKHVRETLLHLLVSLDNFTLIKAVAYAVSLIANVDYPDEWPEVVPAVLHLLQSTNENSINASLDVLDELVDESLVEEQFFIIAPQLASILYQFIFSAPPNDSMRMLQARGIKLFRSCLELIEIYKETKAEHVRVFLEQILPPWMDMFSHKFEVSLVDDRQVILPDSCGYFCIMGEIAMTLTKLRELFPSKLTPYVVTFVELVWNIIEKLLDPYIREVVFSDGLDDSAFGDKYPIRYLVELLLFVSVALQSKFVQNLFVSNTVPVPPLPPCIPLLVQYTQLPKHQIEVYESDVSEYIANEFSMDFASDTVRGAAISVLSAFEEHTTLPIQQSLREMSATYILNNEINWIYQEALLYACCSVDAASDDTYDDYLDPIYEAIKVRIDYSDAPILLLSRFFLFIGYFSESTVVASQFFQIIMNNLVNALQVDTVQYAAMKAIERFCSVGKVKPILSLQPMILEVLSQYASKSSDEALVLLVEAISSAVKLDCAKAAELGNSVIPLLFNLVATNASDPYICGIIEDTFEDIIHAANNYESMCEITLPELLQVLNQEDPIMVNIGATLLSCLIRAGPSPLPNGFVGYVLPPVYKITQIHSGDTELLQLSQEILKGLLEKDTPQLLETEISGSSGFQYILFILHQLLDKESDDSACFLVGPILLELADHASQMVDLQSILLSCIKRLAIAEQPRFIQSIIYVFAKLIVKDSLGMMHFLTSSLLNEQGLTAFEVLMTVWCDNFVYFSNFKNISIICIAMTKIYSFDSPLLDSVQVKGELISHSNRIITRSQSKLHPEEYSYVSVGEKILRLLSEEFVSLSKDAIVEEVSDDGADDWDDGPISAETFGLSANDVNELSKDEFSGVDNSEDEDNTDLQFYLLEFFKEAMKSNLHNINEVVFRLPQEEQDALVQIKEK
Protein: Down syndrome cell adhesion molecule 1, isoform BK (A0A0B4K6R4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVQQFYESEVNNEYVIRGNAAVLKCSIPSFVADFVQVVSWQDEEGQLYGSLGDQQGTDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPIGSVPPKINNINDKFQLMQVKLESSFAMQCPGQAYPVPVVRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVLPRIIPFAFEEGPAQVGQYLTLHCSVPGGDLPLNIDWTLDGQAISEDLGITTSRVGRRGSVLTIEAVEASHAGNFTCHARNLAGHQQFTTPLNVYVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Tax1-binding protein 1 homolog (Liver regeneration-related protein LRRG004) (Q66HA4)
Organism: Rattus norvegicus (Rat)
Function: Ubiquitin-binding adapter that participates in inflammatory, antiviral and innate immune processes as well as selective autophagy regulation. Plays a key role in the negative regulation of NF-kappa-B and IRF3 signalings by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to bind and inactivate its substrates. Disrupts the interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN-beta production. Recruits also A20/TNFAIP3 to ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B signaling pathways. Inhibits virus-induced apoptosis by inducing the 'Lys-48'-linked polyubiquitination and degradation of MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-mediated apoptosis signaling. As a macroautophagy/autophagy receptor, facilitates the xenophagic clearance of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium tuberculosis. Upon NBR1 recruitment to the SQSTM1-ubiquitin condensates, acts as the major recruiter of RB1CC1 to these ubiquitin condensates to promote their autophagic degradation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86VP1}. Mitochondrion {ECO:0000250|UniProtKB:Q86VP1}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q86VP1}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q86VP1}.
Interaction partners:
- Tumor necrosis factor alpha-induced protein 3
- Gamma-aminobutyric acid receptor-associated protein
- Contactin-2
- RING finger protein 11
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Gamma-aminobutyric acid receptor-associated protein-like 1
- TNF receptor-associated factor 6
- Serine/threonine-protein kinase TBK1
- Next to BRCA1 gene 1 protein
- E3 ubiquitin-protein ligase
Sequence:
MTSFQEVPLQTSNFAHVIFQNVAKSYLPNAHLECHYTLTPYIHPHSKDWVGIFKVGWSTARDYYTFLWSPMPEQYVEGSTVNCVLAFQGYYLPNDDGEFYQFCYVTHKGEIRGASTPFQFRAASPVEELLTMEDEGNSDMLVVTTKAGLLELKIEKTLKEKEELLKLVSVLEKETAQLREQVGRMERELSHEKSRCEQLQAEQKGLLEVSQSLRVENEEFMKRYSDATSKAHQLEEDIVSVTHKAVEKETELDSLKDKLRKAQQEKEQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEIQTLKNVDGNKESMITHFKEEIGKLQSCLADKENLHRALLLTTSNKEDTLLLKEQLRKAEEQVQATRQELIFLAKELSDAVNVRDKTMADLHTARLENERVKKQLADTLAELQLHAVKTDQEKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSASSNGVFTKRMGSQQKVNDASINTDPAASASAVDVKPAASCAAETDFDMSAKDHVCEVTKEMAEKVEKYNKCKQLLQDEKAKCNKYADELAQMELKWKEQVRIAENVKLELAELEDSYSLQLAEKDKEINCLASFLENLSREKELTKSLEDQKGRKMEGQSPQQVSRCLNTCSEQSGLLPTLPAAQPVLQYGNPYTAHETRDGADGAFYPDEIQRPPVRGPSWEDNVVCSQPARNLSRPDGLEDPEDSREDENVPIPPDPANQHLRGHGAGFCFDSSFDVHKKCPLCELMFPPNYDQIKFEEHVESHWKVCPMCSEQFPPDYDQQGFERHVQTHFDQNVLNFD
Protein: Maleylacetate reductase (EC 1.3.1.32) (O30847)
Organism: Pseudomonas knackmussii (strain DSM 6978 / CCUG 54928 / LMG 23759 / B13)
Interaction partners:
- Carboxymethylenebutenolidase
- Hydroxyquinol 1,2-dioxygenase
- 3-oxoadipate CoA-transferase
- 3-oxoadipate CoA-transferase
- Maleylacetate reductase
- 3-oxoadipate enol-lactonase 2
- Alpha/beta hydrolase
- Alpha/beta hydrolase
- UPF0065 protein in clcB-clcD intergenic region
- Chlorocatechol 1,2-dioxygenase
Sequence:
MNFIHDYRSPRVIFGPDSLARLPQELERLGIDRALVLTTPEQAPLGRQVAEPVIGHVAAFYDGATMHVPALVAEEACKIARTSEANGVIAIGGGSTIGLAKIVALRTELPIVAVPTTYAGSEMTSIFGITEGGVKKTGRDARVMPRAVIYEPRLTLELPLSISVTSAINAIAHAVEGLYAPDATPLLTIMAQEGIAATVRAISRMYQSPRDLQARGDALYGAWLCASVLGNVSMALHHKLCHTLGGTLDLPHAQTHTVVLPHALAYNARAVPDAMRVLRIALGHDDPPTALYELARDNGAPVALRDLGMREEDIEHVGDLALQDRYPNPRELDRDALLALLRDAYHGRPPSA
Protein: Protein AE7 (AS1/2 enhancer 7) (Asymmetric leaves 1/2 enhancer 7) (Q9C9G6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Central member of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) pathway. Involved in leaf polarity formation. Promotes leaf adaxial identity. May play a role in the cell cycle progression and is required for cell proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:23104832}. Cytoplasm {ECO:0000269|PubMed:23104832}.
Interaction partners:
- MMS19 nucleotide excision repair protein homolog
- Protein CIA1
- Protein NAR1
- Cytosolic Fe-S cluster assembly factor NBP35
- General transcription and DNA repair factor IIH helicase subunit XPD
- Protein CHLOROPLAST IMPORT APPARATUS 2
- Monothiol glutaredoxin-S17
- Fe-S cluster assembly factor HCF101, chloroplastic
- NADPH-dependent diflavin oxidoreductase 1
- ABC transporter B family member 25, mitochondrial
Sequence:
MVSGLINENPIIYPKKERRLRTDTSITDELTPEPIDQLEIFDHIRDIKDPEHPNTLEDLRVVTEDSVEVDDENSYVRVTFTPTVEHCSMATVIGLCVRVKLLRSLPSRYKIDIRVAPGSHATEDALNKQLNDKERVAAALENPNLVEMVDECLPSEE
Protein: Sister chromatid cohesion protein 1 (Q19325)
Organism: Caenorhabditis elegans
Function: Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped (By similarity). At metaphase-anaphase transition, this protein is cleaved and dissociates from chromatin, allowing sister chromatids to segregate (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206}. Chromosome {ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206}. Cytoplasm {ECO:0000269|PubMed:12808038}. Note=Shows cell-cycle dependent localization to chromosomes, with an accumulation on chromosomes apparent during mitotic interphase and telephase, but more diffuse nuclear expression during prometaphase, metaphase and anaphase. {ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Cohesin subunit scc-3
- Structural maintenance of chromosomes protein 1
- Cnd1 domain-containing protein
- Structural maintenance of chromosomes-like protein 1
- Nipped-B-like protein scc-2
- Separin homolog sep-1
- Structural maintenance of chromosomes protein 5
- separase
- Meiotic recombination protein rec-8
Sequence:
MFYAQFVLAKKGPLAKVWLAAHWEKKLTKAQIFETDVPQAIEEVIRPKVKMALRTVGHLLLGIVRIYSKKTRYLLADTNEAYQKMKINFRNGFSFEVDIPENAEIEEDFSNFIDKYNITVPEFHDADYNEQLIMANVSRREDITMKETVNFNVEFNIDADFDGFGDEGESWQLDHLYGSVEPLSLRPTPQPESLMEVERDRDVAANGTEISRIDADSVIFSEGPTRPNLIFDNQEGGNFMPEMNLKVENQTLENDGGVGPADMFSSMIHPVREHAVADVQNDDGMDFDYQPFEPENVEPSRPQSPESFALEPLDVEHMEGRKKRQRKARKLIVDAETMISNDAFREQQEDFSDTMRVVEMAPPTRKMFNLCVSGDLQHLSREPGCKMFNRELLQRYRRCLVTREFDLNYTMQELSDSSSFTPSMEAQAEPWEDLNLNEDIQEDIQAQGPAVDEFFNDVRMDDDDDRQPAQEMDFGDNFDFPQEVEHQECAPIPIQSGFAGENKENEDAEDWSDPFGSSNSSRRGQLEAYGFGNTSTYKEDDGKWAKRAKHILKKVSADIETSGQADFSSVTATAKNRKQAAEQFYSLLTLAKSQAISVDQSEPYGEIVIRPGANFKEACPLSSPKPMGLGNTMENSTMRTPMRPV
Protein: Exocyst complex component 7 (Exocyst complex component Exo70) (Q558Z9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O35250}. Cell membrane {ECO:0000250|UniProtKB:O35250}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35250}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9UPT5}.
Interaction partners:
- Exocyst complex component 6
- Exocyst complex component 1
- Exocyst complex component 2
- Exocyst complex component 3
- Exocyst complex component 5
- Exocyst complex component 8
- Exocyst complex component 4
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 8
Sequence:
MSAPPRLSARLSVLDQKKSNAPSPTSPTGLKTSLGMPPNSGSSGGGGGLKSSVGISSLPTIPSTKSTSPTLPKRNSANLSLLQQQQQQHTNKSTSPSSNTPTATSTTSPFSYLGKQASAQNLNTMMSMMMLNKNPLSPVVPQPGASLFYATPTEADDEEFEHIRNLLNSEYSVTTVQSTGALKSSNLVVMSWKNNATSELTEQDDQLENDKRDLQFIKEQLEKNNSMSKQMIYILDRFNEGLSQLEMDVAPINASMNEWSSIFNNINSTMEQVKSVLDKFDVDKIDSKINDGAKGDYVSYMLALEHVGNAIDYIAEKSHFKSSDKVMDALKQLKATGLNELETSFKSLLLKISNLVDPTTIAKLPNSKRYLAIILPNHVEEISKYIELFEKLHYNAFLKEYKDKRSKFILLSLRKMAPEKFIKQTSETKNLAYVKGSHPLISYVQETLRLYQIEYDLASELFGNQYQLILDEIIDPAHELLLETTEPIIKVRKTPGDKIFSIFPLLDLFDTFTKLLPDFITAISSRDGKHISELKTQIKHLQDTCASLLDFSLDEEKEISSSNRKEIISDATVDEISSNMINYFKRLIEYKHSVELLLKGQDNNNSNSNSNAPSSTSSNSKSSSSSSSSSSSNSASSTILPTSFIGFLEKILKNLIKYLQGRAKKDFPTQPATDFFKPPIKSVIFQINNYHYISTSLKQSKILSNQQFENNELASANHILHEFETCLDNEIKVLNSFWKTIADILITNKSNKEKDEVKSIIKKHTNFLKTFNDLNKLKFDIPDQELKLKLKTEAKNIIGRSYDQFKELCRLEKIHLEKNFVPFETTDDINRKLDRVFDSQ
Protein: Mitochondrial import receptor subunit TOM22 homolog (Translocase of outer membrane 22 kDa subunit homolog) (Q9CPQ3)
Organism: Mus musculus (Mouse)
Function: Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore (By similarity). Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Mitochondrial import receptor subunit TOM7 homolog
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM5 homolog
- Mitochondrial import receptor subunit TOM6 homolog
- Mitochondrial import receptor subunit TOM20 homolog
- Mitochondrial import receptor subunit TOM40 homolog
- Sorting and assembly machinery component 50 homolog
- Mitochondrial import receptor subunit TOM40B
- Metaxin-1
- Mitochondrial import inner membrane translocase subunit Tim23
Sequence:
MAAAVAAAGAGEPLSPEELLPKAEAEKAEEELEEDDDDELDETLSERLWGLTEMFPERVRSAAGATFDLSLFVAQKMYRFSRAALWIGTTSFMILVLPVVFETEKLQMEQQQQLQQRQILLGPNTGLSGGMPGALPPLPGKM
Protein: Interleukin-11 (IL-11) (P47873)
Organism: Mus musculus (Mouse)
Function: Cytokine that stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production. Also promotes the proliferation of hepatocytes in response to liver damage. Binding to its receptor formed by IL6ST and either IL11RA1 or IL11RA2 activates a signaling cascade that promotes cell proliferation, also in the context of various cancers. Signaling leads to the activation of intracellular protein kinases and the phosphorylation of STAT3. The interaction with the membrane-bound IL11RA and IL6ST stimulates 'classic signaling', whereas the binding of IL11 and soluble IL11RA to IL6ST stimulates 'trans-signaling' (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:22253262}.
Interaction partners:
- Interleukin-11 receptor subunit alpha-1
- Interleukin-6 receptor subunit alpha
- Interleukin-6 receptor subunit beta
- Interleukin-11 receptor subunit alpha-2
- Interleukin-6
- Leukemia inhibitory factor receptor
- Oncostatin-M-specific receptor subunit beta
- Ciliary neurotrophic factor receptor subunit alpha
- Oncostatin-M
- Ciliary neurotrophic factor
Sequence:
MNCVCRLVLVVLSLWPDRVVAPGPPAGSPRVSSDPRADLDSAVLLTRSLLADTRQLAAQMRDKFPADGDHSLDSLPTLAMSAGTLGSLQLPGVLTRLRVDLMSYLRHVQWLRRAGGPSLKTLEPELGALQARLERLLRRLQLLMSRLALPQAAPDQPVIPLGPPASAWGSIRAAHAILGGLHLTLDWAVRGLLLLKTRL
Protein: Patatin family protein (Q54QX7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MEKVFVKDEIYKYPTKIICDFKKCQKESTNSDDFHFCLQCNGDRIICKSCATRHQDESEHQTIPYEEFKRVTFFLKYQKFTQGYNDIVKYDRSMDLKNKLLFVNTKTKTIDHGYKWGQIGLSDKDPFLVDSFIGSSGSGKSTTICNLTKTCDHPIPGGDSITSTSSDLNSFIGETVGEEKFKYVIIDSEGINGTFSQKTNDLKERNEKKEKDEKNESLLIKADIRSKYVQSSYPRLLYLCSDVFVLTFYGDARNRGDVIDSLLEFSSVAADSANNPCSPHLIILFNNSNKNKEYDDMKYAKKEYFKDYFHGSKEIETRFQSVSIIFLPNINGKELDSFNRYQSQFKKLEETISEKVLESLKFKNNRTPKISVEKSKCMKRISNLTNFFSKNPIGSPDLVKLNCTGIIDDFSNFQEPKSTNKIFRNFTSNNSNDNNNNNNNNNNNNNNNNNNNNNNNYINFNADEDLPSSSSSSNKIGNMSHYTFSDSSIKSIQNLLGTPITFSINSEESYFEPDILKDREANISNKTTTTTTSSNNNNKNHNNNNNNINNTNNNNNNYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNYIDKTQLEERPIVDGLFQTNPDLDNLHQNHKSGSEESTLPIYSKNQEHSLTDQMINLHANYLFEFFLINYYYFVETFKCNSKESKSYTHCPEYSKKLHPRFESILELVSGEIHGMVPCGSKNVHGYSCTNFRGTHTKHISSETYKPKHTEIFGSFFNQSEVRYTWDGEFDESVKYDDLSLLLSNHLSGKETIKQVFIGHATTNQGVCFGCCLNSPYIEYKCGHFLCLDCSLGIFSQMPDRPKDECRVPGCYGDREYILKEIDFIKTMGARVLSLDGGGVRGILHCNVLQEIQKQLYGIHISKLFDLIVGTSAGGLVALQLASTEKTLPELAISFDILAKKGYERPTLGIITHIFGKPKYKRKKLKECYKTILNDKFLSISFPKIRAAVVTVTQESGDFDECIFSNYQKKTYPSKCSKQTHFISGSKVTDAAEATSAAPKYFRTFEYNSRQFLDGGLKNNNPCKVAMKEYKDMWPCRNLDTLVSLGTGDFPSPENQKNNIFKVGDQEYNLLTQSINSWREVHEIYYGFIWEGKNSFRYNPSFQKSIGLDEMDDNTMNILKQKVNIENDPTVHSIIKKSLSSLFYIDDLIFNKSKKELTGNIKCRLDKIPIEIINQLKKGSAFVLKYSNNDKNFQYFSPSPPHPNNQLNNFSNPFIIKNPPDIIDILCTMVAKNNIKNDTSISGNPFSINNGIENSFITTKN
Protein: Protein S100-A16 (Protein S100F) (S100 calcium binding protein A16) (Q9D708)
Organism: Mus musculus (Mouse)
Function: Calcium-binding protein. Binds one calcium ion per monomer. Can promote differentiation of adipocytes (in vitro). Overexpression in 3T3-L1 preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506}. Cytoplasm {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506}. Note=Primarily nucleolar. A high intracellular calcium level induces nucleolar exit and nucleocytoplasmic transport, whereas a low intracellular calcium level leads to nuclear translocation and accumulation within specific region of nucleoli (PubMed:17030513).
Interaction partners:
- Protein S100-A14
- Protein S100-A3
- S100 calcium binding protein A2
- Protein S100-A6
- Protein S100-A11
- Protein S100-A5
- Annexin A2
Sequence:
MADCYTELEKAVVVLVENFYKYVSKHSLVKNKISKSSFRKMLQRELNHMLTDTGNRKAADKLIQNLDANHDGRICFDEYWTMIGGITSPMANLIRQQECQQESQQECQQESQQESQQESQQGSS