wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phyllopod (Q27934)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential adapter component of E3 ubiquitin ligase complexes; involved in R7 photoreceptor cell differentiation, embryonic nervous system, external sensory organ development and specification of particular muscles. E3 ubiquitin ligase complexes mediate ubiquitination and subsequent proteasomal degradation of target proteins. Required for specification of R7 photoreceptor cell fate in the eye by participating in the ubiquitination and subsequent proteasomal degradation of Tramtrack (ttk), a general inhibitor of photoreceptor differentiation. Acts downstream of Notch signaling to specify the fate of the SOP (sensory organ precursor) cells and their progeny, probably via the sina-mediated proteasomal degradation of ttk. Its restricted pattern of expression, upon Notch and Ras signaling pathways, suggests that it acts as a key determinant in E3 complexes to trigger protein proteolysis in appropriate cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:7859287, ECO:0000269|PubMed:7888014}.
Interaction partners:
- Protein tramtrack, alpha isoform
- E3 ubiquitin-protein ligase sina
- Probable E3 ubiquitin-protein ligase sinah
Sequence:
MSTNQQQQANPSAAVAAPAASSEYLKRTCLICGCHTNQTINIYEPRSGPNIVQLIQAKFKFQPLNEDKFLCFSCNNWLINWHSLQAVNSNEAESQSQSPSHMGNSVLQQERTKLRPVAMVRPTVRVQPQSQPQLQPQVPINPTPAPIVYSKRRASRRSASVSRMSRVLRQCCVESLRRSPKKRNQQSVFVCLRPQGQKRSNAICKVECVAPRRKPVERLVKDVAATATPTPVLNTQSTPTYQRFPQPSVDGKVVAMFRRLGTTLSREEPAAYSAESNPACSKLPQIMSPLKEAPRWTRDLDDDEILLEFDTAISEVLPTARYQVTHEENKENQQAQEMELELEEEEEVDGRAELEVVQEAEAPLEPQSHHKQGNSHQNSHQASIQLAGLRLPMGLSISLV
Protein: Eukaryotic initiation factor 4B (Eukaryotic translation initiation factor 4B, isoform A) (RE54950p) (Q8SYL3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASAGKKGKKNKGTVISLQSFLCNSDAPVGTTQVSKKIRNLDGDDSDDGSGTLPLVYQLPTAPRANRIFDDNSIPHKAPFIAYINNLPFDANEDDLYEFFEGINLISLRLPREDGENGRSRGFGYVELENREDLIHVLSLPDPSIKGRRIRIELSNENDQQSRQKSNRRFDGFGNNGDNRDSGNWRRDSQNNGSNFGYSSNFERSFNRERKSLPDRDDVNTPGSWRTSARPQSIDTSPTRREVEQVSEKYREGRVKIADRYSREETSKVEEERPKLNLKPRTLPLPDVKTIEFEKCDVDEFNLDKQGGTSSLNVFGSAKPVDTAARELEIEQRLALARKQDKGRREQGLNEKLAELQVDKNDNESLSATVSWRTNQDYKESDKINKCPGN
Protein: Calreticulin (Q41799)
Organism: Zea mays (Maize)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
FSVKHEQKLDCGGGYVKLLGGGDVDQKKFGGDTSYSIMFGPDICGYSTKKVHTILTKDGKNHLIKKDVPCETDQLTHVYTLIIRPDATYSILIDNEDKQTGSIYEHWDILPPKKVKDPEAKKPEDWDDKEYIPDPEDKKPEGYDDIPKEIPDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKQKKIKNPNYQGKWKAPMIDNPDFKDDPYIYAFDSLKYIGIELWQVKSGTLFDNIIITDDPALAKTFAEETWGKHKEAEKAAFDEAEKKKEEEDAAKGGDDEDDDLEDEEDDEKADEDKADSDAEDGKDSDDEKHDEL
Protein: Uncharacterized protein (Q54F55)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- 1-phosphatidylinositol-5-phosphate 4-kinase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- GRAM domain-containing protein
- Myotubularin phosphatase domain-containing protein
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Inositol 5-phosphatase 4
- 1-phosphatidylinositol 4-kinase
- Uncharacterized protein
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- LIM-domain containing phosphatase
Sequence:
MDNYTCINDTTIQQLKNQILVTDNSIGNNFLLSLSENDSSQIIKSVGWTKVLSIGNLLKQTTLNKPNEVKSIKLYIVSSSTSTSPININNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNSNSNVINRFNQFNSPSPPSPSKVNSTNSIENKSTNTTKSIIENFNINLTLNSPNSNGIISNNTSTSTSTSISHRNKNHPLRKSKSDLDQYWKLAQIQENNNNNNNNSNNSNDSNTNVNNNNINNIINNSNNSNNSNGSNSNSNSNNTIKNNNNNSSNNNNNKSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNYYKNNMIAPNMPGQLIYQPTARNTEIKSTLTYQQTKSPPKISISPPLQYQQPQPQYQPPPPLQYQQPFNVVSTTTTNTTTTTTTSQATATTTTNKPLNQINLDVLDQMLGQIPQQNREQQKKRSTSFSSHFPSTFFGISSSSNTSSQSSSSSQSSKHSSQNDYYLSSNDIDNINYGRQRNGSISSTTSTSTNIIGKKIFASLTDTPIIYSGELYKKNRNLNIGWKKRFFILTATSLIQSNSSSEQPKSEIILSNYILNITSDSSAKFCIQLTPNTTTTTQPPNLLSYLFSVDTFEQHREWITAFNNSFRCLDYSKPIDISNCSQLITMSSSQSNKQFQSSLEIDYQKKLPSTFRVSYQNDEINYFRFKMSRLLKEIQPFIFKSFNLLSVDLINSNYSLINQSIQIDNQNNNNNNNNQNKRKAIIINNNDINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNIKILNIKVTPTINPTNKAATTTTTTTTSSISVKDNSNIGGILSINNFNEKFLKVIIYHNGLVIKYMVSIESTFEMILNERVDLFGENVSNRFGLKILGSMEHIFNLKIKLKDTVYVNKSVRFRKKFKLKTVDISLQKYCFIPNVMNSLEWRQFQEKINYQYDIKPSNNSNSSQSVHLIDLTSVSMPVSLPKSLTESKLIIEIKSVENIVPILKRYYPTSYTKVPVYVEIQIYYGDLLLTKNKTSSKVNILEWNEKLYFDINLIDFPKECTFLTSIYSNESSSTIIPTLNPGQSSSTSTTTTNSSSSSATTNTTSSSSTISSTTSPLLMPLDILLAQYPFQIQSIEKKKILKNNFEINLLPIFEQQQPIYIQQQQQQLQQQQQLQQENQQQNQHQSRGTLPNHSSSVNFISNENIILKCTIPNITNSIYFKEDSNQNSPSLLSSNSSSSSSSTTTTTFSSNKNLSLLSSSPSSSINSFRKQSFSTSLSNDKLNSLIENLMKFERSNINESDRSILWENREYCKINYPNILPTLLYNYSILSWSSRVELYRLLKDWPMISPSFGLELLSSDFIDDRIREIGVQSINQWPDNQLSLYLPQIVSMLKYEPTNYSALVNFIVKRSICNPIKIGQPVFWLCSNEISPLENKNHIIIRYKLVMEIILEGLGIGVINSTTTTTNNEQQQQQQQQQQQQQQQQQQNSNKFGQSLVSQYLLLRLLKEINIDIIKEPEKQKQIFETRLSLLPKVFTLPTHPYQEFNSFVLEELKVKDSNAAPLWLVFSSIDKEADDTKIIFKKDDVRPDELCLQLFSLMDSILKSNGLDCEFTIFKCLSAKSGLGLIEVVPDSVTLADFMRDTTKYPSIEQWLKLKNPPNSTQHIDIFIKSCSVYCVATYLLGIYDRHNDNLMVSATGHFLHIDFGYFLGKVTKFLMFERETAPFVLTKDIVAMLGSREEEFKVLSCKIYNILRDNSRQLLNLIPSQQGKQLVRDRLQLDLSNIQAEKYFLQLIKDSKNNLRSEFNNKFHVLIHPN
Protein: Plakophilin-2 (Q99959)
Organism: Homo sapiens (Human)
Function: Regulates focal adhesion turnover resulting in changes in focal adhesion size, cell adhesion and cell spreading, potentially via transcriptional modulation of beta-integrins. Required to maintain gingival epithelial barrier function. Required for cardiac sodium current propagation and electrical synchrony in cardiac myocytes (By similarity). Required for the formation of desmosome cell junctions in cardiomyocytes, thereby required for the correct formation of the heart, specifically trabeculation and formation of the atria walls (By similarity). Loss of desmosome cell junctions leads to mis-localization of DSP and DSG2 resulting in disruption of cell-cell adhesion and disordered intermediate filaments (By similarity). Modulates profibrotic gene expression in cardiomyocytes via regulation of DSP expression and subsequent activation of downstream TGFB1 and MAPK14/p38 MAPK signaling (By similarity). May play a role in junctional plaques. Involved in the inhibition of viral infection by influenza A viruses (IAV). Acts as a host restriction factor for IAV viral propagation, potentially via disrupting the interaction of IAV polymerase complex proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:11416169, ECO:0000269|PubMed:11790773, ECO:0000269|PubMed:20613778, ECO:0000269|PubMed:22781308, ECO:0000269|PubMed:28169297, ECO:0000269|PubMed:34368962}. Cell junction, desmosome {ECO:0000269|PubMed:19533476, ECO:0000269|PubMed:20613778, ECO:0000269|PubMed:20859650, ECO:0000269|PubMed:22781308, ECO:0000269|PubMed:23884246, ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:34368962}. Cell junction {ECO:0000269|PubMed:28169297}. Cytoplasm {ECO:0000269|PubMed:34368962}. Note=Colocalizes with CTNNA3 and SCN5A/Nav1.5 at intercalated disks in the heart. {ECO:0000250|UniProtKB:Q9CQ73}.
Interaction partners:
- Desmoglein-2
- Desmoplakin
- Desmocollin-2
- Junction plakoglobin
- Catenin alpha-3
- Desmocollin-3
- Sodium channel protein type 5 subunit alpha
- Gap junction alpha-1 protein
- Desmoglein-1
- Transmembrane protein 43
Sequence:
MAAPGAPAEYGYIRTVLGQQILGQLDSSSLALPSEAKLKLAGSSGRGGQTVKSLRIQEQVQQTLARKGRSSVGNGNLHRTSSVPEYVYNLHLVENDFVGGRSPVPKTYDMLKAGTTATYEGRWGRGTAQYSSQKSVEERSLRHPLRRLEISPDSSPERAHYTHSDYQYSQRSQAGHTLHHQESRRAALLVPPRYARSEIVGVSRAGTTSRQRHFDTYHRQYQHGSVSDTVFDSIPANPALLTYPRPGTSRSMGNLLEKENYLTAGLTVGQVRPLVPLQPVTQNRASRSSWHQSSFHSTRTLREAGPSVAVDSSGRRAHLTVGQAAAGGSGNLLTERSTFTDSQLGNADMEMTLERAVSMLEADHMLPSRISAAATFIQHECFQKSEARKRVNQLRGILKLLQLLKVQNEDVQRAVCGALRNLVFEDNDNKLEVAELNGVPRLLQVLKQTRDLETKKQITDHTVNLRSRNGWPGAVAHACNPSTLGGQGGRITRSGVRDQPDQHGLLWNLSSNDKLKNLMITEALLTLTENIIIPFSGWPEGDYPKANGLLDFDIFYNVTGCLRNMSSAGADGRKAMRRCDGLIDSLVHYVRGTIADYQPDDKATENCVCILHNLSYQLEAELPEKYSQNIYIQNRNIQTDNNKSIGCFGSRSRKVKEQYQDVPMPEEKSNPKGVEWLWHSIVIRMYLSLIAKSVRNYTQEASLGALQNLTAGSGPMPTSVAQTVVQKESGLQHTRKMLHVGDPSVKKTAISLLRNLSRNLSLQNEIAKETLPDLVSIIPDTVPSTDLLIETTASACYTLNNIIQNSYQNARDLLNTGGIQKIMAISAGDAYASNKASKAASVLLYSLWAHTELHHAYKKAQFKKTDFVNSRTAKAYHSLKD
Protein: At3g02555 (Q8LF93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Replication protein A 32 kDa subunit B
- Probable mitochondrial-processing peptidase subunit beta, mitochondrial
- Protein EXPORTIN 1B
- Polypyrimidine tract-binding protein homolog 1
- Lysine-tRNA ligase
- SUPPRESSOR OF GAMMA RESPONSE 1
Sequence:
MNHCSLQQNAFLSREESRGFVPIYSHPVDSVVCPKPRRANNVIRPFRLHFSLSGADDVCDSKAGEDLLDIFRRKESVSSRSPPFFLGSPPSRAANPLAQDARFGDEKLNTVSPSLSPLLPSASRVKSGCGRMKFGVKPATVRVEGFDCLNRDRPNSSIPAMA
Protein: Uroplakin-2 (UP2) (Uroplakin II) (UPII) (P38575)
Organism: Mus musculus (Mouse)
Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in regulating the assembly of the AUM.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1A is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}.
Interaction partners:
- Uroplakin-1a
- Uroplakin-1b
- Uroplakin-3a
- Uroplakin-3b
Sequence:
MASTLPVQTLPLILILLAVLAPGTADFNISSLSGLLSPALTESLLIALPPCHLTGGNATLMVRRANDSKVVKSDFVVPPCRGRRELVSVVDSGSGYTVTRLSAYQVTNLTPGTKYYISYRVQKGTSTESSPETPMSTLPRKNMESIGLGMARTGGMVVITVLLSVAMFLLVVGLIVALHWDARK
Protein: Protein virC1 (P07165)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Interaction partners:
Sequence:
MKLLTFCSFKGGAGKTTALMGLCAAFASDGKRLALFDADENRPLTRWKENALRSNTWGSFCEVYAAEEMALLEAAYEDAELQGFDYALADTHGGSSELNNTIIASSNLLLIPTMLTPLDIDEALSTYRYVIELLLSENLAIPTAVLRQRVPVGRLTTSQRAMSDMLASLPVVQSPMHERDAFAAMKERGMLHLTLLNMRTDPTMRLLERNLRIAMEELVTISKLVSEALEG
Protein: Multidrug resistance protein MdtO (P32715)
Organism: Escherichia coli (strain K12)
Function: Could be involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- Multidrug resistance protein MdtN
- Multidrug resistance outer membrane protein MdtP
- Uncharacterized protein YtcA
- D-allose import ATP-binding protein AlsA
- Linear primary-alkylsulfatase
Sequence:
MSALNSLPLPVVRLLAFFHEELSERRPGRVPQTVQLWVGCLLVILISMTFEIPFVALSLAVLFYGIQSNAFYTKFVAILFVVATVLEIGSLFLIYKWSYGEPLIRLIIAGPILMGCMFLMRTHRLGLVFFAVAIVAIYGQTFPAMLDYPEVVVRLTLWCIVVGLYPTLLMTLIGVLWFPSRAISQMHQALNDRLDDAISHLTDSLAPLPETRIEREALALQKLNVFCLADDANWRTQNAWWQSCVATVTYIYSTLNRYDPTSFADSQAIIEFRQKLASEINKLQHAVAEGQCWQSDWRISESEAMAARECNLENICQTLLQLGQMDPNTPPTPAAKPPSMAADAFTNPDYMRYAVKTLLACLICYTFYSGVDWEGIHTCMLTCVIVANPNVGSSYQKMVLRFGGAFCGAILALLFTLLVMPWLDNIVELLFVLAPIFLLGAWIATSSERSSYIGTQMVVTFALATLENVFGPVYDLVEIRDRALGIIIGTVVSAVIYTFVWPESEARTLPQKLAGTLGMLSKVMRIPRQQEVTALRTYLQIRIGLHAAFNACEEMCQRVALERQLDSEERALLIERSQTVIRQGRDLLHAWDATWNSAQALDNALQPDRAGQFADALEKYAAGLATALSRSPQITLEETPASQAILPTLLKQEQHVCQLFARLPDWTAPALTPATEQAQGATQ
Protein: Syncoilin (Syncoilin intermediate filament 1) (Syncoilin-1) (Q9H7C4)
Organism: Homo sapiens (Human)
Function: Atypical type III intermediate filament (IF) protein that may play a supportive role in the efficient coupling of mechanical stress between the myofibril and fiber exterior. May facilitate lateral force transmission during skeletal muscle contraction. Does not form homofilaments nor heterofilaments with other IF proteins.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EPM5}. Note=In skeletal muscle, colocalizes with DES and DTNA, and is localized at the myotendinous and neuromuscular junctions, sarcolemma and Z-lines. In myotubes, detected in a punctate cytoplasmic pattern (By similarity). {ECO:0000250|UniProtKB:Q9EPM5}.
Interaction partners:
- Dystrobrevin alpha
- Desmin
- Synemin
- Dystrophin
- Vimentin
- Dystrobrevin beta
Sequence:
MASPEPRRGGDGAAQAARKTRVEANSPLPKNSGSLNEAEALNPEVTLSSEGSLNLEDILYLEDTGDLDETLYVQETEKAEEALYIEEAMQPDEALHVEEPGNPEETVCVEETTEPDRIQFVEGPVEPGKPTSPEHVVYEGETVTRAEKSNPEESLRAEQSPSMEENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLLPKSLEQADAPTSQAGGMETQSQGAV
Protein: GH08269p (Trailer hitch, isoform A) (Trailer hitch, isoform B) (Q9VTZ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGGLPELGSKISLISKADIRYEGRLYTVDPQECTIALSSVRSFGTEDRDTQFQIAPQSQIYDYILFRGSDIKDIRVVNNHTLPHHNDPAIMQAQLQNGPPQMPQHFPMPSGMSGPPQQQQVPSQQPPQMPSGGGSGGAGGAGAPGGGGPGYGNGNPFGNLGGPNLANMVGNAGGSLAPGSGAPGSGPFMHIGGNQQQPKPQQQKQPNMLAGASRSTTPISLIVSPTAELTQQQQLHQQQNAGQGGNGRDAGHKRQNHQQQQNQQHQQRGGPSHNNMQQQQQRGGGSGTDFYNQQRDRRDSGRQMDNNYSNNYNNNNNNQRNRGGGNGMQQQQRGGNGGSGGGGGNGGGNNPAWNMHRGNQNSNNMMNMRNRGMGSRGPMRPNQGYRPQSANNQNKPRNKIKFEGDFDFEQANNKFEELRSQLAKLKVAEDGAPKPATNATAATATATNEQVGEKVEGVHTLNGETDKKDDSGNETGAGEHEPEEDDVAVCYDKTKSFFDNISCEAAQDRSKNKKNDWRQERKLNTETFGVSSTRRGSYRGRNQYYNNNGNGGINSGYGGAPGYNRNNYRMGGGGGNFRNRSNNRNNGGGRGGNGMPNITNGNTAAALKAANNAAGHGSNATDSSAPNATTATTKSTSLLPEQTQQVAAVSQ
Protein: DNA mismatch repair protein Msh3 (Protein repair-1) (REP-1) (Protein repair-3) (REP-3) (P13705)
Organism: Mus musculus (Mouse)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to 13 nucleotides long. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis (By similarity).
Interaction partners:
- DNA mismatch repair protein Msh6
- DNA mismatch repair protein Msh2
- Mismatch repair endonuclease PMS2
- DNA mismatch repair protein Mlh1
- MutL homolog 3
- Structure-specific endonuclease subunit SLX4
- DNA polymerase delta catalytic subunit
- PMS1 homolog 1, mismatch repair system component)
- Exonuclease 1
- X-ray repair cross-complementing protein 6
Sequence:
MPRGKSASGGSTAAGPGPGRQTVLSRFFRSAGSLRSSASSTEPAEKVTEGDSRKRSLGNGGPTKKKARKVPEKEEENISVASHHPEAKKCLRPRIVLKSLEKLKEFCCDSALPQNRVQTEALRERLEVLPRCTDFEDITLQRAKNAVLSEDSKSQANQKDSQFGPCPEVFQKTSDCKPFNKRSKSVYTPLELQYLDMKQQHKDAVLCVECGYKYRFFGEDAEIAARELNIYCHLDHNFMTASIPTHRLFVHVRRLVAKGYKVGVVKQTETAALKAIGDNKSSVFSRKLTALYTKSTLIGEDVNPLIRLDDSVNIDEVMTDTSTNYLLCIYEEKENIKDKKKGNLSVGVVGVQPATGEVVFDCFQDSASRLELETRISSLQPVELLLPSDLSEPTEMLIQRATNVSVRDDRIRVERMNNTYFEYSHAFQTVTEFYAREIVDSQGSQSLSGVINLEKPVICALAAVIRYLKEFNLEKMLSKPESFKQLSSGMEFMRINGTTLRNLEMVQNQTDMKTKGSLLWVLDHTKTSFGRRKLKNWVTQPLLKLREINARLDAVSDVLHSESSVFEQIENLLRKLPDVERGLCSIYHKKCSTQEFFLIVKSLCQLKSELQALMPAVNSHVQSDLLRALIVELLSPVEHYLKVLNGPAAKVGDKTELFKDLSDFPLIKKRKNEIQEVIHSIQMRLQEFRKILKLPSLQYVTVSGQEFMIEIKNSAVSCIPADWVKVGSTKAVSRFHPPFIVESYRRLNQLREQLVLDCNAEWLGFLENFGEHYHTLCKAVDHLATVDCIFSLAKVAKQGNYCRPTLQEEKKIIIKNGRHPMIDVLLGEQDQFVPNSTSLSDSERVMIITGPNMGGKSSYIKQVTLVTIMAQIGSYVPAEEATIGIVDGIFTRMGAADNIYKGRSTFMEQLTDTAEIIRRASPQSLVILDELGRGTSTHDGIAIAYATLEYFIRDVKSLTLFVTHYPPVCELEKCYPEQVGNYHMGFLVNEDESKQDSGDMEQMPDSVTFLYQITRGIAARSYGLNVAKLADVPREVLQKAAHKSKELEGLVSLRRKRLECFTDLWMTHSVKDLHTWADKLEMEEIQTSLPH
Protein: DNA gyrase subunit B (EC 5.6.2.2) (P9WG45)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state, while in the absence of ATP it relaxes supercoiled dsDNA. Also catalyzes the interconversion of other topological isomers of dsDNA rings, including catenanes. Gyrase from M.tuberculosis has higher decatenation than supercoiling activity compared to E.coli; as M.tuberculosis only has 1 type II topoisomerase, gyrase has to fulfill the decatenation function of topoisomerase IV as well. At comparable concentrations M.tuberculosis gyrase cannot introduce as many negative supercoils into DNA as the E.coli enzyme, and its ATPase activity is lower, perhaps because it does not couple DNA wrapping and ATP binding as well as E.coli.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.
Interaction partners:
- DNA gyrase subunit A
- Pentapeptide repeat protein MfpA
- DNA-directed RNA polymerase subunit beta
- DNA replication and repair protein RecF
- Enoyl-[acyl-carrier-protein] reductase
- Probable arabinosyltransferase B
- GCN5-related N-acetyltransferase
- Beta sliding clamp
- DNA-directed RNA polymerase subunit beta'
- Nicotinamidase/pyrazinamidase
Sequence:
MAAQKKKAQDEYGAASITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATTVNVVLLEDGGVEVADDGRGIPVATHASGIPTVDVVMTQLHAGGKFDSDAYAISGGLHGVGVSVVNALSTRLEVEIKRDGYEWSQVYEKSEPLGLKQGAPTKKTGSTVRFWADPAVFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTQDEVVDEVVSDVAEAPKSASERAAESTAPHKVKSRTFHYPGGLVDFVKHINRTKNAIHSSIVDFSGKGTGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDRKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQKVCNEQLTHWFEANPTDAKVVVNKAVSSAQARIAARKARELVRRKSATDIGGLPGKLADCRSTDPRKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDIGKLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIENGHVFLAQPPLYKLKWQRSDPEFAYSDRERDGLLEAGLKAGKKINKEDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV
Protein: Mitochondrial membrane-anchored protein domain-containing protein (Q4QI49)
Organism: Leishmania major
Interaction partners:
Sequence:
MLRHTARRMSSLSSFTGIEVDPYTAKSMFLFGFIASVGFLSVYSVKETKKAGPIELPEELEAQRQRHNDPRRPPWPLLHQRVVLLREGKGAPEDIALMWEQTKHYYPADWLIPLELTQVLKYSSGKYLQTYVADPDEMRKEVLMQLLNVKYGRVSDPNGGRVNKDVEEIISMAVDDLENMDLNPAADAVLIPTHT
Protein: Enolase 1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (P30575)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Fructose-bisphosphate aldolase
- Phosphoglycerate kinase
- Pyruvate kinase
- Phosphoglycerate mutase
- Triosephosphate isomerase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Transketolase
- Pyruvate decarboxylase
- Phosphoglycerate mutase
Sequence:
MSYATKIHARYVYDSRGNPTVEVDFTTDKGLFRSIVPSGASTGVHEALELRDGDKSKWLGKGVLKAVANVNDIIAPALIKAKIDVVDQAKIDEFLLSLDGTPNKSKLGANAILGVSLAAANAAAAAQGIPLYKHIANISNAKKGKFVLPVPFQNVLNGGSHAGGALAFQEFMIAPTGVSTFSEALRIGSEVYHNLKSLTKKKYGQSAGNVGDEGGVAPDIKTPKEALDLIMDAIDKAGYKGKVGIAMDVASSEFYKDGKYDLDFKNPESDPSKWLSGPQLADLYEQLISEYPIVSIEDPFAEDDWDAWVHFFERVGDKIQIVGDDLTVTNPTRIKTAIEKKAANALLLKVNQIGTLTESIQAANDSYAAGWGVMVSHRSGETEDTFIADLSVGLRSGQIKTGAPARSERLAKLNQILRIEEELGSEAIYAGKDFQKASQL
Protein: Mitochondrial intermembrane space cysteine motif-containing protein MIX14 (Mitochondrial intermembrane space CX(n)C motif protein of 14 kDa) (Q04341)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:17095012, ECO:0000269|PubMed:22984289}. Note=Imported into mitochondrion intermembrane space through the MIA pathway. {ECO:0000269|PubMed:17095012}.
Interaction partners:
- Mitochondrial intermembrane space cysteine motif-containing protein MIX17C motif protein of 17 kDa)
- Mitochondrial distribution and morphology protein 35
- Cytochrome c oxidase assembly protein COX19
- Mitochondrial intermembrane space import and assembly protein 40
- Cytochrome c oxidase copper chaperone
- Mitochondrial import inner membrane translocase subunit TIM9
- mRNA-binding protein PUF3
- COX assembly mitochondrial protein
- Cytochrome c oxidase-assembly factor COX23
Sequence:
MSDILDEIVIEDVVANCPQEFLQYHKCIRDNEENPGKCKDGRMILSTCIREKVPSVKSIMSECSEPMKKYDQCIRDNMGTRTINENCLGFLQDLRKCAELQVKNKNIKPSINGVNLELIKD
Protein: Putative fibroblast growth factor 1 (FGF-1) (Acidic fibroblast growth factor) (aFGF) (Heparin-binding growth factor 1) (HBGF-1) (Q6PBT8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrins. Its binding to integrins and subsequent ternary complex formation with integrins and FGFR1 are essential for FGF1 signaling.
Subcellular location: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13 (By similarity). Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery (By similarity). {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 1-A
- Fibroblast growth factor receptor 4
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor.
- Protein S100-A11
- receptor protein-tyrosine kinase
- Vascular endothelial growth factor receptor kdr-like
- Vascular endothelial growth factor receptor 2
- Mast/stem cell growth factor receptor kita
Sequence:
MTEADIAVKSSPRDYKKLTRLYCMNGGFHLQILADGTVAGAADENTYSILRIKATSPGVVVIEGSETGLYLSMNEHGKLYASSLVTDESYFLEKMEENHYNTYQSQKYGENWYVGIKKNGKMKRGPRTHIGQKAIFFLPRQVEQEED
Protein: V-set and transmembrane domain-containing protein 4 [Cleaved into: Peptide Lv] (T1NXB5)
Organism: Mus musculus (Mouse)
Function: Peptide Lv enhances L-type voltage-gated calcium channel (L-VGCC) currents in retinal photoreceptors.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Peptide Lv]: Secreted {ECO:0000269|PubMed:22912796}.
Interaction partners:
- Transmembrane protein 170B
Sequence:
MRLRLLALAAAVLLGPAPEVCGALNVTVSPGPVVDYLEGENATLLCHVSQKRRKDSLLAVRWFFAPDGSQEALMVKMTKLRIIQYYGNFSRTANQQRLRLLEERRGVLYRLSVLTLRPTDQGQYVCKVQEISKHRNKWTAWSNGSSATEMRVISLKAGEDSSFEKKKVTWAFFEDLYVYAVLVCCVGILSVLLFTLVIAWQSVFHKRKSRVRHYLVKCPQNSSGETVTSVTSLAPLQPQKGKRQKKKVDVPPAVPAKAPIATTFHKPKLLKPQRKVALPKITEENLTYAELELIKPHRAAKGVPTSTVYAQILFEENQL