wanglab/gogpt-training-data huggingface dataset:
Protein: Sodium-dependent phosphate transport protein 1 (Na(+)/PI cotransporter 1) (Renal Na(+)-dependent phosphate cotransporter 1) (Renal sodium-dependent phosphate transport protein 1) (Renal sodium-phosphate transport protein 1) (Sodium/phosphate cotransporter 1) (Solute carrier family 17 member 1) (Q62795)
Organism: Rattus norvegicus (Rat)
Function: Important for the resorption of phosphate by the kidney. May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. Plays a role in urate transport in the kidney.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q14916}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 17 member 3
- Na
- Solute carrier family 22 member 12
- Solute carrier family 2 member 9
- Organic anion transporter 3
- Sodium-dependent phosphate transport protein 2A
- Solute carrier family 22 member 6
- Broad substrate specificity ATP-binding cassette transporter ABCG2
Sequence:
MENRCLPKKVPGFCSFRYGLAILLHFCNIVIMAQRVCLNLTMVAMVNKTEPPHLSNKSVAEMLDNVKNPVHSWSLDIQGLVLSSVFLGMVVIQVPVGYLSGAYPMEKIIGSSLFLSSVLSLLIPPAAQVGAALVIVCRVLQGIAQGAVSTGQHGIWVKWAPPLERGRLTSMTLSGFVMGPFIALLVSGFICDLLGWPMVFYIFGIVGCVLSLFWFILLFDDPNNHPYMSSSEKDYITSSLMQQVHSGRQSLPIKAMLKSLPLWAIILNSFAFIWSNNLLVTYTPTFISTTLHVNVRENGLLSSLPYLLAYICGIVAGQMSDFLLSRKIFSVVAVRKLFTTLGIFCPVIFVVCLLYLSYNFYSTVIFLTLANSTLSFSFCGQLINALDIAPRYYGFLKAVTALIGIFGGLISSTLAGLILNQDPEYAWHKNFFLMAGINVTCLAFYLLFAKGDIQDWAKETKTTRL
Protein: Coiled-coil domain-containing protein 174 (Q6PII3)
Organism: Homo sapiens (Human)
Function: Probably involved in neuronal development.
Subcellular location: Nucleus {ECO:0000269|PubMed:26358778}. Note=In the nucleus of neuroblastoma cells, it colocalizes with EIF4A3, a component of exon junction complex. {ECO:0000269|PubMed:26358778}.
Interaction partners:
- Eukaryotic initiation factor 4A-III
- Zinc finger protein 830
Sequence:
MDRRKKPLDVTASSLVDLKAELFRKQEEFKQEKLLKDSGVFGKPKTTNKKPSIWSKQNVGVSNRAEKDAEQKIEEQKTLDKAREKLEEKAKLYEKMTKGDFIDEEVEDMYLVDFTQKIIDKRKEMEASGAHRDSQKAGERDDDEENLPEGEIPPPQDPSEEWVDYVDSLGRSRRCMRKDLPDLLEMDKNLQGRLFISPANEKTLLSEDMRKELQRQQWEEEEREALKRPMGPVHYEDIRENEARQLGVGYFAFARDKELRNKQMKTLEMLREQTTDQRTKRENIKEKRKAILEARLAKLRQKKMKKSKEGGTEEENRDGDVIGPLPPEPEAVPTPRPAAQSSKVEVIVQERKDTKPGVPHIREWDRGKEFSFGYWSKRQSDLRAERDPEFAPPSDYFVGQKRTGFSSSQAWSRPGPAQSDPGQCPDQSHGPSPEHTSPTPAPDNPPQAPTVTFKTLDDMISYYKQVT
Protein: Taste receptor type 2 member 123 (T2R123) (Taste receptor type 2 member 2) (T2R2) (Taste receptor type 2 member 23) (T2R23) (Q9JKF0)
Organism: Rattus norvegicus (Rat)
Function: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MFSQKTNYSHLFTFSIIFYVEIVTGILGNGFIALVNIMDWLKRRRISTADQILTALALTRLIYVWSVLICILLLFLCPHLSMRPEMFTAIGVIWVVDNHFSIWLATCLGVFYFLKIASFSNSLFLYLKWRVKKVVLMIILISLIFLMLNISSLGMYDHFSIDVYEGNMSYNLVDSTHFPRIFLFTNSSKVFLIANSSHVFLPINSLFMLIPFTVSLVAFFVLFLSLWKHHKKMQVNAKGPRDASTMAHTKALQIGFSFLLLYAIYLLFIITGILNLDLMRCIVILLFDHISGAVFSISHSFVLILGNSKLRQATLSVLPCLRCRSKDMDTVVF
Protein: NADH dehydrogenase subunit 2 (Q8HCM1)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 4L
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NADH dehydrogenase iron-sulfur protein 2
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 23 kDa subunit, mitochondrial, putative, expressed
- NADH-ubiquinone oxidoreductase chain 6
- NADH dehydrogenase iron-sulfur protein 3
Sequence:
MFNLFLAVSPEIFIINATFILLIHGVVFSTSKKDDYPPLVSNVGWLGLLSVLITLLLLAAGAPLLTIAHLFWNNFFRRDNFTYFCQILLLLSTAGTISMCFDSFEKERFDASEFIVLIPLPTRSMLLMIPAHDLIAMYLAIELQSLCFYVIAASKRKSEFSTEAGSKYLILGAFPSGILLFGCSMIYGSTGATHFDQLAKILTGYEITGAQSSGIFMGILFIAVGFLFKITAVPFHMWAPDIYEGSPTPVTAFLSIAPKISISANMSRVSIVASYGGTLQQIFFFCSIASMILGALAAMAQTKVKRPLAHSSIGHVGYIRTGFSCGTIEGIQSLLIGIFIYASMTIDAFAIVPALRQTRVKYIADLGALAKTNPILAMTFSITMFSYAGIPPLAGFCSKFYLFFAALGCGAYFLAPVGVVTSVIGCFYYIRLVKRMFFDRPRTWILYEPMDRDKSLLLAMTSSFITSSFPYPSPLFDLTHQMALSSYL
Protein: Peroxisomal membrane protein PEX27 (Peroxin-27) (Q08580)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for regulation of peroxisome size and number. Also promotes peroxisome division and biogenesis.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:14517321, ECO:0000269|PubMed:14517338, ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14517321, ECO:0000269|PubMed:14517338, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Peroxisomal membrane protein PMP27
- Peroxisomal membrane protein PEX25
- Peroxisomal membrane protein PEX34
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX18
- Peroxisomal membrane protein PEX15
- Peroxisomal protein PEX21
- Uncharacterized protein YGR168C
- Inheritance of peroxisomes protein 2
- Peroxisomal membrane protein import receptor PEX19
Sequence:
MTSDPVNTNISSPTLTDRNADESWELLKREFNTLFSNLKTDSKEEGNFTDNKGVIAKKPIVLQDNDDSDFTQNQGKVATATSTTSDRSFKRTLGSIEMKKRYVKKNCQAKFVFNTLEGKEVCSKILQHTLGLLSLLLLTRKIRLLNFSSKLRLVIQQLSLFRYYLRFGNFAINLYKIIKRFRWLREMKKLHYKDQSILFYFKNFRFFDIIEAFYNLTDELILFHKLQSMFGKKNTSHANTNRLMTFVKEQHYILWEVLNILAINKNIEQWRQLIRDEIYLSIYNTSGNAIKEYELKYKLPTNDKVNLELRKNNITLDFYKIILNLLSNLINIKGKRDKYNSELAYEIISVGSGVTELLKLWNRAKVTSANEHTSAV
Protein: Coiled-coil domain-containing protein 28B (Q9BUN5)
Organism: Homo sapiens (Human)
Function: Involved in ciliogenesis. Regulates cilia length through its interaction with MAPKAP1/SIN1 but independently of mTORC2 complex. Modulates mTORC2 complex assembly and function, possibly enhances AKT1 phosphorylation. Does not seem to modulate assembly and function of mTORC1 complex.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16327777}. Note=It localizes near centrosomes and basal bodies.
Interaction partners:
- BBSome complex member BBS4
- BBSome complex member BBS1
- BBSome complex member BBS7
- Tetratricopeptide repeat protein 8
- BBSome complex member BBS5
- WD repeat-containing and planar cell polarity effector protein fritz homolog
- Chaperonin-containing T-complex member BBS12
- Tectonic-like complex member MKS1
- BBSome complex assembly protein BBS10
- BBSome complex member BBS2
Sequence:
MDDKKKKRSPKPCLAQPAQAPGTLRRVPVPTSHSGSLALGLPHLPSPKQRAKFKRVGKEKCRPVLAGGGSGSAGTPLQHSFLTEVTDVYEMEGGLLNLLNDFHSGRLQAFGKECSFEQLEHVREMQEKLARLHFSLDVCGEEEDDEEEEDGVTEGLPEEQKKTMADRNLDQLLSNLEDLSNSIQKLHLAENAEPEEQSAA
Protein: Pleckstrin homology domain-containing family A member 5 (PH domain-containing family A member 5) (Phosphoinositol 3-phosphate-binding protein 2) (PEPP-2) (Q9HAU0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22037487}.
Interaction partners:
- PDZ domain-containing protein 11
Sequence:
MAADLNLEWISLPRSWTYGITRGGRVFFINEEAKSTTWLHPVTGEAVVTGHRRQSTDLPTGWEEAYTFEGARYYINHNERKVTCKHPVTGQPSQDNCIFVVNEQTVATMTSEEKKERPISMINEASNYNVTSDYAVHPMSPVGRTSRASKKVHNFGKRSNSIKRNPNAPVVRRGWLYKQDSTGMKLWKKRWFVLSDLCLFYYRDEKEEGILGSILLPSFQIALLTSEDHINRKYAFKAAHPNMRTYYFCTDTGKEMELWMKAMLDAALVQTEPVKRVDKITSENAPTKETNNIPNHRVLIKPEIQNNQKNKEMSKIEEKKALEAEKYGFQKDGQDRPLTKINSVKLNSLPSEYESGSACPAQTVHYRPINLSSSENKIVNVSLADLRGGNRPNTGPLYTEADRVIQRTNSMQQLEQWIKIQKGRGHEEETRGVISYQTLPRNMPSHRAQIMARYPEGYRTLPRNSKTRPESICSVTPSTHDKTLGPGAEEKRRSMRDDTMWQLYEWQQRQFYNKQSTLPRHSTLSSPKTMVNISDQTMHSIPTSPSHGSIAAYQGYSPQRTYRSEVSSPIQRGDVTIDRRHRAHHPKHVYVPDRRSVPAGLTLQSVSPQSLQGKTLSQDEGRGTLYKYRPEEVDIDAKLSRLCEQDKVVHALEEKLQQLHKEKYTLEQALLSASQEIEMHADNPAAIQTVVLQRDDLQNGLLSTCRELSRATAELERAWREYDKLEYDVTVTRNQMQEQLDHLGEVQTESAGIQRAQIQKELWRIQDVMEGLSKHKQQRGTTEIGMIGSKPFSTVKYKNEGPDYRLYKSEPELTTVAEVDESNGEEKSEPVSEIETSVVKGSHFPVGVVPPRAKSPTPESSTIASYVTLRKTKKMMDLRTERPRSAVEQLCLAESTRPRMTVEEQMERIRRHQQACLREKKKGLNVIGASDQSPLQSPSNLRDNPFRTTQTRRRDDKELDTAIRENDVKPDHETPATEIVQLKETEPQNVDFSKELKKTENISYEMLFEPEPNGVNSVEMMDKERNKDKMPEDVTFSPQDETQTANHKPEEHPEENTKNSVDEQEETVISYESTPEVSRGNQTMAVKSLSPSPESSASPVPSTQPQLTEGSHFMCV
Protein: Tumor necrosis factor ligand superfamily member 4 (Glycoprotein Gp34) (OX40 ligand) (OX40L) (TAX transcriptionally-activated glycoprotein 1) (CD antigen CD252) (P23510)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to TNFRSF4. Co-stimulates T-cell proliferation and cytokine production.
Subcellular location: Membrane; Single-pass type II membrane protein.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 4
- Tumor necrosis factor receptor superfamily member 9
- CD27 antigen
- T-cell-specific surface glycoprotein CD28
- CD40 ligand
- Inducible T-cell costimulator
- Tumor necrosis factor ligand superfamily member 9
- ICOS ligand
- Tumor necrosis factor receptor superfamily member 8
- Tumor necrosis factor ligand superfamily member 18
Sequence:
MERVQPLEENVGNAARPRFERNKLLLVASVIQGLGLLLCFTYICLHFSALQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL
Protein: Pyruvate kinase 1 (PK 1) (EC 2.7.1.40) (Q6FIS9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Enolase 2
- Enolase 1
- Malic enzyme
- Glucose-6-phosphate isomerase
- Pyruvate dehydrogenase E1 component subunit beta
- Pyruvate decarboxylase
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Pyruvate carboxylase
- Pyruvate carboxylase
Sequence:
MDSRLARLTTLQTSAGEELRRTSIIGTIGPKTNNPETLVALRKAGLNIVRMNFSHGSYEYHKSVIDNARKSEELYPGRPLAIALDTKGPEIRTGTTTNEVDYPIPPNHEMIFTTDDKYAKACDDKIMYLDYKNITKVISAGRIIYVDDGVLSFEVLQVVDDKTLKVKSLNAGKICSHKGVNLPGTDVDLPALSEKDKADLRFGVENGVHMIFASFIRTAQDVLTIREVLGEDGKDIKIVVKIENQQGVNNFDEILKVTDAVMVARGDLGIEIPAPEVLAVQKKLIAKSNLAGKPVICATQMLESMTYNPRPTRAEVSDVGNAVLDGADCVMLSGETAKGNYPINAVTTMAETALIAEQAIAYLPNYDDIRNCTPKPTSTTETVAASAVAAVFEQKAKAIIVLSTSGTTARLVSKYRPNCPIILVTRNARTARFSHLYRGVFPFVYEKESVSDWTEDVEARLNFGIEQAIEFGILKKGDTYVSIQGFKAGVGHSNTLQVSTA
Protein: Beta-2-glycoprotein 1 (APC inhibitor) (Activated protein C-binding protein) (Apolipoprotein H) (Apo-H) (Beta-2-glycoprotein I) (B2GPI) (Beta(2)GPI) (Q01339)
Organism: Mus musculus (Mouse)
Function: Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein A-II
- Plasminogen
- Annexin A2
- Apolipoprotein B-100
- Apolipoprotein A-I
- Prothrombin
- Apolipoprotein M
- Apolipoprotein C-III
- Haptoglobin
- Apolipoprotein C-I
Sequence:
MVSPVLALFSAFLCHVAIAGRICPKPDDLPFATVVPLKTSYDPGEQIVYSCKPGYVSRGGMRRFTCPLTGMWPINTLRCVPRVCPFAGILENGIVRYTSFEYPKNISFACNPGFFLNGTSSSKCTEEGKWSPDIPACARITCPPPPVPKFALLKDYRPSAGNNSLYQDTVVFKCLPHFAMIGNDTVMCTEQGNWTRLPECLEVKCPFPPRPENGYVNYPAKPVLLYKDKATFGCHETYKLDGPEEAECTKTGTWSFLPTCRESCKLPVKKATVLYQGMRVKIQEQFKNGMMHGDKIHFYCKNKEKKCSYTVEAHCRDGTIEIPSCFKEHSSLAFWKTDASELTPC
Protein: Transient receptor potential cation channel subfamily V member 1 (Transient receptor potential cation channel, subfamily V, member 1) (B6RTA2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSKSMDSSVSSFSLETDDQTEEERTKAKQMKKVSKDKRPMDSNYVDDVVEPSSTIKFNLHFDRGIRNLKEEPAQQDNDRFTIKRLFEAVSSGDVSKMQGLHEYLHKNMKRLTDSQYKSNGKTALLKALLNLRQGENDTIEQLLDIAEKMGDLKNFINAAYTDSYYKGQTALHVAIERRSMKFVQMLVKKGADVHAKACGKFFQPNQKMCFYFGELPLSLAACTNQQDIVDFLMENPHQAVDVRERDCHGNTVLHALVSVADNSPENTEFVIAMYDHILIKADQLHPKTKLEEIENNEGLTPITLAAKKGKLGLFKHIVQRELMGCRHLSRKITEWAYGPVCSSLYDLSSLDTYEKNSALEIVVYGSEIPNRLEMLQIEPLNRLIEEKWDQFAHRMFLFNFIVYVIYLFIFTASAFYHEEGKDYANQTKPPYLYAKSREGYLLLTGHIISITGAFYFFIRGLIDMVRKRPRFQSLIIDGYTDQLFFVQGLLFLASVVLYCYGQYEYLAFLVLCLALSWINLLYFSRGSKNLGIYNVMIQKMVLGEIRRFLVVYMVFLIGFSAALVTLLDQESIDSGSTRDFRLSEDIPSLNPTPDSSNPQSRMTHHQPTTARDGRGRFGLTTDNQYEVCKKPSYKNIYFTTLELFKFTIGMGDLEFTDHYKYKEVFYVLLIVYIVMTYILMLNMLIALMNQSVEMMSVESTSIWKLQRAITTLDMEWILPKCLQGKLRSGEEKDLGGGQEPDRRWCFSVEEVNWTQWNRNMGIIINEDPGKCTQDPSPANVQREPSRGVLQTFSRRRRTQRAQTREGHELSPLAEASSSV
Protein: Granzyme A (EC 3.4.21.78) (Autocrine thymic lymphoma granzyme-like serine protease) (CTLA-3) (Fragmentin-1) (T cell-specific serine protease 1) (TSP-1) (P11032)
Organism: Mus musculus (Mouse)
Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P12544}. Cytoplasmic granule {ECO:0000250|UniProtKB:P12544}. Note=Delivered into the target cell by perforin. {ECO:0000250|UniProtKB:P12544}.
Interaction partners:
- Perforin-1
- Granzyme K
- Protein NKG7
- Tumor necrosis factor ligand superfamily member 6
- Natural killer cells antigen CD94
- C-C motif chemokine 5
- T-cell surface glycoprotein CD3 delta chain
- Granzyme B
- Proteinase-activated receptor 1
- Interferon gamma
Sequence:
MRNASGPRGPSLATLLFLLLIPEGGCERIIGGDTVVPHSRPYMALLKLSSNTICAGALIEKNWVLTAAHCNVGKRSKFILGAHSINKEPEQQILTVKKAFPYPCYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGRFGNKSAPSETLREVNITVIDRKICNDEKHYNFHPVIGLNMICAGDLRGGKDSCNGDSGSPLLCDGILRGITSFGGEKCGDRRWPGVYTFLSDKHLNWIKKIMKGSV
Protein: ribose-5-phosphate isomerase (EC 5.3.1.6) (Phosphoriboisomerase) (A0A8I6AS52)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQRPGPFSTLYGRVLAPLPGRAGGAASGGGGNNWGLSGSHVQLPGRTQSETRGDKGGSSAGGPAPSTMSKAEEAKKLASHTAVENHVKNNQVLGIGSGSTIVHAVQRIAERVKQENLDLICIPTSFQIDLAIDGADEVDAELNLIKGGGGCLTQEKIVAGYASRFIVIADFRKDSKNLGDRWHKGIPIEVIPMAYVPVSRAVTQKFGGEVELRMAVNKAGPVVTDNGNFILDWKFDRVHKWGEVNTAIKMTPGVVDTGLFINMAERVYFGMQDGSVNVREKPF
Protein: Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (NHERF-2) (NHE3 kinase A regulatory protein E3KARP) (Octs2) (SRY-interacting protein 1) (SIP-1) (Sodium-hydrogen exchanger regulatory factor 2) (Solute carrier family 9 isoform A3 regulatory factor 2) (Tyrosine kinase activator protein 1) (TKA-1) (Q9JHL1)
Organism: Mus musculus (Mouse)
Function: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus (By similarity).
Subcellular location: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Apical cell membrane {ECO:0000250}. Note=Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes. Nuclear, in a punctate pattern (By similarity). {ECO:0000250}.
Interaction partners:
- Ezrin
- Sodium/hydrogen exchanger 3
- Lysophosphatidic acid receptor 2
- Radixin
- Podocalyxin
- Moesin
- Cystic fibrosis transmembrane conductance regulator
- Chloride anion exchanger
- Thyroid receptor-interacting protein 6
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
Sequence:
MAAPESLRPRLCRLVRGEQGYGFHLHGEKGRRGQFIRRVEPGSPAEAAALRAGDRLVEVNGVNVEGETHHQVVQRIKAVEGQTQLLVVDKETDEELCRRQLTCTEEMAHRGLPPAHNPWEPKPDWACSGSLGSDTGQKDVNGPPRELRPRLCHLRRGPQGYGFNLHSDKSRPGQYIRSVDPGSPASHSGLRAQDRLIEVNGQNVEGLRHAEVVARIKAQEDEARLLVVDPETDEHFKRLRVVPTEEHVEGPLPSPVTNGTSPAQLNGGSVCSSRSDLPGSEKDNEDGSTWKRDPFQESGLHLSPTAAEAKEKARATRVNKRAPQMDWNRKREIFSNF
Protein: Protein PBDC1 homolog (O59727)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MLSTKIDAENAENAAEIEMQFAVKAVEQAQIYWSLLEMRKGSELKLTKYDDEIFEDLINTFPEFKDPKTASFVNEDEMKSAKGKAAWRPFLMRYEKKVDDYNFGTLLRIKNTDEYEQETTIFVPRMQFLAYEIARNRYGLNDWIKKD
Protein: Centrin-A (Ddcrp) (Q54IY3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays a fundamental role in microtubule-organizing center structure and function.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11713866}. Nucleus {ECO:0000269|PubMed:11713866}. Note=Dissociates from the centrosome during prometaphase.
Interaction partners:
- SAC3/GANP/THP3 conserved domain-containing protein
- Transcription and mRNA export factor ENY2
- DNA repair protein Rad4 family protein
- PCI domain-containing protein 2 homolog
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco11
- Cytochrome b5 heme-binding domain-containing protein
Sequence:
MKTKTCKNLISNEQIQEVQEVYDTFKCRNGEMDKINIQYGFRALGVRLGEEEVEKIFKNQQYINFNSFLDIVTPLIYKIDVYASFEQAFSLFDRDGSGYITFDDLKTVAINLGEARSDSKLYNMIKRADLNGDKKISKIEFIQLLYWKKIY
Protein: Excitatory amino acid transporter 1 (Glial high affinity glutamate transporter) (High-affinity neuronal glutamate transporter) (GluT-1) (Sodium-dependent glutamate/aspartate transporter 1) (GLAST-1) (Solute carrier family 1 member 3) (P56564)
Organism: Mus musculus (Mouse)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28032905, ECO:0000269|PubMed:7903437}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Excitatory amino acid transporter 2
- Glutamine synthetase
- Glutamate receptor ionotropic, NMDA 1
- Solute carrier family 2, facilitated glucose transporter member 3
- Solute carrier family 2, facilitated glucose transporter member 4
- Glial fibrillary acidic protein
- Hexokinase-1
- Cytosolic 10-formyltetrahydrofolate dehydrogenase
- Aquaporin-4
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MTKSNGEEPRMGGRMERLQQGVRKRTLLAKKKVQSLTKEDVKSYLFRNAFVLLTVTAVIVGTILGFALRPYKMSYREVKYFSFPGELLMRMLQMLVLPLIISSLVTGMAALDSKASGKMGMRAVVYYMTTTIIAVVIGIIIVIIIHPGKGTKENMYREGKIVQVTAADAFLDLIRNMFPPNLVEACFKQFKTSYEKRSFKVPIQSNETLLGAVINNVSEAMETLTRIREEMVPVPGSVNGVNALGLVVFSMCFGFVIGNMKEQGQALREFFDSLNEAIMRLVAVIMWYAPLGILFLIAGKIVEMEDMGVIGGQLAMYTVTVIVGLLIHAVIVLPLLYFLVTRKNPWVFIGGLLQALITALGTSSSSATLPITFKCLEENNGVDKRITRFVLPVGATINMDGTALYEALAAIFIAQVNNFDLNFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELKNRDVEMGNSVIEENEMKKPYQLIAQDNEPEKPVADSETKM
Protein: Crossveinless c, isoform A (FI03409p) (Q9VFK2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQRRMSITIREYKFFRSFSQKFENWPKRKAEALWRKMRERKIAEIEAVEACKWLRAAGFPQYAQMYEDHQFPIDLNNVAKDHTNLENDQLQSLYRRLCVLNRCATMRLDQSHKPQTPQQKEESDDENFALSEHWTFQPHIRRWSRIGEMGLELPPPGLLSLNVEKTESSSKESSPDRFEEDGAGITLVTPGCSKAGGIPNDGSSLGEGSDSGRLRRSGSERIKDQAKALLRRVESIKSRRRKRQNRENVVISGPTVLDLSQFGQRSSLRKPDAVYSTPPSPSALSPMHTFPKAPFFGNDLKVPSHSDNFLSPNRSSPKRTPTTPRSMRTSPLHFFSSPMSQLKEGKSDDSSSYYSDSQESSTGGKLSLRKPSKARRFLQRTGKVDDIGAHSDSECHQGRKLLIKDANSNTTEVKVKKLTRGGSLNLGKDPKKRDGFRSSSFRSRSTSRKEAKNDEDTAGATTNGGSKRQPVVRWHSFQMEERPNMIFRKCFSKKIEPLQEDAGGMPFAAMSAGQLQIIRKLALVTLTGHMERYCPSHRSGWNWELPKFIKKIKMPDYKDKKVFGVPLLMILQRSGQTLPLAVRAAFRWLQLNALDQVGIFRKSGGKSRIMKLREQIEVTDSTAECMDVFDLQQAYDVADMLKQYFRELPESLLTTKMSETFVAIFQHLPAEVRLDAVQCAVLLLPDENREILYVLLEFLTIVAANSQQNQMTSNNLGVCLAQSIFHSSISTGSASVSASPRRKGKGSGMPDMKELAEAKASHECLSFMIEHYKQIYTAAKEKLSKCNFSYMEESKPLPLEALGEGMQFHNWRGYLYECTSATIKEGREKTRGWFSINSLNDSSVDIAYKKVGDGHPLRLWRCSTEIEGPPKEVLEFVIKQRASWDTNLLQCQTVKKLDDRTEIYQYALDGQLTTDFCVLRSWQTDLPRGACVIVETSIDHAKAKPLFGAVRGVVLASRYLIEPCGSGRSRVMHLARVDVKGKTPEWYNKNYGHICSHYLSRIRLAFKHVADGPESKV
Protein: Inositol-1-monophosphatase SuhB (I-1-Pase) (IMPase) (Inositol-1-phosphatase) (EC 3.1.3.25) (P9WKI9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the dephosphorylation of inositol 1-phosphate (I-1-P) to yield free myo-inositol, a key metabolite in mycobacteria. Is also able to hydrolyze a variety of polyol phosphates such as glucitol-6-phosphate, inositol 2-phosphate (I-2-P), glycerol-2-phosphate, and 2'-AMP, albeit with reduced efficiency.
Interaction partners:
- Inositol-3-phosphate synthase
- Probable inositol 1-monophosphatase ImpA
- Phospholipase C A
- Phospholipase C D
- Phospholipase C C
- Phospholipase C B
- 3'-phosphoadenosine 5'-phosphate phosphatase
Sequence:
MTRPDNEPARLRSVAENLAAEAAAFVRGRRAEVFGISRAGDGDGAVRAKSSPTDPVTVVDTDTERLLRDRLAQLRPGDPILGEEGGGPADVTATPSDRVTWVLDPIDGTVNFVYGIPAYAVSIGAQVGGITVAGAVADVAARTVYSAATGLGAHLTDERGRHVLRCTGVDELSMALLGTGFGYSVRCREKQAELLAHVVPLVRDVRRIGSAALDLCMVAAGRLDAYYEHGVQVWDCAAGALIAAEAGARVLLSTPRAGGAGLVVVAAAPGIADELLAALQRFNGLEPIPD
Protein: Centrosomal protein 170 (H0Y2V6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XQGEMRVPEEALKHEKFTIQLQLSQKSSESELSKSASAKSIDSKVADAATEVQHKTTEALKSEEKAMDISAMPRGTPLYGQPSWWGDDEVDEKRAFKTNGKPEEKNHEAGTSGCGIDAKQVEEQSAAANEEVLFPFCREPSYFEIPTKEFQQPSQITESTIHEIPTKDTPSSHITGAGHASFTIEFDDSTPGKVTIRDHVTKFTSDQRHKSKKSSPGTQDLLGIQTGMMAPENKVADWLAQNNPPQMLWERTEEDSKSIKSDVPVYLKRLKGNKHDDGTQSDSENAGAHRRCSKRATLEEHLRRHHSEHKKLQKVQATEKHQDQAVVSQTAFMIAFFDEDNPRKRRSYSFTQSAGILCQETTYSTPHTKLEKAKSPTADAKVVSLSLQTSSAHHRGGHGVPHGKLLKQKSEEPSVSIPFLQTALLRSSGSLGHRPSQEMDKMLKNQATSATSEKDNDDDQSDKGTYTIELENPNSEEVEARKMIDKVFGVDDNQDYNRPVINEKHKDLIKDWALSSAAAVMEERKPLTTSGFHHSEEGTSSSGSKRWVSQWASLAANHTRHDQEERIMEFSAPLPLENETEISESGMTVRSTGSATSLASQGERRRRTLPQLPNEEKSLESHRAKVVTQRSEIGEKQDTELQEKETPTQVYQKDKQDADRPLSKMNRAVNGETLKTGGDNKTLLHLGSSAPGKEKSETDKETSLVKQTLAKLQQQEQREEAQWTPTKLSSKNVSGQTDKCREETFKQESQPPEKNSGHSTSKGDRVAQSESKRRKAEEILKSQTPKGGDKKESSKSLVRQGSFTIEKPSPNIPIELIPHINKQTSSTPSSLALTSASRIRERSESLDPDSSMDTTLILKDTEAVMAFLEAKLREDNKTDEGPDTPSYNRDNSISPESDVDTASTISLVTGETERKSTQKRKSFTSLYKDRCSTGSPSKDVTKSSSSGAREKMEKKTKSRSTDVGSRADGRKFVQSSGRIRQPSVDLTDDDQTSSVPHSAISDIMSSDQETYSCKPHGRTPLTSADEHVHSKLEGSKVTKSKTSPVVSGSSSKSTTLPRPRPTRTSLLRRARLGEASDSELADADKASVASEVSTTSSTSKPPTGRRNISRIDLLAQPRRTRLGSLSARSDSEATISRSSASSRTAEAIIRSGARLVPSDKFSPRIRANSISRLSDSKVKSMTSAHGSASVNSRWRRFPTDYASTSEDEFGSNRNSPKHTRLRTSPALKTTRLQSAGSAMPTSSSFKHRIKEQEDYIRDWTAHREEIARISQDLALIAREINDVAGEIDSVTSSGTAPSTTVSTAATTPGSAIDTREEVGDLHGEMHKLVDRVFDESLNFRKIPPLVHSKTPEGNNGRSGDPRPQAAEPPDHLTITRRRTWSRDEVMGDNLLLSSVFQFSKKIRQSIDKTAGKIRILFKDKDRNWDDIESKLRAESEVPIVKTSSMEISSILQELKRVEKQLQAINAMIDPDGTLEALNNMGFPSAMLPSPPKQKSSPVNNHHSPGQTPTLGQPEARALHPAAVSAAAEFENAESEADFSIHFNRFNPDGEEEDVTVQE
Protein: ADP,ATP carrier protein 4 (ADP/ATP translocase 4) (Q9ZD47)
Organism: Rickettsia prowazekii (strain Madrid E)
Function: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MTINASNIENSFSKINSHFSKLTDYIWPIKRHEISKFLFITLLMFCILFIQNLIRALKDSIVTTMIGAETISFLKFWGVMPSAFLITVIYVKLVNRMKAENIFYLIISIFLTFFALFAYVIFPNHEMLHLRPVTVHNLTASLPNLKWFILLLSKWSFSLFYIIAELWPNVVFALLFWQFVNNITTVEESKRFYPLFGLLSQTGIYLAGHFLENLSNINYYVTNKFALQSSFHTLSIQIILTIVLILGIVSIKTFWLLNHKVLDKKHMALLRFKTKNKSITIAKSFQMILSSRHIRLIATLLICYGIAINLVEGPWKAAATKIYKTPTEYAAFIGSYLSYTGVFTIFFVLLGSNIVRRMGWFTSAVITPSIVFITGILFFAVNNFEGFAGLIIANFILTDPALVAITIGAIQNVLSKSSKYTLFDSTKEMAYVPLEPEIKISGKAAADVIGTKLGKSGSAFLQSLIFIILPSASYQSISICLMIIFILTCVTWIWATKELNKEYKNSIKFSQK