wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized mitochondrial protein RF1 (P03881)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Intron-encoded RNA maturase bI4
- Intron-encoded endonuclease I-SceI
- ATP synthase subunit a
- Cytochrome b
- Cytochrome c oxidase subunit 2
- ATP synthase subunit 9, mitochondrial
- Uncharacterized protein YKL183C-A
- Uncharacterized protein YDL159W-A
- Uncharacterized protein YKL096C-B
- Cytochrome b mRNA maturase bI2
Sequence:
MIKWTMINIYLLLMFLIIKNNNNNNNYNNITKYNKDMDLYSIQSPYIKNMNIIKRGYHTSLNNKLIIVQKDNKNNNKNNLEMDNFYKWLVGFTDGDGSFYIKLNDKKYLRFFYGFRMHIDDKACLEKIRNMLNMPSNFEETTKTIMLVNSQKKWLYSNIVTIFDKYPCLTIKYYSYYKWKMAMINNLNGMSYNNKDLLNIKNTINNYEVMPNLKIPYDKMNDYWILGFIEAEGSFDTSPKRNICGFNVSQHKRSINTLKAIKSYVLNNWKPIDNTPLLIKNKLLKDWDSSIKLTKPDKNGVIKLEFNRMDFLYYVILPKLYSLKWYSRKEIDFQLWKTTMEIYMKGLHNTTKGSNLLKLINNNINKKRYYSNYNISKNIIDDVLNMNTIYNYKLPYRMNSDIQRLNSMNNNNTKFINVGVFVYDLNNTLIMTFTGYRPAATYFNCSKHEIAKYIKNGNVFMNKYILKNILLD
Protein: Frizzled-4 (Q9N532)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protein Wnt-1
- Protein Wnt
- Protein mom-2
- Inactive tyrosine-protein kinase RYK
- DiSHevelled related
- DiSHevelled related
- Secreted frizzled-related protein 1
- Protein Wnt-2
- Vang-like protein
- Abnormal cell lineage protein 44
Sequence:
MGPFRGYLGVTWLLLLFVIGVDGQRCQKVDHEMCNDLPYNLTSFPNLVDEESWKDASESILTYKPLLSVVCSEQLKFFLCSVYFPMCNEKLANPIGPCRPLCLSVQEKCLPVLESFGFKWPDVIRCDKFPLENNREKMCMKGPNEQGAIQDERAKFAAKESEDDGNDRVEDIQREVDRLNGKCPQDEVFLNRSSKCVPLCSNPQKVGQTDRESATRLLLFLSLSSVILTILSVFIVGLSIYFRRLEMLHSLTETAMFFSCISFCATSVIYIVSISFKDQFQISCTDYTHHLLFVVGGLSHVPCSSVASLIYYTATCSRLWWLLICVSWNKATRTSHILDDSRTRVIMLILGIPLAPLMLALLAKAVAANPLTGLCFIGAASPGTDWIFNFCRELILFLISSIALSSACCRLLGSDEQDVNGFAGVIAAVYPIAGLFYMLSFVNDATQPFLSLDRSFNAVSATKFSFDLLLSFIMCAFCLIYLLFKLTRSSSKVSKEGYQPAVPKLPQPAIPGSVRSNTYASTFRTNNMI
Protein: Desmocollin-2 (Cadherin family member 2) (Desmocollin-3) (Desmosomal glycoprotein II) (Desmosomal glycoprotein III) (Q02487)
Organism: Homo sapiens (Human)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17963498, ECO:0000269|PubMed:21062920, ECO:0000269|PubMed:23863954}; Single-pass type I membrane protein {ECO:0000269|PubMed:21062920}. Cell junction, desmosome {ECO:0000269|PubMed:17963498, ECO:0000269|PubMed:21062920, ECO:0000269|PubMed:25208567}.
Interaction partners:
- Plakophilin-2
- Desmoglein-2
- Desmoplakin
- Junction plakoglobin
- Transmembrane protein 43
- Desmoglein-3
- Plakophilin-3
- Plakophilin-1
- Plakophilin-4
- Gap junction alpha-1 protein
Sequence:
MEAARPSGSWNGALCRLLLLTLAILIFASDACKNVTLHVPSKLDAEKLVGRVNLKECFTAANLIHSSDPDFQILEDGSVYTTNTILLSSEKRSFTILLSNTENQEKKKIFVFLEHQTKVLKKRHTKEKVLRRAKRRWAPIPCSMLENSLGPFPLFLQQVQSDTAQNYTIYYSIRGPGVDQEPRNLFYVERDTGNLYCTRPVDREQYESFEIIAFATTPDGYTPELPLPLIIKIEDENDNYPIFTEETYTFTIFENCRVGTTVGQVCATDKDEPDTMHTRLKYSIIGQVPPSPTLFSMHPTTGVITTTSSQLDRELIDKYQLKIKVQDMDGQYFGLQTTSTCIINIDDVNDHLPTFTRTSYVTSVEENTVDVEILRVTVEDKDLVNTANWRANYTILKGNENGNFKIVTDAKTNEGVLCVVKPLNYEEKQQMILQIGVVNEAPFSREASPRSAMSTATVTVNVEDQDEGPECNPPIQTVRMKENAEVGTTSNGYKAYDPETRSSSGIRYKKLTDPTGWVTIDENTGSIKVFRSLDREAETIKNGIYNITVLASDQGGRTCTGTLGIILQDVNDNSPFIPKKTVIICKPTMSSAEIVAVDPDEPIHGPPFDFSLESSTSEVQRMWRLKAINDTAARLSYQNDPPFGSYVVPITVRDRLGMSSVTSLDVTLCDCITENDCTHRVDPRIGGGGVQLGKWAILAILLGIALLFCILFTLVCGASGTSKQPKVIPDDLAQQNLIVSNTEAPGDDKVYSANGFTTQTVGASAQGVCGTVGSGIKNGGQETIEMVKGGHQTSESCRGAGHHHTLDSCRGGHTEVDNCRYTYSEWHSFTQPRLGEKVYLCNQDENHKHAQDYVLTYNYEGRGSVAGSVGCCSERQEEDGLEFLDNLEPKFRTLAEACMKR
Protein: Glycine cleavage system H protein, mitochondrial (Lipoic acid-containing protein) (P11183)
Organism: Gallus gallus (Chicken)
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:7440563}.
Interaction partners:
- Glycine dehydrogenase
- Serine hydroxymethyltransferase
- Dihydrolipoyl dehydrogenase
- Lipoyl synthase
- Methylenetetrahydrofolate reductase
- Putative lipoyltransferase 2
- BPL/LPL catalytic domain-containing protein.
- Alanine--glyoxylate and serine--pyruvate aminotransferase.
- Uncharacterized protein.
- Methylenetetrahydrofolate dehydrogenase
Sequence:
MAWLVLRRLGPVLAPRCPRLSLRPQVPAVRRLGTGSLLLSARKFTDKHEWISVENGIGTVGISNFAQEALGDVVYCSLPEIGTKLNKDDEFGALESVKAASELYSPLTGEVTDINAALADNPGLVNKSCYQDGWLIKMTVEKPAELDELMSEDAYEKYIKSIED
Protein: Serine/threonine-protein kinase BUR1 (EC 2.7.11.22) (EC 2.7.11.23) (Bypass UAS requirement protein 1) (Suppressor of GPA1-Vall50 mutation protein 1) (P23293)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine-protein kinase component of the BUR kinase complex involved in transcription regulation. This complex phosphorylates 'Ser-120' of the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B, the localization of the PAF1 complex to the chromatin, and the silencing of telomeric-associated genes. Also required for histone H3 'Lys-4' trimethylation. May phosphorylate the 'Ser-5' of the RBP1 carboxy-terminal domain (CTD) repeats. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase. The kinase activity of the complex requires the presence of BUR2.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein BUR2
- Transcription elongation factor SPT5
- DNA-directed RNA polymerase II subunit RPB1
- CTD kinase subunit beta
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Transcription elongation factor SPT4
- Transcription elongation factor SPT6
- RNA polymerase II subunit A C-terminal domain phosphatase
- RNA polymerase-associated protein CTR9
- CTD kinase subunit gamma
Sequence:
MSDNGSPAVLPKTEFNKYKIGKVKSTPAIQRDAKTNLTYIKLRKRSSEKVYGCTVFQNHYREDEKLGQGTFGEVYKGIHLETQRQVAMKKIIVSVEKDLFPITAQREITILKRLNHKNIIKLIEMVYDHSPDITNAASSNLHKSFYMILPYMVADLSGVLHNPRINLEMCDIKNMMLQILEGLNYIHCAKFMHRDIKTANILIDHNGVLKLADFGLARLYYGCPPNLKYPGGAGSGAKYTSVVVTRWYRAPELVLGDKQYTTAVDIWGVGCVFAEFFEKKPILQGKTDIDQGHVIFKLLGTPTEEDWAVARYLPGAELTTTNYKPTLRERFGKYLSETGLDFLGQLLALDPYKRLTAMSAKHHPWFKEDPLPSEKITLPTEESHEADIKRYKEEMHQSLSQRVPTAPRGHIVEKGESPVVKNLGAIPRGPKKDDASFLPPSKNVLAKPPPSKIRELHQNPRPYHVNSGYAKTAIPPPAAPAGVNRYGPNNSSRNNRFSGNSTAPNNSRNPVNRFHPETNVSSKYNKVPLPLGPQSRYQGNSNESRYKNSPNDSRYHNPRYVNKPETNFNRQPQKYSRQESNAPINKNYNPSNGSRNMAGDHHQGSRPSHPQFPISPSQGQHQLTSKPIEKKNGSFKDERAKPDESKEFQNSDIADLY
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (Q55AZ3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Mitotic spindle assembly checkpoint protein MAD2B
- DNA helicase
- DNA-directed DNA polymerase
- BRCT domain-containing protein
- DNA primase large subunit
- DNA primase
- DNA polymerase alpha subunit B
- DNA helicase
- DNA polymerase epsilon subunit 2
- DNA polymerase epsilon subunit 3
Sequence:
MNNYNEDNNTKQQSRVYFSVRIVDIDYYQTRPVQGLDVMVSPLSSSNNNKTIEEVPIVRIFGSTPAGQKCCLHLHQLFPYFFIEYTENSLSTEYVSTYIRKLVSTLNLALNHSNNNNNNNNNNNNNNNNSNNNINSNNNNNVFLKQYIFNAKLVRGRPFYGYHSTDKIFIKIYLYNPDDINRVANLLRSGMIMSRCFRVFESHIPFILQVFLDYNLSGMSNIEFTNAYFRLPLPEKLKKWGTKEYDLSQLNLNSNISESSSSDDCIENRKWFKDSLINNNKNNNNNNNNNNIKISVVKNRKTTCELEVDAIIYDIFKFDGNNSTPQQDIDVETKLVKSLNIIWNEEALRRKQLGVDSQFTQVPDQIRKPANIGFFSKPLAIKNLQEIIKKEREQINNILIKNQQKQQQKHQQQQQQENTHTNENNNKNNNNNNNTNITMNTTTTSDEISSIPSFNDELKVHLHQQQQEIQKMDDQEFEFSQQFLSTPLSNTSFDQLDSNIKILDDYGDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNNNGKGDNMQIDNQNNMVTVLPVSKDVGGTSTEAEKSFVINGHDDDFNEKLLKDDDNNKSGDVKDVGENDDDNNNINNQDGKLGEQEQEEEQEEEKDDDDSSDNEEFNNQEFQSQREASDIIGTQSKLIDMFLNEEKDADLWALTDSDDEEQKPSPKKRSFTETLQSSNNEIPQIDGPTDKKIFKLKFVTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNSNNNNINNRFNNQTVSLPQPQPAKQLPIVKKLLAFNNNKNNNSNNNKGLKSILLNSSNKKKRNVNKSVRFLDDITIPETQVEYVPETPSSLSSLTTTTSTSNTSKIISVLKTYDNDHNDNDNYSYKPIQKDFKDSLFKLDRGQSAISISNNLDQLLASQLKEKEKEKEKEKEKEKEKEKEKEVKKKVEEEEYDDDIIFETQIPQINFTASIDCSSKIKENNFNIGLQSPPSPPPQSPPSPPPPIYNMVSPLKDTAITTTTTTTTTTSKAASKETSSVPMIVGNNQDKSIIKSLPLQPTQSSFSIGLWTPLSDSDQTTFSKTNNLSDNCPTTTSKTPNNEKGGNSNFLVPFLPIGDSPIKNNEKQLEDKKKNDNNNNNNNNNNNNNNNNNNNNKNNNNNNNKNNNKNSIINSPLSPTPPTFTLDDIIIPNKKIQPLKKPSQQPIQQQQQQQTLKIEAPYVSPNKKSAEDGNINVDISPLKPIYIHFEKSPTPPSPIKFITSPIKKPKFEEQDPKPVLSQQVKYSNSNRAFNDYFEIKEDDLEDAMDILQDFTITSKTIPYSQQQQQQQSSSSPQSLSSPQSLSSSPLISSPYSPPPPIFNYSQQHQQQTTTTKNKVNNNYQNETPPLSDVSNIQDIVFSLNSDQFSQTTINNKKNSSNEKESTKTENNIYSNDNDIDFFNGGSEGEDDDQIINIKGNKVPTTTTAMATTALATTTTTATATATTSTATTTATTTLKTVFKLSNLAPSLNDIYKELNQMNKPINIYQEPFYSNPMDIPRIPRKPVVPLQQFKSNLKEYKGINHWKRVFLPVSPFNNNNNNNQNNISNIFTLAIPPPSKLQLLNELSINMDNNHGCEKTKNKLIVTKNEKEKEKEKEKEKEKEKAKAKDNDFKFNEIKRKENYEQYFSEFSQISQHTPSPIKYVRDFSKKRLQSNQNQNLTILSVEIHCNSRDNLNPNPEFDSIQSIIYCIRDEQSIEIEGDQYQDIKGILMVNDGHYENENNSYGLNCFIKVLHNEFELFKSFVELIRSYDIDILVGFEVQMSSIGYLIERANQLGLSLCDEISRVISNTGLTGQNTTTTKGANRTKRTNYFSKDRDQYSFEHFTGMKIIGRIVLNLWRLLRHEITLDNYTYQNLCFHVLNKRQEEYSFKKLTNWYGGGGGSSNTFQQHQHQHQYQQRWRTLEYYLKKCENNFNLIYAFDLIQRTSEFSRVYGIDFNSVLSRGSQYTVESMLLRLTKPENFILLSPSREEVLSQPMPESIPLVMDPITRLYNSPVVVLDFQSLYPSIMIAYNYCYSTCLGKVQNNFKSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNQGGEEHIDDNDNSKINKKKFGASWLENKLGLLESISIEHLNISPNNVIFTDKSIRTGLFPKLLQEVLDTRIMVKRAMKKIDKGDKKMFNILNARQLGLKMMANVAFGYTAATYSGRMPCIEIGDSIVQTARETLEAAIKIVESSKEWNAKVVYGDTDSLFVLLPGVSREKAFEIGQNIANKVTSLNPSPVKLLFEKVYHPCILVNKKRYVGYKYESPSQTEPIFDAKGIETVRRDSCKVVSKILEKSIRIIFETKDISLVKSYVIRQWEKILQDRFSLSDFIFSKEVRLGTYKCQQQQNNIDDLNGLPPAALIASRLMKSDPRLEPRYGERVKYVVVYGEPNSRLIDLVLTPMEFLERSDRLRINVIYYITKQILPALDRIFKVLNVNVRQWFNDQPKQLLLTPIQRMSKYYYFHHHLKRNQQLKIQYENNNNNNNNNNDHQNTTIDQFYKTSSCLVCGSAIDRTSDEDNNNVDEQQSLSSYPICKSCGMDEQTSYFTLVSRYKYIENQKNKVNDICRSCIRDQSVETIDCISLDCSIFYQRRKLVQLFKNIEIWFKSQQQFDY
Protein: PPR8522 (I1VZH2)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MAVSSPPPPRLHLSLHLRKPIQNSPPSGKKARPAPTAETLRRRFLRRGVSPTPKILHTLRKKEALKALRRARKDTAAAATASRNPCDEEETRFRAAAAEYHALAGRPWDAGTRGMAPPRGLDGEEGGLEGLREMLAARRGDGFRWLLDDDIEAEAAERKQQRRPGAGWDVGTEDEERRIQLLVSRLNGDYLSFRDWRLTRVMKRADIIYSEDNLLRILDGLEARGNWRQALSIIEWVYNENSYRHRKSRFVYTKLLSILGKSLRATEALHIFTIMRGDAQIYPDMPAYHCIAVTLGRAGLLKELIKIIEYMRQKPSKLVMKMRRKDWDPSLEPDVLVYNSVLNACVLSQQWKGVFWVFQQMRIGGLPPTGATYGLAMEVMLKAKKYDFVQKFYEKMQKNGVPPRAITYKVLVRSFWEQDKINEAVEAVNDMEQRGVVGAASVYYELACCLCNNGRWRDAMLQVEKLKQLPLTKPLEYAFTGMILASFNGGYIYDCISIFELMKDHCMPNIGTVNVMLKVYGHCDMFGKAKDLFETTKACFLNSQTYIHEHSSFKADTYTYNSMLEASASAQQWEYFEYVYREMALSHHCLDQSKYSWLLIKACRAGKPYLLEHALDSILERGEIPDVQLITESICQSIAHRDYGRTLQLLNIMTQASIKIKEVEWDYLLQQNMHQFSIDALEGLIKYLSTNGTTNADPAVDLVRALQSQCRDDTSTQQFELSFHGSGNKYSCSSLAELDQLTCKNLCTDIILDVPGSDREMPQLGVSALMCRDISLNGQRVENKHELSDLGQRGPQVSAIDKVLDSMNSYGDNSYGEMPSASKILELWEHER
Protein: Synaptonemal complex central element protein 3 (Testis highly expressed gene 2 protein) (THEG-2) (A1L190)
Organism: Homo sapiens (Human)
Function: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears to require SYCP1. Required for fertility.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:B5KM66}. Chromosome {ECO:0000250|UniProtKB:B5KM66}. Note=Colocalizes with SYCE1 in the central elements. {ECO:0000250|UniProtKB:B5KM66}.
Interaction partners:
- Synaptonemal complex central element protein 2
- Synaptonemal complex central element protein 1
- Testis-expressed protein 12
- Synaptonemal complex protein 1
- Synaptonemal complex protein 3
- Synaptonemal complex protein 2
- Protein SIX6OS1
- Cohesin subunit SA-3
- Structural maintenance of chromosomes protein 1B
- Meiotic recombination protein REC8 homolog
Sequence:
MDDADPEERNYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFVNCKEEMEKNWQELLHETKQRL
Protein: Myosin binding subunit, isoform F (A8JNT6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFRSRSRTQAPLSSRRRSLSSSSRMAPSSGGSGAYNYNGSSYSSSGSTGRPLSTGYFPSSSSASSYQSPYASVYSSRESLYGGGGAGRSSYGSGGGGYDSSRYNPSSYSSAGSSYSTSDRYVSPYSSSYDKGVTTASLTFKSPGLSSSNSFKSSRLLKTKSLSASNSSLNGAYGGPSSNGVTSAGATVAAIAATRSNSLREQERKSRNRTRSKSAAQRSISASSEKSEGYESGSERTSRSRLGSTASTATTSESKSSSSNDKTENGDGIDYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFANATTKNSLSELEKRERRAMERKLSELEEELKQLDAYKSDNHRLKEENAALIRVISKLSK
Protein: Flagellar assembly protein FliX (O32348)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: Required in an early step of flagellar assembly.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
- Transcriptional regulatory protein FlbD
- Chemotactic signal-response protein CheL
- Flagellum biosynthesis repressor protein FlbT
- Magnesium transporter MgtE intracellular domain-containing protein
- FliN family protein
- Endoglucanase
- DUF2336 domain-containing protein
- Flagellar hook-basal body complex protein FliE
- DUF2336 domain-containing protein
- Hpt domain-containing protein
Sequence:
MKVSSTGGVSATGASRAKPAGGSSGFSLPSVNAASGAASTASVGGLTGVGSVDALLALQAAGSVGGPLERRKRAVRRADNILDILGEVRIALIDGDISHATLDRLSRAIREQREATDDPRLEGVLNEIETRAAVELAKLQARAG
Protein: Atypical kinase COQ8A, mitochondrial (EC 2.7.-.-) (Chaperone activity of bc1 complex-like) (Chaperone-ABC1-like) (Coenzyme Q protein 8A) (aarF domain-containing protein kinase 3) (Q8NI60)
Organism: Homo sapiens (Human)
Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates. Shows an unusual selectivity for binding ADP over ATP.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:11888884, ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:33988507}; Single-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:25216398}.
Interaction partners:
- Ubiquinone biosynthesis protein COQ9
- All trans-polyprenyl-diphosphate synthase PDSS1
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS2
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Aprataxin
Sequence:
MAAILGDTIMVAKGLVKLTQAAVETHLQHLGIGGELIMAARALQSTAVEQIGMFLGKVQGQDKHEEYFAENFGGPEGEFHFSVPHAAGASTDFSSASAPDQSAPPSLGHAHSEGPAPAYVASGPFREAGFPGQASSPLGRANGRLFANPRDSFSAMGFQRRFFHQDQSPVGGLTAEDIEKARQAKARPENKQHKQTLSEHARERKVPVTRIGRLANFGGLAVGLGFGALAEVAKKSLRSEDPSGKKAVLGSSPFLSEANAERIVRTLCKVRGAALKLGQMLSIQDDAFINPHLAKIFERVRQSADFMPLKQMMKTLNNDLGPNWRDKLEYFEERPFAAASIGQVHLARMKGGREVAMKIQYPGVAQSINSDVNNLMAVLNMSNMLPEGLFPEHLIDVLRRELALECDYQREAACARKFRDLLKGHPFFYVPEIVDELCSPHVLTTELVSGFPLDQAEGLSQEIRNEICYNILVLCLRELFEFHFMQTDPNWSNFFYDPQQHKVALLDFGATREYDRSFTDLYIQIIRAAADRDRETVRAKSIEMKFLTGYEVKVMEDAHLDAILILGEAFASDEPFDFGTQSTTEKIHNLIPVMLRHRLVPPPEETYSLHRKMGGSFLICSKLKARFPCKAMFEEAYSNYCKRQAQQ
Protein: Sodium/myo-inositol cotransporter 2 (Na(+)/myo-inositol cotransporter 2) (Sodium-dependent glucose cotransporter) (Sodium/glucose cotransporter KST1) (Sodium/myo-inositol transporter 2) (SMIT2) (Solute carrier family 5 member 11) (Q8WWX8)
Organism: Homo sapiens (Human)
Function: Involved in the sodium-dependent cotransport of myo-inositol (MI) with a Na(+):MI stoichiometry of 2:1. Exclusively responsible for apical MI transport and absorption in intestine (By similarity). Can also transport D-chiro-inositol (DCI) but not L-fucose. Exhibits stereospecific cotransport of both D-glucose and D-xylose (By similarity). May induce apoptosis through the TNF-alpha, PDCD1 pathway. May play a role in the regulation of MI concentration in serum, involving reabsorption in at least the proximal tubule of the kidney (By similarity).
Subcellular location: Membrane {ECO:0000305|PubMed:19032932}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Z1F2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z1F2}. Note=Located on apical membrane of enterocytes (By similarity). Located on membrane of kidney brush border membrane vesicles (BBMVs) and apical membrane of proximal convoluted tubules (By similarity). {ECO:0000250|UniProtKB:Q28728, ECO:0000250|UniProtKB:Q9Z1F2}.
Interaction partners:
Sequence:
MESGTSSPQPPQLDPLDAFPQKGLEPGDIAVLVLYFLFVLAVGLWSTVKTKRDTVKGYFLAGGDMVWWPVGASLFASNVGSGHFIGLAGSGAATGISVSAYELNGLFSVLMLAWIFLPIYIAGQVTTMPEYLRKRFGGIRIPIILAVLYLFIYIFTKISVDMYAGAIFIQQSLHLDLYLAIVGLLAITAVYTVAGGLAAVIYTDALQTLIMLIGALTLMGYSFAAVGGMEGLKEKYFLALASNRSENSSCGLPREDAFHIFRDPLTSDLPWPGVLFGMSIPSLWYWCTDQVIVQRTLAAKNLSHAKGGALMAAYLKVLPLFIMVFPGMVSRILFPDQVACADPEICQKICSNPSGCSDIAYPKLVLELLPTGLRGLMMAVMVAALMSSLTSIFNSASTIFTMDLWNHLRPRASEKELMIVGRVFVLLLVLVSILWIPVVQASQGGQLFIYIQSISSYLQPPVAVVFIMGCFWKRTNEKGAFWGLISGLLLGLVRLVLDFIYVQPRCDQPDERPVLVKSIHYLYFSMILSTVTLITVSTVSWFTEPPSKEMVSHLTWFTRHDPVVQKEQAPPAAPLSLTLSQNGMPEASSSSSVQFEMVQENTSKTHSCDMTPKQSKVVKAILWLCGIQEKGKEELPARAEAIIVSLEENPLVKTLLDVNLIFCVSCAIFIWGYFA
Protein: ferric-chelate reductase (NADPH) (EC 1.16.1.9) (Q59PA1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- High-affinity iron permease
- Ferroxidase
Sequence:
MVAINSLLFAAITLVSSAQATDTLTIYHNNKFAVQACKGLIGKTAVLFNETTDKAGFCNVKNQQALGTMAECIELMPHKDSRKEFLKTCKKFNLTEEDYLAAWKNATEFGYVNVTADPDFKKKKLYYKPVLLKKKKVEAAWDAVATRWYNYNYAQWYGIALFSYWFAVMFVAGICNLTYFLFPGFVKSLKGGISNAFRKYITLPALFKKTHAHHKSIFGVFHAILPTRLESILVVAWFIMALIMNLTNYVHVKPNYIWPQKSNELGRKIADRTGQISMWLMPPLVLFAGRNNFMQWVSGWPYARFVYIHKWISRVVFMMSIAHGVGMTYNGKGIGKYYTRNAKPYVRWGYVALVAMSIMVFQGFSYFRRTNYEVFVGVHIILAVFAIAGTWIHTTEQGYQMWMYGAVAVWVFDRVVRIARLATFGLRSATVQLIANETVKVTVSRPGWWKPFPGCHAFIHFMRPTCFWQSHPFTIVDSVTESNTITFYIKVKGGMTHGLYQYLAQQPAQTAQIKVSIEGPYGNRMAIDRFENDVFIAGGNGIPGIYYEATDIAKRLGEKRNVKLYWVVRHYRSLEWFYQELLKLKDLPISTTVYVTQPNVGLADPITTDLTDDEEQQEHEQEKKSDTEESNDYVAQVKKNLSFIQFIETKPDFYQIVGEEIKQSTGPIAFASCAHGNMVDDVRKSVVDNLSNSNHRVELFEQMQNW
Protein: EG:EG0003.6 protein (O96829)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPSPHEKDANKAAETAAKENAADKVSDVENASVTAGVAKAVGAQPERGSKDAAESPAAVDASASAATDDVADKKAKGDSTAVSNTESDAADKKEKSPSPVIKKSNNKDAKKEDNSEKDEENSEDGDEPEDEADEKASDEESEKKKPKLDAEDKIKDATDESKPKSGADKPKKPEPKAKNGKVAKEEDDDEEDEDDEDAEDDDGDENDGLDKNNEVAEDDENVVALAEIDRINENINKTRVDGLQTLHAICFGAQGKNNVVKKNLRSFAGFEFAKDSAEYNKKLEAIKKVDNKGLRSICEILTLDRKGSKNETVLRVLKFLMEPDESLCLEQGDEEEEEDAEDEDLDEDEEDPPSEEDKKRKSGKSSGGAGRGSARNSTGRPRRATAGKKMSAYVDFSSSDDSEQKVAVPKRRRNDDSESGSDVSILRPETMRTIWLICRFAYSTILLPIPTLTVVVVVVLVQQVAKSQAAVDAVVLRAKVAEETLIPRKKRNRKFPMPIVMSQNVNVVPWVNVDDRQLLRQLDEGVEDEVQLPASVKIQIAKMRRYPRMKRRRMSPILPAIKAKYEERPKKSKKPITPAKNSKANNKSKPAGKADSRSKKSKKESSEEDDDVDDKDESDEDEPLTKKGKQAFPTVGSQ
Protein: Inositol phosphatase interacting protein, isoform A (Inositol phosphatase interacting protein, isoform B) (Inositol phosphatase interacting protein, isoform D) (Q9VMI6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- EG:86E4.5 protein
- ADP-ribosylation factor 1
Sequence:
MKINEKNLYVFARTPPFDMEGFLNKRGEVNKAFQRRYFVLKGNLLFYFESRLDKEPLGLIIVEGCTIELSNEVDNYCFEIAFNGNRTYILAAENQDSMETWMKALTCAGYEYKRIILAELKRQLQEMEDARNKMLGSALDGPQNASESAKPRPPPRRTNPFNRPAPPPPDSSLRGGVVMSPLPFINGYFGSSNARLQQEKLMSKQDANGNGSPSGTPRAQRRPTPAPAIANSVFYPDVRDPGAANNNHSTVNGAERQRRQVKALEEFARNHERFRRELMPDVSAYRERQGQPLIQL
Protein: Small ribosomal subunit protein mS25 (28S ribosomal protein S25, mitochondrial) (MRP-S25) (S25mt) (Q9D125)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P82669}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS7m
Sequence:
MPMKGRFPIRRTLQYLGRGDVVFKESVKIMTVNYNTYGELGEGARKFVFFNIPQIQYKNPWVQIMMFKNMTPSPFLRFYLDSGEQVLVDVETKSNKEIMEHIKKILGKKEETLREEELEKQQRFHPGNFGPRKYCLRECMCEVEGQVPCPGLVPLPKEMTGKYKAALKAST
Protein: D-dopachrome decarboxylase-like protein (EC 4.1.1.-) (D-dopachrome tautomerase-like protein) (A6NHG4)
Organism: Homo sapiens (Human)
Function: May have lyase activity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MPFLELDTNLPANRVPAGLEKRLCAAAASILGKPADRVNVTVRPGLAMALSGSTEPCAQLSISSIGVVGTAEDNRSHSAHFFEFLTKELALGQDRFPTVLSTSPAAHGGPRCPGEIIEGKKSCLNEEALFIYFI
Protein: Transmembrane protein 106A (Q96A25)
Organism: Homo sapiens (Human)
Function: Activates macrophages and polarizes them into M1-like macrophages through the activation of the MAPK and NF-kappaB signaling pathway. Upon activation, up-regulates the expression of CD80, CD86, CD69 and MHC II on macrophages, and induces the release of pro-inflammatory cytokines such as TNF, IL1B, IL6, CCL2 and nitric oxide (By similarity). May play a role in inhibition of proliferation and migration.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8VC04}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGKTFSQLGSWREDENKSILSSKPAIGSKAVNYSSTGSSKSFCSCVPCEGTADASFVTCPTCQGSGKIPQELEKQLVALIPYGDQRLKPKHTKLFVFLAVLICLVTSSFIVFFLFPRSVIVQPAGLNSSTVAFDEADIYLNITNILNISNGNYYPIMVTQLTLEVLHLSLVVGQVSNNLLLHIGPLASEQMFYAVATKIRDENTYKICTWLEIKVHHVLLHIQGTLTCSYLSHSEQLVFQSYEYVDCRGNASVPHQLTPHPP
Protein: Reversion-inducing cysteine-rich protein with Kazal motifs (A0A0R4IKU3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Functions together with adgra2 to enable brain endothelial cells to selectively respond to Wnt7 signals (wnt7a or wnt7b). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. Adgra2 is then required to deliver reck-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26051822, ECO:0000269|PubMed:27979830}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:A0A1D5PUP4}. Note=Colocalizes with adgra2 at the plasma membrane. {ECO:0000269|PubMed:26051822}.
Interaction partners:
- Adhesion G protein-coupled receptor A2
- Tetraspanin
Sequence:
MSGCLQILTVLLCCRFWALVFSQDQSCCVHHAADIPRCRDACEQLASIRSESRLRHLLHRLPSYCPETLSELWICINNSLPGASRKSDGWVGLGCCELAISAECRRDCKQASSKNDISKVCKKDTENPLYSCITKNEMGSVCCSYAGRHTTCREYCQAIFRTDSSPTVSQISAVKEYCQSVSPPLILCVENYTRLHPTHRPIDSLHCCDRAEEAHCQLACKRILRTLSTEQEIMDGLISECGSQPLPQDPLWQCFLGSAHPPANTDPESPPIAKMDSAKLHCCFKANTSICRNMCVEISTSWGTQSWQEFDQHCEYNPVEMDLITCLADVREPCQLGCKELSYCTNFNNRPTELFRSCNVQSDQGALNDFKLWSNGSIRMPLMNIPVLDIRRCRPEMWKTVACALQIKPCYSRSRGSVICRSDCVEILRQCGDRRRFAEAQTPERICDLLSPTDDPERCIPLNRYLTASELESSVEEVIHPCNPNPCPSSHLCHVNRKGCHVGHDCLPYYCVPGCKLGEASEFLVPADARLQVPVHSAQPGCYEVCVCGQSGRLENCAEMPCFDTSKSCQIAGQRRSHGSSFRVDCNPCSCFAGDAVCSSRQCVRSDSSEEDRRLFTGLPCGCADHFVPVCAGNGRTYPSACVARCVGFTDSQFVFGSCRSFDPCSPNPCQRNQRCVPRRQVCLTDLSEFPCPQYECVSRPSSCDQKLLDPVCDTDNMEHANLCVLNLRGKTLAYSGHCQDACRRPREVCAHNGESYSTVCEAFSERVAVDYQGRCHAVGLESEFGSDSGCNAVPCPPLASDACQPVTPPGACCPVCAGMLRILWNKAQMNIFAKLNRDQPVSLHDILKILRLHVSVPQCDIFGYLSINSEIIILIAPVDQQPTPLQIEACSKEAEKIDSLINSGSPTLVSHVPLSAFLSSELQLSSVRSSSCVSISVCVLLLLCSLILTLTSDL