wanglab/gogpt-training-data huggingface dataset:
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q585R9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Flavoprotein monooxygenase, putative
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Uncharacterized protein
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- Adrenodoxin reductase, putative
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 8
- Uncharacterized protein
- Complex 1 LYR protein domain-containing protein
- Uncharacterized protein
Sequence:
MLSRTFFAAQRKIPFYPVNPSNPLVYFDISIGSQKAGRVEMELFKDVVPKTAENFRALCTGEKGLGRSGKALSYKGSKFHRVIPQFMCQGGDFTSGNGTGGESIYGLKFPDESFAGRAGKHFGPGTLSMANAGRNTNGSQFFICTAATPWLDGKHVVFGQVTKGYEVIEKVETNGSQSGATRQPITIMDCGQIEQG
Protein: Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser) synthetase) (Q9UTB2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable glutamine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Probable proline--tRNA ligase, mitochondrial
- Putative proline--tRNA ligase C19C7.06
- Tryptophan--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, mitochondrial
- Probable cysteine--tRNA ligase
- Probable asparagine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Putative leucine--tRNA ligase, cytoplasmic
Sequence:
MRLTNRRFSTFLGNALPSKKKGFIFMSQLLYLRTFSTHTSYLRSSWQAILNYKYIYQNAEAVQRNCINRNLQAIAETVPKIRSLIDEKESLKNEFFPLLSLKKEITLQIERCSDPNERGKLVNEAKGLKKKTEEYNKIISKVTNDLYQYCLAVPNTTLPTVPVGPEDKAVVVQKIGSPLVKKTGSLKDHLQIANEGINLEDAAQASGHSFCYTTGDIALLEMAITNYAMDFAISKGWCPVIPPTIVRTDIALACGFQPRDEEGQQIYELDSYTSPLVSSPKQCLIGTAEISLAALGFKKTFNNFTERKVVGVSRAYRREAGARGKENRGLYRLHEFTKVELFAWTHPSRSSEMFNEIVNFQKEFVETLKIPARILNMPTAELGSSASQKYDIEAWMPARQSYGEITSASNCLEYQARRLLTRYRNDKDSGFVHTLNGTAAAIPRLIIAILENHQQEDGTVKVPETLVPYIHKEYLFKAK
Protein: 9130008F23Rik protein (RIKEN cDNA 9130008F23 gene) (Q9D2Z6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNYLPSGMELGRPQGRSECSPRREGCGPPLDSGSPNPALAEAGSAQSIASGNLRKQKGKNLDCQSWVREKVLFLLHPERWLGTQADSACAGLVDSENLPPTIGDHYDSKRKPKLSRRRIATAPGAQPEDPENTPRSLLVRVVDYQVTQEVLWTAWTKGSMTTRTEERSVTAVTFRTQRERE
Protein: Ribulose bisphosphate carboxylase large chain (RuBisCO large subunit) (EC 4.1.1.39) (O03042)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (Probable). Binds to abscisic acid (ABA).
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:12766230}.
Interaction partners:
- Ribulose bisphosphate carboxylase small subunit 1B, chloroplastic
- Ribulose bisphosphate carboxylase small subunit 1A, chloroplastic
- Photosystem II protein D1
- Ribulose bisphosphate carboxylase small subunit 3B, chloroplastic
- Ribulose bisphosphate carboxylase small subunit 2B, chloroplastic
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic
- Photosystem II CP47 reaction center protein
- Phosphoribulokinase, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Maturase K
Sequence:
MSPQTETKASVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEETQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALAALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGDRESTLGFVDLLRDDYVEKDRSRGIFFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAVEGNEIIREACKWSPELAAACEVWKEITFNFPTIDKLDGQE
Protein: Alpha-protein kinase 1 (EC 2.7.11.1) (Q9CXB8)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase that detects bacterial pathogen-associated molecular pattern metabolites (PAMPs) and initiates an innate immune response, a critical step for pathogen elimination and engagement of adaptive immunity (By similarity). Specifically recognizes and binds ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria. ADP-Heptose-binding stimulates its kinase activity to phosphorylate and activate TIFA, triggering pro-inflammatory NF-kappa-B signaling (By similarity). May be involved in monosodium urate monohydrate (MSU)-induced inflammation by mediating phosphorylation of unconventional myosin MYO9A (By similarity). May also play a role in apical protein transport by mediating phosphorylation of unconventional myosin MYO1A (By similarity). May play a role in ciliogenesis (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96QP1}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96QP1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96QP1}. Cell projection, cilium {ECO:0000269|PubMed:30967659}. Note=Localized to the basal body region of the photoreceptor cilium and the region of the adjacent centriole. {ECO:0000269|PubMed:30967659}.
Interaction partners:
- TRAF-interacting protein with FHA domain-containing protein A
Sequence:
MNNQDAVASILHECKQVLDRLLLETPDVSTEDKSEDQRCRASLPSELRTLIQEAEEMKWPFVPEKWQYKQAMSPEDKTNLQDVIGAGLQQLLAALRASILVQDCAAASAIVFLMDRFLYGLDVSGKLLQVAKGLHKLKPATPIAPQVVIRQARVSVNSGKLLKAEYILSSLISNNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEAAELIWASVIGYLTLPQPDKKGISTSLGILADIFVSMSKTDYEKFKKSPKVNLALLKEFDHHLLSAAEACKLAAAFSAYTPLFVLRAVNIRGTCLLSYSCSADCPPGMKSVHLCEAKEAFEIGLLTKKDGELVSGKQELHSFIKAAFGLTTVHSRLHGETDAVRAARQLCSEAVGKLYTFSTSPTSQDREGLSQEIMSLISQVKGHLRVQSFPNLDVCSYVPESFKCGLDRLILHGHVDFQQILETYSQHHTSVCEVFESTCGNSKSNQRDTKSEVCITTLKTETNTADTMVATLERVSSQDSRSTASSKMSKKDQGKLQRERGRSWTRSKAFRVSLDLDMETETEPPNHSNGGTDVFNKSLRDNSSSCSWGRLSGLSSSTSWEEVNCAVQDVVRKGSGQEKHPVEAQSSEAVSEEPKRNRSSRAVFLSSKLRGVSLQTTGDDNLESSPSQLHNHTSILPFNAKDTCLASGAGLVETAEGSNNTSLQSSHSCGSDSWSLSSSDRFTDVTTNPSVQEEEPSGIMGDVPESKYDFKDWHGEKNGGTLTEICTGPELTFAPSSVDPEGETAESTDDGLSPSQVALGCLEGSHSMSTRRTFFPDGSVQNADSAKTGCSVRDQTVDPDASTVDEEGQMLDSTEVCSIGQDGAHRPRALRSGQSAEGPKSFVNGSRPSPIFDEDFSTTEEGEELGSMLKSSQNSSSYSPWWLKSPAFSRSSSDGESSWSLLNSSRSSFASLAGQTSQEILEARTLQPDDLEKLLAGVRHDWLLQRLENTGVLKSNQLQQAHSALLLKYSKKSELWTAQETVVYLGDYLKVKKKGKQRNAFWVHYLHQEETLGRYVGKEYKERKGLRHHFTDVERQMTAQHYVTEFNKRLYEQKIPTQIFYVPSTILLILEDRTIKGCISVEPYILGEFVKLSNNTKVVKNEYKATEYGLAYGHFSYEFSNHRDVVVDLQGWVTGNGKGLIYLTDPQIHSVDQKDVTTNFGKRGIFYFFNNQHASCNEICHRLSLTRPSLEQTSKV
Protein: LIM domain-containing protein unc-97 (PINCH homolog) (Uncoordinated protein 97) (P50464)
Organism: Caenorhabditis elegans
Function: Component of an integrin containing attachment complex, which is required for muscle development and maintenance. Probably function in adherens junction. Affects the structural integrity of the integrin containing muscle adherens junctions and contributes to the mechanosensory functions of touch neurons.
Subcellular location: Cell junction, adherens junction. Nucleus.
Interaction partners:
- Integrin-linked protein kinase homolog pat-4
- Ras suppressor protein 1
- Paralyzed arrest at two-fold protein 6
- Protein unc-112
- Zinc finger protein unc-98
- Vinculin
- FERM domain-containing protein
- CRE-UNC-96 protein
- LIM domain-containing protein unc-95
- Integrin beta pat-3
Sequence:
MDSDHNHINGDLAHGFENMVCVRCNDGFSMQDQMVNSSGQVWHSECFVCAQCFEPFPDGIYFEYEGRKYCEHDFHVLFSPCCGKCNEFIVGRVIKAMNASWHPGCFCCEICNKQLADVGFLRNAGRALCRECNEREKAAGHGRYVCHKCHAMIDDGQHIKFRGDSFHPYHFKCKRCNNELTTASREVNGELYCLRCHDTMGIPICGACHRPIEERVIAALGKHWHVEHFVCSVCEKPFLGHRHYERKGLPYCEQHFHKLFGNLCFKCGDPCCGEVFQALQKTWCVKCFSCSFCDKKLDQKTKFYEFDMKPTCKRCYDRFPTELKKRISESLKDRDVENQRRSMSPGPK
Protein: Coiled-coil domain-containing protein 85C (E9Q6B2)
Organism: Mus musculus (Mouse)
Function: May play a role in cell-cell adhesion and epithelium development through its interaction with proteins of the beta-catenin family (By similarity). May play an important role in cortical development, especially in the maintenance of radial glia.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:22056358}. Cell junction, adherens junction {ECO:0000250|UniProtKB:A6NKD9}. Note=Localizes to the apical junction of radial glia in the wall of lateral ventricles of the developing brain. Colocalizes with TJP1 on the meshwork-like structure of adherens junctions on the lateral ventricles wall. {ECO:0000269|PubMed:22056358}.
Interaction partners:
- Rho GTPase-activating protein 23
Sequence:
MAKPPAVAAAAAAAASEELSQVPDEELLRWSKEELARRLRRAEGEKVGLMLEHGGLMRDVNRRLQQHLLEIRGLKDVNQRLQDDNQELRELCCFLDDDRQKGRKLAREWQRFGRHAAGAVWHEVARSQQKLRELEARQEALLRENLELKELVLLLDEERAALAAAGGAGGGGGGAGSRSSIDSQASLSGPLAGSAAGSGARDVGDGSSTSSAGSGGSPDHHHHVPAALLPPGPHKVPDGKAGATRRSLDDLSAPPHHRSIPNGLHDPSSTYIRPLETKVKLLDGDKLPPQQAGSGEFRTLRKGFSPYHSESQLASLPPSYQEVLQNGPACPVPELPSPPSTVYSSAGQKPEAVVHAMKVLEVHENLDRQLQDSCEEDLSEKEKAIVREMCNVVWRKLGDAASTKPSIRQHLSGNQFKGPL
Protein: Mitochondrial thiamine pyrophosphate carrier 1 (A0A1D8PQ62)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MSKPQTKIQYPFWYGGAASMAACLVTHPLDLAKVRLQTATKPGQSLLSMIYQIITKEGVFKIYSGLTASLLRQATYSTTRFGIYEFLKEQYMESIATTGGTEQKKPSTAVLLPMSMIAGALGGLVGNPSDVVNIRMQNDSTLPINQRRNYRNAFDGIYKICQQEGINSLFRGLTPNLIRGVLMTASQVVTYDIAKSILVDHIHMDPSKKSTHFSASLIAGLVATTVCSPADVVKTRIMNSKGSTGGGSGGDGVNGNAISILKNAVKHEGIGFMFRGWLPSFIRLGPHTIVTFLVLEQLRKFKLGMSRSD
Protein: Protein cappuccino (Q24120)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as an actin nucleation factor and promotes assembly of actin filaments together with spir. May play a role in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000269|PubMed:21730168}; Peripheral membrane protein {ECO:0000269|PubMed:21730168}; Cytoplasmic side {ECO:0000269|PubMed:21730168}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to membranes via its interaction with spir.
Interaction partners:
- Protein spire
- Profilin
- WASH complex subunit 1
- Dynamin associated protein 160, isoform D
- DNA-binding protein K10
- Cdc42 homolog
- Ras-like GTP-binding protein Rho1
- Dynamin
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- GH06923p
Sequence:
MALQLGKKLAQVLGSGAGSPLTPGTMEPCAAGSGSPLANGELFNVSKAKKVELQNLSSRFTAAVTQTPPGVTSSTPNESGVTGPAGPLGATTSSPSLETQSTVIISFKSSQTPVQSQTNSAASENVEDDTAPLPLPPPPPGFGTPTTPLLSSNVLKKVASFTVEKSSAGNNSSNPPNLCPTSDETTLLATPCSSSLTVATLPPEIAVGAAAGGVAGGAGSRRGSSYVPEKLSFAAYEKFEGQMLIKWLISTMQSNPKSSSGDANQELFNTLALQFCNNLKYVGVLKQISNEHLDCGFSPYEMYQWTHTEQPTTSLPLTPGKLDKVAAWPFSSTPSGIRALESASLASLGAGGVAGSLATIATASTASSDNQKTLQQILKKRLLNCTTLAEVHAVVNELLSSVDEPPRRPSKRCVNLTELLNASEATVYEYNKTGAEGCVKSFTDAETQTESEDCEGTCKCGQSSTKVSDNESAKEDGEKPHAVAPPPPPPPPPLHAFVAPPPPPPPPPPPPPPLANYGAPPPPPPPPPGSGSAPPPPPPAPIEGGGGIPPPPPPMSASPSKTTISPAPLPDPAEGNWFHRTNTMRKSAVNPPKPMRPLYWTRIVTSAPPAPRPPSVANSTDSTENSGSSPDEPPAANGADAPPTAPPATKEIWTEIEETPLDNIDEFTELFSRQAIAPVSKPKELKVKRAKSIKVLDPERSRNVGIIWRSLHVPSSEIEHAIYHIDTSVVSLEALQHMSNIQATEDELQRIKEAAGGDIPLDHPEQFLLDISLISMASERISCIVFQAEFEESVTLLFRKLETVSQLSQQLIESEDLKLVFSIILTLGNYMNGGNRQRGQADGFNLDILGKLKDVKSKESHTTLLHFIVRTYIAQRRKEGVHPLEIRLPIPEPADVERAAQMDFEEVQQQIFDLNKKFLGCKRTTAKVLAASRPEIMEPFKSKMEEFVEGADKSMAKLHQSLDECRDLFLETMRFYHFSPKACTLTLAQCTPDQFFEYWTNFTNDFKDIWKKEITSLLNELMKKSKQAQIESRRNVSTKVEKSGRISLKERMLMRRSKN
Protein: Sulfate transporter (Diastrophic dysplasia protein) (Solute carrier family 26 member 2) (P50443)
Organism: Homo sapiens (Human)
Function: Sulfate transporter. May play a role in endochondral bone formation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15294877, ECO:0000269|PubMed:7923357}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O70531}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Solute carrier family 13 member 1
- Matrilin-3
- Solute carrier family 13 member 4
- Collagen alpha-2
- Solute carrier family 13 member 2
- Collagen alpha-1
- Collagen alpha-3
- Thyroid receptor-interacting protein 11
Sequence:
MSSESKEQHNVSPRDSAEGNDSYPSGIHLELQRESSTDFKQFETNDQCRPYHRILIERQEKSDTNFKEFVIKKLQKNCQCSPAKAKNMILGFLPVLQWLPKYDLKKNILGDVMSGLIVGILLVPQSIAYSLLAGQEPVYGLYTSFFASIIYFLLGTSRHISVGIFGVLCLMIGETVDRELQKAGYDNAHSAPSLGMVSNGSTLLNHTSDRICDKSCYAIMVGSTVTFIAGVYQVAMGFFQVGFVSVYLSDALLSGFVTGASFTILTSQAKYLLGLNLPRTNGVGSLITTWIHVFRNIHKTNLCDLITSLLCLLVLLPTKELNEHFKSKLKAPIPIELVVVVAATLASHFGKLHENYNSSIAGHIPTGFMPPKVPEWNLIPSVAVDAIAISIIGFAITVSLSEMFAKKHGYTVKANQEMYAIGFCNIIPSFFHCFTTSAALAKTLVKESTGCHTQLSGVVTALVLLLVLLVIAPLFYSLQKSVLGVITIVNLRGALRKFRDLPKMWSISRMDTVIWFVTMLSSALLSTEIGLLVGVCFSIFCVILRTQKPKSSLLGLVEESEVFESVSAYKNLQIKPGIKIFRFVAPLYYINKECFKSALYKQTVNPILIKVAWKKAAKRKIKEKVVTLGGIQDEMSVQLSHDPLELHTIVIDCSAIQFLDTAGIHTLKEVRRDYEAIGIQVLLAQCNPTVRDSLTNGEYCKKEEENLLFYSVYEAMAFAEVSKNQKGVCVPNGLSLSSD
Protein: Quinidine resistance protein 3 (Acids quinidine resistance protein 2) (P38227)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Multidrug resistance transporter involved in resistance and adaptation to quinidine and to the herbicide barban (4-chloro-2-butynyl [3-chlorophenyl] carbamate).
Subcellular location: Cell membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15649438}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15649438}.
Interaction partners:
- Azole resistance protein 1
Sequence:
MQAQGSQSNVGSLRSNCSDNSLPNNHVMMHCDESSGSPHSEHNDYSYEKTNLESTASNSREHRDNQLSRLKSEEYVVPKNQRRGLLPQLAIIPEFKDARDYPPMMKKMIVFLIAFSSMMGPMGTSIIFPAINSITTEFKTSVIMVNVSIGVYLLSLGVFPLWWSSLSELEGRRTTYITSFALLFAFNIGSALAPDINSFIALRMLCGAASASVQSVGAGTVADLYISEDRGKNLSYYYLGPLLAPLLSPIFGSLLVNRWPWRSTQWFMVILSGCNVILLTVLLPETLRKQDSKGAIAQILAERRIQVDNNERGEIQEDYQRGEDETDRIENQVATLSTEKHNYVGEVRDQDSLDLESHSSPNTYDGRAGETQLQRIYTEASRSLYEYQLDDSGIDATTAQVTRIRSTDPKLARSIRENSLRKLQTNLEEQVKKVLSSNGGEIAPKQVSAVRKVWDTFFVYFIKPLKSLHFLEYPPVALAITFSAISFSTVYFVNMTVEYKYSRPPYNFKPLYIGLLYIPNSVTYFFASIYGGRWVDMLLKRYKEKYGILAPEARISWNVVTSVISFPIALLIFGWCLDKKCHWVTPLIGTALFGYAAMMTIGATLSYLVDSLPGKGATGVALNNLIRQILAATAVFVTTPMLNGMGTGWAFTMLAFIVLGASSVLIILKKHGDYWRENYDLQKLYDKID
Protein: Solute carrier family 22 member 7b.1 (Zgc:63958) (Q7T3D2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKFENLLAEVGGFGKYQFCLMALLVIPRVTLPCHFLLNNFIAAIPSHHCDISSLSADGIFGNLTQEERLTVGVPAQEDGTPVSCHMFSHPQFQLLINSSSSSDLPVVECQNGWRFDNSTFKSTLATEFDLVCDRRGLNKATATIFFAGVMIGAAIFGWLTDRFGRKRMLMLAYLISITFGVASAFAQSFIVFAIMRFFTGMGLTGISIISIVLCIEWADIAHRTIAGVMISLDWSLSCMILSGVAYLVNDWRALILTVTAPIALAMITWRWLPESARWLIANGKLEEAHFYLSKCASVNNRQHNLRDIKPETLANVIIADRGDRTYSYLDLVRSSKMRKLAMLTGITWFGVAFTYYGISFNISGFGLNLYLTQFIYGAIELPSKLVAYVCLDKLGRRYSQVGTMITTGVCIGITVLIPRVLWVPRTVIAVLGKGFSEASFTCVFLYTTELYPTVLRQNGLGYSSFIGRVGVSLAPLVSLLDEVWLPLPQVLFCSVAIVAGLLALLLPETHNVRLPETIEDIEKTRKRSMCSQLEYQPGLEAFKETK
Protein: MINDIN1 (Spondin 2a, extracellular matrix protein) (Spondin-2a precursor) (O42111)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Integrin alpha FG-GAP repeat-containing 2
- Adenosine A2a receptor b.
Sequence:
MMSSEILVPGWLQQLLVVLLRFTLSCAALVNSTNGTECSARGPASYIVVFTGHWSPQTFPKQYPLFRPPAQWSKLMVVTHNEQYRLWQEGAPASDGMKSFAEQGLTVDLVKDAKEARKRRSVGSMYRTAGIPSGIGHSSTEVLLTPRSPLVSLIVKLIPSPDWFVGVDGLNLCEGGKWKQEVTFDLHPFDAGTDSGFTFSSPNFPTTPPENITMITSQKPNHPANSFYYPRLNELPPLATIWVKRQSRLPVRQQNRLSNHILPDASKPHRFSETPLDCEVSMWSSWGLCFGPCARGGLRHRTRYILLKPANSGSPCPELEEQEECTPHNCLADQ
Protein: Chromosome partition protein Smc (Q9X0R4)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
Interaction partners:
Sequence:
MRLKKLYLKGFKSFGRPSLIGFSDRVTAIVGPNGSGKSNIIDAIKWVFGEQSKKELRASEKFDMIFAGSENLPPAGSAYVELVFEENGEEITVARELKRTGENTYYLNGSPVRLKDIRDRFAGTGLGVDFYSIVGQGQIDRIVNASPEELRLLLEEAAGVSIYREKKKETELNLERTKANLDRVKDVLFERERQMKSLYLKAKRAERFKEYTAQLEELQKIYYGNVLKRERKKLEFYQEEEKKTNEKIKNIQKELVELETKWSTLRSEFGEMDQEIERYTKLLEDYKKRQNDLVEMKGFYSSKLADSENKYVELSTRLDELEKRREEYKKRLEEMEYIFKGVMGDYERKAKELEKFEKEKENLLSRFNDKEKEFLRVRDEISKLEKQILKLENELLRIGETLEDLEKRRKITENQILTRRRELEDKKNEFKEISRRVEELDEEEKKLTEELNAVRERLEEIEGEIRRVNLEIDAKEKRLREIQFEKEMIERDMREYRGFSRAVRAVFEEKERFPGLVDVVSNLIEVDEKYSLAVSVLLGGTAQNIVVRNVDTAKAIVEFLKQNEAGRVTILPLDLIDGSFNRISGLENERGFVGYAVDLVKFPSDLEVLGGFLFGNSVVVETLDDAIRMKKKYRLNTRIATLDGELISGRGAITGGREERSSNVFERRIKLKHLEQEMEETERQIAEKRDELASLKTEQENLKNQEALVQRELFELSRKSSSTKTVLSEILRSINQLQEEVENLEKLLVEYRAKEEGLNARREKIFEEIDELKQNRENLQRSLTEYSEELEKEKKILDELNEKIFTLRAEVGNLLETKDRYEKEMRDTGKMIERIARETEDIKLQMTSLEEEMENYRKFIREHEREIEHLKKEMDSVFEAMKLHRSGKEEKMRELQEVENRMDELKEEKERLRNHLHQIDLALQETRLKIANLLEEFSGNEEDVEELDEEKLEEIYRQIKDLENKIKYLGPVDLTAIDEYEKLREEYEEILKQKEDLEEAKRKLEEIIEKTDREAESLLFDVYQRVNESFNRFISLLFFGGEGRLNIVSEAKSILDAGFEISIRKPGRRDQKLSLLSGGEKALVGLALLFALMEIKPSPFYVLDEVDSPLDDYNAERFKRLLKENSKHTQFIVITHNKIVMEAADLLHGVTMVNGVSAIVPVEVEKILEV
Protein: Potassium transporter TRK1 (A0A1D8PTL7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000305|PubMed:19175416}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Kch1p
- Serine/threonine-protein phosphatase
- Tok1p
Sequence:
MLYRVSGFYKRHTRNFTNIDYGYYIRNFIHHIASKIYPYAKVVLPNFRAAHYFYILTLVILGSILVYPVKTCAYIDVLFFTAGASTQAGLNTVNVNDLSLYQQIVLYLLATLATPIFIHGSLLFVRLYYFERHFDNIKERSLMDYRMRKSATLARLGSAPTMSSTRLNTFNNQVLGFQEREAEKGSSSSPQSSSSQTSQPVSTAYNDQGGNDIEHHSEPSDSDDDESGNGPVTFQEKIHFEEPQRPRSQRRHSRTDSGIKFSALPHPRRRKSIDPEDMYRSINMLQEHKKNQEAKSKGIQFLNIGSPVRRKSRSSNIEAFPEEDTNPSRGDEITPATNSVGTGNNDEDEDDILIIKPPIEIENSDEANPIFTKKKKLASQIQFKETPGKAKKWITTKTRKHYNPWTSKLKKTLSNSSKKGSLSVVPTDTEDDSEDEEYASIDSETSDISDNEHAADNAEGSDVDSVGSYEEDEDEDEHNSDDDDDGEGERRLGNGASLTKAQSHLVLPSKDETGGKKYTKRSNTLDTPQQNTSDGRKIRKKAPKRKTPRTQRNASFNQHSNVSIGDGSIENVDTNDSYQRLSRTMSGNYLSWTPTVGRNSTFIKLTDEQKEELGGIEYRAVKLLIKIIVVYYVGFNIIPGVMLSIWIYCMPHYKNLMISSSISPAWWAFFTSQSSFNDLGLTLTSNSMMSFNQNAFVQILCSFLIVIGNTGFPILLRFIIWVMFKTARPLSLYKESLGFLLDHPRRCFTLLFPSVPTWWLFFILVVLNGFDLVIFCILDLHDDTFKGVDMGYRVLNGLFQAFCTRTVGFSVMDLSQLHAATQVSYLIMMYISVLPIAISVRRTNVYEEQSLGVYAKENAEGVDESAPSNYVGSHLRNQLSYDLWYICLGLFIICIAEGKRLKEQDLRFSIFAVLFEIVSAYGTVGMSMGYPGVDCSLSGEFNVISKLVIIAMMIRGRHRGLPYTIDRAIMLPNAAMKRHDRLQEEHAINRHNTMERTTTLGRVATFGNGPIDGGNNLLTRAITNIEHRLRNRRDGRSESSTVSEDPRYVVRTVSEV
Protein: Ribitol-5-phosphate transferase FKTN (EC 2.7.8.-) (Fukutin) (Fukuyama-type congenital muscular dystrophy protein) (Ribitol-5-phosphate transferase) (Q8R507)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of CDP-ribitol to the distal N-acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1). This constitutes the first step in the formation of the ribitol 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1 (By similarity). Required for normal location of POMGNT1 in Golgi membranes, and for normal POMGNT1 activity. May interact with and reinforce a large complex encompassing the outside and inside of muscle membranes. Could be involved in brain development (Probable).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12471058}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:29416295}. Nucleus {ECO:0000269|PubMed:29416295}. Endoplasmic reticulum {ECO:0000305|PubMed:29416295}. Note=In retinal tissue, does not localize with the Golgi apparatus. {ECO:0000269|PubMed:29416295}.
Interaction partners:
- Ribitol 5-phosphate transferase FKRP
- Protein O-mannose kinase
- D-ribitol-5-phosphate cytidylyltransferase
- Protein O-mannosyl-transferase 2
- Protein O-mannosyl-transferase 1
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Ribitol-5-phosphate xylosyltransferase 1
- Dystroglycan 1
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
Sequence:
MSRINKNVVLALLTLTSSAFLLFQLYYYKHYLSARNGPGSSKSKGNRVGFDSTQWRAVKKFIMLTSSQNVPVFLIDPWILESINKNFEQVKNASQGPASECRFFCVPRDFTAFALQYHLWKNEDGWFRIAENMGFQCLKTESKDPRLDGIDSLSGTEIPLHYVCKLTTHAIHLVVFHERSGNYLWHGHLRLKGHMDRKFVPFRKLQFGRYPGAFDRPELQQVTVDGLDMLIPKDPGRFLEEVPHSRFIECRYKEARAFLQQYIDDNTVDAMVFRKRAKELLQLAAKTLKDLGVPFWLSSGTCLGWYRQCGIIPYSKDVDLGIFIQDYKPDIILAFQEAGLPLKHKFGKVEDSLELSFQGKNDVKLDIFFFYEEADHLWNGGTQARTGKKFKYLFPKFTLCWTEFVDIKVHVPCETVDYIEANYGKTWKIPIKTWDWKSSPPNVQPNGIWPISEWDEVIQLY
Protein: LIM/homeobox protein Lhx1 (LIM homeobox protein 1) (Homeobox protein Lim-1) (hLim-1) (P48742)
Organism: Homo sapiens (Human)
Function: Potential transcription factor. May play a role in early mesoderm formation and later in lateral mesoderm differentiation and neurogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- LIM domain-binding protein 1
- Single-stranded DNA-binding protein 3
- LIM domain-binding protein 2
- Single-stranded DNA-binding protein 4
- Cyclin-K
- Neurogenin-2
- Paired box protein Pax-2
- Homeobox even-skipped homolog protein 1
- Homeobox protein Nkx-2.2
- Ras-related protein Rab-2A
Sequence:
MVHCAGCKRPILDRFLLNVLDRAWHVKCVQCCECKCNLTEKCFSREGKLYCKNDFFRCFGTKCAGCAQGISPSDLVRRARSKVFHLNCFTCMMCNKQLSTGEELYIIDENKFVCKEDYLSNSSVAKENSLHSATTGSDPSLSPDSQDPSQDDAKDSESANVSDKEAGSNENDDQNLGAKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLVDRLEPGELIPNGPFSFYGDYQSEYYGPGGNYDFFPQGPPSSQAQTPVDLPFVPSSGPSGTPLGGLEHPLPGHHPSSEAQRFTDILAHPPGDSPSPEPSLPGPLHSMSAEVFGPSPPFSSLSVNGGASYGNHLSHPPEMNEAAVW
Protein: MOB kinase activator-like 1B (Mob1 homolog 1B) (Mps one binder kinase activator-like 1B) (MsMob1-4) (MsMob1-B) (Q2WBN3)
Organism: Medicago sativa subsp. falcata (Sickle medic) (Medicago falcata)
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, phragmoplast. Note=Concentrated in punctuate and fibrillar structures during G2 and M phases. Localized to the cell division plane during cytokinesis. {ECO:0000269|PubMed:16460730}.
Interaction partners:
Sequence:
MSLFGLGSRNQKTFRPKKSAPTGSKGAQLQKHIDATLGSGNLREAVKLPPGEDINEWLAVNTVDFFNQVNTMFGTLTEFCTPSNCPTMTAGPKYEYRWADGVTIKKPIEVSAPKYVEYLMDWMESQLDDETIFPQRLGAPFPPNFRDVVKTIFKRLFRVYAHIYHSHFQKIVSLKEEAHLNTCFKHFVLFTWEFRLIEKAELAPLEDLVDSIIQL
Protein: Thioredoxin-like fold domain-containing protein (Q57TV4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDVSAGVDVTCVIAVGVAVVASVYVCLMRPTHKRWNHTGNVKEVLQTGDNIIRLFIYPRWHLGPSISLPCVAVETFLRLANVPYKVQATYDVFPSPTRTLPYIIHEGKCVAGCTVIIQYLMDTFKLKMDDGLESMQHAVGTALRNMLLYEARFALHHTLAHQAVLYTAPCALRCWKFSAASIACFLLWFRRHVLGTSKLAQLNVLRERYDSSYLMDLEAVETLIGDKPFLFGDRPTSYDCVVYAALLPIVRMKEAKFVSEPFAFAARSLLLREYVNRMTNVAFRDLEHLCCGEEKLSTRGSCVS