wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon-induced GTP-binding protein MxC (IFN-inducible antiviral protein MxC) (Interferon-inducible MxC protein) (Q6DKF0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Protein kinase-containing Z-DNA-binding domains
- Interferon phi 3.
- Interferon phi 2
- Ubiquitin-specific peptidase 18
Sequence:
MSSFDSAEGECNGLNQHYEKKVRPIIDLVDTLRALGVEKDLNLPAIAVIGDQSSGKSSVLEALSGVALPRGIGIVTRCPLILKLKKITRDKNWSGLLTYKDQTEILKEPTGIENAVLKAQIALAGTGEGISHEMITLEIQSCDVPDLTLIDLPGIARVATGNQPEDIEKQIKDLIEKFIKRQETISLVVVPANIDIATTEALKMASTVDPTGQRTLCILTKPDLVDRGMEDTVVRTVNNEVIRLEKGYMIVKCRGQQDINDKLNLVEALEKERRFFDEHPQFSSLLEDGKATIPLLGQRLTEELVEHIAKNVPRLQNQIEMKLQKTFERLKVLGESVPDDDEIELNNFLIKKLRQFMDALEEVKRVEEEPVKSDTRVFSKIRQEFVSWKHILDSKPIKMSTDLQEYVRTHRGKELPGFLNYGTFAGIIRMHVEDLEEPALKLLRNAKDIVHSSVGSIANIHFNGYPNLLLAVKEPIEKCLHEQFQNAEEKIRSQFKLEKTVYCQDDLYTNHLNLLRPKNTVRFGLEASLGNSELRETAFHLTSYLTIACERLANQIPLIVQYHMMNEYNSQLQNAMLGLIGTSDPGMLLCEDSGVARIRKDLKERLERLKDARRALPKVVHSANSW
Protein: Galactose-3-O-sulfotransferase 2 (Gal3ST-2) (EC 2.8.2.-) (Beta-galactose-3-O-sulfotransferase 2) (Gal-beta-1, 3-GalNAc 3'-sulfotransferase 2) (Glycoprotein beta-Gal 3'-sulfotransferase 2) (Q9H3Q3)
Organism: Homo sapiens (Human)
Function: Transfers a sulfate group to the hydroxyl group at C3 of non-reducing beta-galactosyl residues. Acts both on type 1 (Gal-beta-1,3-GlcNAc) and type 2 (Gal-beta-1,4-GlcNAc) chains with similar efficiency.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305|PubMed:11029462}; Single-pass type II membrane protein {ECO:0000305|PubMed:11029462}.
Interaction partners:
- Sialidase-4
- Thymidylate kinase
- Carbohydrate sulfotransferase 5
Sequence:
MMSMLGGLQRYFRVILLLLLALTLLLLAGFLHSDLELDTPLFGGQAEGPPVTNIMFLKTHKTASSTVLNILYRFAETHNLSVALPAGSRVHLGYPWLFLARYVEGVGSQQRFNIMCNHLRFNLPQVQKVMPNDTFYFSILRNPVFQLESSFIYYKTYAPAFRGAPSLDAFLASPRTFYNDSRHLRNVYAKNNMWFDFGFDPNAQCEEGYVRARIAEVERRFRLVLIAEHLDESLVLLRRRLRWALDDVVAFRLNSRSARSVARLSPETRERARSWCALDWRLYEHFNRTLWAQLRAELGPRRLRGEVERLRARRRELASLCLQDGGALKNHTQIRDPRLRPYQSGKADILGYNLRPGLDNQTLGVCQRLVMPELQYMARLYALQFPEKPLKNIPFLGA
Protein: Interphotoreceptor matrix proteoglycan 2 (Sialoprotein associated with cones and rods proteoglycan) (Spacrcan) (Q80XH2)
Organism: Mus musculus (Mouse)
Function: Chondroitin sulfate- and hyaluronan-binding proteoglycan involved in the organization of interphotoreceptor matrix; may participate in the maturation and maintenance of the light-sensitive photoreceptor outer segment. Binds heparin.
Subcellular location: Photoreceptor outer segment membrane {ECO:0000269|PubMed:29777959}; Single-pass type I membrane protein {ECO:0000255}. Photoreceptor inner segment membrane {ECO:0000269|PubMed:29777959}; Single-pass type I membrane protein {ECO:0000255}. Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix {ECO:0000269|PubMed:29777959}.
Interaction partners:
Sequence:
MIMFLPVGRMSLGILILFLTGGNLVSASEERQEPMHAVSVLSPEKSTDLSLPTRKRQLLDATETGRRWLLRRRRSILFPNGVKICSSETVAEAVANHVKYFKARVCQEAIWEAFRTFWDRLPGRDEYRHWMNLCEDGVTSVFEMGAHFSQSVEHRNLIMKKLAYTREAESSSCKDQSCGPELSFPVPIGETSTLTGAVSSASYPGLASESSAASPQESISNEIENVTEEPTQPAAEQIAEFSIQLLGKRYSEELRDPSSALYRLLVEEFISEVEKAFTGLPGYKGIRVLEFRAPEENDSGIDVHYAVTFNGEAISNTTWDLISLHSNKVENHGLVEMDDKPTAVYTISNFRDYIAETLHQNFLMGNSSLNPDPKSLQLINVRGVLLPQTEDIVWNTQSSSLQVTTSSILDNTLQAEWLSADTTTTTTTTISPFGFSSSSPSATGRELQSQSALRDVVSTSKLASPTKVVLSSLPEILGGSSLTLHSVTPAVLQPDLPVAPEGRTSGSFILEDGLASTEELEDTSIDGLPSSPLIQPVPKETVPPMEDSDTALLSTPHLTSSAIEDLTKDIGTPSGLESLASNISDQLEVIPWFPDTSVEKDFIFESGLGSGSGKDVDVIDWPWSETSLEKTTKPLSKSWSEEQDALLPTEGREKLHIDGRVDSTEQIIESSEHRYGDRPIHFIEEESHVRSTIPIFVESATPPTSPIFSKHTSDVPDIDSYSLTKPPFLPVTIAIPASTKKTDEVLKEDMVHTESSSHKELDSEVPVSRPDMQPVWTMLPESDTVWTRTSSLGKLSRDTLASTPESTDRLWLKASMTQSTELPSTTHSTQLEEEVIMAVQDISLELDQVGTDYYQSELTEEQHGKADSYVEMSTSVHYTEMPIVALPTKGGVLSHTQTAGALVVFFSLRVTNMLFSEDLFNKNSLEYKALEQRFLELLVPYLQSNLSGFQNLEILSFRNGSIVVNSRVRFAESAPPNVNKAMYRILEDFCTTAYQTMNLDIDKYSLDVESGDEANPCKFQACNEFSECLVNPWSGEAKCKCYPGYLSVDELPCQSLCDLQPDFCLNDGKCDIMPGHGAICRCRVGSNWWYRGQHCEEFVSEPFVIGITIASVVSFLLVASAVVFFLVKMLQAQNVRRERQRPTSSSRHPDSLSSVENAMKYNPAYESHLAGCELYEKSYSQHPFYSSASEEVIGGLSREEIRQMYESSDLSKEEIQERMRILELYANDPEFAAFVREHQMEEL
Protein: Osteopontin (Bone sialoprotein 1) (Secreted phosphoprotein 1) (SPP-1) (P08721)
Organism: Rattus norvegicus (Rat)
Function: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P10451}.
Interaction partners:
- CD44 antigen
- Integrin beta-1
- Osteocalcin
- Stromelysin-1
- Integrin alpha-9
- SPARC
- Integrin alpha-4
- Interferon regulatory factor 7.
- Bone morphogenetic protein 2
- Integrin alpha-8
Sequence:
MRLAVVCFCLFGLASCLPVKVAEFGSSEEKAHYSKHSDAVATWLKPDPSQKQNLLAPQNSVSSEETDDFKQETLPSNSNESHDHMDDDDDDDDDGDHAESEDSVNSDESDESHHSDESDESFTASTQADVLTPIAPTVDVPDGRGDSLAYGLRSKSRSFPVSDEQYPDATDEDLTSRMKSQESDEAIKVIPVAQRLSVPSDQDSNGKTSHESSQLDEPSVETHSLEQSKEYKQRASHESTEQSDAIDSAEKPDAIDSAERSDAIDSQASSKASLEHQSHEFHSHEDKLVLDPKSKEDDRYLKFRISHELESSSSEVN
Protein: Protein clueless (Clustered mitochondria protein homolog) (A1ZAB5)
Organism: Drosophila melanogaster (Fruit fly)
Function: mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:19638420}.
Interaction partners:
- Metaxin-1 homolog
- AT01806p
- Mitochondrial import receptor subunit TOM40 homolog 2
- Mitochondrial import receptor subunit TOM7 homolog
- FI03495p
- TOMM20-like protein 1
- Mitochondrial import receptor subunit TOM22 homolog
- Eukaryotic translation initiation factor 3 subunit B
- LD34461p
- Mitochondrial import receptor subunit TOM40 homolog 1
Sequence:
MALETEAKNSNATATGDATATATKASGKAKENNNTAGGKKNLNPNSNQQNSNQNLVNGNGTAADGPAAKKKGKKNRNKSPTEPTTEAVLSNGHAEKPTVVDAVEDNADTNANVEKPQEGGAPDAEADGDDIDLDALQDIGITVNISSPGADLLCVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKSINNLEQGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKRTRPDSVDCTPPEYVTPGVSDPPILPLHPNVKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEDKRFHISACSKGFFINQSTDDTFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQTIQKRRTMRHAFERVATPYQVYQWAAPILEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDTKMQMFIWNNIFFSMGFDVRDHYKELGGDAAAFVAPRYDLHGVRVYNAVDIEGLYTLGTVVVDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHVVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVQLSKELVDMGFPIEHRHKLCCLRQELLEAFIEDRHVNFIRIAAARLQQLTTIKQSEKSEANPVPALEGAEAASKVNGAEKPDDKEKKNEEEEKKERSTSGEARAAAIVNAIREAQSNVATSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHADGEEGTSLAKQKVLVQEAAEFLVLKQIPAFIKEHMSHSSSPIDGQSLTESLHSHGINVRYLGKVIKILSQMPRMDYLHRIAVLELIVRATKHIYYTYMQNTEPLHLSAAISHFLNCLLTNGPVNPAVSSEEAHKKRGNGGKHNKHKSSKGGKGQQQQQTTGNQNGSSSGSSNSSSASDWTLMTPRSLWQQIRKEAKVYWDWELDCDSIETAVSKYGILRISLMRAFCLKVGIQVLLREYNFESKHKPTFGDDDIVNVFPIVKHISPRATDAYNFYTTGQAKIQQGLFKEGYELISGALNLLNNVFGALHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGMDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLMVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGDKDMHVALSYHLMARTQSCMGDFRSALNNEKETYSFYKSQLGENHEKTRDSAECLRLLTQQAVLLQRKMNDIYSSGKLTSDLPPIHITPPSMGSVLDMLNTINGILFVKISRKDIVKVRSEIEKHFKTDSTENEVNDAINSIVAAANNNGEAEDAVSKDIKEQPEAGKQLTNGDKAAATEATSS
Protein: Cytochrome P450 71D180 (Carvacrol synthase) (EC 1.14.14.-) (Carveol synthase) (EC 1.14.14.51, EC 1.14.14.53) (Gamma-terpinene hydroxylase) (Limonene hydroxylase) (P0DO38)
Organism: Thymus vulgaris (Thyme)
Function: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (Ref.1). Catalyzes the C2-hydroxylation of gamma-terpinene to produce carvacrol (Ref.1). Mediates also the C6-hydroxylation of (4S)-limonene and (4R)-limonene to form carveol (Ref.1).
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDISISWVVIIVFVLSYLILMDKWRASKLPGNLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVHSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNDDMIFSRYNDHWRQIRKICVSELLSPRNVRSFGFIRQDEMARLIRVFESSEGAAINASEEISKMSCAIVCRAAFGSVLKDQGKLADLVKEALSMASGFELADLYPSSWLLNLLCFNKYRLQRMRGRLDNILDGFLEEHKVKKSGEFGGEDIIDVLYRMQKDTEMKAPITNNGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKMVKAQAEVREKLKGKTNPDVADVQELKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRILVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRVCPGLHFGLANVEVPLAQLLYHFDYKLPSAMTAADMDMSETPGLSGPRKNPLIMIPTIHNPTS
Protein: PIH1 domain-containing protein 2 (Q8WWB5)
Organism: Homo sapiens (Human)
Interaction partners:
- RuvB-like 1
- RuvB-like 2
- Sperm-associated antigen 1
- RNA polymerase II-associated protein 3
- Dynein axonemal assembly factor 6
- Heat shock protein HSP 90-beta
- Protein kintoun
- PIH1 domain-containing protein 1
- Dynein axonemal assembly factor 4
Sequence:
METSSKGLLTQVTQFWNLLDDLAQSDPEGYEKFIQQQLKEGKQLCAAPEPQLCLQTRILKPKEKILFINLCQWTRIPAPQSTTHPVPLTVGKPEDTTEISDAYTVIDVAYNPDVLHAAEKDQVKKNQLIQMAMKCIEEKFQFTLSHSYHITKFRIKGSIQRMKQNLMGIQTDSIDLREKMRRELTLGQIRSSTMSNPDHFPQLLLPKDQVSGKAVCLIEEISSTEIQVEMKMPAYELKIVHDHSEKPLKIELKVELPGINSVSLCDLSVSEDDLLIEVSEKYRLHLNLPKLIDTEMTTAKFIKEKSTLIITMPLV
Protein: Corset-associated protein 17 (Q8WSH5)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MDRKLVEMQAVISRREAEFRKQNIDLFTELLGEMRTEDGLCEKNSKELQYKQKELAKQRAEIEKAEKDVKAKLDKVKLTRSRLAEQMSEIKEKLETLRKWGPADHASPLGLLPAGATAAAPENGSNGPAQTS
Protein: Ubiquitin carboxyl-terminal hydrolase 46 (EC 3.4.19.12) (Deubiquitinating enzyme 46) (Ubiquitin thioesterase 46) (Ubiquitin-specific-processing protease 46) (P62069)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme that plays a role in behavior, possibly by regulating GABA action. May act by mediating the deubiquitination of GAD1/GAD67. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62068}. Note=USP46/WDR48/WDR20 complex is predominantly cytoplasmic. {ECO:0000250|UniProtKB:P62068}.
Interaction partners:
- WD repeat-containing protein 48
- WD repeat-containing protein 20
- WD repeat-containing protein 20
- PH domain leucine-rich repeat-containing protein phosphatase 2
- PH domain leucine-rich repeat-containing protein phosphatase 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Dystrophia myotonica WD repeat-containing protein
- Ubiquitin carboxyl-terminal hydrolase 5
- Polyubiquitin-B
- Zinc finger-containing ubiquitin peptidase 1
Sequence:
MTVRNIASICNMGTNASALEKDIGPEQFPINEHYFGLVNFGNTCYCNSVLQALYFCRPFRENVLAYKAQQKKKENLLTCLADLFHSIATQKKKVGVIPPKKFISRLRKENDLFDNYMQQDAHEFLNYLLNTIADILQEEKKQEKQNGKLKNGNMNEPAENNKPELTWVHEIFQGTLTNETRCLNCETVSSKDEDFLDLSVDVEQNTSITHCLRDFSNTETLCSEQKYYCETCCSKQEAQKRMRVKKLPMILALHLKRFKYMEQLHRYTKLSYRVVFPLELRLFNTSSDAVNLDRMYDLVAVVVHCGSGPNRGHYITIVKSHGFWLLFDDDIVEKIDAQAIEEFYGLTSDISKNSESGYILFYQSRE
Protein: Cytochrome b-c1 complex subunit 8 (Complex III subunit 8) (Ubiquinol-cytochrome c reductase complex 11 kDa protein) (Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C) (P50523)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08525}.
Interaction partners:
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Probable mitochondrial-processing peptidase subunit beta
Sequence:
MGGAAGGKTYLGWWGHLGGPKQKGIITYSLSPFQQRPMAGFFKTSTQNMFRRVMTEGLYVAIPFGIAYYIYCWGKERNEFLNSKHGRHLVEE
Protein: Alpha-2u globulin PGCL4 (Obp3 protein) (Q78E14)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKLLLLLLCLGLTLVCGHAEEASFERGNLDVDKLNGDWFSIVVASDKREKIEENGSMRVFVQHIDVLENSLGFTFRIKENGVCTEFSLVADKTAKDGEYFVEYDGENTFTILKTDYDNYVMFHLVNVNNGETFQLMELYGRTKDLSSDIKEKFAKLCVAHGITRDNIIDLTKTDRCLQA
Protein: Longitudinals lacking protein, isoforms H/M/V (P42284)
Organism: Drosophila melanogaster (Fruit fly)
Function: Putative transcription factor required for axon growth and guidance in the central and peripheral nervous systems. Repels CNS axons away from the midline by promoting the expression of the midline repellent sli and its receptor robo.
Subcellular location: Nucleus {ECO:0000269|PubMed:8050351}.
Interaction partners:
Sequence:
MDDDQQFCLRWNNHQSTLISVFDTLLENETLVDCTLAAEGKFLKAHKVVLSACSPYFATLLQEQYDKHPIFILKDVKYQELRAMMDYMYRGEVNISQDQLAALLKAAESLQIKGLSDNRTGGGVAPKPESSGHHRGGKLSGAYTLEQTKRARLATGGAMDTSGDVSGSREGSSSPSRRRRKVRRRSMENDAHDNSNSSVLQAAASNQSILQQTGAGLAVSALVTTQLSSGPAAGTSSQASSTQQQQPLTSTNVTKKTESAKLTSSTAAPASGASASAAVQQAHLHQQQAQTTSDAINTENVQAQSQGGAQGVQGDDEDIDEGSAVGGPNSATGPNPASASASAVHAGVVVKQLASVVDKSSSNHKHKIKDNSVSSVGSEMVIEPKAEYDDDAHDENVEDLTLDEEDMTMEELDQTAGTSQGGEGSSQTYATWQHDRSQDELGLMAQDAQQRDPQDVSTNQTVVLPHYSIYHYYSNIYYLLSHTTIYEADRTVSVSCPGKLNCLPQRNDLQETKSVTVLYTIHFFLYILMIYIFVLCKILPRIVFVWVST
Protein: PML-RAR protein (Q15156)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKAIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEVPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDRVDMLQEPLLEALKVYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLDTLSGQPGGGGRDGGGLAPPPGSCSPSLSPSSNRSSPATHSP
Protein: At5g03050 (Knotted 1-binding protein) (Q8GY72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNTEMEEDAGNGGFRKRMRASDEEGKGDSRDGISLDHTIENEEAETKLVASDEMELSIAQILDKIESFTQTVSNLLETGKTMLKELSNEFEERLIMIHKEHVEKWQDEIKELRLLDASNEETTSLLHNARYLIQNPSIEQ
Protein: GDP-fucose protein O-fucosyltransferase 2 (EC 2.4.1.221) (Protein O-fucosyltransferase 2) (A5K6G1)
Organism: Plasmodium vivax (strain Salvador I)
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates sporozoite proteins CSP and TRAP. O-fucosylation regulates stability and intracellular trafficking of TRAP but not of CSP (By similarity). Probably by regulating protein O-fucosylation, may play a role in parasite transmission to the mosquito vector and/or infection of the vertebrate host hepatocytes; however, POFUT2 involvement in transmission/infection is controversial (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:W7K6N5}.
Interaction partners:
Sequence:
MKGRAHIWVALLLACLPPRFRNLDKDVSSPVCRTDDVYTGDAFYPFKKKKYVLYDVHIGEGFNLQKEVLYRVALAVYYLNQEERTHVHYLVLPPWCYVTHWGRERTNARIKWSIFFNLKALQNVIPVMEYAEYEGQFGPHTDYILSYRHIIGEWPKRGDKKSFQVLKLDKCQVKGYKLKKNLRKNCDHKYSVEYSGKCTNVKGKKMECLEFFFITSHFVSSTLLDIFQYDADSVLIKHGSNILVAFMNELVDANLEDVLPYSEDLINEGDQFVEKNFKSSKNYISCHLRYTDFRKISTYDVSPVGISLLKLLYIMFLRKSTLIFVSTDEKKEVKKVIDSQFPQFKHFFFFYENEKLHTGQVAIVDQWICARSGTFVGNIFSRFSMHIKWERSLIGKGGPDHNLDLCGYSISTNHELRKKYSDVQDAHLDEEALQKLRPLYMRLSQKDRDFLRTICYDFAHYYPQNVSIYRRGERREEGRLM
Protein: Homer protein homolog 2 (Homer-2) (Cupidin) (Q9NSB8)
Organism: Homo sapiens (Human)
Function: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses. Required for normal hearing. Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25816005}. Cell membrane {ECO:0000250|UniProtKB:O88801}. Postsynaptic density. Synapse. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q9QWW1}. Note=Postsynaptic density of neuronal cells. The stabilization and clustering of the metabotropic glutamate receptors appears to be mediated by isoform 1 and isoform 2 at the cell surface.
Interaction partners:
- Homer protein homolog 1
- Homer protein homolog 3
- Metabotropic glutamate receptor 1
- Metabotropic glutamate receptor 5
- SH3 and multiple ankyrin repeat domains protein 1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Disks large-associated protein 1
- Drebrin
- SH3 and multiple ankyrin repeat domains protein 2
- Disks large homolog 4
Sequence:
MGEQPIFTTRAHVFQIDPNTKKNWMPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRANTVFGLGFSSEQQLTKFAEKFQEVKEAAKIAKDKTQEKIETSSNHSQESGRETPSSTQASSVNGTDDEKASHAGPANTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRNKIDELEEQCSEINREKEKNTQLKRRIEELEAELREKETELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKVELKSFLEVLDGKIDDLHDFRRGLSKLGTDN
Protein: Tumor necrosis factor receptor superfamily member EDAR (Anhidrotic ectodysplasin receptor 1) (Downless homolog) (EDA-A1 receptor) (Ectodermal dysplasia receptor) (Ectodysplasin-A receptor) (Q9UNE0)
Organism: Homo sapiens (Human)
Function: Receptor for EDA isoform A1, but not for EDA isoform A2. Mediates the activation of NF-kappa-B and JNK. May promote caspase-independent cell death.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Ectodysplasin-A
- Ectodysplasin-A receptor-associated adapter protein
- Sodium/potassium/calcium exchanger 5
- Membrane-associated transporter protein
- Tumor necrosis factor
- Protein Wnt-10a
- Sonic hedgehog protein
- Tumor necrosis factor receptor superfamily member 1A
Sequence:
MAHVGDCTQTPWLPVLVVSLMCSARAEYSNCGENEYYNQTTGLCQECPPCGPGEEPYLSCGYGTKDEDYGCVPCPAEKFSKGGYQICRRHKDCEGFFRATVLTPGDMENDAECGPCLPGYYMLENRPRNIYGMVCYSCLLAPPNTKECVGATSGASANFPGTSGSSTLSPFQHAHKELSGQGHLATALIIAMSTIFIMAIAIVLIIMFYILKTKPSAPACCTSHPGKSVEAQVSKDEEKKEAPDNVVMFSEKDEFEKLTATPAKPTKSENDASSENEQLLSRSVDSDEEPAPDKQGSPELCLLSLVHLAREKSATSNKSAGIQSRRKKILDVYANVCGVVEGLSPTELPFDCLEKTSRMLSSTYNSEKAVVKTWRHLAESFGLKRDEIGGMTDGMQLFDRISTAGYSIPELLTKLVQIERLDAVESLCADILEWAGVVPPASQPHAAS
Protein: Trifunctional enzyme subunit alpha, mitochondrial (Monolysocardiolipin acyltransferase) (MLCL AT) (EC 2.3.1.-) (TP-alpha) [Includes: Long-chain enoyl-CoA hydratase (EC 4.2.1.17); Long chain 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211)] (Q8BMS1)
Organism: Mus musculus (Mouse)
Function: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA described here carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities while the trifunctional enzyme subunit beta/HADHB bears the 3-ketoacyl-CoA thiolase activity. Independently of the subunit beta, the trifunctional enzyme subunit alpha/HADHA also has a monolysocardiolipin acyltransferase activity. It acylates monolysocardiolipin into cardiolipin, a major mitochondrial membrane phospholipid which plays a key role in apoptosis and supports mitochondrial respiratory chain complexes in the generation of ATP. Allows the acylation of monolysocardiolipin with different acyl-CoA substrates including oleoyl-CoA for which it displays the highest activity.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P40939}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40939}. Note=Protein stability and association with mitochondrion inner membrane do not require HADHB. {ECO:0000250|UniProtKB:P40939}.
Interaction partners:
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase B, peroxisomal
- 3-ketoacyl-CoA thiolase A, peroxisomal
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
Sequence:
MVASRAIGSLSRFSAFRILRSRGCICRSFTTSSALLTRTHINYGVKGDVAVIRINSPNSKVNTLNKEVQSEFIEVMNEIWANDQIRSAVLISSKPGCFVAGADINMLSSCTTPQEATRISQEGQRMFEKLEKSPKPVVAAISGSCLGGGLELAIACQYRIATKDRKTVLGVPEVLLGILPGAGGTQRLPKMVGVPAAFDMMLTGRNIRADRAKKMGLVDQLVEPLGPGIKSPEERTIEYLEEVAVNFAKGLADRKVSAKQSKGLVEKLTTYAMTVPFVRQQVYKTVEEKVKKQTKGLYPAPLKIIDAVKAGLEQGSDAGYLAESQKFGELALTKESKALMGLYNGQVLCKKNKFGAPQKNVQQLAILGAGLMGAGIAQVSVDKGLKTLLKDTTVTGLGRGQQQVFKGLNDKVKKKALTSFERDSIFSNLIGQLDYKGFEKADMVIEAVFEDLGVKHKVLKEVESVTPEHCIFASNTSALPINQIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTDKTSKDTTASAVAVGLRQGKVIIVVKDGPGFYTTRCLAPMMSEVMRILQEGVDPKKLDALTTGFGFPVGAATLADEVGVDVAQHVAEDLGKAFGERFGGGSVELLKQMVSKGFLGRKSGKGFYIYQEGSKNKSLNSEMDNILANLRLPAKPEVSSDEDVQYRVITRFVNEAVLCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKVVDRLRKYESAYGTQFTPCQLLLDHANNSSKKFYQ
Protein: F-box domain-containing protein (Q9XX49)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKNKPDLPLHTKCDKMSKKKNLKNRKFSQWQKLPEDIMREVLKQLDFEDRSIIRQCSRTEMILADKIPENLNSINFLEGSDPTNKKYYIFLDIDNIPNKKLKNFNQETRMAVGVGAVETFCRIFRNKNSNAKRVVFEFPFRSTHRSIMPLLISELEKSEIIIKAREIAIDCNESTSKWIQKLLSRFEMEYLEKITMKSLSGKVFDKLKITDHFKRAKSLDLHAKKNPRGYTPGVDQTVVVDYAMLSHVEKYMLTVHQLVPEDAWKVIKNFRSRPNLPIGSFFNIEVAVIIDHLQVLRQFDVQPKHQPPTIAALQLSYPAYTYHVQFFDVEDSNNILVVSISIFDVTGSICSRDHIWETFRTKF