wanglab/gogpt-training-data huggingface dataset:
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q384T3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRLLSPSVALSVENGFADIGEFCASSPDTSSSVSESLASAELPQLHQQHKLGGVDLNEVADELEEELVLCLSTGYCNLSQMGFVTTPANIPYESLVTLLLSGNQIKEISESLFTNGNFQFLCKLDLSSNCLESVPKSLFKLMKLEVLLLDHNNITRLPVSVDEQIGSQLLPALQRIGLEFNDLSRFPIELFKHCPSLEAVYLSQNLRMLNEPVSVKQLLQAAAVESSKENHRVLLKVDNKPVFVQQMYDEKWDEVLPWLDVELHKIYPDKVLSFLYLGSLRTAQTPLVYRDLDIGFILSAGRNMTVHVESGMRHLVLPIDDHPGEKLRPIFDMAFNFIDDAREEGKGVLLHCFAGLSRSVTIAVAYLMSRYNYKRDEAIEMIRRVRPSSQPNSGFMDILAQYEQELNNQKHHM
Protein: FI18813p1 (Synaptotagmin 4) (Synaptotagmin IV) (Q9U6P7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ras-related protein Rab-3
- Synaptotagmin 1
- Amyloid-beta-like protein
- Neuronal synaptobrevin, isoform J
- Synaptobrevin
- Syntaxin-1A
- Synapsin
- Protein stoned-B
- Synaptosomal-associated protein 25
- Syntaxin-4
Sequence:
MAEEYIPDASVMDTIVPAILGLTAAAVLSSVACICARQMRLRNKKQSQHDASFPFQPTRRPTAVRSPSGQPPHYLKKSPSPTGGKQMGLLSPMQDQSTSPIAQPNVKYSEEGDGPAQHAEQQNGNQLTVVDGNGLKHSLHNSLHHSPVETIANGSVTITLDDHSLTNGKELTVTDQYGKLGTIYFKLRYLAERNALMVSIIRCRGLPCKGGSSGTGDIPTGMNGRTQAATDPYVKLQLLPDKQHKVKTRVVRNTRNPVYDEDFTFYGLNMNDLQNMSLHFVILSFDRYSRDDVIGEVVCPLTSIEIGDISKEALSISKEIQPRSLKIRAQGRGELLISLCWQPAAGRLTVVLLKARNLPRMDVTGLADPYVKIYLLYNGQRIAKKKTHVKKRTLSPVFNESFAFDIPAAEGAGASLEGVSLELMLLDWDRVTKNEVIGRLELGGPNSSSTALNHWNEVCNSPRRQIAEWHKLNE
Protein: Probable nucleolar complex protein 14 (O43051)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Ribosomal RNA small subunit methyltransferase mra1
- RNA cytidine acetyltransferase
- Uncharacterized protein C57A7.06
- U3 small nucleolar RNA-associated protein 22
- rRNA biogenesis protein rrp5
- U3 small nucleolar RNA-associated protein 20
- KRR1 small subunit processome component homolog
- Uncharacterized protein C1604.06c
- Uncharacterized protein C3B8.09
- Nucleolar protein 58
Sequence:
MGKNGSQLKNLKSSIRQANLGTRPNNKKSRTRSTESHEDRQAKVQKIQSDFNLFDRQFTKRKFDVGGRRVKGTEGKPGVSRGVGEELRRRTIGAELKKRNRSGAIIDRRFGENNPHLSVEEKMLERFSREQQRRSKRELYNLDAEDVLTHGNRPLSDIDSFEEPGFGLDEGEELNDEVVRRMHFGGFEDSDAENEKEGEGAHKSKREVMSEIIAKSKHYKAERQAEKERYEDEREKLDEQMEDLQSFLSDYKKASRKSGIKTQRPIISDGDARYDSFVREMVFDKRAHPTERTKTEEELAQIEADRLRELEDQRISRMEHYQEDSASEAGSIEDEQATDNVFGFGKGLEQENEEEWNGINEEAEESEDEESVNSDTSFVDDEQLKVEEQPLVGSAIKNEGSEKASLAYTYPCPTSHVEFVQLLKGLDYKDYPTVVSRIRTLHHVKLHPDNKSRLENFSVILLQHILHLTRQPMISMELLEHLTEHLHSLAQQFPSALGISFISVVEGMRKRLAKSYVYPEIKFPEISDLLFFNLTGSIFPTSDKKHIVVSPVMLTMAESLSQSPADSLSDVCKKLYIANLFLKFQSYSHRYVPEVITAVSQALYLLYPNFISIVPGTFALPDSLKEKQNLFAIQDISLDEPQRLSLYELEELPTGLLQSSILFITLNLIEMAIDIYFKEQAFIEIFVPIMDMLQLYSLKKELLSKRLSEKLLSTLQAVSDSIESAKANRKPLALQSHRPLGITSQVPKFEEGYSLDKSSHDIDPERAQLNKLRAQHRDAKKGAIRTLRKDARFIARERRQEQRAKDQAYNEKMRKLENRLQHFDPAV
Protein: LysM domain-containing GPI-anchored protein 1 (Q93ZH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required as a cell surface receptor for peptidoglycan (PGN) elicitor signaling leading to innate immunity. Plays an essential role in detecting PGNs and restricting bacterial growth (of Pseudomonas syringae pv. tomato DC3000 for example).
Subcellular location: [Isoform 1]: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- Chitin elicitor receptor kinase 1
- Protein LYK5
- Elongation factor Tu, chloroplastic
- LysM domain receptor-like kinase 3
- Protein LYK2
- Elongation factor Tu
- LRR receptor-like serine/threonine-protein kinase EFR
- Leucine-rich repeat receptor-like protein kinase PEPR1
- At5g62150
- Receptor like protein 23
Sequence:
MKIPEKPIFLIFVSLILASSLTFTATAKSTIEPCSSNDTCNALLGYTLYTDLKVSEVASLFQVDPISILLANAIDISYPDVENHILPSKLFLKIPITCSCVDGIRKSVSTHYKTRPSDNLGSIADSVYGGLVSAEQIQEANSVNDPSLLDVGTSLVIPLPCACFNGTDNSLPAVYLSYVVKEIDTLVGIARRYSTTITDLMNVNAMGAPDVSSGDILAVPLSACASKFPRYASDFGLIVPNGSYALAAGHCVQCSCALGSRNLYCEPASLAVSCSSMQCRNSNLMLGNITVQQTSAGCNVTTCDYNGIANGTILTMLTRSLQPRCPGPQQFAPLLAPPDTVPRDVMYAPAPSPDFDGPGSIASSPRSSMLPGGGILPGNPANGPAGSISTASASSVSYFFITFLISIASFSLALSS
Protein: G protein pathway suppressor 1 (C9JFE4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRELQNAPDAIPESGVEPPALDTAWVEATRKKALLKLEKLDTDLKNYKGNSIKESIRRGHDDLGDHYLDCGDLSNALKCYSRARDYCTSAKHVINMCLNVIKVSVYLQNWSHVLSYVSKAESTPEIAEQRGERDSQTQAILTKLKCAAGLAELAARKYKQAAKCLLLASFDHCDFPELLSPSNVAIYGGLCALATFDRQELQRNVISSSSFKLFLELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIRNRALIQYFSPYVSADMHRMAAAFNTTVAALEDELTQLILEGLISARVDSHSKILYARDVDQRSTTFEKSLLMGKEFQRRAKAMMLRAAVLRNQIHVKSPPREGSQGELTPANSQSRMSTNM
Protein: Uncharacterized protein (Q380Z2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVWYIPFVYQAFFFSTFNAVGSLHAWYMTQRHMMLVSGSLNSSLGAVAVYTHSFDPTLSNACTSIASISAFGHFGLHAFRTKALLRPSAMSFLHFCWCISLLAFGIHRGRWAYTLRHD
Protein: E3 ubiquitin-protein ligase TRIM47 (EC 2.3.2.27) (Gene overexpressed in astrocytoma protein) (RING finger protein 100) (Tripartite motif-containing protein 47) (Q96LD4)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates the ubiquitination and proteasomal degradation of CYLD.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11511098}. Nucleus {ECO:0000269|PubMed:11511098}.
Interaction partners:
Sequence:
MDGSGPFSCPICLEPLREPVTLPCGHNFCLACLGALWPHRGASGAGGPGGAARCPLCQEPFPDGLQLRKNHTLSELLQLRQGSGPGSGPGPAPALAPEPSAPSALPSVPEPSAPCAPEPWPAGEEPVRCDACPEGAALPAALSCLSCLASFCPAHLGPHERSPALRGHRLVPPLRRLEESLCPRHLRPLERYCRAERVCLCEACAAQEHRGHELVPLEQERALQEAEQSKVLSAVEDRMDELGAGIAQSRRTVALIKSAAVAERERVSRLFADAAAALQGFQTQVLGFIEEGEAAMLGRSQGDLRRQEEQRSRLSRARQNLSQVPEADSVSFLQELLALRLALEDGCGPGPGPPRELSFTKSSQAVRAVRDMLAVACVNQWEQLRGPGGNEDGPQKLDSEADAEPQDLESTNLLESEAPRDYFLKFAYIVDLDSDTADKFLQLFGTKGVKRVLCPINYPLSPTRFTHCEQVLGEGALDRGTYYWEVEIIEGWVSMGVMAEDFSPQEPYDRGRLGRNAHSCCLQWNGRSFSVWFHGLEAPLPHPFSPTVGVCLEYADRALAFYAVRDGKMSLLRRLKASRPRRGGIPASPIDPFQSRLDSHFAGLFTHRLKPAFFLESVDAHLQIGPLKKSCISVLKRR
Protein: Factor arrest protein 3 (P46671)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in the control of the reentry into the cell cycle following pheromone treatment.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Factor arrest protein 7
- Vacuolar protein sorting-associated protein 64
- Factor arrest protein 11
- Factor arrest protein 10
- Factor arrest protein 8
- Serine/threonine-protein phosphatase PP2A-like PPG1
Sequence:
MNSGGSDSFDYLLQLTKALSAECRANRQETDRIELLLKRLAKQSGISYDNLSKNIIPDSWKDNASQKASPPTEAQKLISENFKLIYEIEKQEYFNTKAVALINNINEHFSYIKNFIDEQNAIRERNIATFSSEKLDERNKSLQQNYESLKTENEETKKKLHSIIKQFEKLLKEVDWDRISKDSRDYSRFKKQLEYLQDTYQVLK
Protein: Doublesex- and mab-3-related transcription factor DM-W (W-linked doublesex- and mab-3-related transcription factor) (xDM-W) (B0I1G7)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that plays a key role in female sex determination and primary ovary development. Acts as a sex-determining protein by antagonizing the transcriptional activity of male-determination protein dmrt1-a, acting as a dominant-negative type protein.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
Interaction partners:
Sequence:
MQNNEEPYNTGQYPSGPHGKKSPRLHKCARCRNHGYATPLKGHKRFCIWRDCQCQKCSLITERQRVIAAQVALQRQQAQEEELGIYHPIPLPIAAVIKREHGGSSSQLMLESSSTQTTSTPTSAEWIKEEEVAKPAAGLFAPPPSSEEMGMTLAAVGAADAATQTDQPGHLFNMMSAMIQQLMDMSWELQQGWI
Protein: Lens fiber major intrinsic protein (Aquaporin-0) (MIP26) (MP26) (P51180)
Organism: Mus musculus (Mouse)
Function: Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell junction {ECO:0000250|UniProtKB:Q6J8I9}. Note=Localizes to thin cell-cell junctions in lens fiber cells. {ECO:0000250|UniProtKB:Q6J8I9}.
Interaction partners:
- Calmodulin-like protein 4
- Aquaporin-12
- Calmodulin-like protein 3
- Calmodulin-4
- Calmodulin 5
- Aquaporin-11
- Gap junction alpha-8 protein
- Filensin
- Gamma-crystallin S
- Alpha-crystallin A chain
Sequence:
MWELRSASFWRAIFAEFFATLFYVFFGLGASLRWAPGPLHVLQVALAFGLALATLVQTVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYIAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHAGVSVGQATTVEIFLTLQFVLCIFATYDERRNGRMGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFSNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSVSERLSILKGARPSDSNGQPEGTGEPVELKTQAL
Protein: Plexin A, isoform F (H9XVP3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MNFVLSVLLIAILKDKYDYWLPSRTGCQTLAANIWSDKTTAQNEPINLTNANAPIKNAKNLNSTITNVAAFDTKLNHLLVDTITGRVFVGGVNRLYQLSPDLELSETVKTGPQNDSVECSILDCPLNAVRSPTDNYNKVLLIDRATSRLIACGSLFQGTCTVRNLQNVSIIEHEVPDAVVANDANSSTVAFIAPGPPQHPVTNVMYVGVTYTNNSPYRSEIPAVASRSLEKTKMFQIASSAVTTGTRTFINSYARETYFVNYVYGFSSERFSYFLTTQLKHSHHSSPKEYITKLVRICQEDSNYYSYTEIPVECISDAQGGTKFNLVQAGFLGKPSSDLAQSLGISIQDDVLFAVFSKGEGNTPTNNSALCIYSLKSIRRKFMQNIKSCFNGSGMRGLDFISPSMPCVLTKLQTIGEDFCGLDVNSPLGGETPITSVPVAMFNTKLTSVAATSTSGYTVVFVGTSDGFLKKVVIESSSIANEYASFAVDLGSEINRDMQFDNQNLYIYVMSKTKVSKVKVFDCSDYKTCGDCLGARDPYCGWCSLENKCSPRSNCQDDANDPLYWVSYKTGKCTTITSVVPHQLQRTTARTLELIIDHLPQLKENLICAFTTEDKALFTNATKKRNGVNCTTPRTDMLPQIEQGKHHFTAKLSVRTRNGPDLVSTDFTFFDCSTHSSCTRCVSSEFPCDWCVEAHRCTHDTAENCRNDILVTGVSRIGPSYRSGPGFCPTINATGDGSEVLVAGGTSKSIKVKVHIIGQFIVQTRFVCQFNIEGRVTSLNAQLLGDTIYCDSMEFQYTSRSPNLTATFAVIWGGSKPLDNPHNIHVVIYRCREMADSCGICLALSEKYNCGWCSSTNTCEVEEQCNKNKEGKTDWLNRSEICPNPEIHTFQPKTGPWEGGTNITIRGINLGKNYNDIYSGVRIAGINCMPFPQFYIDTKQIVCTVDSPGEQMYRNGKIVVQIGDYRGESKEDYEFVDPKILDFNPKFGPTSGGTEIHITGKHLNAGSRIQASINDHLPCKILSTDSSQAICRTSASPGIIEGRLKMSFDNGPREFNDYNFKYVLDPTVEHVSSGPSGQIKVPKGIPAGGIRISVTGTQFTSIQNPNIYVVYNGEMYASPCRVQSDTEMECASPVVDVDSHVIEAERPILLEYGFLMDNVLRVQNLSKVHNNHFELYPNPEYFIFEERVKYFKSEYLTINGRNLDRACKESDVEVKIGNGFCNITSLSRQQLTCRPPSEATATKSMNGPEVIVRIGTSLEYRIGILSYESSNIILDWGENVIFAVIATIVILLLIFVALLVAYKKKSSESSRVLRNMQEQMDILELRVAAECKEAFAELQTEMTDLTGDLTSGGIPFLDYRSYAMKILFPNHEDHIVLQWERPELLRKEKGLRIFGQLIMNKTFLLLFIRTLESNRYFSMRERVNVASLIMVTLQSKLEYCTDILKTLLGDLIEKCIEGKSHPKLLLRRTESVAEKMLSAWFTFLLYKFLKECAGEPLYMLFRAVKGQVDKGPVDACTHEARYSLSEEKLIRQSIDFRPMNVYASIIQQPIFCNNLDMLPSHTENVSVKVLDCDTIGQVKEKCLETIYRNIPSSQRPRKDDLDLEWRTGATGRVILYDEDVTSKTESEWKKLNTLQHYNVPDGAGLSLVPKQSSIYNFSILSDKNEKSHNRAGSPLNNDMHENGLRYWHLVKHHDSDMQKEGERVNKLVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDDQAQLHGITDPEVVHTWKSNSLPLRFWVNLIKNPNFVFDIHKSNIVDSCLSVVAQTFMDSCSTSDHRLGKDSPSSKLLYAKDIPEYRKWVDRYYRDIRDMSPISDQDMNAMLAEESRLHTTEFNTNCALHELYTYAVKYNEQLTVTLEEDEFSQKQRLAFKLEQVHNIMSSE
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial (EC 2.3.1.41) (Beta-ketoacyl-ACP synthase) (mtKAS) (Q8L3X9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins. Required for mitochondrial fatty acid synthesis (mtFAS). MtFAS are essential for photorespiration and plant development, probably by influencing mitochondrial membrane lipid composition and other lipid metabolic pathways.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14660674}.
Interaction partners:
- Beta-ketoacyl-[acyl-carrier-protein] synthase III, chloroplastic
- EMBRYO DEFECTIVE 3147
- Enoyl-[acyl-carrier-protein] reductase, chloroplastic
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- AT4g13180/F17N18_70
- NAD
- NADPH-dependent aldehyde reductase-like protein, chloroplastic
Sequence:
MATSNLRRHLSASRLRLNRFISTSSSYHSHRRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTLDDLKMKSFDEETKLYTFDQLSSKVAAFVPYGSNPGEFDEALWLNSKAVANFIGYAVCAADEALRDAEWLPTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKFNSSPQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEHATSGTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKRFMPLTTSKKMLVRTAMSNSFGFGGTNASLLFASI
Protein: Protein archease-like (Q9VD92)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RtcB (CG9987).
Interaction partners:
- RNA-splicing ligase RtcB homolog
- ATP-dependent RNA helicase Ddx1
- Eukaryotic peptide chain release factor subunit 1
Sequence:
MEVEFSRENFLLPEMKYEYLDHTADVQIHGWGSSLKEAFEQCGVAMFGYMTELDYVSVEQCFEIEAHGDDLESLLFHFLDELLFLFSAEPYLVCKKLEITKFDVENFEISCHCYGEPFELGKHPQGTEVKAITYSAMQIIQDVEASNYEVFVIIDI
Protein: Alpha-crystallin B chain (Alpha(B)-crystallin) (Heat shock protein beta-5) (HspB5) (Heat shock protein family B member 5) (Renal carcinoma antigen NY-REN-27) (Rosenthal fiber component) (P02511)
Organism: Homo sapiens (Human)
Function: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19464326, ECO:0000269|PubMed:28493373}. Nucleus {ECO:0000269|PubMed:19464326}. Secreted {ECO:0000269|PubMed:32272059}. Lysosome {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (PubMed:19464326). Localizes at the Z-bands and the intercalated disk in cardiomyocytes (PubMed:28493373). Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). {ECO:0000269|PubMed:19464326, ECO:0000269|PubMed:28493373, ECO:0000269|PubMed:32272059}.
Interaction partners:
- Alpha-crystallin A2
- BAG family molecular chaperone regulator 3
- Heat shock protein beta-1
- Beta-crystallin B2
- Gamma-crystallin S
- Gamma-crystallin D
- Heat shock protein beta-2
- Beta-crystallin A3
- Amyloid-beta precursor protein
- Alpha-synuclein
Sequence:
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
Protein: Probable pyridoxal reductase 2 (PL reductase 2) (PL-red 2) (EC 1.1.1.65) (O94521)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable pyridoxamine 5'-phosphate oxidase
- Putative pyridoxal kinase C18.10
- Putative pyridoxal kinase C6F6.11c
Sequence:
MPIVNGFKVGPIGLGLMGLTWRPKQTPIKQAFELMNYALSQGSNYWNAGEFYGINPPTANLDLLADYFEKYPKNADKVFLSVKGGTDFKTLAPHGDPESVTKSVKNALTRLRGKKKLDLFQCARVDHKVPIETTMKALKAFVDSGEISCVGLSEASAESIKRALAIVPIAAVETEYSLFSRDIEKNGILDTCTQLSIPIIAYAPFCHGLLTGRVKTAEDLKDFIKAFPFLRNMDKFNPKVFEKNIPFLKAVEQLAQKFGMSMPEFALNFIIANGKGMIIPIPGSTTVQRAESNLSALKKSLSSEQLEEAKKVLDKHQIFGLRYNKQLESTLSI
Protein: 26S proteasome non-ATPase regulatory subunit 3 (Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 3) (Proteasome 26S subunit, non-ATPase 3) (Q6NYV1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- SEM1 26S proteasome complex subunit.
- Proteasome 26S subunit, ATPase 3
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 8
- Proteasome subunit alpha type
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 7
Sequence:
MKEATAKRREKPKEKNTAEPQDVEMKEEEQRGARELDQTTLDDIREHVKQIEKAVSGKEPRFVLRALRALPSTSRRLNTNVLHKAVSGFFTANAAGKEFLLGFLEQPVEIEGDVPFRPRTGKAAAVPLIPEVEAYLQLLTVVYLTNNKHYTEAQKVSDDLLQKIGSQNRRALDLVAAKCYYYHSRVYEFLNQLDVVRSFLHTRLRTATLRHDADGQATLLNLLLRNYLQYNLYDQAEKLVSKSVFPELANNNEWARYLYYTGRIKAIQLEYSEARRTLTNALRKAPQHTAVGFKQTVHKLLIVVELLLGEIPDRLQFRQPSLKRSLMPYFLLTQAVRTGNLAKFNQVLDQFGEKFQTDGTYTLIIRLRHNVIKTGVRMISLSYSRISLADIAQKLQLDSPEDAEFIVAKAIRDGVIEASINHEKGFVQSKETMDIYSTREPQLAFHQRIAFCLDIHNMSVKAMRFPPKAYNKDLESAEERREREQQDLEFAKEMAEDDDDSFP
Protein: AMP deaminase 2 (EC 3.5.4.6) (AMP deaminase isoform L) (Q01433)
Organism: Homo sapiens (Human)
Function: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle.
Interaction partners:
- Adenylosuccinate synthetase isozyme 2
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Adenylosuccinate lyase
- Inosine-5'-monophosphate dehydrogenase 1
- Inosine-5'-monophosphate dehydrogenase 2
- Hypoxanthine-guanine phosphoribosyltransferase
- AMP deaminase 1
- GMP reductase 1
- Adenylosuccinate synthetase isozyme 1
Sequence:
MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALITQAVQSEMLETIPEEAGITMSPGPQ
Protein: Nuclear factor kappa B subunit 2 (A0A8I6G6F3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDRCYDPGLDGIPEYDDFEFSPSIVEPKDPAPETGQGELPLLITVSLPWNLQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSELGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSKPQGLTEAERRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSKSPGASNLKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVFLQLKRKRGGDVSDSKQFTYYPLVEDKEEVQRKRRKALPTFSQPFGGGSHMGGGSGGSAGGYGGAGGGGSLGFFSSFAYSPYQSGAAPMGCFPGGGGGAQMAGSGRDAEAGEAEEQPRAPSEAPQSEQQALDTLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIAQVIYHAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSAVHLALRAGAAAPDLLQAVLHSGAHALPQMLHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAAERQGGRTPLHLATEMEELGLVTHLVTKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPLPSPPTSGSDSDSEGPETDTQRNFRGHTPLDLTRSTKVKTLLLNAAQNTTEPPLAPPSPAGPGLSLGDAALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLKAPETRDKLPSTEVKEDSAYGSQSVEQEAEKLCPPPEPPGGLCHGHPQPQVH
Protein: ELMO domain-containing protein 2 (Q08DZ3)
Organism: Bos taurus (Bovine)
Function: Acts as a GTPase-activating protein (GAP) toward guanine nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but not for GTPases outside the Arf family.
Interaction partners:
- ADP-ribosylation factor-like protein 3
- ADP-ribosylation factor-like protein 2
- Engulfment and cell motility protein 2
- TBC1 domain family member 9
Sequence:
MFIALWEFFYGHFFRFWMKWLLRQMTGKCELQRIFDTYVGAQRTHRIENSLTYSKNKVLQKATLVVQSEVDRCVEDIMKEKNINPEKDASFKICMKACLLQISGYKQLYLDVESVRKKPYDSDNLQHEKLLIKLWNLLMPTKKLKARISKQWADIGFQGDDPKTDFRGMGILGLINLVYFSENYTSEAHQILSRSNHPKLGYSYAIVGINLTEMAYSLLKSEALKFHLYNFVPGIPTMEHFHQFYCYLVYEFDKFWFEEKPESIMYFNVYREKFHEKIKGLLLDCNVSLTLKI
Protein: Zinc finger protein 445 (Q8R2V3)
Organism: Mus musculus (Mouse)
Function: Transcription regulator required to maintain maternal and paternal gene imprinting, a process by which gene expression is restricted in a parent of origin-specific manner by epigenetic modification of genomic DNA and chromatin, including DNA methylation. Acts by controlling DNA methylation during the earliest multicellular stages of development at multiple imprinting control regions (ICRs). Acts together with ZFP57, but ZFP57 plays the predominant role in imprinting maintenance. In contrast, ZNF445 seems to be the major factor in human early embryonic imprinting maintenance.
Subcellular location: Nucleus {ECO:0000269|PubMed:30602440}. Note=Binds various differentially methylated regions (DMR). {ECO:0000269|PubMed:30602440}.
Interaction partners:
- Transcription intermediary factor 1-beta
- Histone-lysine N-methyltransferase SETDB1
Sequence:
MPPGRWHAARSAQVSREQGCLRMVKEEEEDGYISMQTARPQTLNRPGQELFRQLFRQLRYHESSGPLETLSRLQELCRWWMRPDVLSKAQMLELLVLEQFLSILPGELRTWVQLHCPESGAEVVALLEELQRDLDGTPLKDPCLTQNPDVHWIGTSALQPAQIWSPASHLKNSSALEDHLETSHGIGICDVLAEQTDSPAVSVPDYFQLEEGIEYQEALTFQDVEVTFSQEEWGCLNSAQRNLYRDVILENYGNVVSVVGSSPKPALISWLEARKPWGVNICTVQLKRDADAAPEGGKLQIKPNKFILKQKPSEYIEACVKTSVSPETSVSEETGLKESFKQKSRLQTSCGDSIQMKEMKEGADISQRTGRESEVLRNNDILELKHVKCVSVSRKRLSFKHGYDRNFRKSSHHYNNKYGEGLRGTGEGFGVYQNTGLKENGKDRYGETSRKSWHAHPEHRQPSYSEEGLFQCRVCGKAFKWRSNRIRHEKIHTGVKPYQCSLCEKAFQRLSSYRLHQKTHSKQKRGSSKYKNALTCSLDVSHHLTDRDERKHLHCNQCGKNFSCKSYAIEHQRIHTQEKPYKCTRCRKTFRWKSNFSRHMKLHHKEVYKQEKRQEDFKQSYRQSQVISTVEKTFPCQNCGKTFTQKKSLIEHQRIHTGEKPYQCSGCGETFTYRSSYIIHMKRTQHAIKIKPEHGCLTFSQGAVFPIPRGSHNTEGSNKCKYCGKAFHNRSFLLIHERVHTREKPYQCRECEKAFRWSSNLYRHQRKHFLHKRYKYRESKETSNLQSKILIDQKPFWCQECGKTFTRKRSLLDHKGIHSGERRFKCNLCEKSFDRNYRLVNHQRIHTTEQPQWRDKDFVGIHARSVDQRKHSNTLQSEYGLHSDKPGLSYCQDVRLNIQELSGKLRKECDNPSDESSKSIAFQNVPTKKKACHKCSTCGKTFKKHSHLISHKRCHTKERPFKCIVCGKTFRWSSNLTRHMKNHVRN
Protein: Protein Smaug homolog 2 (Smaug 2) (mSmaug2) (Sterile alpha motif domain-containing protein 4B) (Q80XS6)
Organism: Mus musculus (Mouse)
Function: Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Nanos homolog 1
Sequence:
MMFRDQVGILASWFKGWNECEQTVALLSLLKRVTRTQARFLQLCLEHSLADCNDIHLLESEANSAAIVSQWQQESKEKVVSLLLSHLPLLQPGNTEAKSEYMRLLQKVLAYSIESNAFIEESRQLLSYALIHPATTLEDRNALALWLSHLEERLASGFRTRPEPSYHSRQGSDEWGGPAELAPGEAGPGWQDKPPRENGHVPFHPSSSVPPAINSIGSNANTGLPCQIHPSPLKRSMSLIPTSPQAPGEWPSPEELGARAAFTTPDHAPLSPQSSVASSGSEQTEEQGSSRNTFQEDGSGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNVTKGARHKIALSIQKLRERQSVLKSLEKDVLEGGNLWNALQELQQIIITPIKAYSVLQATPTAKDEGRGEPLLPGAEPPLTHPGSDKGTEAKDPPAAENYPPPPAPAPSDSSEPAPAPVADGDIPSQFTRVMGKVCTQLLVSRPDEENITSYLQLIEKCLTHEAFTETQKKRLLSWKQQVLKLLRTFPRKAALDMQSYRQQKGWAFGSNSLPIAGSVGMGVARRTQRQFPMPPRALPPGRMGLLSPSGIGGVSPRHALTSPSLGGQGRQNLWFANPGGSNSMPSQSRSSVQRTHSLPVHSSPQAILMFPPDCPVPGPDLEINPTLESLCLSMTEHALGDGTDKTSTI