wanglab/gogpt-training-data huggingface dataset:
Protein: Glycosaminoglycan xylosylkinase (EC 2.7.1.-) (Xylose kinase) (Q8VCS3)
Organism: Mus musculus (Mouse)
Function: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22900076}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Xylosyltransferase 1
- Golgi-associated kinase 1A
- UDP-glucuronic acid decarboxylase 1
- Four-jointed box protein 1
- Exostosin-like 2
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Beta-1,3-galactosyltransferase 6
- Xylosyltransferase 2
Sequence:
MKLKQRVVLLAILLVIFIFTKVFLIDNLDTSAANREDQRAFHRMMTGLRVELVPKLDHTLQSPWEIAAQWVVPREVYPEETPELGAIMHAMATKKIIKADVGYKGTQLKALLILEGGQKVVFKPKRYSRDYVVEGEPYAGYDRHNAEVAAFHLDRILGFRRAPLVVGRYVNLRTEVKPVATEQLLSTFLTVGNNTCFYGKCYYCRETEPACADGDMMEGSVTLWLPDVWPLQKHRHPWGRTYREGKLARWEYDESYCDAVKKTSPYDSGPRLLDIIDTAVFDYLIGNADRHHYESFQDDEGASMLILLDNAKSFGNPSLDERSILAPLYQCCIIRVSTWNRLNYLKNGVLKSALKSAMAHDPISPVLSDPHLDTVDQRLLNVLATIKQCTDQFGTDTVLVEDRMPLSHL
Protein: Ankyrin repeat domain 50 isoform 2 (A0A0S2Z6F4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGHREIVEHLLDHGAEVNHEDVDGRTALSVAALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENLNAKL
Protein: Negative regulator of ubiquitin like proteins 1 (C9JRT6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAQKKYLQAKLTQFLREDRIQLWKPPYTDENKKVGLALKDLAKQYSDRLECCENEVEKVIEEIRCKAIERGTGNDNYRTTGIATIEVFLPPRLKKDRKNLLETRLHITGRELRSKIAETFGLQENYIKIVINKKQLQLGKTLEEQGVAHNVKAMVLELKQSEEDARKNFQLEEEEQNEAKLKEKQIQRTKRGLEILAKRAAETVVDPEMTPYLDIANQTGRSIRIPPSERKALMLAMGYHEKGRAFLKRKEYGI
Protein: Protein kinase C inhibitor (Q9I882)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Spindlin-Z
- E2 ubiquitin-conjugating enzyme
Sequence:
MADEIRKAQAARPGGDTIFGKIIRKEIPANIIYEDEQCLAFHDISPQAPTHFLVIPKKPIVRLSEAEDSDESLLGHLMIVGKKCAANLGLTNGFRMVLNEGPEGGQSVYHVHLHILGGRQLGWPPG
Protein: Uncharacterized protein (Q57UZ6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Small ribosomal subunit protein mS41
- Enoyl-CoA hydratase/isomerase domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Opioid growth factor receptor
- LysM domain-containing protein
- Ribosomal protein S9
- Uncharacterized protein
- Pentacotripeptide-repeat region of PRORP domain-containing protein
- Uncharacterized protein
Sequence:
MRRVRDGLFLSHPSSALQCSVAVVSTGEFDHPPFQFRQRHTFNTTPLHDANRFGGRTAYLREIGPVNIKKQGRRFKKDPRTVQFNVDVWCAQQTLRKRWKQRDWEVIEIPFRLVPREQQRVIPELYTDIPQMTDPARNDFSNIRNKVYDREELQGVLFPAAGTMLYPPLQRVDKQAMTLDKYL
Protein: Family with sequence similarity 49 member A (Uncharacterized protein LOC378872 isoform 1) (Uncharacterized protein isoform X2) (Zinc finger protein 395) (Znf395 protein) (Q7ZW35)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
Sequence:
MGNLLKVLTREIENYPHFFLDFENAQPTDCEREVWNQVNAVLQESESILSGLQAYKGAGQEIRDAIQNPNDMLLQERAWNSVCPLVIRLKKFYAFSLKLEQALQSLLESLTCPPYTPTQHLEREQALAKQFAEILHFTLRFDELKMRIPAIQNDFSYYRRTISRNRLNNMNLDIENEVNNEMANRMSLFYAEATPMLKTLSTATTNFVTENKTLPLENTTDCLSTMASVCKVMLETPEYTSRFNSEDTLLFCMRVMVGVIILYDHVHPNGAFNKSSKIDMKGCIKVLKDQPADNVEGLLNALKFTTKHLNDESTPKNIRTMLQ
Protein: Daxx-like protein (DLP) (Q9VMD0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription regulator. Acts as a histone chaperone that facilitates deposition of histone H3.3. Has a role in chromatin remodeling together with asf1 and XNP. Has role in the transcriptional apoptotic response to oxidative and UV stress.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23593018}. Nucleus {ECO:0000269|PubMed:23593018}. Chromosome {ECO:0000269|PubMed:28320872}. Note=Localization to the nucleus is regulated by dj-1beta and oxidative stress (PubMed:23593018). Localizes to pericentric heterochromatin associated with chromosomes X and 4 (PubMed:28320872). {ECO:0000269|PubMed:23593018, ECO:0000269|PubMed:28320872}.
Interaction partners:
- Transcriptional regulator ATRX homolog
- ADD domain-containing protein 1, isoform A
- Ubiquitin carboxyl-terminal hydrolase 7
- Small ubiquitin-related modifier
- Apoptotic signal-regulating kinase 1, isoform C
- Dorsal interacting protein 4
- Mothers against decapentaplegic homolog
- non-specific serine/threonine protein kinase
- Histone H3.3A
- Protein roadkill
Sequence:
MSASVICVDLSSESDEESPAKRRRLEDPLRLLTPSGRQSFPAKLLNIPKASLGSAMVVPVAETGPARETPVIVDPLRSMHIPSGITITKHQKNVLATNGNMNLSLAESNNNNNTTSLNKNVTPKQINVGTGQKVAWSVSSKAPSPNAVITTVPSHQVRVTPFNPIRLAPGSKIIPASNAMPAKIQPILGMGQPQQQAQAQQPKAIIVGFPKPNTAVAQMAQHQKPLTLQIHQKLIAGQQQHIASISQLQQVSLQQQQPLRPVSIQLQQQQNQRNGSLPGKQQKPLECPVPAQQEKLPRGPLPTKPAEPLSGPLPTEPDEPLGGPLPTRPKPPVRSLQQPVNKNTAIGVQIQQSQEPLGGTLPTRQKPLGGQLLTQQKPPVGSIQQSVKQNTGIGVQIQQIPKVVVGQQPQKVYLNKLQQEQQKIFLGHLQQQQQKTFLGQLQQEQQKILGQLQQQKQQQQQQQKKILGQSQQQKVPLGQPQPQQKLPQQLNNSLVQLQQQHQQRTSVGQLQQQQPHQSQQKNSMVHVKQQPQQQKKISVGQFQQQPQQQQKTSVAQLQQQPQQQQKISVGQLQQQSQQQQKPSVGQLQQQSQQQQTPLVGQLQRQTQQQQKTSAGQFQQQPQQQQKISAGQLQEHSQQQQKTLAGQLQQQAQQQLNTSAGQLQQQQKPPKASLAQQAAAQKQGAGLGQQQQFQSQPQQRTSAGLLQQQQMPQKKIVMQPQLPKTSVVLPRPQQLPKNPLLVAQQQSPKTPLVNSVMGPQFPSQQPSLPVVNQITHKSMTIQRLPMLQTVQKILPKQIAPQQTPPPAHIVQKQTMPNAAMQNPPFAHRPPIVRPMTVAKISPVPTNNKVCIPMKPQMASYVSPTDPTMTAARTLPFRSSQRKTSEAPMTSTHVQGFTASATPPQRLLATPPHCAAALNEPLLLNLPPTTSITPQLTPTTTPPPAGPSAAVQQQQLAKAAAIKLNSLPEASISPVNRSPTASAKRIQPITVLKKSDEEWQRHLEQQQQKKHVQLQSSSMTTIVLVESPPTTPPTDKPEPERGPMTVEKSSIKPMATDKQSRAIKRPAVMISTKKSGLVVTEIVDLDEIPDIPPEKRGKECFPPIKNAAKAAPSVNAPFTTEYAALLRLCREVDKSTHMERLVKGELTQYYYSAPESFVMSCGFRNLVTMAMARIRSESYLVYVHLKYVLDELASRRLTKMFPTVRAIPPASQFPLPPASQFPLPPTLTTPKQPAIVKAPGQQTVMAGREQDDEVEEVTLVNVGTVSCEERRRDERIRHFYRTLHAITKRIKMLEEAEVDLNDEDSSYLQLERFKKRACQIYEKICDLKGESKSVRRQLKKPIHFKDSDYPHFNNSLSAFVNRMQDFPDYHDVLQILEKCNKEKELGLAKYEMKRIAYDAFNKVGRMLQSRRKNDLYETVTHYTANGKDPASSDPELLAKLKENNKKQTKISDILEKYALEQDLNAEERQEARLKEKKLKQVKADEEAAKLAALAEDDDKPCTSAQAAAKAAALAALKRGPAARGNVIRKKRAANGRIFKIADDGDDSEEESDSEDDDVEEFVNNFQANSDVSDADSEVEAVTSPKRDALPLAEEEDVIDITRDETGKKNDEGTPNGRLKIMSVSSLNANFVHGQDLHRKPNPMPSAKPVIADQIIISDEES
Protein: Large ribosomal subunit protein uL18 (60S ribosomal protein L5) (Q54XX3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P26321}. Nucleus {ECO:0000250|UniProtKB:P26321}.
Interaction partners:
- 50S ribosomal protein L20
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein eL27
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein eL32
Sequence:
MGFVKVVKTKAYYSRYQVQFRRRREGKTDYQQRHRLITQDKNKYNSPKYRLVARITNTDVIAQVVYSKIVGDFVLCAAYAHELPRFGVKVGLTNYASCYATGLLLARRLLAKLKLADLYKGAEKVDGKVFLVKPVDDKPRPFKANLDVGLARTSTGAKVFAVLKGAVDGGIYVPHGETRFAGYNAESKKLNAETLRGYIFGKHVASYMTLLQTEDEDAYKKIFSQYIKNGVAPKDIETIYANAHKAIRANPAPAAKSTKSYKDIKSKNLSKRTLKQKKARVASIKASYKARL
Protein: Histone deacetylase 1 (HD1) (EC 3.5.1.98) (P56518)
Organism: Strongylocentrotus purpuratus (Purple sea urchin)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Tudor domain-containing protein.
- ARID domain-containing protein.
- Uncharacterized protein.
- HDAC_interact domain-containing protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
Sequence:
MASTGTKKRVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLILNYGLYRKMEIYRPHKAVMEEMTKYHSDDYVKFLRTIRPDNMSEYTKQMQRFNVGEDCPVFDGLYEFCQLSSGGSVAGAVKLNKQQTDIAINWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPLRDGIDDESYDKIFKPIMCKVMEMYQPSAICLQCGADSLSGDRLGCFNLTLKGHAKCVEFMKQYNLPLLLMGGGGYTIRNVARCWTYETSTALGVEIANELPYNDYFEYFGPDFKLHISPSNMTNQNTGEYLDKIKTRLYENMRMIPHAPGVQMQPIPEDAIPDDSDAEDEAENPDKRISIMAQDKRIQRDDEFSDSEDEGETRLPGEGGRRDHRSHKAKRSKIDDSPGKEADKEAKSSDASKEAKPAAEPQAVPMDTTPAPPPKKSEDKPEASKPTEVKAKPAEKEPGEGEASPADLVVPVPKVSAPSEGATLPAVTIPPSSGTSQPPADPPVSAPTPTPASAPAEKQD
Protein: Protein SAAL1 (Synoviocyte proliferation-associated in collagen-induced arthritis protein 1) (SPACIA1) (Q96ER3)
Organism: Homo sapiens (Human)
Function: Plays a role in promoting the proliferation of synovial fibroblasts in response to pro-inflammatory stimuli.
Subcellular location: Nucleus {ECO:0000269|PubMed:22127701}.
Interaction partners:
Sequence:
MDRNPSPPPPGRDKEEEEEVAGGDCIGSTVYSKHWLFGVLSGLIQIVSPENTKSSSDDEEQLTELDEEMENEICRVWDMSMDEDVALFLQEFNAPDIFMGVLAKSKCPRLREICVGILGNMACFQEICVSISSDKNLGQVLLHCLYDSDPPTLLETSRLLLTCLSQAEVASVWVERIQEHPAIYDSICFIMSSSTNVDLLVKVGEVVDKLFDLDEKLMLEWVRNGAAQPLDQPQEESEEQPVFRLVPCILEAAKQVRSENPEWLDVYMHILQLLTTVDDGIQAIVHCPDTGKDIWNLLFDLVCHEFCQSDDPPIILQEQKTVLASVFSVLSAIYASQTEQEYLKIEKVDLPLIDSLIRVLQNMEQCQKKPENSAESNTEETKRTDLTQDDFHLKILKDILCEFLSNIFQALTKETVAQGVKEGQLSKQKCSSAFQNLLPFYSPVVEDFIKILREVDKALADDLEKNFPSLKVQT
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (P31072)
Organism: Trypanosoma brucei brucei
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Interaction partners:
Sequence:
MSMDVGVVGLGVMGANLALNIAEKGFKVAVFNRTYSKSEEFMKANASAPFAGNLKAFETMEAFAASLKKPRKALILVQAGAATDSTTEQLKKVFEKGDILVDTGNAHFKDQGRRAQQLEAAGLRFLGMGISGGEEGARKGPAFFPGGTLSVWEEIRPIVEAAAAKADDGRPCVTMNGSGGAGSCVKMYHNSGEYAILQIWGEVFDILRAMGLNNDEVAAVLEDWKSKNFLKSYMLDISIAAARAKDKDGSYLTEHVMDRIGSKGTGLWSAQEALEIGVPAPSLNMAVVSRQFTMYKTERQANASNAPGITQSPGYTLKNKSPSGPEIKQLYDSVCIAIISCYAQMFQCLREMDKVHNFGLNLPATIATFRAGCILQGYLLKPMTEAFEKNPNISNLMCAFQTEIRAGLQNYRDMVALITSKLEVSIPVLSASLNYVTAMFTPTLKYGQLVSLQRDVFGRHGYERVDKDGRESFQWPELQ
Protein: Vomeronasal 2, receptor 82 (A0A3B2WD03)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLLSWLLIVWFLQMPTFTWIIATHICPTDTKHLIHSDGTVVIGAFFPILHNSRVSKIIDWRYFPMDSDDYFGINARNYQLVLAMLFAVNEINLNSHILPNTSLGLEIYNLPAIGRNIFRTVFSWLTGLSSVIPNYTCRKESKSAATLTGLSWKTSETIWTILDLYKFPQIPHSVCSESCNPGFRKVALESKPTCCFDCTPCPDNEISNETGEGQVSQRIFHSFYSALTKLSKGKK
Protein: Zinc finger protein grt1 (Q9C469)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in the facilitation of anaphase progression in mitosis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:11058086}.
Interaction partners:
- Uncharacterized protein C12C2.04
- Serine O-succinyltransferase
- Brefeldin A resistance protein
- Uncharacterized RING finger protein C6B12.07c
Sequence:
MVLSKRPVRISKACENCRKRKVKCSGGDVCFECQKYNENCVYRQFYRKIKRLKYNNDNSKIDNFSNEQMNIPEFISVRNLNDDSSSIEFFGPASNISFVNQLNHYLRKAERNGYDFLSEGQNDITPEEERKGLEKFGMKLMVLKDNANNFDFSLSNITTEKMNGLLIAYLETWHIPCPIFKAEDLFNLSVRTWKNPSASVHDKALLYLILSIGSAASYFDLQSNSSTLPLARGFFNLALRTVPHIFTELSLDAIRIVFFMSVSAGNLGDTALSYLYSGTAVRMSLAIGLHKCKNFSNDLSDKYQNIRLWVSVWQWEGYWSFCVGRPSCSRQDIPIPAVPNEAFSFSGYGEHGRFLINHEHMRLRVFFSSCCSKIQSEIYSTNRNLLSVLQTVEQISKEVDKEYFSSTNHQLIRSEIGEYCKTLDINSCREWFWIRIYYLYLKLMIFRPFLIFLAYVNISKTSAPDDIIEGLKRGSDQCVQEAIDISKFIVQLNRKVRMLQPIFFICTYLESACTVLLFYIASNSAKIQGQLATEIWAVLRDTCSFLQGSSGPYVGSVSTIAKDALESLNNILVSKKYQDNSVNNTYFDKVMQHVLVHSPAFDDSSDPKFETNRSETPTQYTLDDSANDELMIPDLQGFWEQTLDWINN
Protein: Erbb2 interacting protein (A0A8I6A8N1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTVVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLREFWMDGNRLTFIPGFIGSLRQLTYLDVSKNNIEMVEEGISTCENLQDFLLSSNSLQQLPETIGSLKNVTTLKIDENQLMYLPDSIGGLRSIEELDCSFNEIEALPSSIGQLTNIRTFAADHNYLQQLPPEIGNWKNVTVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPALWEEQRKQRAQVAFECDEDKDEREAPPREGNLKRYPTPYPDELKNMVKTVQTIVHRLKDEETNEESGRDLKQHEDQQVVNKDKGVKPSESITTKSKLDEREKYMNSVPKTSEPEAETNAGNSPVTTNRKSSGNMKHLVNHDDVFEESEELSSDEEMKMAEMRPPLIETSINQPKVVALSNNKKDDAKDTDSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTALCSPAKQIPIDSNSKIRQEDENFNSLLQNGVNLNNSPEEKFKINDKKDFKLPEYDLNIEEQLVLIEKDVDSKATSEDSHQLDHINMNLNKLVTNNIFQPEIMERSKMQDIVLGTGFLSIHSKSEAEHIENGNKFLNSESINKVNGLSEDTAQSPGRIEPQNTSPADVGISKSTEDLSPQRSGPAGSVVKSHSITNMETGGLKIYDILSDDGPQPPGATVKVASTMDGKNIVRSKSATLLYDQPLQVFTASSSSSELLSGTKAVFKFDSNHNPEDPDIIRASIVPGPQSIPQLYGPPQYNVQYSGSAAMKDTLWHPKQNPQIDPVSFPPQRLPRSESAENHSYTKHSANMNFSNHNNVRANTAYHLHQRLAPTRHGEMWAVSPNDRLVPAVSRTTVQRQSSVSSTASVNLGDPGPTRRTEGDYLSYRELHSMGRTPVTSGSQRPLSARAFSIDGPSTSRPQSARPSISEIPERTMSVSDFNYSRTSPSKRPNARVGSEHSLLDPPGKSKVPHDWREQVLRHIEAKKLEKIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFHNAVELIIVREVSS
Protein: T-complex protein 1 subunit theta (TCP-1-theta) (CCT-theta) (P42932)
Organism: Mus musculus (Mouse)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}.
Interaction partners:
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit zeta-2
- Heat shock 70 kDa protein 1B
- Heat shock protein HSP 90-beta
Sequence:
MALHVPKAPGFAQMLKDGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVINRLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGTNFVLVFAGALLELAEELLRIGLSVSEVISGYEIACKKAHEILPELVCCSAKNLRDVDEVSSLLRTSIMSKQYGSETFLAKLIAQACVSIFPDSGNFNVDNIRVCKILGSGIYSSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITETKGTVLIKTAEELMNFSKGEENLMDAQVKAIAGTGANVIVTGGKVADIALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPKLTPPVQEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGGATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALAENSGVKANEVISKLYSVHQEGNKNVGLDIEAEVPAVKDMLEASILDTYLGKYWAIKLATNAAVTVLRVDQIIMAKPAGGPKPPSGKKDWDDDQND
Protein: Leucine rich adaptor protein 1 (Zgc:171930 protein) (A7MC09)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEESNNTCESVPDLKDLELKVGRKTPEGLLKWMREEHKMVSHHQTDNNETEKKGLDGKIRKLKMEMAHLRAADVKILNQLLALHEGIEAVKWLLEERGALTSRCSSLTSSQYSLGEGPDTSWRGSWSSLQDPHDELDNISIGSYLDTLADELDEYCPSSGTESMLCATPMGTGGGVSSSTGSGSRPPQVKTDATKEEAQVWNKAPSETARVNKTNGTLDKTATQLVSSDSPRACLAEKLGKNLSPKVKPYKNGKVELESCKKNGKVQLEYDAHWRWVQSQDDVTFL
Protein: Probable aldo-keto reductase 5 (EC 1.1.1.-) (Q9ASZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NAD
- Aldo/keto reductase
- Aldo-keto reductase family 4 member C8
- Aldo/keto reductase family protein
- NADPH-dependent aldo-keto reductase, chloroplastic
- At2g27680/F15K20.22
- Monodehydroascorbate reductase 2
- Nuclear pore complex protein NUP107
Sequence:
MAEACGVRRIKLGSQGLEVSAQGLGCMGLSAFYGTPKPETEAIALIHHAIHSGVTFLDTSDIYGPETNELLLSKALKDGVREKVELATKYGIRYAEGKVEFKGDPAYVRAACEASLMRVDVACIDLYYQHRIDTRVPIEITIGELKKLVEEGKIKYIGLSEASASTIRRAHAVHPITALQIEWSLWSRDVEEDIIPTCRELGIGIVAYSPLGRGFFASGPKLVENLDNNDVRKTLPRFQQENLDHNKILFEKVSAMSEKKGCTPAQLALAWVHHQGDDVCPIPGTTKIENLNQNIGALSVKLTPEEMSELESLAQPGFVKGERSISILTTFKNSETPPLSSWKAA
Protein: Starvin, isoform E (A8JNS4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Hsc70Cb, isoform G
- Heat shock 70 kDa protein cognate 4
- Endoplasmic reticulum chaperone BiP
- Heat shock protein 68
- E3 ubiquitin-protein ligase CHIP
- Heat shock protein 67B3
- Cyclin-G-associated kinase
Sequence:
MKPTVMAANQAQSNPATAAGNNVSPGGPGVNIPVNREYVSGGYGSPQQSAQFHTPQNAYGSPRQQQQHFQQHQQVPPNQQQQHFQPTFGFEPNMDMDNMFPRSHLGRMHDPFAGFGDSRKRSSLHGPSGQVHADDDFPSYFDDPDFGFPRFSTMGRRGRMAGGANTHMDHDDDFFNRLPSEFRQYIPDGFGGRRGTGAAPAPGQVPQQQQPQPQPQYTQQQPQTHFQFGVPPQQQPVYAGPTQQQVPQTPSKRLCDAAIQTEDPAGRSEVDCAPPTNLNQHGLRNTVDMGVKSVAEQDQGLRSHSAPPPEQQQQNLQYHQQQQQHQQPGVHSQPFGTQTSPPVQGQQFKTYYAPHQQTHPQQKQQTPPPAPQTPGGTYVRTIPIFVEGRSEPIINAHKEIPNQNAPPSAQAQAQAQAYAQAQPQAHAAPQQHNRPTPLNTQAQPEQQVPVEGAAGLPPQTPHTLNSINKIQDIQRDVLELMGKVEQFKGTREEKEYAYLDEMLTRNLLKLDTIDTNGKDSIRLARKEAIKCIQASINVLEAKAEENARAASGAAPAPSATAPAVDTGAVAASEAAGQNAEPVTPQPQDATKMQEPIPLPAPPNAAAVEGAAASEATAAEATQSAVQSETTTTTSE
Protein: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (6PF-2-K/Fru-2,6-P2ase 3) (PFK/FBPase 3) (6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme) (Renal carcinoma antigen NY-REN-56) (iPFK-2) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (Q16875)
Organism: Homo sapiens (Human)
Function: Catalyzes both the synthesis and degradation of fructose 2,6-bisphosphate.
Interaction partners:
- ATP-dependent 6-phosphofructokinase, muscle type
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
- Fructose-1,6-bisphosphatase isozyme 2
- ATP-dependent 6-phosphofructokinase, platelet type
- ATP-dependent 6-phosphofructokinase, liver type
- Fructose-2,6-bisphosphatase TIGAR
- Fructose-1,6-bisphosphatase 1
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
- Mannose-6-phosphate isomerase
- Hexokinase-2
Sequence:
MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH
Protein: S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase alpha chain; S-adenosylmethionine decarboxylase beta chain] (P50244)
Organism: Trypanosoma brucei brucei
Function: In association with the catalytically inactive AdoMetDC prozyme, catalyzes the decarboxylation of S-adenosyl-L-methionine which is essential for the biosynthesis of the polyamine spermidine. Required for growth and survival during the bloodstream life cycle stage.
Interaction partners:
Sequence:
MSSCKDSLSLMAMWGSIARFDPKHERSFEGPEKRLEVIMRVVDGTHVSGLLAHDDDVWQKVIDAICAHIVSREFNEYIRSYVLSESSLFVMKDRVILITCGTITLLNCVPLICEAVSTVCGEVEWVSFMHKNYSFPWEQKGPHLSMAEEFKTLRSHFPSGQPFIFGPIDSDHYFLYFHSDVVQPSCSDDAQLSMTMYGLDRNQTKHWYSDKMLPTGPETAVIREATGLSEVVDDSWILHDLQYEPCGYSINAIRGSEYQTIHITPEEHCSFASYETNTCALNYSKCICGVLRVFDPERFSVIVFIDPDSAVGKSYHSGGTIGVEPEYYPNYEAHHRTVNEYTPGHWVLKVNYVKRAVGTVGTSAASGAKE
Protein: 2'-5' oligoadenylate synthase (EC 2.7.7.84) (Q3ZM02)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGSYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLLKATVQTMRPTIPGRIRNMVTLEHMSTLISLIDPAHSRQHPPHRQKRTGPAPSSECQCILGERAPVLSGPVPSFSGGTLDPEKTKLLSELVYNPGQNPGLLTPGLLCPLSYHR
Protein: 60S ribosomal protein L13 (Q57V54)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L27, putative
- 60S ribosomal protein L7a
- Ribosomal protein
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L28, putative
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L27a
- 60S ribosomal protein L13a, putative
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L6, putative
Sequence:
MPKGNNAIPHVHQRKHWNPCSSQKGNVKVFFNQPAQKQRRRRLRLLKAKKIFPRPLKALRPQVNCPTVRYNMKRRLGRGFSLEELKAAGVKPRYARTIGIRVDRRRKNKSEEGMNINVQRLKTYMSKLVLFPLNRKKPQKGDATEEEVKAATQDRSRYGTAAVGGLVTPAREAPRKVTEEESTKKMYKFLKKNHSAVRFFRARNRRAARKEAKENEKK
Protein: Chromatin-associated protein swi6 (P40381)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Involved in the repression of the silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes.
Subcellular location: Nucleus {ECO:0000269|PubMed:18761674, ECO:0000305|PubMed:20929775}. Chromosome {ECO:0000269|PubMed:18761674}. Note=Disperses from heterochromatin at the G1/S-phase transition. {ECO:0000269|PubMed:18761674}.
Interaction partners:
- Putative JmjC domain-containing histone demethylation protein 1
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Histone H3.1/H3.2
- Histone deacetylase clr3
- Protein Dicer
- Chromo domain-containing protein 1
- Protein argonaute
- Histone deacetylase clr6
- RNA-dependent RNA polymerase 1
- RNA-induced transcriptional silencing complex protein tas3
Sequence:
MKKGGVRSYRRSSTSKRSVIDDDSEPELPSMTKEAIASHKADSGSSDNEVESDHESKSSSKKLKENAKEEEGGEEEEEDEYVVEKVLKHRMARKGGGYEYLLKWEGYDDPSDNTWSSEADCSGCKQLIEAYWNEHGGRPEPSKRKRTARPKKPEAKEPSPKSRKTDEDKHDKDSNEKIEDVNEKTIKFADKSQEEFNENGPPSGQPNGHIESDNESKSPSQKESNESEDIQIAETPSNVTPKKKPSPEVPKLPDNRELTVKQVENYDSWEDLVSSIDTIERKDDGTLEIYLTWKNGAISHHPSTITNKKCPQKMLQFYESHLTFRENE