wanglab/gogpt-training-data huggingface dataset:
Protein: MIP30126p (Polycystic kidney disease 2) (Polycystin-2) (Q9VK95)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Transient receptor potential cation channel trpm
- Inactive
- No mechanoreceptor potential C, isoform H
- Transient receptor potential cation channel subfamily A member 1
- Ankyrin 2, isoform U
- Ankyrin, isoform B
- Intraflagellar transport 20
- No mechanoreceptor potential B, isoform D
Sequence:
MAQQGQSGRSPSGPPGPPPPRPPKTPPGASPRGTPTADSTPGDVTPARGPPPPPATKRVSIGVGSTRSAPPPATDPTGPPPTAGKPVRDTGPSTSPRPSLRDPGQSTSDKPSTSDKPSTSDKPSTSARTTVREPGPSSSPSRPVSTRESGRITFQEAAPSTSAKVVKLAASEPRPAKPPEKEGFSLFKRKKKSVGSSTPPSPSRGHRAPSIIAASALQNRAKTNRILYTTDEEVREALVEFSVFIIFLILTSLVVLSVRHTYMFYFNDTMKKLFTNREMVVAPSVTVGFEKLITVPDWWDYLKYNFLVTLHGDLTFMDDAQANLTSMPPEGSEQGSEQGSEQGSEQSPEEVVGEAPEEAPEMDRLQEDFKYNGNPYIDLRGHRRAKRQSGVDGNSEDGSEDVSGNYLKDDSDSIQANMSFHHLEGRVFLYENLLLGPPRLRQIRVRKESCYVNDAFIRYFNTCYAAYSSGAEDRKPMHKGSPFRTMHDLDSTPIWTVLAFYRTGGYTVNLDYDKDRNVKIINDLKDIHWLDRGSRLCLVEFNLFNENTDIFQSIKLIAEIPPTGGVIPQAHLQTVKMYSFFTDRSMLMTVIYIFWYIMVIYYTIYEITEIRKSGIKIYFCSMLNILDCAILLGCYLALVYNIWHSFKVMSLTARAHSDVTYQSLDVLCFWNIIYVDMMAILAFLVWIKIFKFISFNKTLVQFTTTLKRCSKDLAGFSLMFGIVFLAYAQLGLLLFGTKHPDFRNFITSILTMIRMILGDFQYNLIEQANRVLGPIYFLTYILLVFFILLNMFLAIIMETYNTVKGEITQGRSHLGSYIYRKLSGMLYWITHCGRKRRHHPQASETEDKDAEHDVGAAHDETHEIRKNMTPAEQQYFKDIPQGENQDMVRLNNRVGLLEEILEKLINNMDDILKRVEKDYHNKKK
Protein: Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG8 (EC 3.2.2.n1) (LOG family protein At5g11950) (Protein LONELY GUY 8) (Q84MC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19837870}. Nucleus {ECO:0000269|PubMed:19837870}.
Interaction partners:
- Cytokinin dehydrogenase 7
- Adenylate isopentenyltransferase 1, chloroplastic
- tRNA dimethylallyltransferase 9
Sequence:
MEDNQRSRFRKICVFCGSHSGHREVFSDAAIELGNELVKRKIDLVYGGGSVGLMGLISRRVYEGGLHVLGIIPKALMPIEISGETVGDVRVVADMHERKAAMAQEAEAFIALPGGYGTMEELLEMITWSQLGIHKKTVGLLNVDGYYNNLLALFDTGVEEGFIKPGARNIVVSAPTAKELMEKMEEYTPSHMHVASHESWKVEELGDYPGQENKPQ
Protein: Mcf.2 transforming sequence-like (Q6PDM6)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MALEEMVQRLNAVSKNTDEIMHQDIVPLCAADIQEQLKKRFAYLSGGRGQDGSPVITFPDYPAFSEIPDKEFQNVMTYLTSIPSLQDAGIGFILVIDRRQDKWTSVKASVLRIAASFPANLQLVLVLRPTGFFQRTLSDIAFKFNRDEFKMKVPVMMLSSVPELHGYIDKSQLTEDLGGTLDYCHSRWLCHRTAIESFALMVKQTAQMLQAFGTELAETELPNDVQSTSLVLSAHTEKKAKVKEDLQLALKEGNSILESLREPLAESAAHSVNQDQLDNQATVQRLLAQLNETEAAFDEFWAKHQQKLEQCLQLRHFEQGFREVKTTLDSMSQKIAAFTDVGNSLAHVQHLLKDLTAFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHPKCEELQHLCDHFASEVTRRRGLLSKSLELHSLLETSMKWSDEGIFLLASQPVDKCQSQDGAEAALQEIEKFLETGAENKIQELNEIYKEYECILNQDLLEHVQKVFQKQESTEEMFHRRQASLKKLAAKQTRPVQPVAPRPEALTKSPSPSPGSWRSSENSSSEGNALRRGPYRRAKSEMSEPRQGRTSSTGEEEESLAILRRHVMNELLDTERAYVEELLCVLEGYAAEMDNPLMAHLISTGLQNKKNILFGNMEEIYHFHNRIFLRELESCIDCPELVGRCFLERMEEFQIYEKYCQNKPRSESLWRQCSDCPFFQECQKKLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSKHCEGAEDLQEALSSILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWTDHKKGHTKVKELARFKPMQRHLFLHEKAVLFCKKREENGEGYEKAPSYSYKQSLNMTAVGITENVKGDTKKFEIWYNAREEVYIIQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRALEQSHSLPLPTPSSTSPTKGNTRNVKKLEDRKTDPLSLEGYVSSSLPKPPEKGKDDAVPSSTSESSALSRKRFTLQGLANLKGQKASPTSPDKKAKRHEVKSDPTPFGLRGWSKTSHSLEAPEEDGGWSSAEELINSSDAEEDGGVGPKKLVPGKYTVVMDDEKGGPDTLAMRSGDMVEVVEEGAEGLWYVRDLTSSKEGWVPASSLSTLLGKSSSAQCLSSSGKIHCARQLCPEPAEILSPEPV
Protein: Ephrin-A1 (EPH-related receptor tyrosine kinase ligand 1) (LERK-1) (Immediate early response protein B61) [Cleaved into: Ephrin-A1, secreted form] (P97553)
Organism: Rattus norvegicus (Rat)
Function: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P20827}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P20827}.; SUBCELLULAR LOCATION: [Ephrin-A1, secreted form]: Secreted {ECO:0000250|UniProtKB:P20827}.
Interaction partners:
- Ephrin type-A receptor 2
- Ephrin type-A receptor 1
- receptor protein-tyrosine kinase
- Ephrin type-A receptor 10
- Ephrin type-A receptor 8
- Ephrin type-A receptor 3
- Ephrin type-A receptor 7
- Ephrin type-B receptor 1
- Ephrin type-A receptor 5
- Ras GTPase-activating protein 1
Sequence:
MEFLWAPLLGLCCSLAAADRHIVFWNSSNPKFREEDYTVHVQLNDYLDIICPHYEDDSVADAAMERYTLYMVEHQEYVTCEPQSKDQVRWKCNQPSAKHGPEKLSEKFQRFTPFTLGKEFKEGHSYYYISKPIYHQETQCLKLKVTVNGKITHSPHAHANPQEKRLQADDPEVQVLHSIGHSAAPRLFPLVWAVLLLPLLLLQTQ
Protein: Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (SSAT) (SSAT-1) (P48026)
Organism: Mus musculus (Mouse)
Function: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine (By similarity). This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines (By similarity). Also involved in the regulation of polyamine transport out of cells (By similarity). Also acts on 1,3-diaminopropane and 1,5-diaminopentane (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P21673}.
Interaction partners:
- Ornithine decarboxylase
- Gene model 853
- Spermidine synthase
- Guanidino acid hydrolase, mitochondrial
- Thialysine N-epsilon-acetyltransferase
- Amine oxidase
- Amine oxidase
- Amine oxidase
- Diamine oxidase [copper-containing]
- Amine oxidase [flavin-containing] B
Sequence:
MAKFKIRPATASDCSDILRLIKELAKYEYMEDQVILTEKDLQEDGFGEHPFYHCLVAEVPKEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMAAEE
Protein: Alpha-mannosidase (EC 3.2.1.-) (A0A0G2K8F6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Alpha-mannosidase 2C1
- Alpha-mannosidase
- Zona pellucida-binding protein 2
- Membrane cofactor protein
- ADAM metallopeptidase domain 3A.
- Zona pellucida sperm-binding protein 3 receptor
Sequence:
MGLLRWLPLLGQLLLLWPLAARPASPIRAFVVPHSHMDVGWVYTVQESMRAYAANVYTTVVEELVRGRQRRFIAVEQEFFRLWWDGVASEQQKQQVRQLLDEGRLEFVLGGQVMHDEAVTHLDDQILQLTEGHGFLYETFGIRPQFSWHVDPFGASATTPTLFALAGFNAHLISRIDYDLKDAMQEAQGLQFVWHGSPSLSEQQEIYTHVMDLYSYCTPSHIPFSNRSGFYWNGVAVFPEPPPDGVYPNMSEPVTVDNIHLYAEALVANVKQRAAWFRTPHVLWPWGCDKQFFNASVQFDNMDPLLEYINNRSAQFGISVQYATLNDYFQALHDFNVTWDIRDHHDFLPYSSEPQQAWTGFFTSRSTLKGLARQASALLYAGESMFTRYMWPHPRGTLDPTWALQQLQQLRWAVSEVQHHDAITGTESPKVKNMYMEHLSMGMRGVHKLMASIALDRPPGSGTGAPKNIRGPQVTPVLSVDTRPVGYSASVYNPLAWKITTIITLTVAFPSVSVTDELGRPVSAQIQNSTKDPSAYDLLILTTIPGLSYRHYKVRRTRGDQAGTRELVTPRANTLKFSRKLRNQTSQEGKLLVPVMNDCYTLLFDQDTNMLHSIQDRQSNRTVHMTQEFLEYRANGDVKQGPISDNYLFASNDTAEPSWEAVGMEMVVGTLATDVRQYFYRNITDQGYIYSIHTRLAHVHPSLAGELLCRRIEQQYQVGPLDLNREAILRTSSDLNSQQVLYSDNNGYQMQRRPYKAFKSNPIPRNYYPMVQSAFIEDDKSRLVLLAERPHGVSSQENGQVEVMLHRRLWNNLVWDLNYNLTLNDTSVVHPVLWLLLGPKSTTTALRPRSGVALQHRPVVLLKELTDEEETAIHRPHHPWPVTLPPSLHLQVLSLPGWQYSRNHAQHLKNLQRGHPEKPQVNLQRVLLRLHHLYEAGEDPVLSRPATVDLKIALRGLGSVVAVEERSLTGTWDVQTLQRWHWRTKIGQLKGHPTSPPRSPGGSIITVYPKEIRTFFIYLQQ
Protein: L-xylulose reductase (XR) (EC 1.1.1.10) (Carbonyl reductase II) (Dicarbonyl/L-xylulose reductase) (Kidney dicarbonyl reductase) (kiDCR) (Short chain dehydrogenase/reductase family 20C member 1) (Sperm surface protein P34H) (Q7Z4W1)
Organism: Homo sapiens (Human)
Function: Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Probably recruited to membranes via an interaction with phosphatidylinositol. {ECO:0000250}.
Interaction partners:
- Aldo-keto reductase family 1 member B1
- Sorbitol dehydrogenase
- Aldo-keto reductase family 1 member B10
Sequence:
MELFLAGRRVLVTGAGKGIGRGTVQALHATGARVVAVSRTQADLDSLVRECPGIEPVCVDLGDWEATERALGSVGPVDLLVNNAAVALLQPFLEVTKEAFDRSFEVNLRAVIQVSQIVARGLIARGVPGAIVNVSSQCSQRAVTNHSVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTSMGQATWSDPHKAKTMLNRIPLGKFAEVEHVVNAILFLLSDRSGMTTGSTLPVEGGFWAC
Protein: Protein NLP8 (AtNLP8) (NIN-like protein 8) (Nodule inception protein-like protein 8) (O22864)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00852}.
Interaction partners:
- Abscisic acid 8'-hydroxylase 2
- LOB domain-containing protein 37
- MOB kinase activator-like 1B
- Protein NRT1/ PTR FAMILY 6.3
- Ferredoxin--nitrite reductase, chloroplastic
- MOB kinase activator-like 2A
- Putative MOB kinase activator-like 2B
- LOB domain-containing protein 39
- MADS-box transcription factor ANR1
- Transcription factor TCP20
Sequence:
MENPFASREKGFGNYSDFPTEQMDGLSSNFGSGVRNLISDDMFNPSSELMNFDSLAAWCNSPSATDILFAQYGLSNSQPMPFGAFTSFHVADPKATSLTRSFYDLESSYYGEERSSAQEMNSQFHRSSDSDELSGKRRKVVNQKIGFPNVLNCTIPRSLSHSLDEKMLKALSLFMESSGSGEGILAQVWTPIKTGDQYLLSTCDQAYLLDPRFSQYREVSRRFTFAAEANQCSFPGLPGRVFISGVPEWTSNVMYYKTDEYLRMKHAIDNEVRGSIAIPILEASGTSCCAVMELVTSKEKPNFDMEMDSVCRALQAVNLRTAAIPRPQYLSSSQRDALAEIQDVLRTVCHAHKLPLALAWIPCRKDQSIRVSGQKSGENCILCIEETACYVNDMEMEGFVHACLEHCLREKEGIVGKAFISNQPFFSSDVKAYDISEYPIVQHARKYGLNAAVAIKLRSTYTGEDDYILELFLPVSMKGSLEQQLLLDSLSGTMQRICRTLRTVSEVGSTKKEGTKPGFRSSDMSNFPQTTSSENFQTISLDSEFNSTRSMFSGMSSDKENSITVSQGTLEQDVSKARTPEKKKSTTEKNVSLSALQQHFSGSLKDAAKSLGGETSAYFQAWVYFFCPTTLKRICRQHGIMRWPSRKINKVNRSLRKIQTVLDSVQGVEGGLKFDSATGEFIAVRPFIQEIDTQKGLSSLDNDAHARRSQEDMPDDTSFKLQEAKSVDNAIKLEEDTTMNQARPGSFMEVNASGQPWAWMAKESGLNGSEGIKSVCNLSSVEISDGMDPTIRCSGSIVEPNQSMSCSISDSSNGSGAVLRGSSSTSMEDWNQMRTHNSNSSESGSTTLIVKASYREDTVRFKFEPSVGCPQLYKEVGKRFKLQDGSFQLKYLDDEEEWVMLVTDSDLQECLEILHGMGKHSVKFLVRDLSAPLGSSGGSNGYLGTGL
Protein: SAP domain-containing protein, putative (C0H535)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- RNA helicase
- RNA and export factor binding protein, putative
Sequence:
MSNYQNLKCSELKDLLAKRGLPSHGKKNELLERLLKHEEKDNINSLSSSYILDNSNINNDDNKNNNFSFQNNASNNSLNLQSSSNLIFEKKTVDSFGKVDDNNKKTIPSVNNKEDSNNKIGLNKMKNYIRNILTINSNTPNSTYDKNNGTNDHKNNPNKDSNDQKSKIVIQEITFNDVSSSSQNTLQRNIISTDDNDSYLSEEKKRELRRKRFGVVNTDDALESRAKRFSIVTHKMEEENKRKRAERFGLNVVKMNDFEKKKKRAERFGLLQDSEKLKARALRFGITQ
Protein: Isovaleryl-CoA dehydrogenase, mitochondrial (IVD) (EC 1.3.8.4) (Butyryl-CoA dehydrogenase) (EC 1.3.8.1) (Q9JHI5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P12007}.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Peroxisomal bifunctional enzyme
- Trifunctional enzyme subunit alpha, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit beta
- Electron transfer flavoprotein subunit alpha, mitochondrial
Sequence:
MATAIRLLGRRVSSWRLRPSPSPLAVPRRAHSILPVDDDINGLNEEQKQLRHTISKFLQENLAPKAQEIDQTNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCVNQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMKLKAEKKGDHYVLNGNKFWITNGPDADILVVYAKTDLTAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANVLSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMASRQYVYNVAKACDEGHIIPKDCAGVILYAAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFR
Protein: Protein inhibitor of activated STAT-1 (A9UK05)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus, nuclear body {ECO:0000256|ARBA:ARBA00034306}.
Interaction partners:
Sequence:
MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQIGSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRTYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGSWAPMRSKKEVQEVTASYNGVDGCLSSTLEHQVASHNQSSNKNKKVEVIDLTIDSSSDEEEEEPPAKRTCPSLSPTSPLSNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPATNGSSSGSNSSLVSSNSLRESHGHGVASRSSADTASIFGIIPDIISLD
Protein: F-box/LRR-repeat protein 2 (F-box and leucine-rich repeat protein 2) (F-box protein FBL2/FBL3) (Q9UKC9)
Organism: Homo sapiens (Human)
Function: Calcium-activated substrate recognition component of the SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex, SCF(FBXL2), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. This is the case for the cyclins CCND2 and CCND3 which polyubiquitination and subsequent degradation are inhibited by calmodulin. Through CCND2 and CCND3 degradation induces cell-cycle arrest in G(0). SCF(FBXL2) also mediates PIK3R2 ubiquitination and proteasomal degradation thereby regulating phosphatidylinositol 3-kinase signaling and autophagy. PCYT1A monoubiquitination by SCF(FBXL2) and subsequent degradation regulates synthesis of phosphatidylcholine, which is utilized for formation of membranes and of pulmonary surfactant (By similarity). The SCF(FBXL2) complex acts as a regulator of inflammation by mediating ubiquitination and degradation of TRAF proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5 and TRAF6) (By similarity). The SCF(FBXL2) complex acts as a negative regulator of the NLRP3 inflammasome by mediating ubiquitination and degradation of NLRP3.
Subcellular location: Membrane {ECO:0000269|PubMed:15893726}; Lipid-anchor {ECO:0000269|PubMed:15893726}.
Interaction partners:
- S-phase kinase-associated protein 1
- Geranylgeranyl transferase type-2 subunit beta
- Cullin-1
- Protein prenyltransferase alpha subunit repeat-containing protein 1
- Phosphatidylinositol 3-kinase regulatory subunit beta
- F-box only protein 3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
Sequence:
MVFSNNDEGLINKKLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRIDLFNFQTDVEGRVVENISKRCGGFLRKLSLRGCIGVGDSSLKTFAQNCRNIEHLNLNGCTKITDSTCYSLSRFCSKLKHLDLTSCVSITNSSLKGISEGCRNLEYLNLSWCDQITKDGIEALVRGCRGLKALLLRGCTQLEDEALKHIQNYCHELVSLNLQSCSRITDEGVVQICRGCHRLQALCLSGCSNLTDASLTALGLNCPRLQILEAARCSHLTDAGFTLLARNCHELEKMDLEECILITDSTLIQLSIHCPKLQALSLSHCELITDDGILHLSNSTCGHERLRVLELDNCLLITDVALEHLENCRGLERLELYDCQQVTRAGIKRMRAQLPHVKVHAYFAPVTPPTAVAGSGQRLCRCCVIL
Protein: Symplekin (Q80X82)
Organism: Mus musculus (Mouse)
Function: Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:Q92797}. Nucleus, nucleoplasm {ECO:0000250}. Note=Cytoplasmic face of adhesion plaques (major) and nucleoplasm (minor) (in cells with TJ). Nucleoplasm (in cells without TJ). Nuclear bodies of heat-stressed cells. Colocalizes with HSF1 in nuclear stress bodies upon heat shock. {ECO:0000250|UniProtKB:Q92797}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage stimulation factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 1
- pre-mRNA 3' end processing protein WDR33
- Cleavage stimulation factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 3
- Pre-mRNA cleavage complex 2 protein Pcf11
- Cleavage and polyadenylation specificity factor subunit 4
- Pre-mRNA 3'-end-processing factor FIP1
- WD repeat-containing protein 82
Sequence:
MASSSGDSVTRRSVASQFFTQEEGPSIDGMTTSERVVDLLNQAALITNDSKITVLKQVQELIINKDPTLLDNFLDEIIAFQADKSIEVRKFVIGFIEEACKRDIELLLKLIANLNMLLRDENVNVVKKAILTMTQLYKVALQWMVKSRVISDLQEACWDMVSSMAGEIILLLDSDNDGIRTHAIKFVEGLIVTLSPRMADSEVPRRQEHDISLDRIPRDHPYIQYNVLWEEGKAAVEQLLKFMVHPAISSINLTTALGSLANIARQRPMFMSEVIQAYETLHANLPPTLAKSQVSSVRKNLKLHLLSVLKHPASLEFQAQITTLLVDLGTPQAEIARNMPSSKDSRKRPRDDTDSTLKKMKLEPNLGEDDEDKDLEPGPSGTSKASAQISGQSDTDITAEFLQPLLTPDNVANLVLISMVYLPETMPASFQAIYTPVESAGTEAQIKHLARLMATQMTAAGLGPGVEQTKQCKEEPKEEKVVKPESVLIKRRLSVQGQAISVVGSQSTMSPLEEEVPQAKRRPEPIIPVTQPRLAGAGGRKKIFRLSDVLKPLTDAQVEAMKLGAVKRILRAEKAVACSGAAQVRIKILASLVTQFDSGFKAEVLSFILEDVRARLDLAFAWLYQEYNAYLAAGTSGTLDKYEDCLICLLSGLQEKPDQKDGIFTKVVLEAPLITESALEVIRKYCEDESRAYLGMSTLGDLIFKRPSRQFQYLHVLLDLSSHEKDRVRSQALLFIKRMYEKEQLREYVEKFALNYLQLLVHPNPPSVLFGADKDTEVAAPWTEETVKQCLYLYLALLPQNHKLIHELAAVYTEAIADIKRTVLRVIEQPIRGMGMNSPELLLLVENCPKGAETLVTRCLHSLTDKVPPSPELVKRVRDLYHKRLPDVRFLIPVLNGLEKKEVIQALPKLIKLNPIVVKEVFNRLLGTQHGEGNSALSPLNPGELLIALHNIDSVKCDMKSIIKATNLCFAERNVYTSEVLAVVMQQLMEQSPLPMLLMRTVIQSLTMYPRLGGFVMNILARLIMKQVWKYPKVWEGFIKCCQRTKPQSFQVILQLPPQQLGAVFDKCPELREPLLAHVRSFTPHQQAHIPNSIMTILEATGKQEPEVKEAPSGPLEEDDLEPLALALAPAPAPAPAPAPAPAPAPRPPQDLIGLRLAQEKALKRQLEEEQKQKPTGIGAPAACVSSTPSVPAAARAGPTPAEEVMEYREEGPECETPAIFISMDDDSGLAETTLLDSSLEGPLPKEAAAVGSSSKDERSPQNLSHAVEEALKTSSPETREPESKGNS
Protein: NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 3) (NADH-plastoquinone oxidoreductase subunit 3) (P0C322)
Organism: Oryza sativa subsp. japonica (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01394}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01394}.
Interaction partners:
- NAD
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
Sequence:
MFLLHEYDIFWAFLIIASLIPILAFWISALLAPVREGPEKLSSYESGIEPMGGAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGISVFIEAFIFVLILVVGLVYAWRKGALEWS
Protein: Thymocyte nuclear protein 1 (Thymocyte protein Thy28) (Q9P016)
Organism: Homo sapiens (Human)
Function: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 1
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
MSRPRKRLAGTSGSDKGLSGKRTKTENSGEALAKVEDSNPQKTSATKNCLKNLSSHWLMKSEPESRLEKGVDVKFSIEDLKAQPKQTTCWDGVRNYQARNFLRAMKLGEEAFFYHSNCKEPGIAGLMKIVKEAYPDHTQFEKNNPHYDPSSKEDNPKWSMVDVQFVRMMKRFIPLAELKSYHQAHKATGGPLKNMVLFTRQRLSIQPLTQEEFDFVLSLEEKEPS
Protein: Histone H2B type 1-P (Q8CGP2)
Organism: Mus musculus (Mouse)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H3.2
- Histone H3.1
- Histone H3.3
- Histone H4
- Plasminogen
- E3 ubiquitin-protein ligase BRE1A
- E3 ubiquitin-protein ligase BRE1B
- Histone H2AX
- Histone H2A type 2-C
- Histone H3-like centromeric protein A
Sequence:
MPEPVKSVPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Poly(A) binding protein, nuclear 1 (G3V7Z8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Poly
- Nuclear cap-binding protein subunit 1
- ELAV-like protein 1
- Embryonic polyadenylate-binding protein 2
- Nuclear cap-binding protein subunit 2
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 5
- Serine/arginine-rich splicing factor 9
- Serine/arginine-rich splicing factor 3
- Splicing factor U2AF subunit
Sequence:
MAAAAAAAAAAGAAGGRGSGPGRRRHLVPGAGGEAGEGDPGGAGDYGNGLESEELEPGELLPEPEPEEEPPRPRAPPGAPGPGPGSGAPGSQEEEEEPGLVETDPGDGAIEDPELEAIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSLEEKMEADARSIYVGNVDYGATAEELEAHFHGCGSVNRVTILCDKFSGHPKGFAYIEFSDKESVRTSLALDESLFRGRQIKVIPKRTNRPGISTTDRGFPRARYRARTTNYNSSRSRFYSGFNSRPRGRIYRGRARATSWYSPY
Protein: Regulator of chromosome condensation (D6XFK1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIRDAEFWIEARRLSNRGNSIFTTLLPLLHSRQLALDSGVQVNEINPACKEVPLTENLQRKEPYEENKTLQLPSATAPRGSVSESTLRVLQQAMMFAVPMYALRYQVTGMSMSSKTSAVVDRETKQVATFGAGDGVHIPNNIRCRGCAAGDNFFAVLTDQEEVWASGGLHVLTCDEGTLTASPLGKSNEMKKVASKALMVVGNGQRLSCLTESLSVQPLSVVLNPVTSIFPFRRIRFMDMGYGDDCYMVGMDSVLYKTVVSSRTLGTPRRIMTLSRTTVSRVASGSGFYVFIDENGQLYTIGCNNKGQLGNGQKQHARRRPFLHQSLRHHYFVMAAAGSGHSLALTSSGMVYGAGNNESGQLGLGEHVTEVLTFTPIPLPAKCTGIAAGPKGSMFACANGCVYTCGANDLRQLGLDVDDPVVYRPMPMPAVTSGVEAYYMDFGAYRSPPVAVLRSFCSSIPSLDVSDLDKPEVLPKPVSSTVSVVSEEVPDTPQLPSPLLPEDGVENLPEPSVNHHPSKRRERKEIKEEREKQSCGKCCVVL