wanglab/gogpt-training-data huggingface dataset:
Protein: Cleavage and polyadenylation specificity factor subunit 1 (Cleavage and polyadenylation specificity factor 160 kDa subunit) (CPSF 160 kDa subunit) (Q10570)
Organism: Homo sapiens (Human)
Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction. May play a role in eye morphogenesis and the development of retinal ganglion cell projections to the midbrain (By similarity).
Subcellular location: Nucleus, nucleoplasm.
Interaction partners:
- Symplekin
- Pre-mRNA 3'-end-processing factor FIP1
- Cleavage stimulation factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 4
- pre-mRNA 3' end processing protein WDR33
- Cleavage stimulation factor subunit 2
- Poly
- Pre-mRNA cleavage complex 2 protein Pcf11
Sequence:
MYAVYKQAHPPTGLEFSMYCNFFNNSERNLVVAGTSQLYVYRLNRDAEALTKNDRSTEGKAHREKLELAASFSFFGNVMSMASVQLAGAKRDALLLSFKDAKLSVVEYDPGTHDLKTLSLHYFEEPELRDGFVQNVHTPRVRVDPDGRCAAMLVYGTRLVVLPFRRESLAEEHEGLVGEGQRSSFLPSYIIDVRALDEKLLNIIDLQFLHGYYEPTLLILFEPNQTWPGRVAVRQDTCSIVAISLNITQKVHPVIWSLTSLPFDCTQALAVPKPIGGVVVFAVNSLLYLNQSVPPYGVALNSLTTGTTAFPLRTQEGVRITLDCAQATFISYDKMVISLKGGEIYVLTLITDGMRSVRAFHFDKAAASVLTTSMVTMEPGYLFLGSRLGNSLLLKYTEKLQEPPASAVREAADKEEPPSKKKRVDATAGWSAAGKSVPQDEVDEIEVYGSEAQSGTQLATYSFEVCDSILNIGPCANAAVGEPAFLSEEFQNSPEPDLEIVVCSGHGKNGALSVLQKSIRPQVVTTFELPGCYDMWTVIAPVRKEEEDNPKGEGTEQEPSTTPEADDDGRRHGFLILSREDSTMILQTGQEIMELDTSGFATQGPTVFAGNIGDNRYIVQVSPLGIRLLEGVNQLHFIPVDLGAPIVQCAVADPYVVIMSAEGHVTMFLLKSDSYGGRHHRLALHKPPLHHQSKVITLCLYRDLSGMFTTESRLGGARDELGGRSGPEAEGLGSETSPTVDDEEEMLYGDSGSLFSPSKEEARRSSQPPADRDPAPFRAEPTHWCLLVRENGTMEIYQLPDWRLVFLVKNFPVGQRVLVDSSFGQPTTQGEARREEATRQGELPLVKEVLLVALGSRQSRPYLLVHVDQELLIYEAFPHDSQLGQGNLKVRFKKVPHNINFREKKPKPSKKKAEGGGAEEGAGARGRVARFRYFEDIYGYSGVFICGPSPHWLLVTGRGALRLHPMAIDGPVDSFAPFHNVNCPRGFLYFNRQGELRISVLPAYLSYDAPWPVRKIPLRCTAHYVAYHVESKVYAVATSTNTPCARIPRMTGEEKEFETIERDERYIHPQQEAFSIQLISPVSWEAIPNARIELQEWEHVTCMKTVSLRSEETVSGLKGYVAAGTCLMQGEEVTCRGRILIMDVIEVVPEPGQPLTKNKFKVLYEKEQKGPVTALCHCNGHLVSAIGQKIFLWSLRASELTGMAFIDTQLYIHQMISVKNFILAADVMKSISLLRYQEESKTLSLVSRDAKPLEVYSVDFMVDNAQLGFLVSDRDRNLMVYMYLPEAKESFGGMRLLRRADFHVGAHVNTFWRTPCRGATEGLSKKSVVWENKHITWFATLDGGIGLLLPMQEKTYRRLLMLQNALTTMLPHHAGLNPRAFRMLHVDRRTLQNAVRNVLDGELLNRYLYLSTMERSELAKKIGTTPDIILDDLLETDRVTAHF
Protein: CCA tRNA nucleotidyltransferase, mitochondrial (EC 2.7.7.72) (CCA-adding enzyme) (tRNA CCA-pyrophosphorylase) (tRNA adenylyltransferase) (tRNA nucleotidyltransferase) (P21269)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This enzyme carries out synthesis of the tRNA CCA terminus without the direction of a template using the multiple accepting and donating subsites within its active site.
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:1634528, ECO:0000269|PubMed:8175766}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic+nuclear 1]: Cytoplasm {ECO:0000269|PubMed:1634528, ECO:0000269|PubMed:8175766}. Nucleus {ECO:0000269|PubMed:8175766}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic+nuclear 2]: Cytoplasm {ECO:0000269|PubMed:1634528, ECO:0000269|PubMed:8175766}. Nucleus {ECO:0000269|PubMed:8175766}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 8
- Ribonuclease Z
- Pentafunctional AROM polypeptide
- tRNA
- Exportin-T
Sequence:
MLRSTISLLMNSAAQKTMTNSNFVLNAPKITLTKVEQNICNLLNDYTDLYNQKYHNKPEPLTLRITGGWVRDKLLGQGSHDLDIAINVMSGEQFATGLNEYLQQHYAKYGAKPHNIHKIDKNPEKSKHLETATTKLFGVEVDFVNLRSEKYTELSRIPKVCFGTPEEDALRRDATLNALFYNIHKGEVEDFTKRGLQDLKDGVLRTPLPAKQTFLDDPLRVLRLIRFASRFNFTIDPEVMAEMGDPQINVAFNSKISRERVGVEMEKILVGPTPLLALQLIQRAHLENVIFFWHNDSSVVKFNEENCQDMDKINHVYNDNILNSHLKSFIELYPMFLEKLPILREKIGRSPGFQQNFILSAILSPMANLQIIGNPKKKINNLVSVTESIVKEGLKLSKNDAAVIAKTVDSICSYEEILAKFADRSQLKKSEIGIFLRNFNGEWETAHFASLSDAFLKIPKLETKKIELLFQNYNEFYSYIFDNNLNNCHELKPIVDGKQMAKLLQMKPGPWLGKINNEAIRWQFDNPTGTDQELITHLKAILPKYL
Protein: E1 ubiquitin-activating enzyme (EC 6.2.1.45) (C8VMA9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- E2 ubiquitin-conjugating enzyme
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin-conjugating enzyme E2-16 kDa
- RNA polymerase I specific transcription initiation factor Rrn7, putative
- HECT-type E3 ubiquitin transferase
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin-conjugating enzyme E2 1
- NEDD8-activating enzyme E1 catalytic subunit
- AN1-type domain-containing protein
- Polyubiquitin
Sequence:
MTDTKMQVDTPTQDTVEKIKQGDIDESLYSRQLYVLGHEAMKRMGSSNVLVVGLKGLGVEIAKNIALAGVKSLTLYDPAPVAISDLSSQFFLQPQDVGKPRAEVTAPRVAELNSYVPVTIHEGSSLVENLEQLKRYQAIVLTLTPLKEQLVIADFCHKNGIYLTIADTFGLFGYLFNDFGKNFTVGDSTGEDPVGGIVADISEDGLVSALDETRHGLEDGDFVTFTEVKGMEGLNNSAPRKVTVKGPYSFTIGDVSGLGTYQGGGLFTQVKMPKFIDFEPLSEQIKKPEFLISDFAKFDRPQQLHIGVQALHKFAETKGHFPRPHHESDAQELLQIANGLASSQEEKVELDEKLLKELSYQALGDLNPLAAFFGGIVAQEVLKAVSGKFGPVHQWLYFDSLESLPTSVTRSEETCKPLGTRYDGQIAVFGKEFQDKIANLTQFLVGAGAIGCETLKNWAMMGLGTGPKGKIYVTDMDQIEKSNLNRQFLFRSKDVGKLKSECASAAAVAMNPELEGKIVTLKDRVGPDTEHIFNEEFWEGLDGVTNALDNVEARTYVDRRCVFFRKPLLESGTLGTKGNTQVVLPRITESYSSSQDPPEKSFPMCTLKSFPNRIEHTIAWARDLFQTYFVGPPEAVNMYLSQPNYIEQTLKQAGNEKQTLEHLRDFLVTEKPANFDDCIVWARNQFEAQYNNAIQQLLYNFPRDSTTSTGQPFWSGPKRAPTPLKFDSTNPTHLGFIIAGANLHAYNYGIKNPGVDKGYYRKIVDNMIIPEFTPKSGVKIQASDNDPDPNAEASGSSFDDNDEIKRLVEILPSPKSLEGFRLNPVEFEKDDDTNHHIDFITAASNLRAENYEITPADRHKTKFIAGKIIPAIATTTALVTGLVALELLKIIDGKDDIEQYKNGFVNLALPFFGFSEPIASPKTKYQGKQGEVTIDQIWDRFEVDDIPLQDFLKHFSDLGLEISMVSSGVSLLYASFYGPSKVKDRLPMKMSELVEHISKKPIPDHQKNVIFEVTAEDQTEQDVEIPYVMVKRK
Protein: Skp1-related protein (G5EE67)
Organism: Caenorhabditis elegans
Interaction partners:
- Cullin-6
- Cullin-1
- RING-box protein 1
- F-box/WD repeat-containing protein lin-23
- F-box domain-containing protein
- DUF305 domain-containing protein
- RING-type domain-containing protein
- Retrotrans_gag domain-containing protein
Sequence:
MSDADSQKQIKLTSSDDKTFTVSRKVISQSKTITDIIQNLGIEESGSTSEDTIPLQKVTSTILEKIITWCEHHADDEPKKVDENKKTVDISEWDAEFMKVDQGTLFEIILAANYLDIRGLLDVTTQNVANMMKGKTPSQIRTLFNIENDFSEEEREAMKKENAWCED
Protein: GTP-binding protein YPT10 (P38146)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein transport. Probably involved in vesicular traffic (By similarity). Specifically binds guanine nucleotides.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Vesicle {ECO:0000269|PubMed:32391792}. Note=Colocalizes with CCZ1 to vesicular structures near the vacuole. {ECO:0000269|PubMed:32391792}.
Interaction partners:
- Rab GDP-dissociation inhibitor
- Rab proteins geranylgeranyltransferase component A
- Vacuolar segregation protein PEP7
Sequence:
MEATIKVVLLGDSSVGKTSIVTRLKSGKFLAKHAATIGAAFITKTIEVPSNDSSTEKRIHMEIWDTAGQERYKSLVPMYYRDANIALIVFELGDVSSLQCAKTWFQDLQDRAQGTQVIIVGNKYDLVCEEHSGEVTIPAELQGLPYVAVSAKTGYNFDTLNKIIISLVPESQFKTLSKNNEQGNILEINKKKSGSGCIC
Protein: Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14) (p125) (Q9EP71)
Organism: Mus musculus (Mouse)
Function: Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11168586}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:11168586}. Cytoplasm, cell cortex {ECO:0000269|PubMed:11168586}. Cell junction {ECO:0000250|UniProtKB:Q5U312}. Nucleus {ECO:0000250|UniProtKB:Q9P0K7}. Note=Associated with the cortical actin cytoskeleton structures in terminal web and cell-cell adhesion sites (PubMed:11168586). Highly expressed at the ectoplasmic specialization, an actin-rich cell junction specific to the testis (By similarity). Predominantly nuclear in nonconfluent cells (By similarity). {ECO:0000250|UniProtKB:Q5U312, ECO:0000250|UniProtKB:Q9P0K7, ECO:0000269|PubMed:11168586}.
Interaction partners:
Sequence:
MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSKISQDADLKTPTKPKQHDQVSKISSERSGTPKKRKAPPPPISPTQLSDVSSPRSITSTPLSGKESVFFAEAPFKAEISSIQENKDRLSDSTAGADSLLDISSEADQQDLLVLLQAKVASLTLHNKELQDKLQAKSPKDKEAEADLSFQSFHSTQTDLAPSPGKASDIPSSDAKSSPPVEHPAGTSTTDNDVIIRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLLSQESADGYSHLREAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKPPAEACEELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEALNSLSQLSYSTSSSKRQSQQLDLLQQQVKQLQNQLAECKKHHQEVISVYRMHLLYAVQGQMDEDVQKVLKQILTMCKNQSQKK
Protein: Putative clathrin assembly protein At4g02650 (Q8GX47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane, clathrin-coated pit {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Colocalized with clathrin in the Golgi area. {ECO:0000250}.
Interaction partners:
- Clathrin interactor EPSIN 2
- Calcium-transporting ATPase 2, endoplasmic reticulum-type
- Putative clathrin assembly protein At5g65370
- Ribosome biogenesis protein NOP53
- Reverse transcriptase
- MADS-box transcription factor family protein
- MADS-box transcription factor family protein
- F21D18.12
- Nonsense-mediated mRNA decay factor SMG7-like
- AT4g03420/F9H3_4
Sequence:
MGSSKLKRAIGAVKDQTSVGLAKVGGRSSSLTELEIAVVKATRHDDYPAEDKYIREILCLTSYSRNYVSACVATLSRRLNKTKNWSVALKTLILIQRLLTDGDRAYEQEIFFATRRGTRLLNMSDFRDASQSDSWDYSAFVRTYALYLDERLDYRMQGRRGKKKSGGGGGGDGDSGEEDDHRGTSNDIRSKAIVVKSKPVAEMKTEKIFNRVQHLQQLLDRFLACRPTGNAKNNRVVIVAMYPIVKESFQLYYNITEIMGVLIERFMELDIHDSIKVYEIFCRVSKQFDELDPFYGWCKNMAVARSSEYPELEKITQKKLDLMDEFIRDKSALAAQTTKSSSKRSNKSEEEESKTEYIQENQEDLNSIKALPAPEQKEEEEEEEKMETKKDVEEVVSRQDQEGDLLDLTDEAGVTAGTVGDSLALALFDGVVGTESASGPGWEAFNDNSADWETDLVRSATRLSGQKSELGGGFDTLLLDGMYQYGAVNAAVKTSTAYGSSGSASSVAFGSAGSPAASMLALPAPPPTANGNRNSPVMVDPFAASLEVAPPAYVQMNDMEKKQRLLMEEQIMWDQYNRSGRQGHMNFGQNQQQQYYQLPYSMGPYSYTPRY
Protein: Cellular tumor antigen p53 (Tumor suppressor p53) (P02340)
Organism: Mus musculus (Mouse)
Function: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression (By similarity). Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis, but seems to have to effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity). {ECO:0000250|UniProtKB:P04637}.
Interaction partners:
- Protein Mdm4
- TP53-binding protein 1
- Histone acetyltransferase p300
- E3 ubiquitin-protein ligase Mdm2
- Ubiquitin carboxyl-terminal hydrolase 7
- Histone lysine acetyltransferase CREBBP
- Apoptosis regulator Bcl-2
- Breast cancer type 1 susceptibility protein homolog
- Bcl-2-like protein 1
- Serine-protein kinase ATM
Sequence:
MTAMEESQSDISLELPLSQETFSGLWKLLPPEDILPSPHCMDDLLLPQDVEEFFEGPSEALRVSGAPAAQDPVTETPGPVAPAPATPWPLSSFVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEVLCPELPPGSAKRALPTCTSASPPQKKKPLDGEYFTLKIRGRKRFEMFRELNEALELKDAHATEESGDSRAHSSYLKTKKGQSTSRHKKTMVKKVGPDSD
Protein: Kinesin-like protein KIF9 (Q9HAQ2)
Organism: Homo sapiens (Human)
Function: Essential for normal male fertility and for progressive motility of spermatozoa.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9WV04}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9WV04}.
Interaction partners:
- GTP-binding protein GEM
- Kinesin-associated protein 3
Sequence:
MGTRKKVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGATENYKHRGILPRALQQVFRMIEERPTHAITVRVSYLEIYNESLFDLLSTLPYVGPSVTPMTIVENPQGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEETLSSLRFASRMKLVTTEPAINEKYDAERMVKNLEKELALLKQELAIHDSLTNRTFVTYDPMDEIQIAEINSQVRRYLEGTLDEIDIISLRQIKEVFNQFRVVLSQQEQEVESTLRRKYTLIDRNDFAAISAIQKAGLVDVDGHLVGEPEGQNFGLGVAPFSTKPGKKAKSKKTFKEPLSSLARKEGASSPVNGKDLDYVSTSKTQLVPSSKDGDVKDMLSRDRETSSIEPLPSDSPKEELRPIRPDTPPSKPVAFEEFKNEQGSEINRIFKENKSILNERRKRASETTQHINAIKREIDVTKEALNFQKSLREKQGKYENKGLMIIDEEEFLLILKLKDLKKQYRSEYQDLRDLRAEIQYCQHLVDQCRHRLLMEFDIWYNESFVIPEDMQMALKPGGSIRPGMVPVNRIVSLGEDDQDKFSQLQQRVLPEGPDSISFYNAKVKIEQKHNYLKTMMGLQQAHRK
Protein: Fibronectin type-III domain-containing protein 3A (Human gene expressed in odontoblasts) (Q9Y2H6)
Organism: Homo sapiens (Human)
Function: Mediates spermatid-Sertoli adhesion during spermatogenesis.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytidine and dCMP deaminase domain-containing protein 1
Sequence:
MAEHPPLLDTTQILSSDISLLSAPIVSADGTQQVILVQVNPGEAFTIRREDGQFQCITGPAQVPMMSPNGSVPPIYVPPGYAPQVIEDNGVRRVVVVPQAPEFHPGSHTVLHRSPHPPLPGFIPVPTMMPPPPRHMYSPVTGAGDMTTQYMPQYQSSQVYGDVDAHSTHGRSNFRDERSSKTYERLQKKLKDRQGTQKDKMSSPPSSPQKCPSPINEHNGLIKGQIAGGINTGSAKIKSGKGKGGTQVDTEIEEKDEETKAFEALLSNIVKPVASDIQARTVVLTWSPPSSLINGETDESSVPELYGYEVLISSTGKDGKYKSVYVGEETNITLNDLKPAMDYHAKVQAEYNSIKGTPSEAEIFTTLSCEPDIPNPPRIANRTKNSLTLQWKAPSDNGSKIQNFVLEWDEGKGNGEFCQCYMGSQKQFKITKLSPAMGCKFRLSARNDYGTSGFSEEVLYYTSGCAPSMPASPVLTKAGITWLSLQWSKPSGTPSDEGISYILEMEEETSGYGFKPKYDGEDLAYTVKNLRRSTKYKFKVIAYNSEGKSNPSEVVEFTTCPDKPGIPVKPSVKGKIHSHSFKITWDPPKDNGGATINKYVVEMAEGSNGNKWEMIYSGATREHLCDRLNPGCFYRLRVYCISDGGQSAVSESLLVQTPAVPPGPCLPPRLQGRPKAKEIQLRWGPPLVDGGSPISCYSVEMSPIEKDEPREVYQGSEVECTVSSLLPGKTYSFRLRAANKMGFGPFSEKCDITTAPGPPDQCKPPQVTCRSATCAQVNWEVPLSNGTDVTEYRLEWGGVEGSMQICYCGPGLSYEIKGLSPATTYYCRVQALSVVGAGPFSEVVACVTPPSVPGIVTCLQEISDDEIENPHYSPSTCLAISWEKPCDHGSEILAYSIDFGDKQSLTVGKVTSYIINNLQPDTTYRIRIQALNSLGAGPFSHMIKLKTKPLPPDPPRLECVAFSHQNLKLKWGEGTPKTLSTDSIQYHLQMEDKNGRFVSLYRGPCHTYKVQRLNESTSYKFCIQACNEAGEGPLSQEYIFTTPKSVPAALKAPKIEKVNDHICEITWECLQPMKGDPVIYSLQVMLGKDSEFKQIYKGPDSSFRYSSLQLNCEYRFRVCAIRQCQDSLGHQDLVGPYSTTVLFISQRTEPPASTNRDTVESTRTRRALSDEQCAAVILVLFAFFSILIAFIIQYFVIK
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (P52209)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- GDH/6PGL endoplasmic bifunctional protein
- Ribose-5-phosphate isomerase
- Probable gluconokinase
- Ribulose-phosphate 3-epimerase-like protein 1
- 6-phosphogluconolactonase
- Ribulose-phosphate 3-epimerase
- Transaldolase
- Transketolase
- Phosphoglucomutase-1
Sequence:
MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKEMVSKLKKPRRIILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKGILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKTIFQGIAAKVGTGEPCCDWVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFYDGYRHEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGTVSSSSYNA
Protein: ETS translocation variant 5b isoform 1 (ETS variant transcription factor 5b) (A0A2R8QC01)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MDGFYDQQVPFMVPPNKSHMQEPSCRTFNDRKRKFVDTELAQDTEELFQDLSQLQEIWIAEAQVPDDEQFVPDFQSDNLMFHGPPQTKIKREMSPSREFSPCGQEQRLSPYGEKCLYNYSAFDRKPFTFNKPLTPPSTPASPFGSSSTATHPVQKRAMPPAQTQTQGAPLLPGPNHSSTSPHQRAQTPLHSQSPPFAVPCTPVNHPDASYSTDHRFHRQLSEPCLPFPQSDGRCQTPYPPQTRGHFPRHSRPPYQRQMSEPLVPMPPQGFKKEMVDPRYNEQGVQNMGPPRAPLFHQLSIKQEPRDFGFDSEVQNCHSSFGKSSNFYGGNGEGFGYDGEAHLYYDDACVVPDRLEGKLKQEGGVFRDGPPYQRRGSLQLWQFLVTLLDDPSNGHFITWTGRGLEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVKVAGERYVYKFVCDPDALFSMAFPDNQRPSLKAEPDSLQVPEDDTVPLSHFDEANRAPYPADARDQCLVVPSFPESYTF
Protein: Cytochrome c oxidase assembly protein cox16, mitochondrial (Q9UTK1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- mRNA export factor elf1
- Elongation factor 3
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS15
Sequence:
MLFYRFKSWYRLQAKKSPFIYVGLPFLSSVLLVWSCLIPISQVKFNRRDEQVKSLSRDAELDIIKRRRKVDVNEEYYRILLDQLNLQNEEYENKRVKRLKGEPTWEGNSSDKE
Protein: Porimin (Keratinocytes-associated transmembrane protein 3) (KCT-3) (Pro-oncosis receptor inducing membrane injury) (Transmembrane protein 123) (Q8N131)
Organism: Homo sapiens (Human)
Function: Implicated in oncotic cell death, characterized by cell swelling, organelle swelling, vacuolization and increased membrane permeability.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGLGARGAWAALLLGTLQVLALLGAAHESAAMAASANIENSGLPHNSSANSTETLQHVPSDHTNETSNSTVKPPTSVASDSSNTTVTTMKPTAASNTTTPGMVSTNMTSTTLKSTPKTTSVSQNTSQISTSTMTVTHNSSVTSAASSVTITTTMHSEAKKGSKFDTGSFVGGIVLTLGVLSILYIGCKMYYSRRGIRYRTIDEHDAII
Protein: PPTX (Q5UMH8)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MLPGGVLSLLMLFCVFRASASVLDEGDDYDLMYVNLDNEIEGPVLGTEESASCDCQREHTEWDKLFIMLENSQMKENMMLQALEDGLKADVQAIRAELNQLTAGLAGTFSSTVQQLTSHALAQLEQALQRNGDQPEDAERLCESQQGKVLEQVLQLSHNVSARLGQLESSWLRWAEREAQETAFQLQQDKLGHSREDNLLLNTLWKELQQTRSELKASQKWASQHLLPAGYETAILFPMRSRKIFGSIHPTAAMTLSSFTVCVWVKATEALDKTIIFSYGTKLNPYEIQLYLSRQSAVLAVGSAQHKLAARDVVVPGKWIHLCGTWSSDNGTASLWVDGELTATAVGIADTHIVPDGGILQVGQEKNGCCVGGGFDEALAFSGKLTGLNLWDRVLSTEEIAAQGGEDACSSRGNIVGWGVTEVLLYGGAQYVS
Protein: Meis homeobox 1 (A0A8I5ZVB5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAQRYDDLPHYGGMDGVGIPSTMYGDPHAARSMQPVHHLNHGPPLHSHQYPHTAHTNAMAPSMGSSVNDALKRDKDAIYGHPLFPLLALIFEKCELATCTPREPGVAGGDVCSSESFNEDIAVFAKQIRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDDREGGSKSDSEDVTRAANLTDQPSWNRDHDDTASTRSGGTPGPSSGGHTSHSGDNSSEQGDGLDNSVASPSTGDDDDPDKDKKRHKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNN
Protein: Meiotically up-regulated gene 43 protein (Q10308)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Meiotic coiled-coil protein 6
- Meiotic coiled-coil protein 5
Sequence:
MNNITRDIYTKGQPADLKRLLMKRNSFRRPLLNMRCNSVLQYSLEKRKLTVQDLKDTRMELNNMIRILTEAMAAHEWTVDNVNIADIQSLQSTIHSTLKNFQKINVLQLNINASDNSLAYLSKPEESYNFLTIYFSTLLSYEKVENLIKKSLTVIDSLYGLLNYQINAQHSLGCIPLNQDSFKQLKLLICILEEDIKLDDCGLEISASKNEYLEKIKTHYKTWLRIHTFLTLFPVPSVLSSNLKKQMYGWFEDLRDESLKSIILASLSE
Protein: Nuclear RNA export factor 1 (B5BM32)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNRKGFGGHRDAKQLSRTKNRFARLDPDTQSRYEDDDEPAVPVRASLTSASSRGRGGSSRGFGQSAASIANTGVRNADIVYKCRATGAAKKVDAKWLIKQLNQIIENFKPLLWTDNARGDFEWYVRDEDTASTIRANNRRVVHKESGTRVEFYTSKVPAPWMKLKREEIEIIHRVVDKRHNAENRVLDLSNFHEDEEFKAKDMMMNLTKGNVMLTVLDHIDDKYGNIVALSLSNNRIRHLDYASALVSIAKFVMELDLSHNHISTEKELEKFAGLPVERFFFEGNPVVESFTQRAAYISYIHQSFPRCNMLDGVEVQPLVVGPDLDIHDAMPFRAGYYPNPQIRVLVEQFVTSYFDFYDGPDGQRTRRNLHNAYDADASTFSLTIEHLRGSSHARHHNDECFAQYAGVSHNVLKQERFARHRASRSARGAMDIAVALSKLPTSSHMRDTFIVDVFLQSNDLLGFTVQGLFCDGDLTQTPSPSFFSRSFLVSPRENDSVAVISDQLFITVASLDRLEKFKKLYDQSIANGAAVEQVSAVQIAQIGVNGMGFDGAPALPIREEMIKAMCQFSGMIPPFSEKCLADCAWNFDFACQKFNEIKSSVPAEAFAH
Protein: Transmembrane protein 72 (Kidney-specific secretory protein of 37 kDa) (A0PK05)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MQLQVFWTGLEYTCRLLGITTAAVLIGVGTETFLQGQFKSLAFYLLFTGAAVSICEGAYFVAQLLAICFQCQPGSLADRVREKAHWLGCFQKFLAYLLLSVACFLHPVLVWHVTIPGSMLIITGLAYFLLSKRKKRKAAPEVLASPEQYTDPSSSAVSTTGSGDTEQTYTFHGALKEGPSSLFIHMKSILKGTKKPSALQPPNTLMELSLEPADSLAKKKQVHFEDNLVRIVPSLAEGLDDGDSEPEETTSDTTPIIPPPQAPLFLSSLTATGLF
Protein: Signal transducer and activator of transcription (A0A494C164)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
Sequence:
MAQWEMLQNLDSPFQDQLHQLYSHSLLPVDIRQYLAVWIEDQNWQEAALGSDDSKATMLFFHFLDQLNYECGRCSQDPESLLLQHNLRKFCRDIQPFSQDPTQLAEMIFNLLLEEKRILIQAQRAQLEQGEPVLETPVESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFCFRYKIQAKGKTPSLDPHQTKEQKILQETLNELDKRRKEVLDASKALLGRLTTLIELLLPKLEEWKAQQQKACIRAPIDHGLEQLETWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDPLTKGVDLRNAQVTELLQRLLHRAFVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQGFRKFNILTSNQKTLTPEKGQSQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKNQQFFSNPPKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLPFWTWLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTMSGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDELQQPLELKPEPELESLELELGLVPEPELSLDLEPLLKAGLDLGPELESVLESTLEPVIEPTLCMVSQTVPEPDQGPVSQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEIMPNGDPLLAGQNTVDEVYVSRPSHFYTDGPLMPSDF