wanglab/gogpt-training-data huggingface dataset:
Protein: Protein tfg-1 (Q9U1W1)
Organism: Caenorhabditis elegans
Function: In its hexameric form, promotes the accumulation of sec-16A.1 and the COPII subunit npp-20 at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER), to positively regulate secretory cargo trafficking from the endoplasmic reticulum to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) and Golgi apparatus. Required for the assembly of proteins, such as the GTPase rab-6, at the Golgi apparatus. Plays a role in negatively regulating cell death and promoting cell and body growth.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:21478858}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:21478858}. Mitochondrion {ECO:0000269|PubMed:18635357}. Note=In oocytes, co-localizes with sec-16A.1 at endoplasmic reticulum exit sites (ERES) (PubMed:21478858). In proximal oocytes, localizes to a cloud-like region at endoplasmic reticulum exit sites that spreads to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (PubMed:21478858). {ECO:0000269|PubMed:21478858}.
Interaction partners:
- Protein transport protein sec-16A.1
- WD_REPEATS_REGION domain-containing protein
- Yeast SEC homolog
- Protein transport protein SEC23
Sequence:
MVHSNGAITSTILKARHADVVRKTSLHHANDLTLIDLVLNVQRLLALPSDANFVLKYKDEEGDLVTLAEDSDLLLALHTSGATLDVTVVVDSRAREAVHDVQKQVEQIKLDVGKLLGALSALDVAQIAEQSNTSVANLSAPKQSHHDNIVFQKSFEAAPPSPVPSEKAELPATIQPSVHEQFNHRPAHVEEEIPLENHYAPPPHQQIPDDLNTSFSSQPPPPIEQFGAIPPPNATIPSFPTSNAASPPVQEFAPPPPQQQQQQFQAPPPPMASHSSISSTPVQQQGFAPPQQFGGPPPSGPPSEYGGYAPPQQQQQQFGAPPPQGAPQQGFGAPPQGPPQGGPPQGSFGAPPPQQFHAPSPQSFGGPPPPVSSAPGNFAPPPQSGPPGAFAPPPSAFGAPQGPGGPGGYGPPPPGGPGAPGSYGPPQGGPGGFGPPPPGGPGAYGPPPTGFPPVGAPPPGAAGAPGGNPFARGPSATGYRQSPYQQ
Protein: Psoralen synthase (EC 1.14.14.141) (Cytochrome P450 CYP71AJ3) (C0SJS2)
Organism: Pastinaca sativa (Wild parsnip) (Anethum pastinaca)
Function: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes. Involved in linear furanocumarin (psoralen) biosynthesis. Converts marmesin to psoralen and, with much lower affinity, 5-hydroxymarmesin to bergaptol.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
YFFPLFLVTIFLYKWLVKKTPSKNLPPSPPRLPIIGNLHQIGPDPQISLRDLAREYGPVMHLKFGSVPVLVVSSADGAREIFKTHDLVFADRPYSSVANRIFYNGRDMVFARYTEYWRQVKSTCVTQLLSVKRVQSFHNVREEEVALLLDNIENSKSKVINLSEMLIELTGNVVCRAALGSGYNVDSYKSLLLQIMDMLGYSRSIEDFFPSLGWVDWITGLKGKVEKAANGVDAFLEGVLKNHTNPSTSSANKDFVSILLEIQEADAGSSMDKECIKSLIWDMLGAGTETIATALEWTIGALIKSPDAMSKLQKEVREIGKGKSRIEEGDLVKMDYLKAVMKESMRLYFTAPLLVPREARQDVKFMGYDIKSGTQVLINAWAIARDPSSWDNPEEFRPERFLNSPIDYKGFNYEYIPFGAGRRGCPGIQFAISVNELVVANVVNKFNFELPDGKRLEEMDMTASTGITFHKKS
Protein: Transmembrane protein (Q551Y7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Phosphatidylinositol glycan, class F
- Emp24/gp25L/p24 family protein
- Mannosyltransferase
Sequence:
MTSFNSLYEDEDNNNTISSSSSSGSSINNNNNKNGNPLSLSSMIPIRNRKLSDPTSYDNNSNSSINIENDYLMENHQSPNNSSNNLLPFLIPSVNLSSDNSENSNSNNYLSNPMGGRASSLSLGSSSDNAYIKNLHHGGGYHNQQHHNYNQQQQQQQQQLQQQQQQQQQQQQQQQNNLNNQKKKYKKSERNLMCWVSFVLVITQLLGIFMFSQGFFPRKTTLEGYNSFANYEPSCTADNGDIKVEAQFGKVVFMLVDAFKSNFLFGEENSQAMSFTQSLLDSGRAHGYIARADAPTVTLPRIKALLSGGIPSFVDFVNNFNSQTLKEDNILYQMKQSNKSMLFFGDDTWLKLFPDYFKRHDGTTSFYVADTVEVDLNVTRHLEPELNNNDWDVMFLHYLGLDHIGHLEGPHSNLMKPKQKEIDNIIKLIHTKLLEKDKIEMENYLNLINNTNNNNNNKNKIEKPLPTLFIFCSDHGMNEIGNHGGSSDSETSAVLVLMSSLYYNQNDIIVDHNNFEIKNHHNDNNNNNNNNNNNNNNNNNTEINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINDNNKTEELITKKEIEDNLMIGQGRSDTHYHDPEILPKFQPGLPPKEISQVDLVPTLSLLLGLPIPKNSLGSLIPELFEKFIPSEQYLRALEINCQQQIEIIKHNSIFWKDGVASNAHISSLLKMFTDAQQYHSSWITTPSHSSFNDNAAELYLEFLSKVQDQFKSLLTTFDDNLLMVGILLIGSSALVTLLITISTIGVSEHNGTFEIKGVKFVMTFVGLIIILLTIHFGIICKSNNNNNDSSSLDDGSSSSPSKIINNLNPFCTNEFRYGVFSFIFTALSLLIGFNALFSKNNIKFWSLATLSPLQLRKEKYVLIVGTILHLISLFGSSLVEEEHLTWYFLTTSVILLQMAPHSISLFFYFTNWISSYTTNNSNNNIINNNNNSNNNNNSNNNNNNNNNNINSSTGINSYNTNQQNRNTKQQQQSLQQMFILLGILVCLRIFRIWNQTGIKWMDDPKLLEEGSSYIDVGRFLNAPNIISSTTMWILSLISIIAPCYYVFGVLDDLEEQRGGISTLLSKIYKTTIVILSVFLFCYKWEYIGKELINPAYIARVVYFCWAILQVITFSFPYFSKKDRVSIQLQQQNLIILPQTWFIATLKYLPTLVTVNMYMLFLLLHKVHNMFLLTIMGVIAHYYILYLLEDTGRRAKSGMTGVCVGMICLGWLGQFGYFAFGNSNSLASIDISGSYTALIDYNQYLVGIQTLLIGYTSQLFFFFVSLAYVTHLAVKSISNSNHQQEPSLLPSPGTSSDIIDELQWYGLVSALLDCGIRWTNIFIFSICILIQRYHLFIWTVFSPKYIYEVLDVTLVLIKSILLAAFIIYLRLLSFVKEKQVENNSLASSQNINKEE
Protein: DNA repair protein Rad26 (G5EB71)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MENFDDDVFSDDGFDDLPPDALEQLEQDAFRATQAEHPTQREPEPRQNWAEREVTIRYAQINPINVANATLRPPAQLHTGLTNDYGSLDVGESDAEVFDDEAAIGLNETVTISDRPSHYAHDSIALGEKPMETDGGLSFYSALQREHEILTAKLQQETERYARLENEFANVKSLAETKTGEIAIIRSNHAKIVNDYERQLSGLRKAMDEETAKHREELEAIREQGKTLATENAFLKQDLAEEVSRVHQIRAKMRTEEKSAPVTPKKPKALPFRDGFDDEEILAVSPSKSGRSKQATPTVTGKKRRRTSQGSPSRLHLSPHREQNLGIAGGAVDEALSESAIDLPMKESSQEAGHQDTHIIKQILNHRTVPHKTDIEIIAELAFPSEPGRTLYSILLEETTQLDLGSYAMEHMRAIISLWSRALKEKFYKPIPILLETTRLILAIDATAVLRQIDRLIPVLLDTSDINGVPRFKHSPYASQSFGKVTQTPASQLEPLVDSTEVVRVLYQIACRSLSDDQLVEDLWRHIRYSFVLMMLSCSQPASDIKLTLSLLMTSVRPNSFASIQESEQDQKSNENWVVDRVASLMWETLQPDEGQPPYTRAEICDVRLEALAFLMTVTFNPIEPNNTHGSLVIASHHTALAKLVRAMHDELDALYSYPPERDMHSAMVNGLMRLIYSIIQRHPKEADLQLKLHRVPGGKQKFLVVLTRLAFSEGIVLEAGIEDETVEMAHSILDDAVNPQEAEALLEAFPHAKGEDTEAKNAEDTEMMEVMEEDLAL
Protein: Chemokine receptor CXCR4 (Q9DGI1)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Late endosome {ECO:0000256|ARBA:ARBA00004603}. Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
Sequence:
MDGLDLSSGILIEFADNGSEEIGSADYGDYGEPCFQHENADFNRIFLPTIYSIIFLTGIIGNGLVIIVMGYQKKQRSMTDKYRLHLSVADLLFVITLPFWSVDAAISWYFGNVLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKIVYVGVWLPAVLLTVPDIIFASTSEVEGRYLCDRMYPHDNWLISFRFQHILVGLVLPGLIILTCYCIIISKLSHSKGHQKRKALKTTVILILTFFACWLPYYIGISIDTFILLGVIRHRCSLDTIVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQNALTSVSRGSSLKILSKSKRGGHSSVSTESESSSFHSS
Protein: Proton-transporting V-type ATPase complex assembly regulator TMEM9 (v-ATPase assembly regulator TMEM9) (Dermal papilla-derived protein 4) (Transmembrane protein 9) (Protein TMEM9) (Q9P0T7)
Organism: Homo sapiens (Human)
Function: Transmembrane protein that binds to and facilitates the assembly of lysosomal proton-transporting V-type ATPase (v-ATPase), resulting in enhanced lysosomal acidification and trafficking. By bringing the v-ATPase accessory protein ATP6AP2 and the v-ATPase subunit ATP6V0D1 together, allows v-ATPase complex formation and activation. TMEM9-controlled vesicular acidification induces hyperactivation of Wnt/beta-catenin signaling, involved in development, tissue homeostasis and tissue regeneration, through lysosomal degradation of adenomatous polyposis coli/APC. In the liver, involved in hepatic regeneration.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:12359240, ECO:0000305|PubMed:30374053}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:12359240, ECO:0000269|PubMed:30374053}; Single-pass type I membrane protein {ECO:0000255}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:30374053}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase MINDY-3
- Growth hormone-inducible transmembrane protein
- Transmembrane protein 45A
Sequence:
MKLLSLVAVVGCLLVPPAEANKSSEDIRCKCICPPYRNISGHIYNQNVSQKDCNCLHVVEPMPVPGHDVEAYCLLCECRYEERSTTTIKVIIVIYLSVVGALLLYMAFLMLVDPLIRKPDAYTEQLHNEEENEDARSMAAAAASLGGPRANTVLERVEGAQQRWKLQVQEQRKTVFDRHKMLS
Protein: Cation-transporting ATPase (EC 7.2.2.-) (Q54X63)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
Interaction partners:
Sequence:
MGKETKIDKFEKSKYNKRYNEPNDPLEIDYMRGYQTTTLSNILHYGLIILSAGLLLLVYHWVPRWGIKMRFKECKLNDANYVYVKAKDKKYELSQVKHVLIGKKDLEFSESEKKDKYIEFKFTRLFYNVEKDLFIRPISNTDYHRSKINELVKTGLSMNKYQEGRDLFGPNLISVPLKSIPSLLLDEILHPFFIFQIYSIILWCTEDYYVYAGAILFIALVTAIFTLRETRNNLLRLNEIATYRCDVTVLRDGKLQVVSSETLVPGDIIEIQKSLVLPCDFCLLTGTVILNESMLTGESIPVTKYSLEECSGDQLSVDPLVNKRCAMSGGTKVVKTQAKEKDAKIFAMVTNTSWLTTKGGLVLSMLYPKESHFKFFEQSLKFLGVLCFIALIGFGVSVWRLIKAGEQLSEVVTKALDLITIVVPPALPMAQSVGTGFSIVRLKANKIFCISPPRVNMAGKVEVYCFDKTGTLTEDGLDLFGVLPSHQDSNNSGGFGTVIKTDLNRMTGPLFLTMATCHTLAHIDEQVSGDPLEEKIFTATNAKLNDNGEFGFCASIQLSKVDNISMVHQEYPISTVDVETSDQIALVERFEFQSALQRMSVVIRGIRATDGSTQSSKDLAIVKGSPEMIKKLSNPTSIPSDFEHVLSTYTKKGYRVLGCGYKEWDPSDSIGKTKDEIRSMVERDLMFLGFIIMENKIKPETAGALKVLKDANIRIIMVTGDNVLTAVSVSRECGLVTKEKTIFSSQLVNDPVTGKPTMVEWFDVTSPEESIPFTLDPYTLTINNAGGGSNYDDEYSLAVTGDVWKYYYDQFKANGQPTICFNQILRKGQVFARMTPDQKQNLIEELQVLGLYVGMCGDGANDCGALKAAHVGISLSQAEASIAAPFTSTITNVTCTYNLIKEGRASLTVSFKLFQFIGMYSLIQFCQVILLYFDGSVLNNYQYLYQDLWVIFPLVIFMGRTEPCSKLSIKRPSSRLISSTVIGSLLSHVTLTFVFQLLVYIFVRRNSWYKDLPDTSSNENEPRLDHLLASLFIYGNMQYSVMCFIYSWGKPFLRPIYTNRALFIFFCVTLTTSSLLLLLPVSIRFFGTTWLMDLPVRWRVELLILFIINAALAMAAEWIIIVYREIRSKSKRKLKQKQNSDPNIIAKNTVNERYTSLN
Protein: Glutathione S-transferase F8, chloroplastic (AtGSTF8) (EC 2.5.1.18) (AtGSTF5) (GST class-phi member 8) (Glutathione S-transferase 6) (Q96266)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17670748}. Cytoplasm, cytosol {ECO:0000269|PubMed:17670748}.
Interaction partners:
- Glutathione S-transferase U19
- Methionine--tRNA ligase, cytoplasmic
- Glutathione S-transferase DHAR2
- Glutathione S-transferase DHAR1, mitochondrial
- Probable glutathione peroxidase 2
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Probable glutathione peroxidase 5
- Putative glutathione peroxidase 7, chloroplastic
- Glutathione S-transferase U7
- Glutathione S-transferase U5
Sequence:
MGAIQARLPLFLSPPSIKHHTFLHSSSSNSNFKIRSNKSSSSSSSSIIMASIKVHGVPMSTATMRVLATLYEKDLQFELIPVDMRAGAHKQEAHLALNPFGQIPALEDGDLTLFESRAITQYLAEEYSEKGEKLISQDCKKVKATTNVWLQVEGQQFDPNASKLAFERVFKGMFGMTTDPAAVQELEGKLQKVLDVYEARLAKSEFLAGDSFTLADLHHLPAIHYLLGTDSKVLFDSRPKVSEWIKKISARPAWAKVIDLQKQ
Protein: Small ribosomal subunit protein eS7A (40S ribosomal protein S7-A) (RP30) (RP40) (P26786)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. eS7 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}.
Interaction partners:
- Small ribosomal subunit protein uS11B
- U3 small nucleolar RNA-associated protein 9
- Small ribosomal subunit protein eS27A
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein eS10A
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein eS26A
Sequence:
MSAPQAKILSQAPTELELQVAQAFVELENSSPELKAELRPLQFKSIREIDVAGGKKALAIFVPVPSLAGFHKVQTKLTRELEKKFQDRHVIFLAERRILPKPSRTSRQVQKRPRSRTLTAVHDKILEDLVFPTEIVGKRVRYLVGGNKIQKVLLDSKDVQQIDYKLESFQAVYNKLTGKQIVFEIPSETH
Protein: Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 (Centaurin-delta-3) (Cnt-d3) (Dual specificity Rho- and Arf-GTPase-activating protein 1) (Q8R5G7)
Organism: Mus musculus (Mouse)
Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts preferentially on ARF5 and on RHOA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15546919}. Cell membrane {ECO:0000269|PubMed:15546919}; Peripheral membrane protein {ECO:0000269|PubMed:15546919}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15546919}. Cell projection, lamellipodium {ECO:0000269|PubMed:15546919}. Cell projection, ruffle {ECO:0000269|PubMed:15546919}. Note=Cytoplasmic, and associated with F-actin-rich membrane ruffles and lamellipodia.
Interaction partners:
- Transforming protein RhoA
- Ras-related protein Rap-1b
- RIKEN cDNA 4930544G11 gene
- Ras-related protein Rap-1A
- SH3 domain-containing kinase-binding protein 1
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
Sequence:
MAAPQDLDIAVWLALVHLEQYADTFRRHGLATAGAAQHLGHEELRHLGISATGHRKRILRLLRAGSAEGFLDSHLDNTMEPTPSPAPDAQPPKPVPKPRTVFGLSNPATAQRPGLSPIFWDPEVSRNSECTQRSSPLLPSSSEQPSVPNTMEMMPNAIYFGLDLRGRAQAAQDVTPDSSQATVPTPAFRPTTGTVHIMDPGCLYYGVQPVGIPGASDRRDGRGVCQERAEHRQDLETREDAGYASLELPGDSILSLPTQDAETSDDLISPYASFSSTADRPVPLLSGWLDKLSPQGNYVFQRRFVQFNGRSLMYFGSDKDPFPKGVIPLTAIEMTRSSKDNKFQVITGQRVFVFRTESEAQRDLWCSTLQSCLKEQRLLGHPRPPHPPRPLRTGTLELRGHKAKVFAALIPGELALYKSEQAFSLGIGICFIELQGCSVRETKSRSFDLLTPHRCFSFTAESGGARQSWAAALQEAVTETLSDYEVAEKVWSNPANRHCADCRASRPDWAAVNLGVVICKQCAGQHRALGSGISKVQSLKLDTSVWSNEIVQLFIVLGNDRANCFWAGALPPGEGLHPDSAPGPRGEFISRKYKLGLFRKPHPRHPDHSQLLQALCAAMAGPNLLKNMAQLLCVETSEGEEPLSPSALNGSLLSLLPSDSPGVYNEVVVPATYRGFLYCGSISNKAGAPPLRRGRDAPPRLWCVLGAALEMFASESSPEPLSLLQPQDIVCLGVSPPPADPGDLDRFPFSFELILTGGRIQHFATDGADSLEAWISAVGKWFSPLSCHQLLGPGLLRMGRLWLRSPSHAGLAPGLWLSGFGLLRGDHLFLCPAPGPGPPAPEDMVHLRRLQEISVVSAADTPDKKEHLVLVETGRTLYLQGEGRLDFAAWNTAIGGAAGGGGTGLQEQQMSRGDIPIIVDACISFVTQHGLRLEGVYRKGGARARSLRLLAEFRRDARSVKLRPREHFVEDVTDTLKRFFRELDDPVTSARLLPRWREAAELSQKNQRLEKYKEVISCLPRVNRRTLATLIGHLYRVQKCASLNQMCTRNLALLFAPSVFQTDGRGEHEVRVLQELIDGYISVFDIDSDQAAQIDLEVSLITTWKDVQLSQAGDLIMEVYIEQQLPDNCVTLKVSPTLTAEELTNQVLEMRGAASGTDLWVTFEILEHGELERPLHPKEKVLEQALQWCQLPEPCSASLLLRKVSMAHAGCLFTGVRRESPRVGLLRCREEPPRLLGNRFQERFFLVRGRCLLLLKEKKSSKPEREWSLEGAKVYLGIRKKLKPPTLWGFTLILEKMHLCLSCMDEEEMWDWTTSILKAQHDDQQSVVLRRRSSSDLARQKFGTMPLLPIRGDDSGATLLSANQTLRRLHNRRTLSMFFPMKSPQGSVEEQDELEEPVYEEPVYEEVGAFPELTKDTTFSSTWEWSAKSDPSLTSQRSFDQPPLSKASMLGHEERIPDPPPGPPSKSSSQARGSLEEQLLQELNNLILRKGEPASCPESSSQPTSPQAPSPTSLPTPTPSLPTQPPCTSNPPSSQPLT
Protein: NF-kappa-B essential modulator (NEMO) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier) (Q6TMG5)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much highr affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6K9}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000250|UniProtKB:Q9Y6K9}.
Interaction partners:
- TGF-beta activated kinase 1
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- TNF receptor-associated factor 6
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Receptor-interacting serine/threonine-protein kinase 1
- Mitogen-activated protein kinase kinase kinase 7
- Interleukin-1 receptor-associated kinase 4
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- TNF receptor-associated factor
Sequence:
MSRHLWKNQLSEMVQPSGGPAEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVETSQPPLLPAPAHHSFHLALSNQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
Protein: ST3 beta-galactoside alpha-2,3-sialyltransferase 7 (EC 2.4.99.9) (Zgc:153853 protein) (Q08BF4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Lactosylceramide alpha-2,3-sialyltransferase
- Beta-1,4 N-acetylgalactosaminyltransferase
- Beta-hexosaminidase.
- Beta-1,4 N-acetylgalactosaminyltransferase.
- Beta-hexosaminidase
- Notochord granular surface
- Beta-galactosidase.
- Beta-galactosidase-1-like protein precursor
- UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 6.
Sequence:
MVTLKHLSVNDNDEDGVPLLPEASSLESPTTQHSRAESRDFFLSRRYNFIVSIVLLLSLYSALLVPAYLPTAEPIWTNESSAENLALLNQSASLLSQSCHSGWSVERMRTMLSTPAGLLKIPVFLENGTGDWALPPPLGLQGSEEMAEQALKALPFTAVPTGPETCRRCVVVGSGGILHGKNLGAHIDQYNIIIRVNNAPVFGFESDAGSRTTIRLIYPEGAPSHIQEYERTEVVALVVFKSLDLAWMTSVVTKEPLSWWSKLWFWKDVIDSIPLQPENVRILNPEIMYRTGQVLQTYAEQQRKMVPTLGITAVVVALQVCDEVSIAGFGYDLQHPGAPLHYYGSLRMDAMKTQVVHDVSAETVFLKELVKAGAVRDLTGAL
Protein: 2-deoxyglucose-6-phosphate phosphatase 1 (2-DOG-6-P 1) (2-deoxyglucose-6-phosphatase 1) (EC 3.1.3.68) (P38774)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphatase that is active on 2-deoxy-D-glucose 6-phosphate (2-DOG-6P), as well as on fructose-1-P.
Interaction partners:
Sequence:
MAEFSADLCLFDLDGTIVSTTVAAEKAWTKLCYEYGVDPSELFKHSHGARTQEVLRRFFPKLDDTDNKGVLALEKDIAHSYLDTVSLIPGAENLLLSLDVDTETQKKLPERKWAIVTSGSPYLAFSWFETILKNVGKPKVFITGFDVKNGKPDPEGYSRARDLLRQDLQLTGKQDLKYVVFEDAPVGIKAGKAMGAITVGITSSYDKSVLFDAGADYVVCDLTQVSVVKNNENGIVIQVNNPLTRA
Protein: Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit) (O13339)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular location: Nucleus. Chromosome, telomere.
Interaction partners:
- Telomere elongation protein est1
- Protection of telomeres protein tpz1
- Coiled-coil quantitatively-enriched protein 1
- Protection of telomeres protein 1
- Telomere length regulator taz1
- Protection of telomeres protein poz1
- DNA-binding protein rap1
- La-related protein 7 homolog
- H/ACA ribonucleoprotein complex subunit nop10
- ATP-dependent DNA helicase II subunit 1
Sequence:
MTEHHTPKSRILRFLENQYVYLCTLNDYVQLVLRGSPASSYSNICERLRSDVQTSFSIFLHSTVVGFDSKPDEGVQFSSPKCSQSELIANVVKQMFDESFERRRNLLMKGFSMNHEDFRAMHVNGVQNDLVSTFPNYLISILESKNWQLLLEIIGSDAMHYLLSKGSIFEALPNDNYLQISGIPLFKNNVFEETVSKKRKRTIETSITQNKSARKEVSWNSISISRFSIFYRSSYKKFKQDLYFNLHSICDRNTVHMWLQWIFPRQFGLINAFQVKQLHKVIPLVSQSTVVPKRLLKVYPLIEQTAKRLHRISLSKVYNHYCPYIDTHDDEKILSYSLKPNQVFAFLRSILVRVFPKLIWGNQRIFEIILKDLETFLKLSRYESFSLHYLMSNIKISEIEWLVLGKRSNAKMCLSDFEKRKQIFAEFIYWLYNSFIIPILQSFFYITESSDLRNRTVYFRKDIWKLLCRPFITSMKMEAFEKINENNVRMDTQKTTLPPAVIRLLPKKNTFRLITNLRKRFLIKMGSNKKMLVSTNQTLRPVASILKHLINEESSGIPFNLEVYMKLLTFKKDLLKHRMFGRKKYFVRIDIKSCYDRIKQDLMFRIVKKKLKDPEFVIRKYATIHATSDRATKNFVSEAFSYFDMVPFEKVVQLLSMKTSDTLFVDFVDYWTKSSSEIFKMLKEHLSGHIVKIGNSQYLQKVGIPQGSILSSFLCHFYMEDLIDEYLSFTKKKGSVLLRVVDDFLFITVNKKDAKKFLNLSLRGFEKHNFSTSLEKTVINFENSNGIINNTFFNESKKRMPFFGFSVNMRSLDTLLACPKIDEALFNSTSVELTKHMGKSFFYKILRSSLASFAQVFIDITHNSKFNSCCNIYRLGYSMCMRAQAYLKRMKDIFIPQRMFITDLLNVIGRKIWKKLAEILGYTSRRFLSSAEVKWLFCLGMRDGLKPSFKYHPCFEQLIYQFQSLTDLIKPLRPVLRQVLFLHRRIAD
Protein: eIF-4F 25 kDa subunit (Q9VAR1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic initiation factor 4A
- Eukaryotic translation initiation factor 4G1, isoform B
- Polyadenylate-binding protein
- Eukaryotic translation initiation factor 4E-binding protein
- Eukaryotic initiation factor 4B
- ATP-dependent RNA helicase
- Cytoplasmic FMR1-interacting protein
- ATP-dependent RNA helicase me31b
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 4 gamma 2
Sequence:
MENLRQTKESSEFKMGTSLDNNKLASLGATNKHRLQNTWTLWGVKYDPEISWEDMLKEIDSFNTVEDFWNLYFRIDTPSKLNRGCDYMLFKKGIRPMWEDPPNKGGGRWTYKVDKRSTAELDKTWLDVLLCMIGEACDHCDQICGAFVRIRKNINKISVWTKADAGDECNEQC
Protein: Cytoplasmic dynein 1 light intermediate chain 1 (LIC1) (Dynein light chain A) (DLC-A) (Dynein light intermediate chain 1, cytosolic) (DLIC-1) (Q9Y6G9)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores.
Subcellular location: Cytoplasm {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19229290}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19229290}. Recycling endosome membrane {ECO:0000269|PubMed:20026645}. Note=During interphase, localized in vesicles continuously moving from peripheral sorting endosomes in the cell towards the pericentrosomal endosomal recycling compartment (ERC). {ECO:0000269|PubMed:20026645}.
Interaction partners:
- Protein bicaudal D homolog 2
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 1 heavy chain 1
- Dynactin subunit 1
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 1 light intermediate chain 2
- Dynein light chain Tctex-type 3
- Dynein light chain Tctex-type 1
- Dynein light chain roadblock-type 1
- Protein Hook homolog 3
Sequence:
MAAVGRVGSFGSSPPGLSSTYTGGPLGNEIASGNGGAAAGDDEDGQNLWSCILSEVSTRSRSKLPAGKNVLLLGEDGAGKTSLIRKIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDAVSLKDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKQMEQKLIRDFQEYVEPGEDFPASPQRRNTASQEDKDDSVVLPLGADTLTHNLGIPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKAEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVSGGSPAGGAGGGSSGLPPSTKKSGQKPVLDVHAELDRITRKPVTVSPTTPTSPTEGEAS