wanglab/gogpt-training-data huggingface dataset:
Protein: Protein suppressor of sable (P22293)
Organism: Drosophila melanogaster (Fruit fly)
Function: RNA-binding protein that suppresses transcription of some RNAs. Together with Wdr82, part of a transcription termination checkpoint that promotes transcription termination of RNAs and their subsequent degradation by the nuclear exosome. Promotes transcription termination of aberrant RNAs, transcripts from genes containing a transposon inserted at their very 5' end or RNAs from heat-shock-inducible repetitive element. Binds RNA preferentially at a sequence that resembles a cryptic 5'-splice site.
Subcellular location: Nucleus {ECO:0000269|PubMed:11027289, ECO:0000269|PubMed:1703632, ECO:0000269|PubMed:9121479}. Chromosome {ECO:0000269|PubMed:15082769, ECO:0000269|PubMed:19687295}. Note=Localizes to polytene chromosomes. {ECO:0000269|PubMed:15082769, ECO:0000269|PubMed:19687295}.
Interaction partners:
- Homeobox protein goosecoid
- AT27166p
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- polynucleotide adenylyltransferase
- Cleavage and polyadenylation specificity factor subunit 1
- Symplekin
- Something that sticks like glue, isoform A
- Factor interacting with poly
- Protein suppressor of forked
- Cleavage and polyadenylation specificity factor 73
Sequence:
MSVALADEPLIDLEEDLEDGEIDDDEEDEQQSSKIQVQKKTFVGDDDVQFVGVEAKNQNDDEDVVYVGPSTDAVCLQNSNSTKSKKPRPLEDDHASSIELAIANALKKKGIEPPMPRMRSSNQDTSDQSLEGSGEGLATANPLLQSTRSSRRRKRKKEREREQKKDKEQQNRSRRDENDVSVVPGGVEDMDEYEMMNVRGGSPPPGGAAPPLSSCGQRFSGADWDMDDGSAATGAAGLGAGGGGGYNSHSSYDSYSDEETNGPGLMNQRRRTRRDNEKEHQRGVNNRKRRDRDRLEGGLAGSGSKRNRRDSGEGGGGGQEKMGGSNRVEPRKLELCKFYLMDCCAKRDKCSYMHKEFPCKYYYLGMDCYAGDDCLFYHGEPLSEQLRNVLLKHMETAPKEILGDFKRISRDIAIVQMTRRHEQLCDQLNRENTWNSIGCGLMGKRQDHQMQQQQQQLQHQQLQQQQEQQQTQQQAAADGGGCIPSLLDMVINPPLSENKRKSRWTEKMGAKAAAGAAGSSERDSTSPDAKPLPPHLDLANLSHVLSAENMAKLNKLGITNLEQMLQVPFGQLTEAGLTLVEIGEIQRKAEDAKPQTQAELESSTPPSKRETEANNSNSKSNGLIMVDYTQYLKDAHVSFSGNDPLDDDRDDDEQLIIDDGNDSTAEEDQQPKKAKAPPAATHESSTEEAPLPSVFDLPSFMNNMLGQGSSARQLLPASATSPNQENAHLPGGDQSTHKSAPIGGGTSTNVLGRILFGDKQSDPEARAAFYRDIIRNPFKAHSGDGDVDSSNENSNSNSHSLTPTPTPEPGSQSPKPEDHDQDMPELPVIAPALPPTTPSLYVRRSMYDFDPVKEQEHGRQELLTEEKEQYQRDTDMRLPFEPMKHYMPATEIDAAIFSHTPIRWQLHEVTIEESSYAQIRASALHKEQRELRDPRMRRILGLPETPDNSGPLGSVPIMGPSSFSVDNIARCATTIASPDLETAVRDSTPSSPPPSVVNLPSMSVPPPSMRVPPPNIQVEKPTVRTDPRRDPRRAVLQAPTKGASTANTTAPNASGGSKQISEIRSLLQVSNWYNNLGTNNKIMVNQQLALVFTELKKFHQLPNDAPKIFDVSFIVNNTTLQQIFAKLFIFVDDNGEVVQIPEEPNGNGAALGGGGDSGGGVGGGGGGGGVVLPNLSQPPPNLSQMLRLPPPNIRMLRMSGMMMQMGNVGPPFNQPPPRGGLMGMPPNGNGLNQGVGNLGGLGQLGINQGGGPVPNGNPFNPFGGNNGGGAGVMNNMNSMGNMGMGFNNFNNNGGRGGHFPGGGSGGNGNGNNRNQRGGNHRNRNI
Protein: Arylamine N-acetyltransferase (Q9HUY3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Acetyltransferase PA3944
- N-acetyltransferase domain-containing protein
- N-acetyltransferase domain-containing protein
Sequence:
MTPLTPEQTHAYLHHIGIDDPGPPSLANLDRLIDAHLRRVAFENLDVLLDRPIEIDADKVFAKVVEGSRGGYCFELNSLFARLLLALGYELELLVARVRWGLPDDAPLTQQSHLMLRLYLAEGEFLVDVGFGSANPPRALPLPGDEADAGQVHCVRLVDPHAGLYESAVRGRSGWLPLYRFDLRPQLWIDYIPRNWYTSTHPHSVFRQGLKAAITEGDLRLTLADGLFGQRAGNGETLQRQLRDVEELLDILQTRFRLRLDPASEVPALARRLAGLISA
Protein: Late embryogenesis abundant protein 32 (LEA 32) (Embryogenic cell protein 31) (AtECP31) (Q9LJ95)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: LEA proteins are late embryonic proteins abundant in higher plant seed embryos. The function of those proteins is not known.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25005920}. Nucleus {ECO:0000269|PubMed:25005920}.
Interaction partners:
- Late embryogenesis abundant protein ECP63
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Late embryogenis abundant protein 2
- Glutamate racemase
- At2g23110
- Expansin-A22
- Late embryogenesis abundant protein 6
- Gb|AAF18257.1 hydroxyproline-rich glycoprotein family)
- Proline-rich extensin-like protein EPR1
- Agamous-like MADS-box protein AGL81
Sequence:
MSQEQPRRPREPVKYGDVFEVSGELADKPIAPEDAKMMQSAETHVFGHTQKGGPAAVMQSAATTNIRGGFVHPDDKTELVAERGATVEQTVPAATVTTEFVGGQVVGQHVEPRRVVAAARTDEEALQSTITIGEALEATVKTAGNKPVDQSDAAAIQAAEMRASGTNVIALAGVAASAQSAADHNATVDRDERKIKLRDVLTGAAGKLSADRAVTREDAEGVVSAEMRNNPKLCTHPGGVAASLTVAARLNERVDI
Protein: Glycine dehydrogenase (decarboxylating) 1, mitochondrial (EC 1.4.4.2) (Glycine cleavage system P protein 1) (Glycine decarboxylase 1) (Glycine decarboxylase P-protein 1) (AtGLDP1) (Glycine dehydrogenase (aminomethyl-transferring) 1) (Q94B78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Aminomethyltransferase, mitochondrial
- Serine hydroxymethyltransferase 1, mitochondrial
- Glycine cleavage system H protein 3
- Glycine cleavage system H protein 1
- Glycine cleavage system H protein 2
- Serine--glyoxylate aminotransferase
- Serine hydroxymethyltransferase 5
- Serine hydroxymethyltransferase 2, mitochondrial
- Serine hydroxymethyltransferase 6
- Serine hydroxymethyltransferase 3, chloroplastic
Sequence:
MERARRLAYRGIVKRLVNDTKRHRNAETPHLVPHAPARYVSSLSPFISTPRSVNHTAAFGRHQQTRSISVDAVKPSDTFPRRHNSATPDEQTHMAKFCGFDHIDSLIDATVPKSIRLDSMKFSKFDAGLTESQMIQHMVDLASKNKVFKSFIGMGYYNTHVPTVILRNIMENPAWYTQYTPYQAEISQGRLESLLNFQTVITDLTGLPMSNASLLDEGTAAAEAMAMCNNILKGKKKTFVIASNCHPQTIDVCKTRADGFDLKVVTSDLKDIDYSSGDVCGVLVQYPGTEGEVLDYAEFVKNAHANGVKVVMATDLLALTVLKPPGEFGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRMMPGRIIGISVDSSGKQALRMAMQTREQHIRRDKATSNICTAQALLANMAAMYAVYHGPAGLKSIAQRVHGLAGIFSLGLNKLGVAEVQELPFFDTVKIKCSDAHAIADAASKSEINLRVVDSTTITASFDETTTLDDVDKLFKVFASGKPVPFTAESLAPEVQNSIPSSLTRESPYLTHPIFNMYHTEHELLRYIHKLQSKDLSLCHSMIPLGSCTMKLNATTEMMPVTWPSFTDIHPFAPVEQAQGYQEMFENLGDLLCTITGFDSFSLQPNAGAAGEYAGLMVIRAYHMSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIITVGTDAKGNINIEEVRKAAEANKDNLAALMVTYPSTHGVYEEGIDEICNIIHENGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLHKTFCIPHGGGGPGMGPIGVKNHLAPFLPSHPVIPTGGIPQPEKTAPLGAISAAPWGSALILPISYTYIAMMGSGGLTDASKIAILNANYMAKRLEKHYPVLFRGVNGTVAHEFIIDLRGFKNTAGIEPEDVAKRLMDYGFHGPTMSWPVPGTLMIEPTESESKAELDRFCDALISIREEIAQIEKGNADVQNNVLKGAPHPPSLLMADTWKKPYSREYAAFPAPWLRSSKFWPTTGRVDNVYGDRKLVCTLLPEEEQVAAAVSA
Protein: Fibrinogen beta chain [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain] (P02676)
Organism: Bos taurus (Bovine)
Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:11593005}.
Interaction partners:
- Fibrinogen gamma-B chain
- Fibrinogen alpha chain
- Prothrombin
- Plasminogen
- Integrin beta
- Antithrombin-III
- Kininogen-1
- Alpha-2-HS-glycoprotein
- Vitamin D-binding protein
- Albumin
Sequence:
QFPTDYDEGQDDRPKVGLGARGHRPYDKKKEEAPSLRPVPPPISGGGYRARPATATVGQKKVERKPPDADGCLHADPDLGVLCPTGCKLQDTLVRQERPIRKSIEDLRNTVDSVSRTSSSTFQYITLLKNMWKGRQNQVQDNENVVNEYSSHLEKHQLYIDETVKNNIPTKLRVLRSILENLRSKIQKLESDVSTQMEYCRTPCTVTCNIPVVSGKECEKIIRNEGETSEMYLIQPEDSSKPYRVYCDMKTEKGGWTVIQNRQDGSVDFGRKWDPYKQGFGNIATNAEGKKYCGVPGEYWLGNDRISQLTNMGPTKLLIEMEDWKGDKVTALYEGFTVQNEANKYQLSVSKYKGTAGNALIEGASQLVGENRTMTIHNSMFFSTYDRDNDGWKTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGAYTWDMAKHGTDDGVVWMNWQGSWYSMKKMSMKIRPYFPEQ
Protein: Coagulation factor VIIi (Q8JHC9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTLGAAAVLLCVLTLRSTSAVFLSKDEASALLQRFRRANSGFLEEMKAGNLERECVEEICDYEEAREVFEDDDRTKQFWLSYSNKEPCLTNPCRNNGTCVYLADSYYCLCSEGYEGKYCEKGLEETLKCQYVNGGCEQFCDGSGARRSCSCAEGYALADDGTSCVSQVDYPCGKIPVQKNTSQNQFLGGIHCPRGHCPWQVLIDYNGESVCGGALLEGPWLITAAHCVHQKDTRFLKAVTGEHDLDVLDGSEEPYEVSAVFIHPNYDPETLDSDLALLRLRVPVQRSLYAVPICLPTPQLARSELWAARFHTLSGWGTRTAGHNLRREKGLKGPASGTLQRLAVPLLPAAQCGNANTTANMFCAGYTEGDHASCRGHDGSPLVTRYGETSFLTGVVSWGRGCGPPGYYWIYTKVENFLIWMDTVMKTNTEDKSEQIANVSTKN
Protein: Phytanoyl-CoA dioxygenase, peroxisomal (EC 1.14.11.18) (Phytanic acid oxidase) (Phytanoyl-CoA alpha-hydroxylase) (PhyH) (P57093)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the 2-hydroxylation of racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA. Shows activity also towards a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (By similarity). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl-and 4-methyl-branched acyl-CoAs (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:10588950}.
Interaction partners:
- Peroxisomal targeting signal 2 receptor
- Peroxisomal targeting signal 1 receptor
- Alkyldihydroxyacetonephosphate synthase, peroxisomal
- Peroxisomal membrane protein PEX13
- 2-hydroxyacyl-CoA lyase 1
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Dihydroxyacetone phosphate acyltransferase
- Alpha-methylacyl-CoA racemase
- 3-ketoacyl-CoA thiolase A, peroxisomal
Sequence:
MDYTRAGARLQVLLGHLGRPSALQIVAHPVSGPASPANFCPEQFQYTLDNNVLSLEQRKFYEENGFLVIKNLVSDDDIQRFRAEFERICRKEVKPPGMTVMKDVAIAKQGYAPSERVVTKIQDFQQNEELFRYCALPQIVKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHFFPFRPSNLIVCAWTAMEHIDRNNGCLVVLPGTHKGPLKPHDYPKWEGGVNKMYHGIQDYDPDSPRVHLVMEKGDTVFFHPLLIHGSGRNRTQGFRKAISCHYGSSDCKYISVKGTSQENIAREVIEIAEKRYGVQGALDFEDTWKFRCRLVKGERINL
Protein: Vomeronasal type-2 receptor 116 (Vomeronasal type-2 receptor P5) (E9Q6I0)
Organism: Mus musculus (Mouse)
Function: Receptor for the Esp1 pheromone. Mediates the response to Esp1 which enhances female sexual receptive behavior (lordosis) upon male mounting, resulting in successful copulation.
Subcellular location: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Exocrine gland-secreted peptide 22
- Vomeronasal type-1 receptor
- Vomeronasal type-1 receptor
Sequence:
MFTLIFLFLFLNIPLLVADFISPRCFWKMKQNEYRDRHHGTGCIFLILAIQQPVKKEYFSHILNIQTHTENHKYALALAFSIYEINRNPDLLPNMSLIFIFSADSCEWESELSLIRFGLQNSDNLPNYLCEELTKCILALTNMNWATTVTLHTILSNFLSDQLLHITYGTFHPALSDHEKFPYLHQMASDHTSLALALVSFIIHFGWNWVGLVISDSDQGIQFLSYLRREMEKYTLCFAFVNMIPLNINLYMSRAEVYYNQIMTSSTNVVIIYGDTDSTLAVSFRMWESLGIQRLWITTSQWDVSPSMKDFTFGNKYGTFAFEQHHSEISGFKHFVQTLNSVKCPDEYLVKLEWMHFNCEVSASKCKTLKNCSSNHSLKWLMVHTFDMAFIEESYYIYNAVYAFAHVLHQFTFQKFDNLPKDNGKEHNYSCKKLYSYLRKNHFINPVGDRVSMNQRDKLQEEYDIVYIWNFPQGLGLRVKIGMFSPYFPNGQQVHLSEDMLKWARGSTQVPTSMCSADCGPGSRKFRMDGMAACCFHCKPCPENEISNETNVDNCVQCPEDQYANTEQNHCIRKAVVFLSYEEPLGVALSLLSLCFSAFTTVVLGIFVKHHNTPIVKANNRTLTYLLLISLIFCFLCPLLFIGHPNSATCILQQLTFGVVFTVSLSTVLAKTITVVLAFKIIASQRMMKYFLISGAINYIIPICILIQVIVCAVWLRASPPSVDIDAHSEHGQIIIVCHKGSVNAFYCVLGYLAILAFGSFTLAFLSRNLPGAFNEAKSITFSMLVFCSVWVTFIPVYHSTKGKVMVAVEIFSTLASSAGMLGCIFVPKCYTILFRQDQNSLEMIRVKSSSNVHVS
Protein: Glycerol dehydrogenase 1 (GDH) (GLDH) (EC 1.1.1.6) (O13702)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Glycerol dehydrogenase involved in the assimilation of glycerol.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Dihydroxyacetone kinase 1
- Dihydroxyacetone kinase 2
- Uncharacterized oxidoreductase C26F1.07
- Putative monoglyceride lipase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Alcohol dehydrogenase 4
- Fructose-1,6-bisphosphatase
- DNA-binding protein scr1
- Cardiolipin synthase
Sequence:
MIGPRLCAATPRFPLVSLAHRNSKVFALASSNAVAQRWGKRFYAPIETETPHKVGVEFEESKDRIFTSPQKYVQGRHAFTRSYMYVKKWATKSAVVLADQNVWNICANKIVDSLSQNGMTVTKLVFGGEASLVELDKLRKQCPDDTQVIIGVGGGKTMDSAKYIAHSMNLPSIICPTTASSDAATSSLSVIYTPDGQFQKYSFYPLNPNLIFIDTDVIVRAPVRFLISGIGDALSTWVETESVIRSNSTSFAGGVASIAGRYIARACKDTLEKYALSAILSNTRGVCTEAFENVVEANTLMSGLGFENGGLAAAHAIHNGMTAIHGPVHRLMHGEKVAYGTLVQVVLEDWPLEDFNNLASFMAKCHLPITLEELGIPNVTDEELLMVGRATLRPDESIHNMSKKFNPSQIADAIKAVDSYSQKWQEQTGWTERFRLPPSRHSPHLTDIHP
Protein: Collagen alpha-2(IX) chain (Q07643)
Organism: Mus musculus (Mouse)
Function: Structural component of hyaline cartilage and vitreous of the eye.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen, type IX, alpha 3
- Collagen alpha-1
- CD44 antigen
- Platelet glycoprotein VI
- Collagen alpha-1
- Matrilin-3
- Integrin alpha-1
- Collagen alpha-2
- Collagen alpha-2
- Integrin beta-4
Sequence:
MTAVPAPRSLFVLLQVLWLALAQIRGPPGEPGPPGPPGPPGVPGSDGIDGDKGPPGKVGPPGSKGEPGKPGPDGPDGKPGIDGLMGAKGEPGPVGTPGVKGQPGLPGPPGLPGPGFAGPPGPPGPVGLPGEIGTPGPKGDPGPEGPSGPPGPPGKPGRPGTIQGLEGSADFLCPTNCPAGVKGPQGLQGVKGHPGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGEAGEKGDVGSQGARGPQGITGPKGITGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQGPPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDIGAPGVQGYPGLPGPRGLVGDRGVPGQPGRQGVVGRAASDQHIVDVVLKMIQEQLAEVAVSAKREALGAAGMVGLPGPPGPPGYPGKQGPNGHPGPRGIPGIVGAVGQIGNTGPKGKRGEKGDRGEMGHGHPGMPGPPGIPGLPGRPGQAINGKDGDRGSPGAPGEAGRPGRPGPVGLPGFCEPAACLGASAYTSARLTEPGSIKGP
Protein: R4 protein (O25555)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Addiction module toxin RelE
- Type II toxin-antitoxin system antitoxin
- Type II toxin-antitoxin system YafQ family toxin
Sequence:
MPNTTAKKDYTKYSKKQLFNLIHQLERKIKKMQNDRISFKEKMAKELEKRDQNFKDKIDALNELLQKISQAFDDKRDCCLGHEIPNIETQQAMRDVGNKETDLIVEDFSSYSNERKRALGVEAQS
Protein: Guanine nucleotide exchange factor LTE1 (Low temperature essential protein 1) (P07866)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GDP-GTP exchange factor for TEM1, a Ras-like protein, component of the mitotic exit network (MEN). Activation of TEM1 by LTE1 in the bud ultimately leads to activation of CDC15 followed by the release of CDC14 from the nucleolus, which then inactivates cyclin-dependent kinases (CDKs) activity by several mechanism. Required for TEM1 localization to the bud cortex during mitotic exit. Fine-tunes the timing of the mitotic exit and couples this event with cytokinesis.
Subcellular location: Cytoplasm. Bud. Note=The localization to the bud requires interaction with KEL1, as well as the presence of septins, CDC42, CLA4 and RAS2.
Interaction partners:
- Protein TEM1
- Kinetochore protein SLK19
- Sporulation-specific protein 12
- Protein phosphatase PP2A regulatory subunit B
- Tyrosine-protein phosphatase CDC14
- Cell division control protein 15
- Mitotic check point protein BUB2
- Serine/threonine-protein kinase KIN4
- Kelch repeat-containing protein 1
- Mitotic check point protein BFA1
Sequence:
MEIFSQKDYYPTPSSNVISYESDCVSKPVNSADLPALIVHLSSPLEGVDYNASADFFLIYRNFITPQDLHDLLIYRFRWCIREITTNAAKAKRRRIGEVALVRTFVLLRHSILNYFVQDFLPNITLRLRLIEFLNDKHIEQYPKIISSCIINLKKNWVHCSKLVWENIELNEPDKLDFDAWLHYSLKDFTQLESLHKRGSRLSIYARQSFASPDFRNQSVLSLYKTSDVFRLPEKLQSSNSSKNQRSPSMLLFPDNTSNVYSKHRIAKEPSVDNESEDMSDSKQKISHLSKVTLVSTLMKGVDYPSSYAVDKIMPPTPAKKVEFILNSLYIPEDLNEQSGTLQGTSTTSSLDNNSNSNSRSNTSSMSVLHRSAIGLLAKWMKNHNRHDSSNDKKFMSAIKPANQKPEMDAFVKYVVSISSLNRKSSKEEEEEFLNSDSSKFDILSARTIDEVESLLHLQNQLIEKVQTHSNNNRGPTVNVDCERREHIHDIKILQQNSFKPSNDNFSAMDNLDLYQTVSSIAQSVISLTNTLNKQLQNNESNMQPSPSYDALQRRKVKSLTTAYYNKMHGSYSAESMRLFDKDNSSSRTDENGPQRLLFHETDKTNSEAITNMTPRRKNHSQSQKSMTSSPLKNVLPDLKESSPLNDSREDTESITYSYDSELSSSSPPRDTVTKKSRKVRNIVNNTDSPTLKTKTGFLNLREFTFEDTKSLDEKKSTIDGLEKNYDNKENQESEYESTKKLDNSLDASSEANNYDITTRKKHSSCNHKIKQAVVRPASGRISISRVQSIAITPTKELSIVDPEQNKSNSVIEEISEIEPLNLEYNKKSALYSDTSSTVISISTSKLFESAQNSPLKQTQNPQREFPNGTSVSETNRIRLSIAPTIESVVSDLNSITTGSTVETFETSRDLPVPHQRIINLREEYQRGNQDIISNTSSLHELKTIDLSDSNNDLESPSTHAKNNKYFFSPDDGSIDVASPMKNVEELKSKFLKNESETNSNISGSVLTMDDIDINDTSSARNTRRANSESAFTGSLNKKNLNEIANMLDDSINDDPITVALMKLEGTYEKIPEKPENTKSSDAIGIKTSKLADEVEMLNLNNLPSFQNSPAEKRKSLLIERRRQTIMNIPFTPDQSEKEGFTSSSPEKIDVSANVDVAVQAAQIQELIGQYRIHDSRLMISNNESHVPFILMYDSLSVAQQMTLIEKEILGEIDWKDLLDLKMKHEGPQVISWLQLLVRNETLSGIDLAISRFNLTVDWIISEILLTKSSKMKRNVIQRFIHVADHCRTFQNFNTLMEIILALSSSVVQKFTDAWRLIEPGDLLTWEELKKIPSLDRNYSTIRNLLNSVNPLVGCVPFIVVYLSDLSANAEKKDWILEDKVVNYNKFDTNVQIVKNFIQRVQWSKFYTFKVNHELLSKCVYISTLTQEEINELST
Protein: Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase (EC 2.4.1.258) (Asparagine-linked glycosylation protein 3) (Dol-P-Man-dependent alpha(1-3)-mannosyltransferase) (Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase) (Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase) (HM-1 killer toxin resistance protein) (P38179)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol. Sensitive to H.mrakii HM-1 killer toxin.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:11308030}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Glc:Glc
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Man:Man
- Alpha-1,2-mannosyltransferase ALG9
- GDP-Man:Man
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichol-phosphate mannosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
Sequence:
MEGEQSPQGEKSLQRKQFVRPPLDLWQDLKDGVRYVIFDCRANLIVMPLLILFESMLCKIIIKKVAYTEIDYKAYMEQIEMIQLDGMLDYSQVSGGTGPLVYPAGHVLIYKMMYWLTEGMDHVERGQVFFRYLYLLTLALQMACYYLLHLPPWCVVLACLSKRLHSIYVLRLFNDCFTTLFMVVTVLGAIVASRCHQRPKLKKSLALVISATYSMAVSIKMNALLYFPAMMISLFILNDANVILTLLDLVAMIAWQVAVAVPFLRSFPQQYLHCAFNFGRKFMYQWSINWQMMDEEAFNDKRFHLALLISHLIALTTLFVTRYPRILPDLWSSLCHPLRKNAVLNANPAKTIPFVLIASNFIGVLFSRSLHYQFLSWYHWTLPILIFWSGMPFFVGPIWYVLHEWCWNSYPPNSQASTLLLALNTVLLLLLALTQLSGSVALAKSHLRTTSSMEKKLN
Protein: E3 ubiquitin-protein ligase listerin (EC 2.3.2.27) (RING-type E3 ubiquitin transferase listerin) (O74349)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Ubiquitination leads to cdc48 recruitment for extraction and degradation of the incomplete translation product.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q04781}. Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribosome quality control complex subunit 2
- Cell division cycle protein 48
- Ribosome quality control complex subunit 1
- Nuclear protein localization protein 4
- Ubiquitin fusion degradation protein 1
- Large ribosomal subunit protein eL6
Sequence:
MKKKSTDLYGRKNPGMQSMSGSFSSLQIALDESSSNFSTIYEPPDLSGLDAEMIVIVKNLQKRDIVTKCRALQDLIQWNDPSQFDNEQFLNALAVLFPRLSIEVERHVRLKIFVFMSVLSSALQKKLAPWLKFYITPWVMGFFDSDRAVSVSAKDSFKNLLSEEKWPHVWLKFGSTIAPIVTDVFLHEDKESLTDLRFFSNEEAESKVTRVKSSCLLTLSFLFKQTADLENLETDKKIDKQTFKSSLYENLSTLFKSDEFWSLVSSPQDGVTVSLSDLLLIILKYDKPFVTQYKEKYFKRVSRMISRLTSLTCVPMLRLLSNMISNFPNEVHQFANDSKRPLSKLFSNLITKRISLPNSGFYTSLLNLFKSIGAMQLVPSIESVDELCDAFLETANQEQRFLSTEVYDCLLNFLSFVYTDSSDPQIKDHVRDRLRTIFTRYFKGEFVLRCSTSDFDHCLQSVFDKNSDFASLWNEVLFGFFNDESMDIETIPFDSLSRNLSLTVQTVLYLKNRNFQTGNEVMSILGPCLSFLMKLSTHKNERIACLSASQLITVCHIFSDTTLIKPVKELFQKYLVNDLPSSILKLGPQSPAFTLLRDILLLLKDYADLSEPWENVANQFTVSFDELENIRVLNSLPSLFADGKLRGKISLVKTLVEYYDTAVFAIMQNPGNDWDMIRACIGSKEILVPEETIKNILFTTLEYFLTNDWVDNHLIILCASLHSLKAHLPTIFDENKSLYSLLPVILFSKPEDDGHVAAHFESIFSLLKEKALEDSGFSLKLCSEVQEWSLNKVLNGSINEKLAADKCVLVFNSFGKLPSNFFTFPASFWDAKISSCIPFFSNKLFIDQDFILGFLDLVASEPINVDMTDVGTQFVHIFHASLYTLYYVETTGCDGDALFNLTFAYLLIRIYLQNGIQSIIDVPIRDAGIFVESFECYFKGEVVKFMRDKDALTVLNELLIDDIDGKMPVLFKRFKNLSSAENTTSFSIFAAQGLTDFLIVVSNLLEMDEKHVDVVLGKLGLSSSKSPIFVSSILEGLKPLEVDSEIIQRIRFKAVNDLTGKLHSANEVSKSLLILNAATTQQITEKPLLPITRCRLFLENITNWCSESGIKSLELLPVCCFLRFMYYFLPTVFSLSGSYWNSIFDYIKYAMKMSVVDAPIVKSFELFALRLYNALSKNYEMNSDIKDCIVESNESMNYLLLKRFLFTHESTLRNSVTARMCNQYLVKLLENCPGKVVRSFQYQEFFPSLCNSNDLQMESVCMKFLREKLSHELKELTVYYMVESDYEPDVSLCPELLSLAIDFPGDPFVMVSKMEKYEHALRVYLLVWDLIFYHFEETTYNIKLSIINQLHAMDLLRPLLNTLVEILNLSYDRPINVDKYPKIDYNLMDYSSATDRIRCLAIHIYYQCLRHLSSSVRSYWSEVKNRAFTSTVESFTGYNVSPLLISASLDDVERSIESEDFQSVGDVNVKVNRNTREISFIYNVDEHKLEMAIKIPSVYPLQNVQVEGIERVGVNERQWRSWILASQSILSSQNGSITDALLVLKKNISMHFEGVEECAICYSVLSVERTLPNKRCGTCRHKFHASCLYKWFKSSNSSRCPLCRSSFTFV
Protein: 10 kDa heat shock protein, mitochondrial (Hsp10) (10 kDa chaperonin) (Chaperonin 10) (CPN10) (Early-pregnancy factor) (EPF) (Heat shock protein family E member 1) (P61604)
Organism: Homo sapiens (Human)
Function: Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- 60 kDa heat shock protein, mitochondrial
- GrpE protein homolog 1, mitochondrial
- Stress-70 protein, mitochondrial
- Mitochondrial disaggregase
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- Heat shock protein HSP 90-alpha
- GrpE protein homolog 2, mitochondrial
- Heat shock 70 kDa protein 4
- Heat shock protein HSP 90-beta
- T-complex protein 1 subunit alpha
Sequence:
MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD