wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4KAX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MVFPQRLYLHALLVACCCVLLLADAQRTHPSEVTALRSVKRSLLDPKDYLRNWNRGDPCRSNWTGVICFNEIGTDDYLHVRELLLMNMNLSGTLSPELQKLAHLEILDFMWNNISGSIPNEIGQISSLVLLLLNGNKLSGTLPSELGYLSNLNRFQIDENNITGPIPKSFSNLKKVKHLHFNNNSLTGQIPVELSNLTNIFHVLLDNNKLSGNLPPQLSALPNLQILQLDNNNFSGSDIPASYGNFSNILKLSLRNCSLKGALPDFSKIRHLKYLDLSWNELTGPIPSSNFSKDVTTINLSNNILNGSIPQSFSDLPLLQMLLLKNNMLSGSVPDSLWKNISFPKKARLLLDLRNNSLSRVQGDLTPPQNVTLRLDGNLICTNGSISNANLFCESKGKEWISLPNNSTNSALDCPPLACPTPDFYEYSPASPLRCFCAAPLRIGYRLKSPSFSYFPPYIDQFGEYVTDFLQMEPYQLWIDSYQWEKGPRLRMYLKLFPKVNETYTRTFNESEVLRIRGIFASWRFPGSDLFGPYELLNFTLQGPYSYVNFNSERKGVSWRRLAAITAGAVVTAVAISAVVAALLLRRYSKHEREISRRRSSSKASLLNSGIRGFSFKELAEATDDFSSSTLVGRGGYGKVYRGVLSDNTVAAIKRADEGSLQGEKEFLNEIELLSRLHHRNLVSLIGYCDEESEQMLVYEFMSNGTLRDWLSAKGKESLSFGMRIRVALGAAKGILYLHTEANPPVFHRDIKASNILLDPNFNAKVADFGLSRLAPVLEDEEDVPKHVSTVVRGTPGYLDPEYFLTHKLTDKSDVYSIGVVFLELLTGMHAISHGKNIVREVKTAEQRDMMVSLIDKRMEPWSMESVEKFAALALRCSHDSPEMRPGMAEVVKELESLLQASPDRETRVELASSSSVLSTSSSNVTRDLYESSSLLGSDLSSGFVPSIAPR
Protein: Ras-like protein rasZ (EC 3.6.5.2) (Q55CA9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Probable serine/threonine-protein kinase roco5
- Uncharacterized protein
- Rac guanine nucleotide exchange factor B
Sequence:
MASYKNNNLVRLCIMGDGGVGKTAVTIQFISNHFVYYYDPTIEDSYRKQCVIDDQVYMLDILDTAGQDELTAMRDQWIRSCEGFVLVYSITSRSSFDQVQFFREQIIRVLDRDDVPIMMIGNKSDLDDERQVTYQEGKDLARCLGMSFMEVSAKSRANIEEVFNETVRSVKRREESLLKKDKSKDGKDIKKKNSIIKKLNQKVNNTKTSICKMM
Protein: Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (POMGnT2) (EC 2.4.1.312) (Extracellular O-linked N-acetylglucosamine transferase-like) (Glycosyltransferase-like domain-containing protein 2) (Q5NDE5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: O-linked mannose beta-1,4-N-acetylglucosaminyltransferase that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D-mannosylprotein. Involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NAT1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8NAT1}.
Interaction partners:
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Protein O-mannosyl-transferase 1
- Protein O-mannosyl-transferase 2
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase
- Protein O-mannose kinase
- Dystroglycan 1
- Ribitol-5-phosphate xylosyltransferase 1
- Fukutin.
- Ribitol-5-phosphate transferase
- Beta-1,4-glucuronyltransferase 1
Sequence:
MNLPAVLNGLLVSVVAALLWKYVRLVEHTSQLEEELQLTRQSQEFSQVRIDYHGALLALQEHGTRMVCTGKMHTDRICRFDYLCYCTEAEEFVFFHSNASVMLPNLGSRRFQPALLDLSSVEDHNTQYFNFLELPAAALKFMPKPVFVPDVTLILNRFNPDNLMHIFHDDLLPVYYTMQQYSDLDDEARLVFMEGWGEGAHFDLYRLLSSKQPLLKDQLKTFGKLMCFTKSYVGLSKMTTWYQYGFVQPQGPKANILISGNEIRQFASFLMERLNITREEEEEDDDYIVVFKRTTNRLILNEAELLLALAQEFQMRTVTVSLEEQSFDNIIQIISRAAMLVSMHGAQMITSMFLPRGAAVVELFPYGVNPEQYTPYKTLASLPGMDLQYVAWRNTMEENTVTFPDRPWDQGGIVHLEKEEQERILASKEVPRHLCCRNPEWLFRIYQDTTVDLASFLDVLRDGLKKLNLKKAKVASTVHPGRVREPKCQTSVQATNEAKLSVSWQIPWNLKYLKVKEVKYEVWIQEQGENTYMPYILPHQNYTFSENIKPFTTYLVWVRCIFNKNLLGPFADVLICKT
Protein: Homeobox protein MSX-2 (Homeobox protein Hox-8) (P35548)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional regulator in bone development. Represses the ALPL promoter activity and antagonizes the stimulatory effect of DLX5 on ALPL expression during osteoblast differentiation. Probable morphogenetic role. May play a role in limb-pattern formation. In osteoblasts, suppresses transcription driven by the osteocalcin FGF response element (OCFRE). Binds to the homeodomain-response element of the ALPL promoter.
Subcellular location: Nucleus.
Interaction partners:
- Runt-related transcription factor 2
- Homeobox protein MSX-1
- Twist-related protein 1
- Homeobox protein DLX-5
- Msx2-interacting protein
- Osteocalcin
- Bone morphogenetic protein 4
- Paired box protein Pax-9
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor 2
Sequence:
MASPSKGNDLFSPDEEGPAVVAGPGPGPGGAEGAAEERRVKVSSLPFSVEALMSDKKPPKEASPLPAESASAGATLRPLLLSGHGAREAHSPGPLVKPFETASVKSENSEDGAAWMQEPGRYSPPPRHMSPTTCTLRKHKTNRKPRTPFTTSQLLALERKFRQKQYLSIAERAEFSSSLNLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPSSFSLPFPISSPLQAASIYGASYPFHRPVLPIPPVGLYATPVGYGMYHLS
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258 (Oligosaccharyl transferase subunit TMEM258) (Transmembrane protein 258) (P61165)
Organism: Homo sapiens (Human)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Involved in ER homeostasis in the colonic epithelium (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:28716842}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:26472760, ECO:0000269|PubMed:27974209}. Cytoplasm {ECO:0000269|PubMed:12427278, ECO:0000269|PubMed:28716842}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1
- Oligosaccharyltransferase complex subunit OSTC
- Malectin
Sequence:
MELEAMSRYTSPVNPAVFPHLTVVLLAIGMFFTAWFFVYEVTSTKYTRDIYKELLISLVASLFMGFGVLFLLLWVGIYV
Protein: Large ribosomal subunit protein uL30 (60S ribosomal protein L7) (P05426)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P18124}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL5
Sequence:
MEAVPEKKKKVAAALGTLKKKKVPAVPETLKKKRRNFAELKVKRLRKKFALKTLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASVNMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNSLVARSLGKFGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN
Protein: E3 ubiquitin-protein ligase APD2 (EC 2.3.2.27) (Protein ABERRANT POLLEN DEVELOPMENT 2) (Q6DBH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits E2-dependent E3 ligase activity. Involved in pollen mitosis II (PMII) regulation during male gametogenesis.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:22897245}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with intracellular membranes and in the tonoplast and endosomes in the germinating pollen tubes. {ECO:0000269|PubMed:22897245}.
Interaction partners:
- Plant-specific TFIIB-related protein PTF2
- Probable protein phosphatase 2C 68
- Probable protein phosphatase 2C 63
- Probable protein phosphatase 2C 79
- Probable protein phosphatase 2C 46
- V-type proton ATPase subunit c''2
- Probable protein phosphatase 2C 38
- Probable protein phosphatase 2C 64
- Probable protein phosphatase 2C 42
- Probable protein phosphatase 2C 67
Sequence:
MSLPDSLPSSSSSPPVTREETGFHRFEHHGNDSGFDHRDRPPWNRSEYDYRHGSVVASENVRNNSTSEDPWSCVVVVATFCIFVSMTLILGLYGTTNVWLGPNSSFLIKPTSVFVQNVIVEELGNKGSGLILYGLNQAPQLDVLTKWSEVHYLAVPNDSYKYWIQYLNKGSRVKVSYNVESVGSSLYLVIAQGVDGLSEWVQDPTRPDTTLSWHIISDSGYIEQDITKSSSYYVAVGNVYLNEVKATIDIQVEGVLYDTTNAYYNCSFPNDKCTLSVPLFGTNAAVLTSPGPKLNNSKNEFCAKLSYEPRWIAYIVCMGVVTALLLIVSSLFNKRQPVTEDETVDENDDVAPLIPGKDDDNSSWCSSYSSILTSTEELEGAHGEGHSSTRYLCAICYDAPRDCFFLSCGHCVACFQCGTRIAETSGFCPVCRKKIRKVKKIFNV
Protein: Putative kinase-like protein TMKL1 (P33543)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Does not seem to have conserved a kinase activity.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- C2 calcium/lipid-binding endonuclease/exonuclease/phosphatase
Sequence:
MGMEALRFLHVIFFFVLILHCHCGTSLSGSSDVKLLLGKIKSSLQGNSESLLLSSWNSSVPVCQWRGVKWVFSNGSPLQCSDLSSPQWTNTSLFNDSSLHLLSLQLPSANLTGSLPREIGEFSMLQSVFLNINSLSGSIPLELGYTSSLSDVDLSGNALAGVLPPSIWNLCDKLVSFKIHGNNLSGVLPEPALPNSTCGNLQVLDLGGNKFSGEFPEFITRFKGVKSLDLSSNVFEGLVPEGLGVLELESLNLSHNNFSGMLPDFGESKFGAESFEGNSPSLCGLPLKPCLGSSRLSPGAVAGLVIGLMSGAVVVASLLIGYLQNKKRKSSIESEDDLEEGDEEDEIGEKEGGEGKLVVFQGGENLTLDDVLNATGQVMEKTSYGTVYKAKLSDGGNIALRLLREGTCKDRSSCLPVIRQLGRIRHENLVPLRAFYQGKRGEKLLIYDYLPNISLHDLLHESKPRKPALNWARRHKIALGIARGLAYLHTGQEVPIIHGNIRSKNVLVDDFFFARLTEFGLDKIMVQAVADEIVSQAKSDGYKAPELHKMKKCNPRSDVYAFGILLLEILMGKKPGKSGRNGNEFVDLPSLVKAAVLEETTMEVFDLEAMKGIRSPMEEGLVHALKLAMGCCAPVTTVRPSMEEVVKQLEENRPRNRSALYSPTETRSDAETPF
Protein: Potassium channel domain-containing protein (Q3T9D4)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVDRGPLLTSAIIFYLAIGAAIFEVLEEPHWKEAKKNYYTQKLHLLKEFPCLSQEGLDKILQVVSDAADQGVAITGNQTFNNWNWPNAMIFAATVITTIGYGNVAPKTPAGRLFCVFYGLFGVPLCLTWISALGKFFGGRAKRLGQFLTRRGVSLRKAQITCTAIFIVWGVLVHLVIPPFVFMVTEEWNYIEGLYYSFITISTIGFGDFVAGVNPSANYHALYRYFVELWIYLGLAWLSLFVNWKVSMFVEVHKAIKKRRRRRKESFESSPHSRKALQMAGSTASKDVNIFSFLSKKEETYNDLIKQIGKKAMKTSGGGERVPGPGHGLGPQGDRLPTIPASLAPLVVYSKNRVPSLEEVSQTLKNKGHVSRPLGEEAGAQAPKDSYQTSEVFINQLDRISEEGEPWEALDYHPLIFQNANITFENEETGLSDEETSKSSVEDNLTSKERPEQGPMAEAPLSSTGEFPSSDESTFTSTESELSVPYEQLMNEYNKADNPRGT
Protein: Ras-related protein rab-39 (Rab family rab-39) (Q18969)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96DA2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96DA2}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q96DA2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96DA2}. Golgi apparatus {ECO:0000250|UniProtKB:Q96DA2}.
Interaction partners:
- Guanine nucleotide exchange protein smcr-8
- Rab8
- ALS/FTD Associated gene homolog
- Rab GDP dissociation inhibitor
- Rab proteins geranylgeranyltransferase component A 1
- Geranylgeranyl transferase type-2 subunit alpha
- Ras-related protein Rab-7a
Sequence:
METNFIGDDYGPLFHYQYRLIVIGDSTVGKSSLLRYFTEGKMAEISDPTVGVDFYARMIELRPGYRVKLQLWDTAGQEKFRSITKSYYRNSVGVLAIYDTTNRESFEHVENWVKEAALNLGGPSPSKCVFQLVGTKSDMDSQRQVNYEEGEYFAKYHKMKFIETSSRTGDNVNEAFHMIAQEIQNRVDDGELRPVDGWEGLKTGIMRSQSVCLSERSFPQNSSAGACGC
Protein: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (Q5AGZ8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_03184}.
Interaction partners:
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Phosphotransferase
- Phosphotransferase
- Hexokinase-2
- N-acetylglucosamine kinase 1
- Fructose-bisphosphate aldolase
- Transketolase
- Transaldolase
- Pyruvate kinase
Sequence:
MISIVNGTSTLSLVAGSVETLNQAINFYTNILGLSVHSEQNDWTYLSNDDNKMIVKIQLDTKSGLSLDQINDRRTEIIAKLNITDWRSLDTTSVLKVQNLVALIETLTTFNYTLQITPNELYPNEVYCVDPLGYIIGFTACDEPLTLVPPLQKSHPKPGLVSNLMSKSGSQSRNIEETKAVRRNIAVMTSGGDSQGMNAAVRAVVRATIFHGSKAFAVQEGYAGLVKGGPEYIKEMKWQDVRGFLSEGGTNIGTARCMEFKERWGRLKGCKNLIDAGIDGLIVCGGDGSLTGADLFRHEWPSLIQELKDKGEITNEQFERHKHLYICGMVGSIDNDMAMTDATIGGYSALERICRAIDYIDATANSHSRAFVVEVMGRHCGWLALMAGIATSADYIFIPEKPASSKDWQDQMCDIVGKHRAQGKRKTIVIVAEGAITSDLKPITSDEVKDVLVDRLGLDTRITVLGHVQRGGTAVAFDRTLATLQGVEAVKAILELTPDVPSPLIAIDENKICRRPLVEAVRITKSVASAIEAKDFEKAMSLRDHEFKEHLANFMAMNTANHEKPTLPREKRKKIAIINIGAPAGGMNSAVYAMATYCMSRGHTPYAIHNGFAGLSRHESVKSIEWIDIEGWNSIGGSEIGTNRQTPEETDIGMIAHYFEKYQFDGLIIVGGFEAFVSLEQLERSRAMYPSFRIPMVLIPATISNNVPGTEYSLGADTCLNSLMEYCDIVKQSASATRGTAFIIDVQGGNSGYIATFASLISGAQASYVPEEGISLQQLEMDINSLREAFAVEQGMTKSGKLIIKSSNASKVLTPHTLADIFNDECHGDFDTKTAIPGHVQQGGLPSPIDRSRGDRFAIRAVQFIEDHCDVLAPYRYELDFPIDDKKILNTAAVLGIKSSRLRFTSIRHLFDFETELGRRMPKTIYWNTIRDISDQLVGRTRLDKP
Protein: Wdr62 protein (Q5M9F2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
TNGKLPLWAKRLLGDDDVTDSSAFHAKRSYQPHGRWAERAEQEPLKTILDAWALDSYFTPMKPGNLEDSVLDSVEPQNLAGLLSESGSPKEDSRGHPSYLPLQREGTETRELILCSPEVEVTVTGMHREYYEEAEAGPEDQQGDSYLRVSSVSSKDQSPPEDSGESEAELECSFAAAHVSAPRTDPGPHLTMTEHSSTDELAQPGVPGLGNGSLPQTPEQEKFLRHHFETLTDAPAEELFPGSLGDIKISETDDYFFNPRLSISTQFLSRLQKTSRFPPRLPLHLMKSPEVQPVGQGGNQPKAGPLRAGTGYMSSDGTNVLSGQMAEETPEASCLPTPPITGLASCVPPSSVIPTDRKPPTPTSGLTTGREQSIPAPSPCSYLESTTSSHAKMTRSTSLGDSEGPVTGELPRPLHKPVSPGQEPQAVPTTVALTSSVKGHEPALPAWGNHEARASLRLTLSSVCEQLLSPPQLEPPTTPVWSQEAVDVPPSMAVTVASFSAPSPEDMSTLGLHSSVFLPKTSASGPLTPPAHPNSLQLLETRSRMPGSTPALLEPTPDASSGSPDSPGHCGEPGRRAEVPPPGPLELDSVESVLYRLQTAFQEALDLYRMLASSNQLGAEQQQAQTELASAFHWIHHQLEASNCVGAASVAPPLTLPSPGPPSPPTLCPLASPNLQALLEHYSELLVQAVRRKVRGD
Protein: Polyadenylate-binding protein (PABP) (Q803E7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
Sequence:
MNSGGPAYPLASLYVGDLHADVTEAMLYQKFSPAGQIMSIRVCRDVITRRSLGYAYINFQQPADAECALDTMNYEVIKGRPIRIMWSQRDPGLRKSGVGNIFIKNMDESIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAANRAIETMNGMLLNDRKVFVGHFKSRKEREAEMGAKAVEFTNVYIKNFGEDIDSEKLKNIFTEFGKTLSVCVMTDERGRSRGFGFVNFVNHGDARRAVTEMNGKELNGRVLYVGRAQKRLERQGELKRKFEQIKQERIQRYQGVNLYVKNLDDSIDDEKLRKEFAPYGTITSAKVMTDGGHSRGFGFVCFSSPEEATKAVTEMNGRIVSTKPLYVALAQRKEERKAILTNQYIQRLASIRAIPGPAIPTTYQQGSGYYMTSVPQVRSFYNAVPNLRPAPRWAFQAPRTQGPFPAQFVRQAVPRRPSTTISTVRQASTQVPHINNTQRMANIGTQTAGGRAAGTAVRGVSQYKYSAGVRNVQQVINAPAPVVHQVVQNTEPAVHMKGQEPLTASMLAAAPLKEQKQLLGERLYPLIQILHPALAGKITGMLLEIDNSELLHMLESPESLHAKVEEAVAVLQAHQAKEMSAK
Protein: E3 ubiquitin-protein ligase HUL5 (EC 2.3.2.26) (P53119)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-essential E3 ubiquitin-protein ligase that specifically catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains (By similarity). Accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Associates with the proteasome and promotes elongation of ubiquitin chains on substrates bound to the proteasome. Elongation of ubiquitin chains on substrates bound to the proteasome promotes proteasomal processivity. Also promotes ubiquitin elongation of 26S proteasome subunit RPN10. Involved in the stress response required to maintain cell fitness following heat-shock: acts by mediating ubiquitination of cytosolic misfolded proteins, leading to their subsequent degradation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21983566, ECO:0000305|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21983566}.
Interaction partners:
- E3 ubiquitin-protein ligase listerin
- Ubiquitin carboxyl-terminal hydrolase 6
- Protein SAN1
- Uncharacterized membrane protein YGL140C
- Ubiquitin carboxyl-terminal hydrolase RPN11
- Ubiquitin fusion degradation protein 4
- E3 ubiquitin-protein ligase UBR1
- E4 ubiquitin-protein ligase UFD2
- ERAD-associated E3 ubiquitin-protein ligase DOA10
- Polyubiquitin
Sequence:
MLNFTGQTRRRNVNLGNRTRNSKKDLLEKAKRERERRAQDKLKEDASKTIQKSIRRHFSNVRLFKNTFTSSQLVHMIPAYGGKLIYYISQYDLQQLLKLSHNFLSSYPNSLGNRQLLSLLKLYQDDALVAETLSDLNMDCPTVDEFLDSLSVYLCRASFLSYSSASKLADVIEAWEVMHSSASISIFSISIGSYEKRPFALQFYCILAERNLLPQLINTNPILWDNMAKTYSHCSKGGQKNIAKLLIPNFNNHIAPSVLRSDNDYVLKFYEKAFIDEVIATTANYVSDEDHVKNLMCYIASSPNQSCKNSVLITLLSNKDFVRRLSWEFFHTKFNASKTEAHPLFSVLAQLIDMHLLISTDRELLDYNSVIPIEELKKFTSTLKDFTFRQYWELPKSERNPMLKEAVPLLSKVYERDSRLHFLSTENNPTYWENSEKQFLNLRFYEELQEYEDLYREHLEEESDEDMEKEIDLDKERPPLKSLLLNKMKKRLKSSLRFRKLEILLELPFFIPFEERVDLFYMFIALDKKRLSLDDDHNLINMFTPWASTGMRKQSAIISRDNVLEDAFNAFNSIGERFKASLDVTFINEFGEEAGIDGGGITKEFLTTVSDEGFKDPKHELFRTNDRYELYPSVVYDATKLKYIWFLGKVVGKCLYEHVLIDVSFADFFLKKLLNYSNGFLSSFSDLGSYDSVLYNNLIKLLNMTTDEIKSLDLTFEIDEPESSAKVVDLIPNGSKTYVTKDNVLLYVTKVTDYKLNKRCFKPVSAFHGGLSVIIAPHWMEMFNSIELQMLISGERDNIDLDDLKSNTEYGGYKEEDQTIVDFWEVLNEFKFEEKLNFLKFVTSVPQAPLQGFKALDPKFGIRNAGTEKYRLPTASTCVNLLKLPDYRNKTILREKLLYAINSGARFDLS
Protein: DNA-directed RNA polymerase I subunit 1 (DNA-directed RNA polymerase I subunit RPA1) (DNA polymerase I subunit A1) (EC 2.7.7.6) (Nuclear RNA polymerase A1) (Q9SVY0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from NRPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P10964}.
Interaction partners:
- DNA-directed RNA polymerase I subunit 2
- DNA binding / DNA-directed RNA polymerase
- DNA-directed RNA polymerase family protein
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase subunit
- RNApolymerase 14 kDa subunit
- DNA-directed RNA polymerase III subunit 2
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerase subunit 10-like protein
Sequence:
MAHAQTTEVCLSFHRSLLFPMGASQVVESVRFSFMTEQDVRKHSFLKVTSPILHDNVGNPFPGGLYDLKLGPKDDKQACNSCGQLKLACPGHCGHIELVFPIYHPLLFNLLFNFLQRACFFCHHFMAKPEDVERAVSQLKLIIKGDIVSAKQLESNTPTKSKSSDESCESVVTTDSSEECEDSDVEDQRWTSLQFAEVTAVLKNFMRLSSKSCSRCKGINPKLEKPMFGWVRMRAMKDSDVGANVIRGLKLKKSTSSVENPDGFDDSGIDALSEVEDGDKETREKSTEVAAEFEEHNSKRDLLPSEVRNILKHLWQNEHEFCSFIGDLWQSGSEKIDYSMFFLESVLVPPTKFRPPTTGGDSVMEHPQTVGLNKVIESNNILGNACTNKLDQSKVIFRWRNLQESVNVLFDSKTATVQSQRDSSGICQLLEKKEGLFRQKMMGKRVNHACRSVISPDPYIAVNDIGIPPCFALKLTYPERVTPWNVEKLREAIINGPDIHPGATHYSDKSSTMKLPSTEKARRAIARKLLSSRGATTELGKTCDINFEGKTVHRHMRDGDIVLVNRQPTLHKPSLMAHKVRVLKGEKTLRLHYANCSTYNADFDGDEMNVHFPQDEISRAEAYNIVNANNQYARPSNGEPLRALIQDHIVSSVLLTKRDTFLDKDHFNQLLFSSGVTDMVLSTFSGRSGKKVMVSASDAELLTVTPAILKPVPLWTGKQVITAVLNQITKGHPPFTVEKATKLPVDFFKCRSREVKPNSGDLTKKKEIDESWKQNLNEDKLHIRKNEFVCGVIDKAQFADYGLVHTVHELYGSNAAGNLLSVFSRLFTVFLQTHGFTCGVDDLIILKDMDEERTKQLQECENVGERVLRKTFGIDVDVQIDPQDMRSRIERILYEDGESALASLDRSIVNYLNQCSSKGVMNDLLSDGLLKTPGRNCISLMTISGAKGSKVNFQQISSHLGQQDLEGKRVPRMVSGKTLPCFHPWDWSPRAGGFISDRFLSGLRPQEYYFHCMAGREGLVDTAVKTSRSGYLQRCLMKNLESLKVNYDCTVRDADGSIIQFQYGEDGVDVHRSSFIEKFKELTINQDMVLQKCSEDMLSGASSYISDLPISLKKGAEKFVEAMPMNERIASKFVRQEELLKLVKSKFFASLAQPGEPVGVLAAQSVGEPSTQMTLNTFHLAGRGEMNVTLGIPRLQEILMTAAANIKTPIMTCPLLKGKTKEDANDITDRLRKITVADIIKSMELSVVPYTVYENEVCSIHKLKINLYKPEHYPKHTDITEEDWEETMRAVFLRKLEDAIETHMKMLHRIRGIHNDVTGPIAGNETDNDDSVSGKQNEDDGDDDGEGTEVDDLGSDAQKQKKQETDEMDYEENSEDETNEPSSISGVEDPEMDSENEDTEVSKEDTPEPQEESMEPQKEVKGVKNVKEQSKKKRRKFVRAKSDRHIFVKGEGEKFEVHFKFATDDPHILLAQIAQQTAQKVYIQNSGKIERCTVANCGDPQVIYHGDNPKERREISNDEKKASPALHASGVDFPALWEFQDKLDVRYLYSNSIHDMLNIFGVEAARETIIREINHVFKSYGISVSIRHLNLIADYMTFSGGYRPMSRMGGIAESTSPFCRMTFETATKFIVQAATYGEKDTLETPSARICLGLPALSGTGCFDLMQRVEL
Protein: Inwardly rectifying potassium channel 1, isoform E (A0A0B4JCZ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
Sequence:
MKRLMTWERDLVDAMYEYRQTRFSSRRVRKRVVFKHGECNVVQGNVAKRRRRYLQDIFTTLVDAQWRWTLLVFAASFVFSWAFFGFIWWIIAYAHNDLEYTNLKNQSPDLVANITHTVCVTQVSNMMSAFLYSVETQTTIGYGNRYVTEECPEAIFTMCIQCITGVFIQAFMVGIVFAKLSRPKKRAQTLLFSRNAVICHRDGVPCLMFRVGDMRKSHIIEAHVRAQIIRKKVTKEGEVLPFYQQELHIGADGGEDRLMFIWPTTIVHKIDRNSPLYMLSASDMLKERFEVVVMLEGVIESTGMTTQARSSYLPSEVLWGHRFVNVVSFRKETGEYEVDYTLFNNTYDVDTPLCSAKQLDELKSEYSKSAKCVNAPFADRTLSASLFQRIASAASVDHLDPASDESLDSGRLQIRSHSIPNGVLASELEPLNNNKHGASFTMGGLTITTTAPSIPNLSSINEKTNSGNSINSSNYSNNNSLSTLTGGGSAASGPGGGITIVAGSGNHGGAGGGGGGGGRHKSNPRRLSIKQDQLPIDSIC
Protein: T-complex protein 1 subunit gamma (TCP-1-gamma) (CCT-gamma) (Q3T0K2)
Organism: Bos taurus (Bovine)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit epsilon
- Uncharacterized protein
- Chaperonin containing TCP1 subunit 8 like 2
- T-complex protein 1 subunit zeta-2
Sequence:
MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDTSNRDTMLNIINSSITTKVISRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSRPEELREEDVGTGAGLLEIKKIGDEYFTFITECKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQSRQGGAPDAGQE
Protein: Cholecystokinin (CCK) [Cleaved into: Cholecystokinin-33 (CCK33); Cholecystokinin-12 (CCK12); Cholecystokinin-8 (CCK8)] (P09240)
Organism: Mus musculus (Mouse)
Function: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion.
Subcellular location: Secreted {ECO:0000269|PubMed:23863714}.
Interaction partners:
- Cholecystokinin receptor type A
- Gastrin/cholecystokinin type B receptor
- C-C motif chemokine 28
- Gastrin
- Appetite-regulating hormone
- Somatostatin
- Protachykinin-1
- Annexin A5
- Pro-neuropeptide Y
- Pro-glucagon
Sequence:
MKSGVCLCVVMAVLAAGALAQPVVPAEATDPVEQRAQEAPRRQLRAVLRTDGEPRARLGALLARYIQQVRKAPSGRMSVLKNLQSLDPSHRISDRDYMGWMDFGRRSAEDYEYPS