wanglab/gogpt-training-data huggingface dataset:
Protein: I[[h]] channel, isoform G (B7YZE8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MHVKHTQRRVSGPGAFGTFTNDQRASRDNLCPDNQQQQQQRHSHSHQHLVRQSLVSLSNGQPAASAAPDSVSLLRAGDDQQQHPQQPHLQQQQQQQQHLQQQQQRHRSSSSRLSTSGISKQNSSDSRSGLRILDSSHSPVSCGTQSVSSTGGQSALYDACHEYSRSLSAAAAEGAASLLKSHYSDQQLAQTEPDPEPDPERDRDRDRDRDRDRERERRHLTNLNLNLSSEYDYSGSDKQQLVNETYIFKCIANSPSFLRTNKIKEQSKKLRNLSLKTRTAKKKGQIISKSNAVSDNSLHPGDKYLNLYLVEKKHSLQPQVASTSSSINTTHPQASSAPASSSSTCTKAPQLPALSAVAARQQQLLLNGSLKGKGQSQSQGQSRQTLPGHRASVRSESGSGSSHTIPATGKSPPVPHSLAAKISSSASGSKNCNLLSASSNSCHKLNAHAQGSGAGSGSGSGSGSGPPGHSHYAAASPKSSVSSNGHLNKYCLTDLTRRKAEFNRQLSAPTDYTHHSSSNGSQQEGSSEANEGHEPVGESTITVASAGVSYPHPYSYPYHYAHHASSATAPANLKASLQLHSFGSHHPCPYPARPTSTSCTNSFNRRHIRRHKGKLGDRLLSGDSEESVRCSYCSVLNVNDNDLRISFENTCTDSLVTAFDDEALLICDQGTEMVHFDDVSLYGTPKEEPMPNIPIVSEKVSANFLKSQLQSWFQPTDNRLAMKLFGSRKALVKERIRQKTSGHWVIHPCSSFRFYWDLCMLLLLVANLIILPVAISFFNDDLSTRWIAFNCLSDTIFLIDIVVNFRTGIMQQDNAEQVILDPKLIAKHYLRTWFFLDLISSIPLDYIFLIFNQDFSDSFQILHAGRALRILRLAKLLSLVRLLRLSRLVRYVSQWEEVYILQNLQKKSADRRGRMNRKDKDGLTKSNLILKFLNMASVFMRIFNLICMMLLIGHWSGCLQFLVPMLQGFPSNSWVSINELQESYWLEQYSWALFKAMSHMLCIGYGRFPPQSLTDMWLTMLSMISGATCYALFLGHATNLIQSLDSSRRQYREKVKQVEEYMAYRKLPRDMRQRITEYFEHRYQGKFFDEELILGELSEKLREDVINYNCRSLVASVPFFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGEVATSLSDGSYFGEICLLTNARRVASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTMETVAAERLNKIGKNPNIMHQKDEQLSNPESNTITAVVNALAAEADDCKDDDMDLKENLLHGSESSIAEPVQTIREGLPRPRSGEFRALFEGNTP
Protein: Mucosal addressin cell adhesion molecule 1 (MAdCAM-1) (hMAdCAM-1) (Q13477)
Organism: Homo sapiens (Human)
Function: Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Isoform 2, lacking the mucin-like domain, may be specialized in supporting integrin alpha-4/beta-7-dependent adhesion strengthening, independent of L-selectin binding.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin alpha-4
- L-selectin
- Atypical chemokine receptor 2
- Integrin beta-7
- C-C chemokine receptor type 9
- C-C motif chemokine 25
- Immunoglobulin kappa variable 2D-29
- Protein N-terminal asparagine amidohydrolase
- Vascular cell adhesion protein 1
- Intercellular adhesion molecule 1
Sequence:
MDFGLALLLAGLLGLLLGQSLQVKPLQVEPPEPVVAVALGASRQLTCRLACADRGASVQWRGLDTSLGAVQSDTGRSVLTVRNASLSAAGTRVCVGSCGGRTFQHTVQLLVYAFPDQLTVSPAALVPGDPEVACTAHKVTPVDPNALSFSLLVGGQELEGAQALGPEVQEEEEEPQGDEDVLFRVTERWRLPPLGTPVPPALYCQATMRLPGLELSHRQAIPVLHSPTSPEPPDTTSPESPDTTSPESPDTTSQEPPDTTSPEPPDKTSPEPAPQQGSTHTPRSPGSTRTRRPEISQAGPTQGEVIPTGSSKPAGDQLPAALWTSSAVLGLLLLALPTYHLWKRCRHLAEDDTHPPASLRLLPQVSAWAGLRGTGQVGISPS
Protein: Ubiquitin-like modifier-activating enzyme 1 (EC 6.2.1.45) (Ubiquitin-activating enzyme E1) (Q55C16)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin-like domain-containing protein
- E1 ubiquitin-activating enzyme
- Ubiquitin-conjugating enzyme E2
- GST C-terminal domain-containing protein
- GST C-terminal domain-containing protein
- Probable ubiquitin-conjugating enzyme E2 C
- E2 ubiquitin-conjugating enzyme
- Ubiquitin-conjugating enzyme E2
Sequence:
MSKPMDVEQEPKIDDALYSRQLYALSHETMKKITSTSVLVVGLQGLGIEIVKDLSLAGVKSVTLYDKELVEIKDLSSQFYFSPEQVGKVGRADACFQKVVDLNNYVRIDVHNGELSDEFLKKFNVVVLANQPLALQLKVNEFCHANKIHFISVETRGVFGQLFNDFGEQFTITDTNGENPNAYMISSISQDKEGIVTVVEEQKLQLLDGDLVTFKEVNGMSALNDLPPQKIKTISPLTFSIGDTTNLPPYTSGGYVTEVKQPKVVDFKPLKNILESGENIFITDDFKFTQPTNLLAGFQAIHKFAEKNKHMPRPHNKEDANAVIEIAKGLLKKPDDELDEKMITQLSFGAQGDIVPMQAILGGITAQEVLKACSGKFTPIHQLAFFDSVECLPEDLETLPEEEFQPIGSRYDGQIITFGKTLQNKIENLNYFLVGAGAIGCEMLKNFAMMGLGAGPKGLVHVTDMDTIEKSNLNRQFLFRSSDIQQLKSQTAANAVRVMNPDLNVKAYSLRVGPDTESHYNEEFFNSLDGVCNALDNVEARLYMDSQCVYYGKPLLESGTLGTKGNTQVVVPHLTESYSSSRDPPEKGIPVCTLHNFPNAIEHTIQWARDTFEGLFKNNADNVNSYLTNPAYVQSLKTQNPFVRLETLASIKASLMDRPLDFNQCIAWARLKFEEYFNNNIEQLLYNFPKDMVTTTGTPFWSGPKRAPTPLKFDVENPLHLEFIVAAANLRAFNYGIKAETNIEVIQKQAANVIVPDFTPKKVKIQTSENEPAPSSNTQQAGGDAEDDQCDTILSQLPQPSEMAGYKINSIQFEKDDDTNHHIDFITATSNLRATNYAISPADKHKTKGIAGKIIPALVTTTAVVAGFVCIELIKVIQNKALEKYKSTFMNLGIPFFGFVEPIAAPKNKIREGWTWTLWDRFDVDGDITLKEFLDLFEKKHGLDISMLSCKVTLLYALFTDKKTKEERLKMKISQLYETLSKKPLPKDKKYLLLEICCNDTETGDDVDVPSVRYKYN
Protein: EG:165H7.3 protein (O46055)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRSELEPRASGAHSDRNIQITDTRKDRKGHGKCTSNARKREIETNLLAFKSQPEAWQLCLRVATSSDTTENQFLWFFSTSTLEHTITRRWTQLTSTDKTLLRETLWNSYAQLGATPNVAKRHRDTLAQLIALLGKREFPEQDPNYMQHCMELTKTRFQLGINLLKITSEEVVSNRGDLTTEWKQYFYSCISMCVPDVLDLVTKYLLIAVCHINGKDIQTTIPNTLMDFSLTSALPNDNQLSSSILDLLGCVQHLVSWIRTELISEYFLMSILDLSQWRPAHEPISLAALSVLNELLYLQKPLPFPGPLMGGVTSLLEQHNNNRRQSEMYSDKFRELLRLYTTKYAAKLMQEPDLLETFLNLLYSCTTELHGALDFTEKLEIWTPIIKGIAQHPAKITRYNNVLTQLVDEIMRRTQFEANKPELEVLDNELMEDDTSATEWQQFLDQCFESLALLANTRGAHIVFAQVYNHWSRPQMYLLSLEHALDHGSARSYEAARKLKGANVGEILRDFATVCQAVVRLAPLMDSSTAAPGVADEMECQLQMLSDSLLQTLQLLASNRLYSGGSEMDKATFQTDLDNLYAQVLLAMRSIFPLTKAMSGEELLHRLFAILGSIFACNGSLTAASPIVQQAASELLLFISTVIRPKCLLDIPQIQSLLQAGSRLGAQLPRQVCINVHISLVSYMVLPWKSVPEQQQEYPRRLWMLREYVQGLAQNFLDLDLGQANESKVAATTLSLLGTFTALIEYFKATGGNAKDMLASTFKPILTKALMIFNNFGQSSIAMAITVAEFSLSMLRTLPTHLGAQFIKEMITLFISVSSREQLTLSRLAVMEKILQMFKLIVEQPGSASLGLLPSILDFSTQQILPLLQQQNAATDNSEITSLLYALFDSVLTCKWQFFYKNQLSNGHSGGGSGNFNCSDNLHPAHFMAILNAYGQMLVSGTDPSNVRSVLFSMQNVNERSRLYQRALFKEQLLASFQRALLNLLLSGEGSLHFDMIAQALYAMGQVDRRQLLESFVHASLPVAQTSLEEICQTNDIPTFTQKLTQLMQDAHCVHLNETA
Protein: SPI-1 type 3 secretion system translocon protein SctE (SPI-1 T3SS translocon protein SctE) (Cell invasion protein SipB) (Effector protein SipB) (Q56019)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in association with its chaperone SicA, is regulated by binding of InvE.
Subcellular location: Secreted {ECO:0000269|PubMed:10972796, ECO:0000269|PubMed:10972831, ECO:0000269|PubMed:17768243, ECO:0000269|PubMed:7608068}. Host membrane {ECO:0000269|PubMed:10972796, ECO:0000269|PubMed:10972831, ECO:0000269|PubMed:23544147}; Multi-pass membrane protein {ECO:0000269|PubMed:12068811}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS) (PubMed:17768243, PubMed:7608068). Becomes surface exposed upon contact with host cells (PubMed:19364837). Inserted into the host cell membrane (PubMed:23544147). {ECO:0000269|PubMed:17768243, ECO:0000269|PubMed:19364837, ECO:0000269|PubMed:23544147, ECO:0000269|PubMed:7608068}.
Interaction partners:
- Chaperone protein SicA
- Inositol phosphate phosphatase SopB
- Cell invasion protein SipA
- SPI-1 type 3 secretion system translocon protein SctB
- Cell invasion protein SipD
- Protein PrgH
- Guanine nucleotide exchange factor sopE2
- Secreted effector protein SptP
- Surface presentation of antigens protein SpaN
- SPI-1 type 3 secretion system secretin
Sequence:
MVNDASSISRSGYTQNPRLAEAAFEGVRKNTDFLKAADKAFKDVVATKAGDLKAGTKSGESAINTVGLKPPTDAAREKLSSEGQLTLLLGKLMTLLGDVSLSQLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAKSVYDAATKKLTQAQNKLQSLDPADPGYAQAEAAVEQAGKEATEAKEALDKATDATVKAGTDAKAKAEKADNILTKFQGTANAASQNQVSQGEQDNLSNVARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQAEMEKKSAEFQEETRKAEETNRIMGCIGKVLGALLTIVSVVAAVFTGGASLALAAVGLAVMVADEIVKAATGVSFIQQALNPIMEHVLKPLMELIGKAITKALEGLGVDKKTAEMAGSIVGAIVAAIAMVAVIVVVAVVGKGAAAKLGNALSKMMGETIKKLVPNVLKQLAQNGSKLFTQGMQRITSGLGNVGSKMGLQTNALSKELVGNTLNKVALGMEVTNTAAQSAGGVAEGVFIKNASEALADFMLARFAMDQIQQWLKQSVEIFGENQKVTAELQKAMSSAVQQNADASRFILRQSRA
Protein: Small ribosomal subunit protein eS27 (40S ribosomal protein S27) (Q71TY3)
Organism: Rattus norvegicus (Rat)
Function: Component of the small ribosomal subunit (By similarity). Required for proper rRNA processing and maturation of 18S rRNAs (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P42677}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P42677}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS7
- Ubiquitin-ribosomal protein eL40 fusion protein
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein eS8
Sequence:
MPLAKDLLHPSPEEEKRKHKKKRLVQSPNSYFMDVKCPGCYKITTVFSHAQTVVLCVGCSTVLCQPTGGKARLTEGCSFRRKQH
Protein: Ribosomal protein L1p/L10e family (T2D23.8 protein) (Q9LMI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ribosome biogenesis protein BOP1 homolog
- AT5g04600/T32M21_200
- Bystin
- Periodic tryptophan protein 2
- At4g28200
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Putative U3 small nucleolar ribonucleoprotein
- Nucleolar protein
- Putative WD-repeat membrane protein
- Probable rRNA-processing protein EBP2 homolog
Sequence:
MSTTTTTAALPQRHQSKVDPQNVNRAVKSLLKWWDSKSKTENSESLENDGFVYLIVTLKRIPQLDRTNPLMIPLPHPLIDLVAEDPPELCLIIDDKHKNKITKEAALKKIEAEKIPITTVIKVSKLKSDLRKLEEEKRFELYFAERRLMPMLPKLLGKEFVKKNKTPIAINLRHGSWKEQIEKACESALFFVGTGTCSVVKVAKLSMGRNEIAENVVAAMNGIGDLVPGRWKNVKLFHLKLLESLALPVYQSVA
Protein: Nuclear elongation and deformation protein 1 (Q9UUJ6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May have a role in the maintenance of the nuclear envelope structure and in minichromosome stability.
Interaction partners:
- Probable diacylglycerol pyrophosphate phosphatase 1
- CTP-dependent diacylglycerol kinase 1
- Diacylglycerol O-acyltransferase 1
- Sporulation-specific protein spo7
- Nuclear envelope morphology protein 1
- Phospholipid:diacylglycerol acyltransferase
- Putative phosphatidate cytidylyltransferase
- Uncharacterized acyltransferase C1851.02
- Putative lysophosphatidic acid:oleoyl-CoA acyltransferase
- Lysophospholipid acyltransferase
Sequence:
MQYVGRAFDSVTKTWNAINPSTLSGAIDVIVVEQEDKTLACSPFHVRFGKFSLLLPSDKKVEFSVNGQLTGFNMKLGDGGEAFFVFATENAVPRELQTSPIVSPTTSPKQTPSINVTEPQDLELDKVSQDHEKDQSNTYLMEDGYEFPLTRDLIRRSKSDADQTPPTGFKHLRHSSCLEMAGSDRTPSMPATTLADLRLLQKAKELGKRLSGKELPTRVGDNGDVMLDMTGYKSSAANINIAELARETFKDEFPMIEKLLREDEEGNLWFHASEDAKKFAEVYGHSPPASPSRTPASPKSDSALMDEDSDLSRRHSLSEQSLSPVSESYPQYAKTLRLTSDQLRSLNLKPGKNELSFGVNGGKAICTANLFFWKHNDPVVISDIDGTITKSDALGHMFTLIGKDWTHAGVAKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNIEQNGYSLPDGPVILSPDRTMAALHREVILRKPEVFKMACLRDLCNIFALPVPRTPFYAGFGNRITDAISYNHVRVPPTRIFTINSAGEVHIELLQRSGHRSSYVYMNELVDHFFPPIEVSTRDEVSSFTDVNFWRSPLLELSDEEEDDTNKSTSKSPKTPKNTKFGYQEFEGIDEEDAQDYSPSPLIKSFNELMFEGEEDEEGEEDVENAV
Protein: Ubiquitin carboxyl-terminal hydrolase 4 (EC 3.4.19.12) (Deubiquitinating enzyme 4) (Ubiquitin thioesterase 4) (Ubiquitin-specific-processing protease 4) (Vacuole biogenesis protein SSV7) (P32571)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Involved in the ammonium-induced down-regulation of the GAP1 permease and the UME3 destruction in response to oxidative stress. Has a role in the RAD9 checkpoint response to TOP1 poisons. Required for promoting coordination of DNA replication and avoids DNA overreplication.
Subcellular location: Cytoplasm. Late endosome membrane; Peripheral membrane protein. Note=Recruited to the late endosome by BRO1.
Interaction partners:
- Vacuolar-sorting protein BRO1
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein-sorting-associated protein 24
- Vacuolar-sorting protein SNF7
- DOA4-independent degradation protein 4
- Vacuolar protein sorting-associated protein 4
- Polyubiquitin
- Vacuolar protein sorting-associated protein 27
- E3 ubiquitin-protein ligase RSP5
- Ubiquitin carboxyl-terminal hydrolase 5
Sequence:
MEQNIISTIRDECIRHRSKYLTIAQLTAIAEAKINEFIITGKAKDQDLSSLLDKCIDILSIYKKNSKDIKNIISCKNKGAMISSNSVMIIQLNYVYYKVIHIIVTTNIPHLSEFAKIKLHKSTSDEGNGNNNNNEFQLMNIYNTLLETLLKDENIAKIKSFIKSSIKQTKLNHEQEECNLMRTGSYITSNQLNSLISSSANSASSQMEILLIDIRSRLEFNKSHIDTKNIICLEPISFKMSYSDHDLEKKSLITSPNSEIKMFQSRNLFKFIILYTDANEYNVKQQSVLLDILVNHSFEKPISDDFTKIFILESGFPGWLKSNYGRQVSSSFPSNNNIKDDSVYINGNTSGLSLQHLPKMSPSIRHSMDDSMKEMLVAPTPLNHLQQQQQQQSDNDHVLKRSSSFKKLFSNYTSPNPKNSNSNLYSISSLSISSSPSPLPLHSPDPVKGNSLPINYPETPHLWKNSETDFMTNQREQLNHNSFAHIAPINTKAITSPSRTATPKLQRFPQTISMNLNMNSNGHSSATSTIQPSCLSLSNNDSLDHTDVTPTSSHNYDLDFAVGLENLGNSCYMNCIIQCILGTHELTQIFLDDSYAKHININSKLGSKGILAKYFARLVHMMYKEQVDGSKKISISPIKFKLACGSVNSLFKTASQQDCQEFCQFLLDGLHEDLNQCGSNPPLKELSQEAEARREKLSLRIASSIEWERFLTTDFSVIVDLFQGQYASRLKCKVCSHTSTTYQPFTVLSIPIPKKNSRNNITIEDCFREFTKCENLEVDEQWLCPHCEKRQPSTKQLTITRLPRNLIVHLKRFDNLLNKNNDFVIYPFLLDLTPFWANDFDGVFPPGVNDDELPIRGQIPPFKYELYGVACHFGTLYGGHYTAYVKKGLKKGWLYFDDTKYKPVKNKADAINSNAYVLFYHRVYGV
Protein: cDNA FLJ20813 fis, clone ADSE01247 (cDNA: FLJ23023 fis, clone LNG01678) (Q9NWJ2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVSSQQGEIMESRIFFQGSHAHFPTCMNVDTAATVLAVNVNLASNHCSQGNVPIRRRLSGTLILTGRWDILRDPEAGCHLLNFPEGCLESVSSHSELFFLLWLTKNMEPHKVHCNSFIFVK
Protein: Protein WAVE-DAMPENED 2 (AtWVD2) (Q84ZT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Microtubule-associated protein (MAP) that regulates the orientation of interphase cortical microtubules. Able to bundle microtubules in vitro. Modulates both rotational polarity and anisotropic cell expansion during organ growth. Promotes clockwise root and etiolated hypocotyls coiling, clockwise leaf curling, but left-handed petiole twisting.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17319849}.
Interaction partners:
- Flavin-containing monooxygenase FMO GS-OX-like 3
- Flavin-containing monooxygenase FMO GS-OX-like 5
- Protein SPIRAL1
- Flavin-containing monooxygenase FMO GS-OX-like 9
- Flavin-containing monooxygenase FMO GS-OX-like 8
- Putative flavin-containing monooxygenase 2
- Plasma membrane-associated cation-binding protein 2
- Flavin-containing monooxygenase FMO GS-OX-like 1
- Flavin-containing monooxygenase FMO GS-OX-like 4
- Flavin-containing monooxygenase FMO GS-OX-like 6
Sequence:
MRREVFESVSTNASNERVHVAPKIAAEEQDYEEKECTEENSLSQNHKSSNVITENDSKKKNLDEEDDCSVASSMKNAKSKVTHGTAPRFRSAQRAEKRKEYYQKLEEKHQALEAERIELEQRQKEEQEAAIKQLRKNLKFKANPVPDFYYQRPPVKPELKKFPLTRPKSPKLNLSRRKSCSDAITSSGEENSNSQNRQSVVE
Protein: Large ribosomal subunit protein uL3 (60S ribosomal protein L3) (Maintenance of killer protein 8) (RP1) (Trichodermin resistance protein) (YL1) (P14126)
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. uL3 plays a role in coordinating processes of accommodating the aminoacyl-tRNA in the PTC.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS26B
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL24A
- Large ribosomal subunit protein eL21A
- Large ribosomal subunit protein eL6A
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein uL5A
Sequence:
MSHRKYEAPRHGHLGFLPRKRAASIRARVKAFPKDDRSKPVALTSFLGYKAGMTTIVRDLDRPGSKFHKREVVEAVTVVDTPPVVVVGVVGYVETPRGLRSLTTVWAEHLSDEVKRRFYKNWYKSKKKAFTKYSAKYAQDGAGIERELARIKKYASVVRVLVHTQIRKTPLAQKKAHLAEIQLNGGSISEKVDWAREHFEKTVAVDSVFEQNEMIDAIAVTKGHGFEGVTHRWGTKKLPRKTHRGLRKVACIGAWHPAHVMWSVARAGQRGYHSRTSINHKIYRVGKGDDEANGATSFDRTKKTITPMGGFVHYGEIKNDFIMVKGCIPGNRKRIVTLRKSLYTNTSRKALEEVSLKWIDTASKFGKGRFQTPAEKHAFMGTLKKDL
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (A0A0U1ZFN5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAGNVKKSSGAGGSGSGGSGAGGLIGLMKDAFQPHHHHHHHLSPHPPCTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTVLSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQVERPSSPFSMAPQASLPPVPPRLDLLQQRAPVPASTSVLGTASKASSSSLHKDKPLPIPPTLRDLPPPPPPDRPYSVGTETRPQRRPLPCTPGDCPSRDKLPPVPSSRPGDSWLSRPIPKVPVATPNPGDPWNGRELTNRHSLPFSLPSQMEPRADVPRLGSTFSLDTSTTMNSSPVAGPESEHPKIKPSSSANAIYSLAARPLPVPKLPPGEQGDSEEDTEYMTPTSRPVGVQKPEPKRPAETAQSSRACDCDQQIDSCTYEAMYNIQSQALSVAENSACGEGNLATAHTSTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGEPTNFNEGSQVPERPPKPFPRRINSERKASSYQQGGGAMANPAAAAPSPQLSSEIERLMSQGYSYQDIQKALVIAHNNIEMAKNILREFVSISSPAHVAT
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (A0A060XXZ0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- COP9 signalosome complex subunit 5
- 26S proteasome non-ATPase regulatory subunit 14
- Ubiquitin-like protein NEDD8
- Ubiquitin-like protein NEDD8
- Ubiquitin-like protein NEDD8
- Ubiquitin-like protein NEDD8
Sequence:
MDGQRWLPLEANPDVMNQFLRQLGLLPTWQFGDVYGMDPELLSMVPRPVCAVLLLFPVTEKYESFRLEEEAKIKAQGQDVSPDVYFMKQTIGNACGTIGLIHAVANNQEHLEFETDSPLKMFLVQSTKLSPENKATFLEKDESIRVTHESSAQEGQTEAPSLDEKVDLHFIAFVNVGGHLYELDGRKPFPIAHGKTSEVRFLEDATEVCKTFMARDPQELRFTVVALSKA
Protein: Acetolactate synthase, mitochondrial (EC 2.2.1.6) (AHAS) (ALS) (Acetohydroxy-acid synthase) (P36620)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion.
Interaction partners:
- Probable acetolactate synthase small subunit
- Probable ketol-acid reductoisomerase, mitochondrial
- Threonine dehydratase, mitochondrial
- 3-isopropylmalate dehydrogenase
- Dihydroxy-acid dehydratase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- 2-isopropylmalate synthase
- NAD-dependent malic enzyme
- NAD-dependent malic enzyme
- Pyruvate kinase
Sequence:
MTVLAPLRRLHTRAAFSSYGREIALQKRFLNLNSCSAVRRYGTGFSNNLRIKKLKNAFGVVRANSTKSTSTVTTASPIKYDSSFVGKTGGEIFHDMMLKHNVKHVFGYPGGAILPVFDAIYRSPHFEFILPRHEQAAGHAAQAYSRVTKKPGVVLVTSGPGATNVITPIADALADGTPLVVFSGQVATSAIGSDAFQEADMVGISRSCTKWNVMVKDVADLPRRIDEAFEIATSGRPGPVLVDLPKDVTASVLKEPIPILSSVPSMNRRMKEVLEEGSKNVTAKIDRVANLLKLAKKPVIFCGHGVLANPECPTLLRKFSERLQIPVTTSLLGLGAVDERSDLSLHMLGMHGSGYANMAMQEADLILALGVRFDDRVTGNVSLFAPQARLAAAEERGGIIHFDISPKNIGKVVQPTEAIEGDVYESLKLLDSATKNIKIPSRFDWLSQIQTWKERFPFTFTRSAPGELVKPQEVIQELDKQTSDIKDKVTITTGVGAHQMWAATFYRWTKPSSLVTSGGLGTMGFGLPAAIGASVAAPKDIVIDIDGDASFSMTGMELATVRQFDIPVKILILNNEEQGMVTQWQNLFYEKRYSHTHQKNPNFVKLADAMGIKALRVEKREDLAKKMKEFLSTKGPVLMEVLVAQKEHVYPFVPGGKALHQFILHESLS
Protein: tRNA wybutosine-synthesizing protein 2 (tRNA-yW-synthesizing protein 2) (EC 2.5.1.114) (tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase) (Q04235)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112
- tRNA wybutosine-synthesizing protein 3
- tRNA wybutosine-synthesizing protein 4
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
- tRNA
- 18S rRNA aminocarboxypropyltransferase
- tRNA
- Large ribosomal subunit protein mL49
- UPF0507 protein YML002W
- UPF0507 protein YML003W
Sequence:
MSDETMPVEFLVSDKRLLKTIKVKLETNGLFVTPIYSDNDNKVIKSSIEDLNHPLAVEINNIAGVKARFHESGNLERSEGHLKHQSNSITEFTKSFLKDHGLANDKIFLSHLLDHLPLKYTIYPPVVLFNNSTVRSFNHPIWQKAFQLKLFDPNEYYRELLCFLSPGKPSKGTSLHPNNRLLTHLAINNPITEADVLRRPFNIQPLYGKLIDDSILDDNDNTLWENPSQEQLNSSIWCKVIQNGVTQIWSPVFTMFSRGNIKEKKRVLTTFPDICNNDVVDLYAGIGYFTFSYLTKGARTLFAFELNPWSVEGLKRGLKANGFNKSGNCHVFQESNEMCVQRLTEFLSQNPGFRLRIRHINLGLLPSSKQGWPLAIKLIYLQGASLEKVTMHIHENVHIDAIEDGSFEKNVIVELDAINESIALIRNRGIKLQFVRSKLERIKTFAPDIWHVCVDVDVIVST
Protein: ATP synthase subunit alpha, mitochondrial (P0C522)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
Interaction partners:
- ATP synthase subunit a, chloroplastic
- F-ATPase gamma subunit
- ATP synthase epsilon chain, chloroplastic
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit c, chloroplastic
- ATP synthase subunit d
- Os06g0714700 protein
- ATP synthase subunit a
- ATP synthase F1, delta subunit family protein, expressed
- Os06g0646500 protein
Sequence:
MEFSPRAAELTTLLESRMTNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGKGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRGTNESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVSKQPQYEPLPIEKQIVVIYAAVNGFCDRMPLDRISQYEKAILSTINPELLKSFNEKGGLTNERKIELDAFLKQTAKEIN