wanglab/gogpt-training-data huggingface dataset:
Protein: UDP-rhamnose/UDP-galactose transporter 5 (UDP-Rha/UDP-Gal transporter 5) (Bi-functional UDP-rhamnose/UDP-galactose transporter) (Q9SZ96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleotide-sugar transporter that transports UDP-rhamnose or UDP-galactose and UMP in a strict counter-exchange mode.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:25053812}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- DNAJ heat shock N-terminal domain-containing protein
- U6 small nuclear RNA
Sequence:
MAPVKKSDKKATLDAAAWMFNVVTSVGIIIVNKALMATYGFSFATTLTGLHFATTTLMTLVLRCLGYIQPSHLPFTELLKFILFANFSIVGMNVSLMWNSVGFYQIAKLSMIPVSCLLEVVFDKIRYSRDTKLSIGLVLVGVGVCTVTDVSVNTKGFVAAFVAVWSTALQQYYVHYLQRKYSLSSFNLLGHTAPAQAATLLIVGPFLDYWLTDKRVDMYDYNSVSVMFITLSCTIAIGTNLSQFICIGRFTAVSFQVLGHMKTILVLVMGFFFFDRDGLNLHVILGMIIAVLGMIWYGNASSKPGGKEKKNYSLPTTRQQKLGATSDSDEHRDKA
Protein: Radish, isoform I (X2JDH0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH22922p
Sequence:
MSKLRHYRSMDQPCSSTCVVIRKKTMTAICFVCNLPIMSHQVGLVWQGGNGWDDLVREQLEESTIRQRLGGRRDSAAQITTPPSTSPPPGLQRRRRSSLAQLTDILREWSGGTKQQQQHHSQQQQQQLQQASRSKAQLNRRETLADLARSLPWRTSTTTDASTGAGGSGGGGCTTYMAPRKRRESSADSGIRSMRSRRDSNTAEFVRHWNRRESGAVEEQPSVSVPVVVECSKSASRRGSGESYLSSSRRDSNVAGRVTTPPPPGKYQMTKKRDSLAAPEFPNFRQEQRPSTSSAGSCSDHSMPLISTHSSTHHLAHQQVDSACQALPPPTIITSSVTPPATSPTAPKGRRDSQTQCGRVNRRDSKAGVSPERAPRLQRLQRQATAFDEGCLPGGSRRGSQPALSPDPPDDCERRTSRRDSLSPDSASRGGRRDSRTHLSPDRSHERDGSPRRHTLRRQSSSAARSPRSPDSNSCCSSRDPSPCSRPQTQTTVEQNQRPAIRRQSTTEEILIARGFRRQSTTEEMIRCRNFRRQSSQSDDVCRYRGRRDSSAQIIDGTIGTMTVETTSTFFDSSTQTEPSPLYDNNHYHEECLRCNSCGLNLTGPNQKRARRFKNQILCDLHFADVALMECSDFMQQLRSFKPQSLGCAVARRKSSTTLIFPLPPQACSDEFCEEYPHNLMPTPGYWIECSRQKITMPTPHTIWDESDSEHEDIRAGSASDAYLERECSDLYEDDEDSEATPSPRKKTTIEEQWDQQGAFELISVEQETYEKYFYGTEHWNYFTSDEDLGPVILSIKQETLNGRDQFRILVRAGSYTVHGLIPASCVFADRYNREEVVRSLGKEVNLNPPLTLGQLPDTPEELLKLDQVFIKSELKVGVIFVKEDQYTEEQILDNNENSPLFDEFLTLLGDRVRLRGFDKYKGGLDTVHDLTGLFSVYTNWRNIEIMFHVSTLLPYEKHDPQKLQRKRHIGNDIVCVVFLEADNTRFSPACIKSHFLHTFILVRVSARIKHKPTRYEVSVVTRDEVGAYKPYLWEQSVFEKGPMFREWLLTKIVNGERASYSAPKFARMQERTRSQMLEDLVMNLSNHAETGQIPKPYRRGSWRPIGEDEYIKMLHARVLDNNTHHEQQQQLLLQQQHMQHTQHMQHLPSHNICCYCNNNATELHTAGAIHNNNDNNNTTTTTTFTHRHNNNNNNYSEQQQQQLPQQQQHDSQQQQQLLQPQQHQLLHQLQLSTSSLTHTSCCAMLHLCARHSHMRPSSPLLDSVRDQFEDYDQLAKDFTRVFLNEEPSCLTNAHLFDVVFLVGQSKQKARFIGVRAILGVRSRVFQEMLYGIQTGFGSPQIPVAEIFARPAPSLVSPQNQKPKSNNYLTVPDSDSIRPKSVPSSPMVKRAFSRLGTITAGWGRSIRNKNTNQLNPDDKKKWISSTDCSNRDSKDKDKDKPGNNQLAVPRLSVCADAQKVDRAKLAQTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACFHHCKQFLRIEVVCPMLISLENYYWRYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCRELQTPEIRKFEAMLAWAQHKVGKLKNHPNKDTQFEFECIMERLTRDLNLCRISPSELLTVVLPSKSMKNERIMETLMVQVNLGTYRMPELDAYRQQLRQQESAEATVQVHRAHQNHHNPPPIDARAYAMASLAAALEMQNSSNPLQSNAARDAADEEVELYASFDNAPSTSRVAAQMQAAKEARRKRWAADGASGSSGDGGCASGSSGSGRRY
Protein: Casein kinase 1-like protein 13 (EC 2.7.11.1) (Protein CASEIN KINASE I-LIKE 13) (Q5XF24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48730}. Cell junction, plasmodesma {ECO:0000269|PubMed:16126836}. Note=Present in punctate particles with granular structure. {ECO:0000269|PubMed:16126836}.
Interaction partners:
- At3g49990
- Bystin
- Serine/threonine-protein kinase RIO2
Sequence:
MDRVVGGKFKLGRKLGSGSFGEIFLGVNVQTGEEVAVKLEPLRARHPQLHYESKLYMLLQGGTGIPHLKWFGVEGEFNCMVIDLLGPSMEEFFNYCSRSFSLKTVLMLADQMINRVEYMHVKGFLHRDIKPDNFLMGLGRKANQVYIIDYGLAKKYRDLQTHKHIPYRENKNLTGTARYASVNTHLGIEQSRRDDLESLGYLLMYFLRGSLPWQGLRAGTKKQKYDKISEKKRLTPVEVLCKNFPPEFTSYFLYVRSLRFEDKPDYSYLKRLFRDLFIREGYQFDYVFDWTILRYPQFGSSSSSNSKPRPTLRPAMNIPVPSADKAEKPPIGQDSRERFSGVFEAYTRRNGSGTGVQADQSSRPRTSENVLASKDTQNQERPNSLSRNLSSSRKAIAGSSVRATSSADFTENRLSRLIPNNDRSSTTLRTQFAPSSSSVATKAAPTRAARDITLQSLELLSIGNSKRK
Protein: Quinate/shikimate dehydrogenase (NAD(+)) (QSDH) (EC 1.1.1.-) (EC 1.1.1.24) (Q9X5C9)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids, and plays a key role in the quinate degradation pathway. Catalyzes the NAD(+)-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively. It can only use NAD.
Interaction partners:
- Shikimate kinase
- 3-dehydroquinate dehydratase
- 3-dehydroquinate synthase
- 3-dehydroshikimate dehydratase
- Chorismate synthase
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- shikimate dehydrogenase
- Shikimate 5-dehydrogenase
- 3-phosphoshikimate 1-carboxyvinyltransferase
- Guanylate kinase
Sequence:
MNDSILLGLIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTLGSRASGQDLKTLLDAALYLGFNGLNITHPYKQAVLPLLDEVSEQATQLGAVNTVVIDATGHTTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQALADVINNAVGREAVVGVDARGIEDVIAAADGVVNATPMGMPAHPGTAFDVSCLTKDHWVGDVVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVSRMRETFLSL
Protein: F-box protein 7 (SKP1-interacting partner 32) (Q9XI00)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Required for efficient protein synthesis during temperature stress conditions.
Subcellular location: Nucleus {ECO:0000269|PubMed:17240087}. Mitochondrion {ECO:0000269|PubMed:17240087}.
Interaction partners:
- SKP1-like protein 1A
- SKP1-like protein 1B
- Agamous-like MADS-box protein AGL11
- SKP1-like protein 11
- SKP1-like protein 4
- Interferon-related developmental regulator family protein / IFRD protein family
- Cullin-3A
- Cullin-2
- Cullin-3B
- Putative cullin-like protein 2
Sequence:
MTSDALTIPSELESALRLRTVQYFITKRPWLDLYGVHVRPVPPFGSTSRKPHFDPALIHRCLPDELLFEVFARMMPYDLGRASCVCRKWRYTVRNPMFWRNACLKAWQTAGVIENYKILQSKYDGSWRKMWLLRSRVRTDGLYVSRNTYIRAGIAEWKITNPVHIVCYYRYIRFYPSGRFLYKNSSQKLKDVAKYMNFKASKSENLYKGTYTLSMSDDKIEAAVLYPGTRPTVLRIRLRLRGTAIGANNRMDLLSLVTSGVNDEEISSTEEDILGLVEGWEDDETHNPDIPAVSHKRGMTAFVFVPFEEVDESVLNLPPEKMDYYVTG
Protein: Large ribosomal subunit protein eL24y (60S ribosomal protein L24-2) (Protein SHORT VALVE 1) (P38666)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might have an extraribosomal function in reinitiation of translation of ETTIN and MONOPTEROS genes that are involved in the auxin-mediated gynoecium patterning. Essential in leaf polarity establishment, probably having a role for translation in leaf dorsoventral patterning to specify leaf adaxial identity.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:11598216}. Nucleus {ECO:0000250|UniProtKB:O82204}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O82204}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O82204}.
Interaction partners:
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein eL43y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL6z/uL6y
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein eL28z
- Large ribosomal subunit protein uL1y
Sequence:
MVLKTELCRFSGQKIYPGRGIRFIRSDSQVFLFLNSKCKRYFHNKLKPSKLAWTAMYRKQHKKDAAQEAVKRRRRATKKPYSRSIVGATLEVIQKKRAEKPEVRDAAREAALREIKERIKKTKDEKKAKKVEFASKQQKVKANFPKAAAASKGPKVGGGGGKR
Protein: Protein ROS1C (EC 3.2.2.-) (DNA glycosylase 701) (Protein REPRESSOR OF SILENCING 1 homolog c) (B8YIE8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Bifunctional DNA glycosylase/lyase, which excises 5-methylcytosine (5-meC) and 5-hydroxymethylcytosine (5-hmeC), leaving an apyrimidinic (AP) site that is subsequently incised by the lyase activity. Is responsible for the demethylation of methylated cytosine residues of Tos17 retrotransposon DNA. Demethylation of Tos17 cytosine residues promotes its transposition. May be involved in seed development.
Subcellular location: Nucleus {ECO:0000269|PubMed:21896764}.
Interaction partners:
Sequence:
MAKDENPSYLHLIFLSSRIRVFILDPPLSLPLSHGQCELQVVEEAAMDPSGLNLQGNPAENQESWTSGVSVGRGTPNLGVGTAVAGRSCPSSTLFPGSSLSSTALLNTMHEGSFPQTALVAGSVSSADEQHGAPPVRPSYNLPAGCTQVPISILVFHRRLTGRGSRCRSPQSRSFMPAPALSGVSEADGAYGPIPQSDFLSLRGPSEVFPGDMAMNHSEPATSYGYNSEYAPMHLQPNGLYTEASNTESEREASQLQQSAEAVICDSLSKLESAMEKIQGQNPQESSGLVAEGSADDNIHKYHQKAKRARTQITHSDKIDLPTQAVSACKEKTITQIEMQIADAERTEALKGEDAPAQKLKTRRRKHRPKVIREDRPAKKQMATTSEEKPLNQKPKRKYVRKNRNPSSLEKCAEPFSDHSISRESRTTVRSSIASVRRRLQFEFGEHGVQRDQSSMTNSWYQNQEKPVNAESSLCSVTKSSVQVEHGQELHMENSPEGLFFGINSKLNKILDEYIHLPEAAPKPSEQIPLAASGHVSEELARKQYDVRHTHDPDSTSYNIERSGLITTKGHKKDLDLNYSNTNGFQMYCSASLLPEMDSTKGSMTKVSKMDKNKKRHYGGESSLAGTQSSIIMRTAAEMLAVYQACGIKKKRSARVRRNSFLSVMDLEKNTSQESTRLPRSCMEALYESSYIKFMTKKRSQKARLNSPNSIQPNIDQKNRFSSETVFSGGFNGLKRSEETFQKTLPQIPDDKRINLDIHCKVPVESSPNTSTPPYMDYLQGVTSKFRYFDLNTEQVHKTEMHLSQTMPSLSSLGATNYLPNALVPYVGGAVVPYQTQFHLVKKQRPRAKVDLDFETTRVWNLLMGKAADPVDGTDVDKERWWKQEREVFQGRANSFIARMRLVQGDRRFSPWKGSVVDSVVGVFLTQNVADHLSSSAYMALAASFPTGSHGNCNDGIAGQDNEEIISTSAVGDRGTFEFFYNGSRPDIGLNFEFSMACEKIHMEPKDNTTVNELTKGENYSLHCKESAGSLCDHETEIDHKAKSISDFSAVELTACMKNLHATQFQKEISLSQSVVTSESILQPGLPLSSGMDHARRNFVGSISDTASQQVGSNFDDGKSLTGNDVTANETEYHGIKAAATNNYVVDEPGIPSGSSLYPFFSAIDCHQLDGRNDTHVSSTSPNCSICSASSNFKIGTIEENSSLFMPFDAHLAQRNGNMIVDTNLSSALESTELPVKLLHCGKRSCYEASEFQDHESLYATGGVIPETATKADDSTLKSGFASFNGLPDTAAQASKPKKSRTTSKKNSENFDWDKLRRQACGNYQMKERIFDRRDSVDWEAVRCADVQRISHAIRERGMNNVLAERIQKFLNRLVTDHGSIDLEWLRDVPPDSAKDYLLSIRGLGLKSVECVRLLTLHHLAFPVDTNVGRICVRLGWVPIQPLPESLQLHLLELYPVLETIQKYLWPRLCKLDQQTLYELHYQMITFGKVFCTKSKPNCNACPMRSECRHFASAFASARLALPSPQDKRLVNLSNQFAFHNGTMPTPNSTPLPQLEGSIHARDVHANNTNPIIEEPASPREEECRELLENDIEDFDEDTDEIPIIKLNMEAFSQNLENCIKESNKDFQSDDITKALVAISNEAASIPVPKLKNVHRLRTEHYVYELPDSHPLMQQLALDQREPDDPSPYLLAIWTPDELKDTREAPKPCCNPQTEGGLCSNEMCHNCVSERENQYRYVRGTVLVPCRTAMRGSFPLNGTYFQVNEVFADHSSSHNPINIPREQLWNLHRRMVYFGTSVPTIFKGLTTEEIQHCFWRGFVCVRGFNMETRAPRPLCPHFHLAASKLRRSSKKAATEQTH
Protein: FAD-binding monooxygenase ausC (EC 1.14.13.-) (Austinoid biosynthesis clusters protein C) (C8VE79)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-binding monooxygenase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Multifunctional dioxygenase ausE
Sequence:
MYASNKTYPSSRALPCLVEKVEAQHVDGAIRVRITTLEQKDWRQAKAAAVEAKYEAEREIQLRAHGNVKDIEITRESAFEHFATDPWAQHVGVDIEAQRERLLAEPGSRKILIIGAGFGGLLFAVRLIQTGRFTAEDITMIDSAAGFGGTWYWNRYPGLMCDTESYIYMPLLEETGYMPRNKYASGNEIREHAERIAQTYGLATRAMFRTVVEKLDWNEAEKVWTVAGSMLGIANNGQRDNMMSFQMVSQFTIMASGSFASPRVPDYPNIFDYKGKLFHTARWDYNYTGGSVENPKMLGLADKTVAIIGTGASAVQIVPQLAKYSNKLIVFQRTPAAVDARNNCPTDPVWWETETQAEGTGWQKRRQENFNAFTCNEKPLPSVNKVDDGWTRMPSFSILIGGPQGLDPDYVDRMRAVDMNRQEKIRARAHNIVQSEGSADLLTPWYPGWCKRPCFHDDYLSAFNLPNVELVDIRHNGISHFTANGLVANDIEYELDVIILSTGYTVPVTRASPSSRANIAVSGRNGTTMEAKWANGLATLHGVMTRDLPNLFFAGTSQAGACVNLVYALDQNATHVAYILANAFDRRPSDSARVIIEPTPGSEEAWAMQVLQRAAGFRGIAGCTPGYLNGYGMDASSLSPEQQINAARLAAWGEGIASYVRYLEAWRAKGDLNGIELTFFAKF
Protein: Transferrin-binding protein 1 Tbp1 (B3GYQ0)
Organism: Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
Sequence:
MKNKLNLISLALLSLFAVQSYAEQAVQLNDVYVTGTKKKAHKKENEVTGLGKVVKTPDSLSKEQVLGMRDLTRYDPGISVVEQGRGATTGYSIRGVDRNRVGLALDGLPQIQSYVSQYSRSSSGAINEIEYENLRSIQISKGASSSEFGSGSLGGSVQFRTKEVSDIIKPGQSWGLDTKSAYSSKNQQWLNSLAFAGTHNGFDALVIYTHRDGKETKAHKDAESRSKSIQRVDLADNNPQGSNWFKVKNDCPSLNCEPRQQVGVSYDGQKYITEQLSAKEYTGEERALPDPVKYKSDSWLVKLGYSLSPKHYVAGVYEHSKQRYDTRDMTYPAYWQLSDLKNGDKWYPMNNAKGLYRDNALDGVAIDYFTEDGVKSSKGLRWAKARFIDEWHTRDRLGALYRYTNQDGNRLIDRLSLSFDQQKINLSTRLRENNCSEYPTIDKNCRATLDKLWSSTKNEQSSYEEKHDTIQLSLDKTVQTGLGKHQLNMLLGSDRFNSTLKRHEILSEFSVGTWHRIRGNGYKDTPYIYELKDQAIYSKNECDYSGTIAGRADCATSKIKGHNHYIALRDNFAITKYLDIGLGYRFDKHKFRSTHRWANQGDYKNSAWNIGIVAKPTSFLSLSYRASSGFRVPSFQELFGLRYDGAMKGSSDAYQKTEKLSPEKSLNQEVAATFKGDFGVVEVSYFKNDYKQLIAPAERMHQTQSMINYFNVQDIKLDGINLIGKLDWNGVFDKIPEGIYTTLAYSKMRVKEVKNYQGYMNIRSPLLDTIQPARYVVGVGYDQPDEKWGVNLTMTHSSGKNPNELRGNEQVGFANYERTATKKRTRSWHTFDLTGYITPWKHTTVRAGVYNLMNYRYTTWESVRQSSLNAIHQHTNVKDYARYAAPGRNYVVSFEMKF
Protein: Inner membrane assembly complex subunit 22 (INA complex 22 kDa subunit) (P40576)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the INA complex (INAC) that promotes the biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the assembly of the peripheral stalk and promotes the assembly of the catalytic F(1)-domain with the membrane-embedded F(0)-domain.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:24942160}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inner membrane assembly complex subunit 17
- Mitochondrial inner membrane protease ATP23
- Mitochondrial ATPase complex subunit ATP10
- ATPase synthesis protein 25, mitochondrial
- Protein CBP3
- mRNA-binding protein PUF3
- Cytochrome B pre-mRNA-processing protein 6
- Putative uncharacterized protein OPI8
Sequence:
MFMARQVLRNGLFLRSLAPIKITARTVASANAGIKRKSRFDKTMIKPLLLVMIFGSILNAVIAEKRNIIDMERKYKLKLDKLKELIRRVHDNNGKVDFDADDELKLVNLRLGIVGKNATGMKEDETDIVVPKEESLEEIWQSIIDEAKKEVIEKTPDAGVKNKEGIVTDLNVLKDLEKSKKEDEKVYLSGDVHMMMNQPGDLNEIAKEHDKIPKFL
Protein: Small ribosomal subunit protein eS8 (40S ribosomal protein S8) (Q59T44)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (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.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Small ribosomal subunit protein eS30
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein uS8A
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL33
Sequence:
MGISRDSRHKRSATGAKRAQFRKKRKFELGRQPANTKIGPKRIHSVRTRGGNQKFRALRVETGNFSWGSEGVSRKTRIAGVVYHPSNNELVRTNTLTKSAVVQIDATPFRQWYENHYGATLGKKKGGAHAAHAAEVADAKRSRKVERKLAARSGAAAIESAVDSQFGSGRLYAVISSRPGQSGRCDGYILEGEELAFYLRRLTAKK
Protein: Mitochondrial acidic protein MAM33 (P40513)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Not known. Binds to the sorting sequence of cytochrome b2.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Upstream activation factor subunit UAF30
- Uncharacterized protein YPR153W
- L-lactate dehydrogenase
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS4m
- Small ribosomal subunit protein bS21m
- Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
- Ribosome assembly protein RSM22
- Protein PET54
- MIOREX complex component 6
Sequence:
MFLRSVNRAVTRSILTTPKPAVVKSSWRVFTVANSKRCFTPAAIMRNQETQRVGDILQSELKIEKETLPESTSLDSFNDFLNKYKFSLVETPGKNEAEIVRRTESGETVHVFFDVAQIANLPYNNAMDENTEQNEDGINEDDFDALSDNFANVNVVISKESASEPAVSFELLMNLQEGSFYVDSATPYPSVDAALNQSAEAEITRELVYHGPPFSNLDEELQESLEAYLESRGVNEELASFISAYSEFKENNEYISWLEKMKKFFH
Protein: 12-oxophytodienoate reductase 3 (EC 1.3.1.42) (12-oxophytodienoate-10,11-reductase 3) (OPDA-reductase 3) (LeOPR3) (Q9FEW9)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Specifically cleaves olefinic bonds in cyclic enones. Involved in the biosynthesis of jasmonic acid (JA) and perhaps in biosynthesis or metabolism of other oxylipin signaling moleclules. It is required for the spatial and temporal regulation of JA levels during dehiscence of anthers, promoting the stomium degeneration program (By similarity). In vitro, reduces 9S,13S-12-oxophytodienoic acid (9S,13S-OPDA) and 9R,13R-OPDA to 9S,13S-OPC-8:0 and 9R,13R-OPC-8:0, respectively.
Subcellular location: Peroxisome {ECO:0000269|PubMed:12445129}.
Interaction partners:
- allene-oxide cyclase
- Uncharacterized protein
- Uncharacterized protein
- Allene oxide synthase 1, chloroplastic
- Coronatine-insensitive 1
- Lipoxygenase
- Lipoxygenase
- Lipoxygenase
- Lipoxygenase
- Lipoxygenase
Sequence:
MASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRNAYQGTFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
Protein: Carbonic anhydrase 5A, mitochondrial (EC 4.2.1.1) (Carbonate dehydratase VA) (Carbonic anhydrase VA) (CA-VA) (P43165)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial carbonic anhydrase that catalyzes the reversible conversion of carbon dioxide to bicarbonate/HCO3. Mitochondria are impermeable to HCO3, and thus this intramitochondrial carbonic anhydrase is pivotal in providing HCO3 for multiple mitochondrial enzymes that catalyze the formation of essential metabolites of intermediary metabolism in the urea and Krebs cycles (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:7937950}.
Interaction partners:
- Carbonic anhydrase 5B, mitochondrial
Sequence:
MLRAKMLGRGPYKPLAILRHMGPLCATRPQHWRFQHSYAEKHSNCARHPLWTGPVSSPGGTQQSPINIQWTDSVYDPKLAPLRVSYDAASCRYLWNTGYFFQVEFDDSCEESGISGGPLGNHYRLKQFHFHWGATDEWGSEHMVDGHAYPAELHLVHWNSMKYENYKKATTGENGLAVIGVFLKLGAHHEALQRLVDILPEVRHKDTQVTMGPFDPSCLLPACRDYWTYPGSLTTPPLAESVTWIVHKMPIEVSPSQLSTFRTLLFSGRGEDEEVMVNNFRPLQPLRGRNVRSSFQVPRVGTKS
Protein: Mitochondrial import inner membrane translocase subunit Tim10 (P62073)
Organism: Mus musculus (Mouse)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit Tim22
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Mitochondrial import inner membrane translocase subunit Tim8 A
- Putative mitochondrial import inner membrane translocase subunit Tim8 A-B
- Mitochondrial import inner membrane translocase subunit Tim29
- Acylglycerol kinase, mitochondrial
- Mitochondrial import inner membrane translocase subunit Tim8 B
- Mitochondrial intermembrane space import and assembly protein 40
Sequence:
MDPLRAQQLAAELEVEMMADMYNRMTSACHRKCVPPHYKEAELSKGESVCLDRCVSKYLDIHERMGKKLTELSMQDEELMKRVQQSSGPA
Protein: E3 ubiquitin-protein ligase ARIH1 (EC 2.3.2.31) (H7-AP2) (HHARI) (Monocyte protein 6) (MOP-6) (Protein ariadne-1 homolog) (ARI-1) (UbcH7-binding protein) (UbcM4-interacting protein) (Ubiquitin-conjugating enzyme E2-binding protein 1) (Q9Y4X5)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets. The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes. Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear. According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest. According to another report EIF4E2 ubiquitination leads to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2. In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, nuclear subcellular localization and nuclear morphology.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11278816, ECO:0000269|PubMed:21590270, ECO:0000269|PubMed:23059369}. Nucleus {ECO:0000269|PubMed:23059369}. Nucleus, Cajal body {ECO:0000269|PubMed:23059369}. Note=Mainly cytoplasmic (PubMed:11278816). Present in Lewy body (PubMed:21590270). {ECO:0000269|PubMed:11278816, ECO:0000269|PubMed:21590270}.
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-like protein NEDD8
- Cullin-1
- Polyubiquitin-C
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- Cyclin-dependent kinase inhibitor 1B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-conjugating enzyme E2 L5
- Cullin-3
- Eukaryotic translation initiation factor 4E type 2
Sequence:
MDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDTLDLGEVELVEPGLGVGGERDGLLCGETGGGGGSALGPGGGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVLLQHVHEGYEKDLWEYIED