wanglab/gogpt-training-data huggingface dataset:
Protein: Gamma-aminobutyric acid receptor subunit gamma-1 (GABA(A) receptor subunit gamma-1) (GABAAR subunit gamma-1) (Q8N1C3)
Organism: Homo sapiens (Human)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000255}. Cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inactive phospholipase C-like protein 1
- Vesicle-fusing ATPase
- Trafficking kinesin-binding protein 2
- Huntingtin-associated protein 1
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor subunit beta-2
- GABA type A receptor associated protein like 1
- Gamma-aminobutyric acid receptor subunit alpha-1
Sequence:
MGPLKAFLFSPFLLRSQSRGVRLVFLLLTLHLGNCVDKADDEDDEDLTVNKTWVLAPKIHEGDITQILNSLLQGYDNKLRPDIGVRPTVIETDVYVNSIGPVDPINMEYTIDIIFAQTWFDSRLKFNSTMKVLMLNSNMVGKIWIPDTFFRNSRKSDAHWITTPNRLLRIWNDGRVLYTLRLTINAECYLQLHNFPMDEHSCPLEFSSYGYPKNEIEYKWKKPSVEVADPKYWRLYQFAFVGLRNSTEITHTISGDYVIMTIFFDLSRRMGYFTIQTYIPCILTVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCFIFVFAALMEYGTLHYFTSNQKGKTATKDRKLKNKASMTPGLHPGSTLIPMNNISVPQEDDYGYQCLEGKDCASFFCCFEDCRTGSWREGRIHIRIAKIDSYSRIFFPTAFALFNLVYWVGYLYL
Protein: Proteasome subunit alpha 1 (20S proteasome alpha subunit 1) (Proteasome core protein PsmA 1) [Cleaved into: Proteasome subunit alpha 1, N-terminally processed] (Q9V2V6)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
Interaction partners:
- Proteasome subunit beta
- Proteasome-activating nucleotidase 1
- Proteasome-activating nucleotidase 2
- Proteasome subunit alpha 2
- S-adenosylmethionine-dependent methyltransferase
- Glycerol kinase
- Ribonuclease P protein component 3
- Ribonuclease P protein component 2
- Large ribosomal subunit protein eL15
- Thermosome subunit 1
Sequence:
MQGQAQQQAYDRGITIFSPDGRLYQVEYAREAVKRGTASIGVRTPEGVVLAADKRSRSPLMEPTSVEKIHKADDHIGIASAGHVADARQLIDFARRQSQVNRLRYGEPIGIETLTKEVTDHIQQYTQVGGARPFGVALLIGGVENGTPRLYETDPSGTPYEWKAVSIGADRGDHQEHLEENFRDDLTLDEGIELALEAIASTSDEGTAPDGVDVATVSAETERFVELSNDEIESYLEANDLLATEDDEQTEE
Protein: Iroquois homeobox 7 (Iroquois homeodomain transcription factor Ziro7) (Iroquois7) (Q90YX8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- BarH-class homeodomain transcription factor
Sequence:
MPASSTGFANFFMDRNINMPAGYQLLGCPPGMQQPPPHLVGMAGMPLPFSGIPGYSFIPYPHPGHMAHISNSYDLKAASPYHQALLGRGGPYYTPYRPIPADDPSRVTKVATRESTSALKAWLSEHLKNPYPTKGEKIMLAIVTKMSLTQVSTWFANARRRLKKENRVSWASKGKSDEEDEEEEGESEEEGSLRKGTEDEDEIDPQTVDDEDEEDVVVSKSVEHRLAGGLEQQKESDKSDTLTKRESYKQIADVQKPKIWSLAETATSDIVKKPSDLKHLQTSPDFGQWWAGWPSRDSYSPVNLSTHDLLKQSQ
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJE0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- ATP-dependent RNA helicase SUV3, mitochondrial
- Exosome complex component RRP45
- Candida glabrata strain CBS138 chromosome J complete sequence
- Ribosomal RNA-processing protein 42
- Ribosomal RNA-processing protein 43
- Candida glabrata strain CBS138 chromosome E complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Ribosomal RNA-processing protein 41
Sequence:
MKVRVQRRWFHCCRRLDNAPLENSVKNYLARTKGLEPDFEIRQLPQIISGFNKRYRARYLEPSQRWFKADWKASDHGEDKATRLLRPEVFDKFIINSDFHRGNMEQYQKAQKLSFDPAELLRTSLNVGDIVLLKQCTSELTMCVNLPQSTTDPRYTFAKKDGTLVYAMKNSVILRIPKDLPEEVNQLLKRESNHPYQKIGTIKNSSNETEILPVLTRQLIVSFTLATFTKFAWTQLPIVLKKLELIHRYLQDSRGSKHVNFMSLVRIIKNLNIKEATDAINGDAYVRKVIDESMSVVNKSIDPTTLLATYWGVREQQQNNLWGSVYTNTALLSPTTVAVLPLKKAHLFYQEVITRLESNDYQEIKAFAKLVNDKDYHSIAKRYDYIRTLLNDYAAGNIEENAVLTTIISKIFRHIDMYRDQDVTRSLCGKLLVEISPQSNSSNFILGNWDLNIPKSSGISSVEQKLYDTAMPTIVSDTDRYDFGDMPVFCIDSEDAHEIDDGISIEELDGVRSRIHIHIADPAGLFPESFDYTKSGISDDVLRVSLKRAFTTYLPDLVVPMLPKSFCNRADLGKHDRKTETISFSFELVNKEDGGLHVDYDTFQVRLGIVSNFPKVTYDKVDSILNGDDNSLPSKQKKQLELLHTLATKLLHKRIHDDNAVVFGDGFNKGLVSLSPDDDGELCIPTFYDQSQTKSTLLVSEFMILTNKLCAAFFQENKIPGVYRCYNGLNLGNQAKAQFELLKENIKLGKLPSLKDITKISSQLSSSFYSPFPLPHKMIGNTAYLTVTSPMRRGPDLINHLQLHRFLKKLPLCFKQEYLDQYVWSFQARADILKIFQRHSSTYWTLKHLEQSGTKTHDVIVTSVPQNGTVNCLFPEYSYARGTLKLDPAMKKIPRIGDTIRHCKVESIHPLDGILTLTHVNRK
Protein: Endospore coat-associated protein YutH (O32123)
Organism: Bacillus subtilis (strain 168)
Function: Involved in sporulation.
Subcellular location: Forespore outer membrane {ECO:0000269|PubMed:15231775}; Peripheral membrane protein {ECO:0000269|PubMed:15231775}. Spore coat {ECO:0000269|PubMed:15231775}. Note=Initially localizes to a focus at one end of the forespore, which then undergoes transformation into a ring adjacent to the forespore. Next, the ring becomes a cap at the mother cell pole of the forespore that eventually spreads around the entire developing spore.
Interaction partners:
- Uncharacterized protein YsxE
- Uncharacterized protein YlbD
- Stage VI sporulation protein D
- Endospore coat-associated protein YheD
- Sporulation membrane protein YtrI
- UPF0736 protein YjbA
- Uncharacterized protein YaaC
- Uncharacterized protein YqfQ
- Uncharacterized protein YqfX
- Spore germination protein GerM
Sequence:
MVKGTIKEKYGIHIRQLSMYQHTYQCFQTPNSYFLIVPVSQFSETELAELYYMSQYLQEQSDPYVSVFIFTKEGELTFEHEGKTYALLKAAPPYSNRAFSIGAELAEFHRKGRGYPYEVKAAGRIGQWKDLWGKRIDQLEAFWQRKVQTPPHEPFDKKMIESFPYYLGLSENAIQYLVDTELDDKPQAADSGTICHQRMERHTWSPESLIRIPADWVFDHASRDLAEYMRHTFLHHRQDFNQQGFLFLQEYEQVTPLSSFSKRLLYSRLLFPLHYFEIVESYYMSSESEKHYFEEQLDFILNDCGRYEQFLNTAQEFMNMRAQKLFVPRVSWLGKGSSR
Protein: Glucose-6-phosphate isomerase, cytosolic (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (P34795)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm.
Interaction partners:
- Probable phosphoglucomutase, cytoplasmic 1
- Probable phosphoglucomutase, cytoplasmic 2
- Hexokinase-like 1 protein
- Phosphoglucomutase, chloroplastic
- Hexokinase-3
- Probable hexokinase-like 2 protein
- Hexokinase-1
- Hexokinase-4
- Hexokinase-2
- Triosephosphate isomerase, chloroplastic
Sequence:
MASSTALICDTEAWKDLKGHVEDIKKTHLRDLMSDANRCQSMMMEFDGLLLDYSRQRATVETMDKLLNLAKASQLTEKISRMFNGEHINSTENRSVLHVALRAPKDAVIKADGMNVVPEVWNVLDKIKEFSDKIRSGSWVGATGKPLKDVIAIGIGGSFLGPLFVHTALQTDPEALESAKGRQLRFLANIDPVDVARNISGLNPETTLVVVVSKTFTTAETMLNARTLREWITAALGASAVAKHMVAVSTNLALVEKFGIDPNNAFAFWDWVGGRYSVCSAVGVLPLSLQYGFSMVEKFLKGASSIDQHFQSTPFEKNIPVLLGLLSVWNVSFLGYPARAILPYSQALEKFAPHIQQVSMESNGKGVSIDGLPLPFETGEIDFGEPGTNGQHSFYQLIHQGRVIPCDFIGIVKSQQPVYLKGEVVSNHDELMSNFFAQPDALAYGKTPEQLQKENVSENLIPHKTFSGNRPSLSLLLPELTAYNVGQLLAIYEHRVAVQGFVWGINSFDQWGVELGKVLATQVRKQLHSSRTQGTAPEGFNYSTTTLLKRYLETSSEPQM
Protein: Ubiquitin-ribosomal protein eL40 fusion protein (Ubiquitin A-52 residue ribosomal protein fusion product 1) [Cleaved into: Ubiquitin; Large ribosomal subunit protein eL40 (60S ribosomal protein L40) (CEP52)] (P62985)
Organism: Gallus gallus (Chicken)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm {ECO:0000250|UniProtKB:P62984}.
Interaction partners:
- 60S ribosomal protein L6
- Ribosomal protein L36a like
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL15
- 60S ribosomal protein L29
- S5 DRBM domain-containing protein
- 40S ribosomal protein S7
- Ribosomal protein L37
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS19
Sequence:
NIQKESTLHLVLRLRGGIIEPSLRQLAQKYNCDKMICRKCYARLHPRAVNCRKKKCGHTNNLRPKKKVK
Protein: Phosphomannomutase (EC 5.4.2.8) (Q7ZTZ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU361118}.
Interaction partners:
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Mannose-6-phosphate isomerase
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha-B
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha-A
- Hexokinase 1.
- Hexokinase-2
- Hexokinase 2.
- Phosphomannomutase
- SMAD family member 9.
- GDP-Man:Man
Sequence:
MSGSTVDSTTLCLFDVDGTLTAARQKATADMHEFLSKLKQRVKVGVVGGSDLDKIKEQLGDDVIDRVDYVFAENGLVAYRFGKLHSVQNIQAYLGEDILQEFINFCLNYLSKIKLPKKRGTFIEFRNGMLNVSPIGRSCSQQERIEFFELDKKEKIRETFVSVLKEEFAGKGLAFSIGGQISFDVFPEGWDKRYCLGIVEKDSYQHIHFFGDKTMPGGNDYEIFVDPRTIGHEVKSPEDTQRICRELFFS
Protein: Eosinophil cationic protein 2 (ECP 2) (EC 3.1.27.-) (Eosinophil secondary granule ribonuclease 2) (EAR-2) (Ribonuclease 3-2) (RNase 3-2) (P97425)
Organism: Mus musculus (Mouse)
Function: Cytotoxin and helminthotoxin with ribonuclease activity. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities.
Subcellular location: Cytoplasmic granule {ECO:0000250}. Note=Matrix of eosinophil's large specific granule. {ECO:0000250}.
Interaction partners:
Sequence:
MGPKLLESRLCLLLLLGLVLMLASCLGQTPSQWFAIQHINNNANLQCNVEMQRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSDNISRNCHNSSSRVRITVCNITSRRRTPYTQCRYQPRRSLEYYTVACNPRTPQDSPMYPVVPVHLDGTF
Protein: Chemotaxis protein CheY1 (P71403)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Chemotactic response regulator protein that modulates the rotation direction of bacterial flagellar motors. Plays an important role in the colonization and infection of Helicobacter pylori. Upon phosphorylation by CheA, interacts with the flagellar motor protein FliM to cause clockwise flagellar rotation and bacterial reversals, as opposed to straight swimming when CheY1 is not phosphorylated.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor histidine kinase CheAY
- Chemotaxis protein CheW
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliN
- Methyl-accepting chemotaxis protein
- Methyl-accepting chemotaxis transducer
- Methyl-accepting chemotaxis protein
- Flagellar motor switch protein FliN
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Ribosomal protein L11 methyltransferase
Sequence:
MKLLVVDDSSTMRRIIKNTLSRLGYEDVLEAEHGVEAWEKLDANADTKVLITDWNMPEMNGLDLVKKVRSDSRFKEIPIIMITTEGGKAEVITALKAGVNNYIVKPFTPQVLKEKLEVVLGTND
Protein: Kinesin-like protein KIF26A (Q52KG5)
Organism: Mus musculus (Mouse)
Function: Atypical kinesin that plays a key role in enteric neuron development. Acts by repressing a cell growth signaling pathway in the enteric nervous system development, possibly via its interaction with GRB2 that prevents GRB2-binding to SHC, thereby attenating the GDNF-Ret signaling. Binds to microtubules but lacks microtubule-based motility due to the absence of ATPase activity.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-associated protein 3
- Growth factor receptor-bound protein 2
Sequence:
MVGRGASLCAVQPAVAECGPARETPPLEVSPRKRLPAGLDQDPCSSRPAPEGAGASAEQSHSAGGGGWCRHCHTKLVELKRQAWKLVSGPGTPLRDPCLSTLLLDKLPASGVQPACRPDTESRCDVCTTHLHQLTREALRLLQTPASHEDPNASRGGLAAPSSRDPPGPVGLMGRQPPVGPDRRKATAWPPGPSVQVSVAPAGLGGALSTVTIQAQQCLEGVWSLSRVNSFLPPTCLAEAAVAAVAVADTVRDCAPAAGPERMSKAWGRGAACTTALVTPAPGTSAGGSTGPSAAASFFIRAAQKLSLASKRKKHHPPPAPSTRGTSTYPTDFSGSLQLWPPPVPPCLLRAASKAKENPSSFGKVKVMLRIWPAQGVQRSAESTSFLKVDSRKKQVTLYDPAAGPPGCAGLRHAPTAPVPKMFAFDAIFPQDSEQAEVCSGTVADVLQSVVSGADGCIFSFGHMSLGKSYTMIGKDSSPQSLGIVPCAISWLFRLIDERKERLGTRFSIRVSAVEVCGHDQSLRDLLAEVASGSLQDTQSPGVYLREDPVCGTQLQNQNELRAPTAEKAAFYLDAALAARSTSRAGCGEEARRSSHMLFTLHVYQYRVEKCGQGGMSGGRSRLHLIDLGSCDAAVGRGGEASGGPLCLSLSALGSVILALVNGAKHVPYRDHRLTMLLRESLATTNCRTTMIAHISDSPAHHAETLSTVQLAARIHRLRRKKGKHASSSSGGESSCEEGRARRPPHLRPFHPRAVVLDPDRSAPGLSGDPDYSSSSEQSCDTVIYVGPGGMALSDRELTDNEGPPDFVPIIPALSRRRPSEGPRDADHFRCSTFAELQERLECIDGSEAFPGPQGGSDGAQASPARGGRKPSLPEATPSRKAVAPTVVTSCPRGSPGHDTHRSASDPSKTGTQSEQRVDGSRPEPPASDKTSGGGGRRPLPSPAPPPPRQPEAQGIPKEPGGEGTDSVLRTPPVGMSGQAALPPLLSDSAYLSPSARGRHLERGLLTTTVTLQQPVELNGEDELVFTVVEELPLGGLAGATRPSSLASMSSDCSLQALASGSRPVSIISSINDEFDAYTSQMSEGPGDPGEFPEGTAWAGGSPASSIGSWLSDVGVCLSESRGPTPQPPFSPNSAAGPGPPEFPTPGSSLEESKVRSSECGRPDNPGSARSLHPGEAVATTQTQPGREPWARSPHEVASAQTIHSSLPRKPRTTSTASRARPSRGPYSPGGLFEDPWLLRAEDCDTRQIASTGRAPSPTPGSPRLPETQMMLACAQRVVDGCEVASRMSRRPEAVARIPPLRRGATTLGVTTPAASCGDAPAEAVVHSGSLKTTSGSKKSVSPKGAFFPRPSGAGPPAPPVRKSSLEQSTALTPTQALGLTRAGAPSAFRGEEEARPSGRSDSSVPKATSSLKARAGKMDVPYRPSGHMSLERCEGLAHGSSKVRDVVGRPPRAVPRLGVPSASPPLGPAPACRNSPAKGVGATKPPAGGAKGRNLGPSTSRALGAPVKPLGPVAGKTAGGAVPGPRAAPRAVPGIGAKAGRGTIMGTKQAFRAAHSRVHELAASGSPSRGGLSWGSTDSDSGNDSGVNLAEERQPSSPALPSPYSKVTAPRRPQRYSSGHGSDNSSVLSGELPPAMGRTALFYHSGGSSGYESMIRDSEATGSASSAPDSMSESGTASLGARSRSLKSPKKRATGLQRRRLIPAPLPDAAALGRKPSLPGQWVDLPPPLAGSLKEPFEIKVYEIDDVERLQRHRLPLRENEAKPSQDAEKGPVCISSKLRLAERRQQRLQEVQAKRDHLCEELAETQGRLMVEPGRWLEQFEVDPELEPESAEYLVALEQATAALEQCVNLCKAHVMMVTCFDIGVAATTAVPGPQEVDV
Protein: Large ribosomal subunit protein eL22 (60S ribosomal protein L22) (P47198)
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.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P35268}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL15
Sequence:
MAPVKKLVAKGGKKKKQVLKFTLDCTHPVEDGIMDAANFEQFLQERIKVNGKAGNLGGGVVTIERSKSKITVTSEEPFSKRYLKYLTKKYLKKNNLRDWLRVVANSKESYELRYFQINQDEEEEEDED
Protein: CCR4-NOT transcription complex subunit 6-like (EC 3.1.13.4) (Q8VEG6)
Organism: Mus musculus (Mouse)
Function: Poly(A) nuclease with 3'-5' RNase activity. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in mRNA decay mediated by the major-protein-coding determinant of instability (mCRD) of the FOS gene in the cytoplasm. Involved in deadenylation-dependent degradation of CDKN1B mRNA. Its mRNA deadenylase activity can be inhibited by TOB1. Mediates cell proliferation and cell survival and prevents cellular senescence (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96LI5}. Nucleus {ECO:0000250|UniProtKB:Q96LI5}. Note=Predominantly cytoplasmic. {ECO:0000250|UniProtKB:Q96LI5}.
Interaction partners:
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 8
- CCR4-NOT transcription complex subunit 6
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 2
- CCR4-NOT transcription complex subunit 3
- CCR4-NOT transcription complex subunit 10
- CCR4-NOT transcription complex subunit 11
- CCR4-NOT transcription complex subunit 4
Sequence:
MRLIGMPKEKYDPPDPRRIYTIMSAEEVANGKKSHWAELEISGRVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRVLPYELGRLFQLQTLGLTGNPLSQDIMSLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKERDQILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAKIMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGTGMKPIHAADKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVADNHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENNITGCPHPHIPSDHFSLLTQLELHPPLLPLVNGVHLPNRR
Protein: Paired box protein Pax-4 (P32115)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the differentiation and development of pancreatic islet beta cells. Transcriptional repressor that competes with PAX6 in binding to a common element in the glucagon, insulin and somatostatin promoters.
Subcellular location: Nucleus.
Interaction partners:
- Neurogenin-3
- Homeobox protein Nkx-2.2
- Neurogenic differentiation factor 1
- Pro-glucagon
- Hepatocyte nuclear factor 1-alpha
- Insulin gene enhancer protein ISL-1
- DNA-binding protein RFX6
- Somatostatin
- Insulin-1
- Insulin-2
Sequence:
MQQDGLSSVNQLGGLFVNGRPLPLDTRQQIVQLAIRGMRPCDISRSLKVSNGCVSKILGRYYRTGVLEPKCIGGSKPRLATPAVVARIAQLKDEYPALFAWEIQHQLCTEGLCTQDKAPSVSSINRVLRALQEDQSLHWTQLRSPAVLAPVLPSPHSNCGAPRGPHPGTSHRNRTIFSPGQAEALEKEFQRGQYPDSVARGKLAAATSLPEDTVRVWFSNRRAKWRRQEKLKWEAQLPGASQDLTVPKNSPGIISAQQSPGSVPSAALPVLEPLSPSFCQLCCGTAPGRCSSDTSSQAYLQPYWDCQSLLPVASSSYVEFAWPCLTTHPVHHLIGGPGQVPSTHCSNWP
Protein: Cytochrome c oxidase, cbb3-type, CcoO subunit (Q9I3G1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Cbb3-type cytochrome c oxidase subunit
- cytochrome-c oxidase
- Cbb3-type cytochrome c oxidase subunit
- cytochrome-c oxidase
- cytochrome-c oxidase
- cytochrome-c oxidase
- Cytochrome c oxidase, cbb3-type, CcoQ subunit
- Oxygen-independent coproporphyrinogen III oxidase
- Probable ferredoxin
- Outer membrane protein OprG
Sequence:
MKHEILEKNVGLLALCMAVAVSIGGLTQIVPLFFQDVTNTPVEGMKPYTALQLEGRDIYIREGCVGCHSQMIRPFRAETERYGHYSVAGESVWDHPFLWGSKRTGPDLARVGSRYSDDWHRAHLFNPRNVVPESKMPAYPWLVENKLDGKDIEKKLEVMRTLGVPYTDEDIKGAKDSLKGKTEMDAVVAYLQVLGTSIKNKR
Protein: Coiled-coil-helix-coiled-coil-helix domain containing 2, isoform B (X2JFJ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSAPPSAVGMPAPQQPSMFQQMAATAGGVAVGSAIGHTVGHGLTSLFSGSGDKEAAAPAPAAAAPAPQQPYYAQQQQPNEPQGACAWELKQFIQCAQGQADLTLCEGFNEALRQCKQSHHLQ
Protein: Protein artemis (DNA cross-link repair 1C protein) (Q581T3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Proliferating cell nuclear antigen
- KU70 protein
- KU80 protein
- Flap endonuclease 1
- Endo/exonuclease Mre11
- Mitochondrial DNA polymerase beta-PAK
- Enkurin domain-containing protein
- DNA polymerase
- DNA repair protein RAD50
- BRCT domain-containing protein
Sequence:
MAGGAAGKVTRTGDDMPDTLKKYMLTREVYRNASVAILVDAFVHTRRYLKSCRADGDGASSGLGPAGESFRGLFFLSHFHSDHYSGITEKWSHGTIYASRATGNVLCWKLGVRRSCVECLDLAVTYIFSLRNGDLVKKEEGRAECGEGCFSVELIPANHCPGAVMFLFRSADFGTILHTGDFRFSSPAVPALSIKHRCWEPDLRSNPVLKSMGNVDVLFLDNTYCQPQFTFPDRAAIFQTVNKEVLDMIMGCERRLSYSQSQEHMQTKEEGQTVSVAVIVGSYFIGKEIIALSVQENFPSKKSGDGAPAYAPIYVTPERYEAMRQLDYFPERFTPHHMKEPQDIYLGYRMGGNGESGGECTGRFTTCEVKLPVDSEISTSKTAGEMSSDHVAPDSMTGGVKYSLALFLVPLSLTTYSALAPAFGRPVRRRHGEGTAIDGGAADTGDETVSLWGNERVDLKQFDGVLFVNPTGWAAKVSRQKINERVSLLNIPYSEHCCFSELIDFVEFVNPALVVPTVSKEAFAQHESLFAEKAPRLRTRYSNMQPICRLLARASSVDSPETRTQPGDAKQEESIKTEKQRNPFAIGRSLNAEPSKGLSSANTCESRKGPECVDVEDEESTASEDTHNRNESGSLPNLVENARNEVVCKEMNIQPERVMSTVCRLGSVTQIRKRGRPHSRKPPSVAATTQAAIRRWCQSGYKSSDRANAKEVIDLSSDSE
Protein: PAT complex subunit Asterix (Protein associated with the ER translocon of 10kDa) (PAT-10) (PAT10) (WD repeat domain 83 opposite strand) (WDR83 opposite strand) (Q9Y284)
Organism: Homo sapiens (Human)
Function: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. Within the MPT complex, the PAT subcomplex sequesters any highly polar regions in the transmembrane domains away from the non-polar membrane environment until they can be buried in the interior of the fully assembled protein (By similarity). Within the PAT subcomplex, WDR83OS/Asterix binds to and redirects the substrate to a location behind the SEC61 complex (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:32814900, ECO:0000269|PubMed:36261522}; Multi-pass membrane protein {ECO:0000305|PubMed:12475939}.
Interaction partners:
- PAT complex subunit CCDC47
- Tubulin beta-2B chain
- Transmembrane protein 208
- Tubulin beta-4B chain
- Tubulin beta-2A chain
Sequence:
MSTNNMSDPRRPNKVLRYKPPPSECNPALDDPTPDYMNLLGMIFSMCGLMLKLKWCAWVAVYCSFISFANSRSSEDTKQMMSSFMLSISAVVMSYLQNPQPMTPPW
Protein: Type 1 fimbriae regulatory protein FimE (P0ADH7)
Organism: Escherichia coli (strain K12)
Function: FimE is one of the 2 regulatory proteins which control the phase variation of type 1 fimbriae in E.coli. These proteins mediate the periodic inversion of a 300bp DNA segment that harbors the promoter for the fimbrial structural gene, fimA. FimE switches fimA off.
Interaction partners:
- Type-1 fimbrial protein, A chain
- Uncharacterized fimbrial-like protein SfmA
- Chaperone protein FimC
- Probable fimbrial chaperone SfmC
- Zinc chaperone YeiR
- Type 1 fimbrin D-mannose specific adhesin
- Uncharacterized fimbrial-like protein SfmH
- Protein FimF
- Fimbrin-like protein FimI
- Uncharacterized fimbrial-like protein SfmF
Sequence:
MSKRRYLTGKEVQAMMQAVCYGATGARDYCLILLAYRHGMRISELLDLHYQDLDLNEGRINIRRLKNGFSTVHPLRFDEREAVERWTQERANWKGADRTDAIFISRRGSRLSRQQAYRIIRDAGIEAGTVTQTHPHMLRHACGYELAERGADTRLIQDYLGHRNIRHTVRYTASNAARFAGLWERNNLINEKLKREEV
Protein: Copper chaperone for superoxide dismutase (Superoxide dismutase copper chaperone) (Q9JK72)
Organism: Rattus norvegicus (Rat)
Function: Delivers copper to copper zinc superoxide dismutase (SOD1).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Copper-transporting ATPase 1
- Copper-transporting ATPase 2
- Superoxide dismutase
- Copper transport protein ATOX1
- Extracellular superoxide dismutase
- Cytochrome c oxidase copper chaperone
- High affinity copper uptake protein 1
- Cytochrome c oxidase copper chaperone COX11
- Synthesis of cytochrome C oxidase 1
- Metallothionein
Sequence:
MASKSGDGGTMCALEFTVQMSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQTTLPSQEVQALLESTGRQAVLKGMGSSQLKNLGAAVAIMEGSGTVQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNPDGASHGGPQDTDRHRGDLGNVHAEASGRATFRIEDKQLKVWDVIGRSLVVDEGEDDLGRGGHPLSKVTGNSGKRLACGIIARSAGLFQNPKQICSCDGLTIWEERGRPIAGQGRKDSAQPPAHL