wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized lipoprotein YbaY (P77717)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Osmotically-inducible protein Y
- Potassium binding protein Kbp
- Uncharacterized protein YgaM
- Protein ElaB
- NAD
- Uncharacterized protein YbgS
- Osmotically-inducible putative lipoprotein OsmE
- Peroxiredoxin OsmC
- Colanic acid biosynthesis protein WcaK
Sequence:
MKLVHMASGLAVAIALAACADKSADIQTPAPAANTSISATQQPAIQQPNVSGTVWIRQKVALPPDAVLTVTLSDASLADAPSKVLAQKAVRTEGKQSPFSFVLSFNPADVQPNARILLSAAITVNDKLVFITDTVQPVINQGGTKADLTLVPVQQTAVPVQASGGATTTVPSTSPTQVNPSSAVPAPTQY
Protein: Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (AIR carboxylase) (AIRC) (Q92210)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Bifunctional aminoimidazole ribotide synthase/glycinamide ribotide synthase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Adenylosuccinate lyase
- Amidophosphoribosyltransferase
- Phosphoribosylformylglycinamidine synthase
- Orotidine 5'-phosphate decarboxylase
- Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase
- Phosphoribosylglycinamide formyltransferase
- 3-isopropylmalate dehydrogenase
- Imidazoleglycerol-phosphate dehydratase
Sequence:
MDSKTVGILGGGQLGRMIVEAAHRLNIKTVILDAAKSPAKQINALDDHVDGSFTNYDSIVKLAEKADVLTVEIEHVDVDALIKVQEKFPKVEIYPLPETIRLIQDKYLQKNHLIKHDVAVTESVAVETNTVDDLLHIGEKFGYPYMLKSRTLAYDGRGNFVVKDKSYCEKALEFLKDRPLYAEKWCPFTKELAVMVVRSLEGEVFAYPTVETIHENNICHLVYAPARIPDTLAKKASILAKNAVKSFLGCGIFGVEMFLLENNELLINEIAPRPHNSGHYTIDACVTSQFEAHVRAVTGLPMPKGFTEFSTSITNAIMLNVLGDKATPNKELEICRRALETPHASVYLYGKTTRPERKMGHINVVTSSMQDAESRLSYILGDTTEIPKSLATDKESPLVGIIMGSDSDLPVMAVGARILKQFGVPFELTIVSAHRTPHRMSEYAIEAPKRGLKCIIAGAGGAAHLPGMVAAMTPLPVIGVPVKGSTLDGVDSLHSIVQMPRGIPVATVAINNSTNAALLAIRILGAYDSKWLTEMNQYMLNMETEVLGKAETLEEIGYEDYLTDKLKK
Protein: ADIPOR-like receptor IZH4 (Implicated in zinc homeostasis protein 4) (Q99393)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ADIPOR-like receptor IZH3
- Zinc-responsive transcriptional regulator ZAP1
Sequence:
MVSLTTIEQSPVKCETTTEKESNDTRGTDSNENAETKETKKGFPFHDLAKLQKQYKNKSSRNESLVALIYLLGSMLSFCLLIFFTDFYLIPLFPTTTTMTDYIVFNFYLLNVFVFCMVHFIYHFVKNISLQQHLEHWQKFSYLSNINLLISSQITILYYLFYDYVFFFKIFTLLMNFIGLVAYFFILTDKLISSKRFNKTVFFISVSVVCCSLPLLTAIITFDGLENLKERIKVNAITWELVALVAASIIYVTRFPESLFRRNKKEEGWNHSEYLFHLLISGTAFYHFFILIQSYILMHSSLNQPELINFKS
Protein: Pinoresinol reductase 1 (AtPrR1) ((+)-pinoresinol reductase) (EC 1.23.1.1) ((-)-pinoresinol reductase) (EC 1.23.1.3) (Pinoresinol-lariciresinol reductase 1) (AtPLR1) (Q9FVQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reductase involved in lignan biosynthesis. Involved in secondary cell wall biosynthesis in fiber cells. Unlike conventional pinoresinol reductases that can reduce both pinoresinol and lariciresinol, PRR1 shows a strict substrate preference toward pinoresinol. Active on both (+) and (-)-pinoresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
Interaction partners:
- Pinoresinol reductase 2
- Cell division cycle 5-like protein
- Laccase-11
- Dirigent protein
- Laccase-17
- Laccase-4
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
Sequence:
MGESKRTEKTRVLVVGATGYIGKRIVRACLAEGHETYVLQRPEIGLEIEKVQLFLSFKKLGARIVEGSFSDHQSLVSAVKLVDVVVSAMSGVHFRSHNILVQLKLVEAIKEAGNVKRFLPSEFGMDPPRMGHALPPGRETFDQKMEVRQAIEAAGIPYTYVVGACFAAYFAGNLSQMVTLLPPKEKVNIYGDGNVKVVFADEDDIAKYTAKTLNDPRTLNKTVNIRPPDNVLTQLELVQIWEKLTGKELEKTNIAAQDFLANIEQMEIPHQAGIGHFYHIFYEGCLTDHEVGEDEEASSLYPDVKYKRMDDYLRMFL
Protein: Maf-like protein (F4K330)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Tyrosine decarboxylase 2
- Acetylserotonin O-methyltransferase
Sequence:
MESNHPHFKLILGSSSIARRKILTDMGYQFTLMSADIDEKSIRKEKPEELVLALAEAKADAIVSKLQISECEDEEQPRVLIASDTAEAIMQRIPDGENIEEDKSTLLITCDQVVVYEDAVREKPSSVEEAREYIRGYSKGHTATVSSVAVTNLKTGVRKGGVDRVEIYFNEIPEETIEKLIEEGMVLKVAGALLIEHPLILPCVKEVVGTTDSVMGLPKELTEKLIKEVLAST
Protein: Semaphorin-2A (Sema-2a) (Protein male abnormal 20) (Q95XP4)
Organism: Caenorhabditis elegans
Function: Regulates the formation or stabilization of cell-cell contacts at several stages of epithelial morphogenesis. In early embryonic development, required for proper ventral closure of the epidermis. During male tail morphogenesis, regulates precursor cell sorting and allows the formation of distinct sensory rays. Seems to control cell-cell contact formation through 2 parallel pathways, one involving efn-4 and one involving plx-2 and unc-129. Involved in follower axon guidance. In particular, it is required for the guidance of axons from neurons, including SubL neurons and AIY interneurons, into the nerve ring. Probably by binding receptor plx-2, regulates fln-1-mediated remodeling of the actin cytoskeleton and thus axon guidance and/or fasciculation of DD/VD neurons.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Plexin-2
- Sema domain-containing protein
- Ephrin-4
- Semaphorin-1A
- Immunoglobulin domain-containing protein Y54G2A.25
- Ephrin receptor 1
- Ephrin RBD domain-containing protein
Sequence:
MRNFLVFSVIFIAYNSCEAANIQADNTFADPNIGEFRELLIDPKAGALFVGSEGAIFRLWAYNINDTGENVFAKKQLVLSESEESECRSTASDERLCRPSTRFLAFTNNLDSIYVCSSVGMRPEIRVLDSLSLRDQQEPRTEIGICVVDPTFNFTAVVVDSGNPEDATSVYSGIRTGMGGENHLIYRPPLTKNGKQLHASIRTIYSDNKWLNEPQFVGSFDVGQHVFFFFREIAHDNSFGERIVHSRVARVCKKDIGGRNVLRQVWTSFVKARLNCSVSANFPFYFDHIQSVKRVDKHGETYFYATFSTSETAFTSSAICMFQLSSINHLLDTGLLMEETANGQFSVTADEIPAHRPGTCSQNSHSISDTDLHFAKTHLLVSDSISGGTPILPLRDHVFTHIVVDQLPNQNVIFAFDSANRRVWKISHWKEGNEWKSNLIEEKSLKIAASRINDVALLPAEFFFVTSGAGVSQFSVARCSEQPSCALCSLDPYCSWNAVNSKCSLKTKTNEKSVGWISSSWAGRISPECSAVEKLTVKDVYLGDGLRLVGAKNGVWQKDGRSVESGQRHVVTRNGELVVLDAQLEDAGTYECLRDNIILVRARIVVHENCARPTSVAEYRSCQREWCKKADAYKAALNIWSDSNKKNVQCKANTSSAH
Protein: Polyadenylate-binding protein (PABP) (Q62029)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
- Polyadenylate-binding protein-interacting protein 1
- Cold shock domain-containing protein E1
- Eukaryotic translation initiation factor 4E
- PAN2-PAN3 deadenylation complex catalytic subunit Pan2
- Heterogeneous nuclear ribonucleoprotein D0
- Eukaryotic initiation factor 4A-I
- Heterogeneous nuclear ribonucleoprotein Q
- Polyadenylate-binding protein
- Polyadenylate-binding protein 1
- Polyadenylate-binding protein 2
Sequence:
MNSSDPGCPMASLYVGDLHPDVTEAMLYEKFSSAGPILSIRVYRDVITRRSLGYASVNFEQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRRSGVGNVFIKNLNKTIDNKALYDTFSAFGNILSCKVVSDENGSKGHGFVHFETEEAAERAIEKMNGMLLNDRKVFVGRFKSQKEREAELGTGTKEFTNVYIKNFGDRMDDETLNGLFGRFGQILSVKVMTDEGGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKHIYVGRAQKKDDRHTELKHKFEQVTQDKSIRYQGINLYVKNLDDGIDDERLQKEFSPFGTITSTKVMTEGGRSKGFGFVCFSSPEEATKAVSEMNGRIVATKPLYVALAQRKEERQAHLTNQYIQRMASVRSGPNPVNPYQPASSSYSVAAVPQTQNCVPCCPSQIAQPRPSARWIAQGSRPHPFPNVPGAIHPAAPRSSLTTVRPSSSHVQVTTAHRITNTSAQITGQRPAPASSATATPVHSIPQYKYAAGVQNSQQHLNAQLAQQPAVCIQGQEPWTASMLVTAPQEPKQMLGERLFPLIQAMHPTLAGKITGMLLDIDNSEPLRMLESPVSRCSRAEEAVATLQAHQVKEAAQKAVGSTSGVPTV
Protein: Protein YfjI (P52124)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YfjJ
- UPF0380 protein YafZ
Sequence:
MFNGRPFPVDAFPKIIRNAIYEVEQHTQAPQGLIAASALGVISLACQNRIDVCRLNNLRGPVSLFLMTLAESGERKSTVDKLLMKPLYQLEEDLFEKYTHDLTAWRNDEAIFNIEKKALMSKLKSDIRRNKDHLATNERLKELLTTNPKAPVRFKFLFNDATPAAIKAHLCGHWRSVGIMSDEAGIIFNGYTLNELPFINKMWDGSIFTVERKNEPEKLIRDARITLSLMVQPNVFKGYIDRKGDMAKGIGFFARCLMCQPASTQGNRKISNPIFSNEHLPVFHQRLMEIVNESIIKINENNRICLRFSAEAERHWIEFYNQVESEMRMIGLLYDFKDYASKMAENMARLAALLHYFSGDGGDISVTAVKAAVEIVAWYIEEYIRLFSKKEEFSLDVSEADELYCWIKDYCTQKFSSCIKKNIILQFGPNKFRNRDKANELIRILISQNKIFISSWGKTKIINITHCVF
Protein: Dual-specificity RNA pseudouridine synthase RluF (EC 5.4.99.-) (EC 5.4.99.21) (23S rRNA pseudouridine(2604) synthase) (Ribosomal large subunit pseudouridine synthase F) (rRNA pseudouridylate synthase F) (rRNA-uridine isomerase F) (tRNA(Tyr) pseudouridine(35) synthase) (P32684)
Organism: Escherichia coli (strain K12)
Function: Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-2604 in 23S ribosomal RNA and from uracil-35 in the anticodon of tRNA(Tyr). Can, to a small extent, also react with uracil-2605.
Interaction partners:
- Dual-specificity RNA pseudouridine synthase RluA
- tRNA pseudouridine synthase B
- tRNA pseudouridine synthase A
- tRNA pseudouridine synthase D
- tRNA pseudouridine synthase C
- Uncharacterized protein YjbD
- Ribosomal large subunit pseudouridine synthase D synthase)
Sequence:
MLPDSSVRLNKYISESGICSRREADRYIEQGNVFLNGKRATIGDQVKPGDVVKVNGQLIEPREAEDLVLIALNKPVGIVSTTEDGERDNIVDFVNHSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPITEEFIRGMSAGVPILGTVTKKCKVKKEAPFVFRITLVQGLNRQIRRMCEHFGYEVKKLERTRIMNVSLSGIPLGEWRDLTDDELIDLFKLIENSSSEVKPKAKAKPKTAGIKRPVVKMEKTAEKGGRPASNGKRFTSPGRKKKGR
Protein: Extracellular cellulase CelA/allergen Asp F7-like, putative (AFU_orthologue AFUA_5G08030) (Q5AVE5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Uncharacterized protein
Sequence:
MKYQHFSSIALAALSASTFVSAAPLAPEENGSCPAGYSPSVYYITVTAEPSSTVRPTSSAPISSTPTSTSTSTSTSETSLTTLASTSTGDVTVTSSSTAGLIETIPAVVVNAATSTTSESATSTSALSISETAPTQVAVARPSTTTAAEKTSSTSTSSSSSSTSTNSGATTGEATFYGGNLSGGTCSFTDYTLPSHLSGVAFSGQAWDNAAECGACIAVTGPNGNTVKVMVVDKCPECAQTHLDLFESAFTTLASASEGQIPISYSITPCGITSPLILRNKSGTSAYWFSMQVVNANGAVKSLEVSTDNGSTWQETTRSDYNFFENSSGFGTDTVDVRVTGVDGGVITVKNVSVASGESVTADGNF
Protein: Outer capsid glycoprotein VP7 (A2T3P5)
Organism: Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Function: Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7 (By similarity).
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:1649333, ECO:0000269|PubMed:19036817}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04131}.
Interaction partners:
Sequence:
MYGIEYTTVLTFLISIILLNYILKSLTRIMDFIIYRFLFIIVILSPFLRAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTNIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDATTFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDILDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVDQIIQVMSKRSRSLNSAAFYYRV
Protein: Histone-arginine methyltransferase CARM1 (EC 2.1.1.319) (Coactivator-associated arginine methyltransferase 1) (Protein arginine N-methyltransferase 4) (Q6DC04)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me) and activates transcription via chromatin remodeling.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q86X55}. Cytoplasm {ECO:0000250|UniProtKB:Q86X55}. Chromosome {ECO:0000250|UniProtKB:Q86X55}.
Interaction partners:
- Histone H3.2
- Histone H3
- Nuclear receptor coactivator 2
- Nuclear receptor coactivator 3
- E1A-binding protein p300 b.
- histone acetyltransferase
- Estrogen receptor
- E1A-binding protein p300 a.
Sequence:
MAVSVFSGVRLLSIGDANGDIQRHSEQQPLRLEIKMNQDAAQIILSNNEETCVFKCTVLRETECSRVGKQSFIITLGCNSVLLQFASPADFSSFYNLLKICRGQKGDRSVFSDRTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNRLSERVVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKFLKPSGKMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPIVDTFDIRILMAKSVKYTVNFLEAKEEDLYKIEIPFKFHMMHSGLVHGLAFWFDVAFIGSVMTVWLSTAPTEPLTHWYQVRCLLQSPLFAKAGDTMSGTALLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPAPPPGSHYSSPSENMWNTGGTYSMSQGMAVSGMPTAYDLSTVIGGSGTTVSHNNLIPLGTDTHALNTGIVNHTHSRMGSIMSTGIVQGATTAQQGPSSASLHYPVTNQFTMGGPAISMASPMAIPSNTMHYGS
Protein: Retinoic acid receptor beta (Nuclear receptor subfamily 1 group B member 2) (D3ZFD9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Mediator of RNA polymerase II transcription subunit 1
- Retinoic acid receptor RXR-beta
- Retinoic acid receptor, alpha
- Nuclear receptor coactivator
- Retinoic acid receptor RXR-gamma
- Cellular retinoic acid-binding protein 2
- Nuclear receptor corepressor 2
- Arginine--tRNA ligase, cytoplasmic
- Cytochrome P450 26A1
Sequence:
MFDCMDVLSVSPGQILDFYTASPSSCMLQEKALKACLSGFTQAEWQHRHTAQSIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEPSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPNSSGNTAEHSPSVSPSSVETSGVSQSPLLQ
Protein: DNA-directed RNA polymerase II, putative (Q388R6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-dependent RNA polymerases, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase I subunit RPA1
Sequence:
MDSVKSFKMIRLYRAFNTVIQMAIDRGFVVSHPSDVANAIRDSRLYDITDGLNYQWFTQRCSSYLQRHRQTTAEEEEEAKQEGRPGKDPSKSKRTKALRDASQDFLYSSLELVCKGSSSRIGFGGGAISCKTEDEVDGRGPTAEPSSRKKNETILCAFFVQSLGVDVLNNLREVAQRRNASSMIVVVGSKVRGGRRSIREAGGGLHPGTTGQVIRIQVFEEDELAYNISRHQSVPKHVPMTDVEVRAFLEQRKLMITQLPRILNDDPMVEYLDLPRGSIIRIERRTDEGSTYEMYRHVI
Protein: tRNA (guanosine(18)-2'-O)-methyltransferase (EC 2.1.1.34) (tRNA [Gm18] methyltransferase) (Q72GI1)
Organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
Function: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA.
Interaction partners:
Sequence:
MRERTEARRRRIEEVLRRRQPDLTVLLENVHKPHNLSAILRTCDAVGVLEAHAVNPTGGVPTFNETSGGSHKWVYLRVHPDLHEAFRFLKERGFTVYATALREDARDFREVDYTKPTAVLFGAEKWGVSEEALALADGAIKIPMLGMVQSLNVSVAAAVILFEAQRQRLKAGLYDRPRLDPELYQKVLADWLRK
Protein: WD repeat-containing protein 74 (Q8VCG3)
Organism: Mus musculus (Mouse)
Function: Regulatory protein of the MTREX-exosome complex involved in the synthesis of the 60S ribosomal subunit. Participates in an early cleavage of the pre-rRNA processing pathway in cooperation with NVL (By similarity). Required for blastocyst formation, is necessary for RNA transcription, processing and/or stability during preimplantation development.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6RFH5}. Nucleus {ECO:0000269|PubMed:21799883}. Note=Nucleolar location depends on active PolI transcription of pre-rRNA. {ECO:0000250|UniProtKB:Q6RFH5}.
Interaction partners:
- Protein MAK16 homolog
- Ribosome production factor 1
- Pescadillo homolog
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Ribosome biogenesis protein WDR12
- ATP-dependent RNA helicase DDX18
- Probable rRNA-processing protein EBP2
- Ribosome biogenesis protein BOP1
- Eukaryotic translation initiation factor 6
- GTP-binding protein 4
Sequence:
MATASARWNHVWVGTETGILKGVNLQRKHAANFTPSGQPRREEAVNALCWGTGGETQILVGCADRTVRYFNAEEGTFLSQRYCPGGEGTFRGLAQADGTLITCVDSGILRVWCENDKEASSDPLLELKVGPGVCRMRQDPTHTHVVATCGKENALKVWDLQGSEEPVFRAKNVRNDWLDLRVPIWDQDTQFLPGSQKLVTCTGYHQVRVYDPVSPQRRPVLEATYGEYPLTAMTLTPEGNSVIVGNTHGQLAEIDFRQGRLLGCLKGLAGSVRGLQCHPSKPLLASCGLDRVLRIHRIRNPRGLEHKVYLKSQLNCLLLSGRDNWEDEPQEPQEPNQVPSEDTETDELWASLEAAAKRKLPDLDQTQGALQRRKKKKRPGSTSP
Protein: Uronate isomerase (EC 5.3.1.12) (Glucuronate isomerase) (Uronic isomerase) (P0A8G3)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Altronate dehydratase
- D-mannonate oxidoreductase
- Mannonate dehydratase
- Altronate oxidoreductase
- Beta-glucuronidase
- Starvation-sensing protein RspB
- 2-dehydro-3-deoxygluconokinase
- Hexuronate transporter
- 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
- KHG/KDPG aldolase
Sequence:
MTPFMTEDFLLDTEFARRLYHDYAKDQPIFDYHCHLPPQQIAEDYRFKNLYDIWLKGDHYKWRAMRTNGVAERLCTGDASDREKFDAWAATVPHTIGNPLYHWTHLELRRPFGITGKLLSPSTADEIWNECNELLAQDNFSARGIMQQMNVKMVGTTDDPIDSLEHHAEIAKDGSFTIKVLPSWRPDKAFNIEQATFNDYMAKLGEVSDTDIRRFADLQTALTKRLDHFAAHGCKVSDHALDVVMFAEANEAELDSILARRLAGETLSEHEVAQFKTAVLVFLGAEYARRGWVQQYHIGALRNNNLRQFKLLGPDVGFDSINDRPMAEELSKLLSKQNEENLLPKTILYCLNPRDNEVLGTMIGNFQGEGMPGKMQFGSGWWFNDQKDGMERQMTQLAQLGLLSRFVGMLTDSRSFLSYTRHEYFRRILCQMIGRWVEAGEAPADINLLGEMVKNICFNNARDYFAIELN
Protein: Long-chain-fatty-acid--AMP ligase FadD32 (FAAL) (EC 6.2.1.20) (Acyl-AMP synthetase) (FAAL32) (O53580)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of mycolic acids. Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension. Can use dodecanoate (C12), tetradecanoate (C14) and hexadecanoate (C16). In vitro, displays a preference for long-chain over medium and short-chain fatty acid substrates.
Interaction partners:
- Polyketide synthase Pks13
- Biotin-dependent long chain acyl-coenzyme A carboxylase beta4 subunit
- Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- Peptide synthetase MbtE
- Carboxylesterase/lipase Culp6
- Uncharacterized MFS-type transporter EfpA
- Enoyl-[acyl-carrier-protein] reductase
- Peptide synthetase MbtF
Sequence:
MFVTGESGMAYHNPFIVNGKIRFPANTNLVRHVEKWAKVRGDKLAYRFLDFSTERDGVARDILWSDFSARNRAVGARLQQVTQPGDRVAILCPQNLDYLISFFGALYSGRIAVPLFDPAEPGHVGRLHAVLDDCAPSTILTTTDSAEGVRKFIRARSAKERPRVIAVDAVPTEVAATWQQPEANEETVAYLQYTSGSTRIPSGVQITHLNLPTNVVQVLNALEGQEGDRGVSWLPFFHDMGLITVLLASVLGHSFTFMTPAAFVRRPGRWIRELARKPGETGGTFSAAPNFAFEHAAVRGVPRDDEPPLDLSNVKGILNGSEPVSPASMRKFFEAFAPYGLKQTAVKPSYGLAEATLFVSTTPMDEVPTVIHVDRDELNNQRFVEVAADAPNAVAQVSAGKVGVSEWAVIVDADTASELPDGQIGEIWLHGNNLGTGYWGKEEESAQTFKNILKSRISESRAEGAPDDALWVRTGDYGTYFKDHLYIAGRIKDLVIIDGRNHYPQDLECTAQESTKALRVGYAAAFSVPANQLPQTVFDDSHAGLKFDPEDTSEQLVIVGERAAGTHKLDHQPIVDDIRAAIAVGHGVTVRDVLLVSAGTIPRTSSGKIGRRACRAAYLDGSLRSGVGSPTVFATSD
Protein: Thymidine kinase a (AtTK1a) (EC 2.7.1.21) (Q9S750)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of the salvage pathway for purine and pyrimidine deoxyribonucleotide synthesis. Phosphorylates preferentially purines over pyrimidines. Mediates tolerance to genotoxins, such as ultraviolet-C (UV-C) irradiation, MMC, a DNA crosslinker, and ZEO, a DNA intercalator, that induce double-strand breaks and thus contributes to several DNA repair pathways by providing deoxythymidine triphosphate that serve as precursors for DNA repair and to balance deoxyribonucleotides pools.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04183}.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Bifunctional dihydrofolate reductase-thymidylate synthase
- dCMP deaminase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Thymidylate kinase
- Cytidine deaminase 2
- Cytidine deaminase 5
- Cytidine deaminase 3
- Cytidine deaminase 7
Sequence:
MATLKASFLIKTLDSDVTGDFLSDLERRGSGAVHVIMGPMFSGKSTSLLRRIKSEISDGRSVAMLKSSKDTRYAKDSVVTHDGIGFPCWALPDLMSFPEKFGLDAYNKLDVIGIDEAQFFGDLYEFCCKVADDDGKIVIVAGLDGDYLRRSFGAVLDIIPIADSVTKLTARCEVCGHKAFFTLRKNCDTRTELIGGADVYMPVCRKHYITNHIVIKASKKVLEDSDKARAESCVAATI
Protein: Transmembrane channel-like protein (Q8C5T3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MYFQCWAVMCCNVPEARVFKASRSNNFYLGMLLLILFLSTMPVLYMIVSLPPSFDCGPFSGKNRMFEVIGETLEHDFPSWMAKILRQLSNPGLVIAVILVMVLTIYYLNATAKGQKAANLDLKKKMKQQALENKMRNKKMAAARAAAAAGGQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4JI10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- TORTIFOLIA1-like protein 4
- Putative zinc finger protein At1g68190
- Auxin-responsive protein SAUR27
- Auxin-responsive protein SAUR29
- Protein kinase superfamily protein
- non-specific serine/threonine protein kinase
- Pyruvate, phosphate dikinase regulatory protein 1, chloroplastic
Sequence:
MTMSIFNPDSINNELSKPTSIFGLKLWVVIGILLGSLIVIALFFLSLCLTSRRRNRKPRHADFASAAVATPPISKEIQEIVRPPAQDHCHPTQPVAAEIQVDIGKTEHRVVFSDRVSSGESRGTVSETASYSGSGCVGPEVSHLGWGRWYTLRELEAATNGLCEENVIGEGGYGIVYSGILTDGTKVAVKNLLNNRGQAEKEFRVEVEAIGRVRHKNLVRLLGYCVEGAYRMLVYDYVDNGNLEQWIHGDVGDKSPLTWDIRMNIILCMAKGLAYLHEGLEPKVVHRDIKSSNILLDRQWNAKVSDFGLAKLLFSESSYVTTRVMGTFGYVAPEYACTGMLTEKSDIYSFGILIMEIITGRNPVDYSRPQGEVNLVEWLKTMVGNRRSEEVVDPKIPEPPTSKALKRVLLVALRCVDPDANKRPKMGHIIHMLEAEDLFYRDQERRATREHASRDFNQPRTEISPAVAETSESDSSKDRR
Protein: C3a anaphylatoxin chemotactic receptor (C3AR) (C3a-R) (Complement component 3a receptor 1) (O09047)
Organism: Mus musculus (Mouse)
Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Complement C5
- Complement C3
- C5a anaphylatoxin chemotactic receptor 1
- Integrin alpha-M
- Complement C4-B
- Complement C1q subcomponent subunit A
- Complement factor B
- Integrin beta-2
- High affinity immunoglobulin epsilon receptor subunit gamma
- Complement factor H
Sequence:
MESFDADTNSTDLHSRPLFQPQDIASMVILGLTCLLGLLGNGLVLWVAGVKMKTTVNTVWFLHLTLADFLCCLSLPFSLAHLILQGHWPYGLFLCKLIPSIIILNMFASVFLLTAISLDRCLIVHKPIWCQNHRNVRTAFAICGCVWVVAFVMCVPVFVYRDLFIMDNRSICRYNFDSSRSYDYWDYVYKLSLPESNSTDNSTAQLTGHMNDRSAPSSVQARDYFWTVTTALQSQPFLTSPEDSFSLDSANQQPHYGGKPPNVLTAAVPSGFPVEDRKSNTLNADAFLSAHTELFPTASSGHLYPYDFQGDYVDQFTYDNHVPTPLMAITITRLVVGFLVPFFIMVICYSLIVFRMRKTNFTKSRNKTFRVAVAVVTVFFICWTPYHLVGVLLLITDPESSLGEAVMSWDHMSIALASANSCFNPFLYALLGKDFRKKARQSIKGILEAAFSEELTHSTNCTQDKASSKRNNMSTDV