wanglab/gogpt-training-data huggingface dataset:
Protein: 4-coumarate--CoA ligase-like 9 (EC 6.2.1.-) (4-coumarate--CoA ligase isoform 4) (At4CL4) (Q84P23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors. Converts 12-oxo-phytodienoic acid (OPDA) into OPDA-CoA. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:15677481}.
Interaction partners:
- Trans-cinnamate 4-monooxygenase
- Cinnamoyl-CoA reductase 2
- Cinnamoyl-CoA reductase 1
- Cytochrome P450 84A1
- F5F19.5 protein
- Flavone 3'-O-methyltransferase 1
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 3
- Phenylalanine ammonia-lyase 1
- Phenylalanine ammonia-lyase 4
Sequence:
MLTKTNDSRLIDRSSGFDQRTGIYHSLRPSLSLPPIDQPLSAAEFALSLLLKSSPPATAGKNIEALTYLVNSSSGDNLTYGELLRRVRSLAVSLRERFPSLASRNVAFILSPSSLDIPVLYLALMSIGVVVSPANPIGSESEVSHQVEVSEPVIAFATSQTVKKLQSSSLPLGTVLMDSTEFLSWLNRSDSSSVNPFQVQVNQSDPAAILFSSGTTGRVKGVLLTHRNLIASTAVSHQRTLQDPVNYDRVGLFSLPLFHVFGFMMMIRAISLGETLVLLGRFELEAMFKAVEKYKVTGMPVSPPLIVALVKSELTKKYDLRSLRSLGCGGAPLGKDIAERFKQKFPDVDIVQGYGLTESSGPAASTFGPEEMVKYGSVGRISENMEAKIVDPSTGESLPPGKTGELWLRGPVIMKGYVGNEKASAETVDKEGWLKTGDLCYFDSEDFLYIVDRLKELIKYKAYQVPPVELEQILHSNPDVIDAAVVPFPDEDAGEIPMAFIVRKPGSNLNEAQIIDFVAKQVTPYKKVRRVAFINAIPKNPAGKILRRELTKIAVDGNASKL
Protein: Keratin, type I cytoskeletal 15 (Cytokeratin-15) (CK-15) (Keratin-15) (K15) (P19012)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin, type II cytoskeletal 6A
- Keratin, type II cytoskeletal 5
- Keratin, type I cytoskeletal 14
Sequence:
MTTTFLQTSSSTFGGGSTRGGSLLAGGGGFGGGSLSGGGGSRSISASSARFVSSGSGGGYGGGMRVCGFGGGAGSVFGGGFGGGVGGGFGGGFGGGDGGLLSGNEKITMQNLNDRLASYLDKVRALEEANADLEVKIHDWYQKQTPTSPECDYSQYFKTIEELRDKIMATTIDNSRVILEIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEEMKEFSSQLAGQVNVEMDAAPGVDLTRVLAEMREQYEAMAEKNRRDVEAWFFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAGIAIREASSGGGGSSSNFHINVEESVDGQVVSSHKREI
Protein: Lys14p (Q5AC02)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSQSPSSLSPATASSSGVNSPSDQPPLPPRVRKSYSRNGCRECKRRKIRCPEEKPYCSTCVRLGKQCSYPLAGEKVLRISRRLIKEEIENMGKSTQFLPVQYDIPRRIKPQTQSVIKPSPLNIENLINSNDFLNGADLNVLTADLNNLVSDIIEVSNIPILEEDFQFDFLNEPIIVEQITKNVPIDYIKLPRKHEQLYWEEFYNNFAQIIEPFQAYDTKTKKTSNPARDIILQTAATEPFLLAAILAEGANTCYLKYKRPEDERAYGAYLSKCLKLLEPARETDINANIEAVLLTLLLLTAATATSQTQKWRPHLMGAKSLLLKAINQNVSKKFVFCKYWFVSIEILAGLSTNLGGTLQTDAEIDQLVTPGNEFEIEVLRDLGIISDQGFNILMGYDNTCLACFRDLLKILNKKRLNMYIDTMSYVKLLSDFYNQANIVYIDSRGVIAENELTRYVPGLPIEELRINNASYWISWQDISHQSYVLSSLIMILTRFFVIDVSGLVDKVIQFIHYLNQFSDVQQHASPYLLLMIQWPLLVTGLSTTKLEQRHLLLKYFSMVGQIGAAAANVSIQILLKHWKGTIDIENDDTLIY
Protein: Cadherin-13 (Q8VDK4)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQPRTPLTLCVLLSQVLLVTSADDLECTPGFQQKVLHIHQPAEFIEDQPVLNLTFSDCKGNEKLHYEVSSPHFKVNSDGTLVALRNITAVGRTLFVHARTPHAEDMAELVIVGGKDIQGSLQDIFKFARTSPVPRQKRSIVVSPILIPENQRQPFPRDVGKVVDSDRPEGSKFRLTGKGVDQDPKGTFRINENTGSVSVTRTLDRETIATYQLYVETTDASGKTLEGPVPLEVIVIDQNDNRPIFREGPYIGHVMEGSPTGTTVMRMTAFDADDPATDNALLRYNIRQQTPDKPSPNMFYIDPEKGDIVTVVSPALLDRETLENPKYELIIEAQDMAGLDVGLTGTATATIVIDDKNDHSPKFTKKEFQATVEEGAVGVIVNLTVEDKDDPTTGAWRAAYTIINGNPGQSFEIHTNPQTNEGMLSVVKPLDYEISAFHTLLIKVENEDPLVPDVSYGPSSTATVHITVLDVNEGPVFYPDPMMVTKQENISVGSVLLTVNATDPDSLQHQTIRYSVYKDPAGWLSINPINGTVDTTAVLDRESPFVHNSVYTALFLAIDSGNPPATGTGTLLITLEDINDNAPVIYPTVAEVCDDARNLSVVILGASDKDLHPNTDPFKFEIHKQTVPDKVWKISKINNTHALVSLLQNLNKANYNLPIMVTDSGKPPMTNITDLRVQVCSCKNSKVDCNGAGALHLSLSLLLLFSLLSLLSGL
Protein: ER membrane protein complex subunit 6 (Transmembrane protein 93) (Q9VBZ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Membrane magnesium transporter
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 7
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 8/9 homolog
- Dynactin subunit 4
Sequence:
MNRVKTTQSKTGEIIAYSEGAIRNNISAVEYCRTSMAAISGCAAGILGLSGTLGFLFYFLSVFVLWILVLVKSGTQWRKFFINRRNLLTNQFMGGLCTYVLFWTFLYGMVHVY
Protein: ADP,ATP carrier protein 3 (ADP/ATP translocase 3) (Adenine nucleotide translocator 3) (ANT 3) (P18238)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell. Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P18239}; Multi-pass membrane protein {ECO:0000269|PubMed:24474793}.
Interaction partners:
- ADP,ATP carrier protein 2
- Cytochrome c isoform 2
- Eukaryotic translation initiation factor 5A-2
- Uncharacterized mitochondrial carrier YFR045W
- Non-selective voltage-gated ion channel 1
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MSSDAKQQETNFAINFLMGGVSAAIAKTAASPIERVKILIQNQDEMIKQGTLDKKYSGIVDCFKRTAKQEGLISFWRGNTANVIRYFPTQALNFAFKDKIKLMFGFKKEEGYGKWFAGNLASGGAAGALSLLFVYSLDFARTRLAADAKSSKKGGARQFNGLTDVYKKTLKSDGIAGLYRGFMPSVVGIVVYRGLYFGMFDSLKPLVLTGSLDGSFLASFLLGWVVTTGASTCSYPLDTVRRRMMMTSGQAVKYNGAIDCLKKIVASEGVGSLFKGCGANILRSVAGAGVISMYDQLQMILFGKKFK
Protein: Vitelline membrane outer layer protein 1 homolog (Q7Z5L0)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MERGAGAKLLPLLLLLRATGFTCAQTDGRNGYTAVIEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIPGDDTALNGIRLHCARGNVLGNTHVVESQSGSWGEWSEPLWCRGGAYLVAFSLRVEAPTTLGDNTAANNVRFRCSDGEELQGPGLSWGDFGDWSDHCPKGACGLQTKIQGPRGLGDDTALNDARLFCCRS
Protein: Protein eyes shut (Protein spacemaker) (A0A1F4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for the formation of matrix-filled interrhabdomeral space: critical for the formation of epithelial lumina in the retina. Acts together with prominin (prom) and the cell adhesion molecule chaoptin (chp) to choreograph the partitioning of rhabdomeres into an open system.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:17011488, ECO:0000269|PubMed:17036004}. Note=Secreted by photoreceptor cells, through the stalk membrane into the interrhabdomeral space (IRS). Although secreted, lacks a canonical signal sequence and contains a predicted transmembrane domain. The discrepancy may be explained by protein cleavage after the transmembrane region.
Interaction partners:
- non-specific serine/threonine protein kinase
- Chaoptin
Sequence:
MSNVHQFDTQTMAESPQIRRDMGRLCATWPSKDSEDGAGTALRAATPLTANGATTTGLSVTLAPKDMQRNHLLKMPTATIEKPTITATIASSSSTSTSTTRKSVTATRSLKLNPNILLPTLRILARGLLLPALILAILVGSSQAGFACLSNPCVFGVCIDGLNSSYSCYCIDGYTGIQCQTNWDECWSSPCQNGGTCVDGVAYYNCTCPEGFSGSNCEENVDECMSNPCQNGGLCRDRTNGYICTCQPGYLGSHCELDVAVCETGTGARCQHGGECIEGPGLEFTCDCPAGWHGRICQEEINECASSPCQNGGVCVDKLAAYACACPMGYTGINCEEEILICADNPCQNNALCLMEEGVPTCYCVPDYHGEKCEFQYDECQLGPRCMNGGVCIDGVDTFSCSCPPLLTGMLCECLMVGEESLDCNYTAPATQSPPRRTTTTSTMAPPTVRPVTPPETTVSPSRASEEVEIIVVTTSAPAEVVTSVLSPSSSSSSSEEGVSVEIKTPTVAPPESGSHSISVEQTTAVPAQPEPESEQEPESKPHPESESASESETETEEEIIPGTTARPPTSRSSSSSEESPSIFTTLPPLPGKPQTSASSESSGEVVTSEEYTTVPHFEVSGSKSESGSEEVTTVRPTAAPSITISVDITSSGSSSSSSESVEVFTTPAPVFVQRVTTIETSISIDYVTPTPLPETTTPRVVPVPRPTFAPEPPLDVVETTASTHHLWTEVPTTAAPFFTEYPAEVLITTHRTSAGRFTTVQPPAGVTTTSPTEDSSVELPTPHTPQIVVTILDSNEVIPSLITTTGSPTTHHHHHHHPHHEAEGTTLQPLEEDEHHHHHHHDEFTTPQPVEITTGHPLQTEDLIGVQEPAVVTTESPFAPAETTVVPVVVPATIAPLGTAAPPATPAPVPPATTTPPPSPPSLATETPTLPPTLPPVTLPPVTQPPPTIPPTPPSTQSAQTLPPPTSAINVYTTPDGPPTASQTKPSVTESSEEVEGTNTVSTGGRGSGGVPEEKAGDVDCIKLGCYNGGTCVTTSEGSRCVCRFDRQGPLCELPIIIRNAAFSGDSYVSHRIYKDIGGHESLDAVLPMHIQLKVRTRATNGLIMLAAAQGTKGGHYMALFLQKGLMQFQFSCGLQTMLLSELETPVNTGHEITIRAELDFSRNYTHCNASLLVNDTLAMSGDQPTWLKLLPPRLHTPEAILNTWLHLGGAPQAPIGLIIELPPAQSGSGFTGCLHTLRINGQAREIFGDALDGFGITECGSLACLSSPCRNGAACIKIETNDLDENGEKAEKWKCKCPTGYMGPTCEISVCEDNPCQYGGTCVQFPGSGYLCLCPLGKHGHYCEHNLEVALPSFSGSVNGLSSFVAYTVPIPLEYSLELSFKILPQTMSQISLLAFFGQSGYHDEKSDHLAVSFIQGYIMLTWNLGAGPRRIFTQKPIDFRLDAPRVPYEIKVGRIGRQAWLSVDGKFNITGRSPGSGSRMDVLPILYLGGHEIANFNTLPHDLPLHSGFQGCIYDVQLKAGQVTVPLQETRGVRGRGVGQCGTRECHRHACQHDGACLQHGATFTCICQEGWYGPLCAQPTNPCDSFNNKCYEDATCVPLVNGYECDCPVGRTGKNCEEVIRSLSDVSLTGRRSYLAVRWPYLYDGGDKLGAKRSQMVSYRNFTKKLMPPKPITTPSSHFVMKLLNEVEKQRSFSPVPLMGSKSFEEHHRVQFFFIEFQLRPLSERGLLLYFGTLNNNQDKKIGFVSLSLQGGVVEFRISGPSNHVTVVRSVRMLAIGEWHKIKMAQRGRWLTLWVEGSASSALAPSAEVLVEPDSLLYIGGLKDVSKLPHNAISGFPIPFRGCVRGLVVSGTRIVLNETNIVESRNIRDCDGTACGGDSCESGGHCWLDEKLQPHCICPEYAKGDRCEYSETCKLIPCKNNGRCLRSGRCSCPNGWGGFYCEIAMSKPTTPSFRGNSYLILPPPRIPMKDKRRGPSLYVRPREAIQVSLNFSTIEPDGLLLWSEHERSKFLGLGLEAGHLKLASNLLGSTNDTVRAPASGFIADGAWHWTSVLLDRSRLELQLDGEVIFTERLPEGGRSLGSTTPRSTLAGRRKNSSKEPTISYEDVFYLGGFPNSDSVSRRTKGRFFDPFKGCLQDIQFGAEPTAIISDFSTYQGENIGSCDLHGDEPLTV
Protein: Membrane-spanning 4-domains subfamily A member 14 (Testis development protein NYD-SP21) (Q96JA4)
Organism: Homo sapiens (Human)
Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MESTSQDRRATHVITIKPNETVLTAFPYRPHSSLLDFLKGEPRVLGATQILLALIIVGFGTIFALNYIGFSQRLPLVVLTGYPFWGALIFILTGYLTVTDKKSKLLGQGVTGMNVISSLVAITGITFTILSYRHQDKYCQMPSFEEICVFSRTLFIVLFFLPSDVTQNSEQPAPEENDQLQFVLQEEFSSDDSTTNAQSVIFGGYAFFKLTLSRSPLVSQPGNKGREFVPDEQKQSILPSPKFSEEEIEPLPPTLEKKPSENMSIQLDSTFKQMKDEDLQSAIVQPSQMQTKLLQDQAASLQVFPSHSALKLEDISPEDLPSQALPVEGLSEQTMPSKSTSSHVKQSSNLTANDLPPQGILSQDTSSQDMLFHDMTSQDMQSLDMLSQDTPSHAMPPQDIPSQDMLSQALSAHAILPEASTSHIVQFPEIQHLLQQPPDLQPENTEPQNQQILQMSYQDIRSEVMEETKEWKSEEELHRRKSSRRHSLNQQTKALQYLRRHSLDVQAKGQKSSKRHSLDQQSKGWQSPKQKSLDQQIKDWLSPKRHSVDKQAQLNQTKEQLPDQQAEDQQAKGEQYPEGQSKDGQVKDQQTDKEQNSKKQTQDQQTEDQPAQEKKSPKGQFQNVQAEGQQAQVEKVPKLLCQDSESQIQQYQFWQFHKGNLQAGQPRTVNLLAKNPLTG
Protein: Protein C10 (U3KQ85)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDEARDNACNDMGKMLQFVLPVATQIQQEVIKAYGFSCDGEGVLKFARLVKSYEAQDPEIASLSGKLKALFLPPMTLPPHGPAAGGSVAAS
Protein: Nitrogen permease regulator 2 homolog (O42857)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediates inactivation of the TORC1 complex in response to amino acid starvation. Post-transcriptional regulator of nitrogen permeases (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nitrogen permease regulator 3-like protein
- Uncharacterized WD repeat-containing protein C12G12.01c
- Vacuolar membrane-associated protein iml1
- Uncharacterized RWD, RING finger and WD repeat-containing protein C11E3.05
- Nucleoporin seh1
- Uncharacterized WD repeat-containing protein C4F8.11
- GTP-binding protein gtr1
- Protein transport protein sec13
- GTP-binding protein gtr2
- Mitochondrial inner membrane protease subunit 1
Sequence:
MEYSEEGWMDQADSFPPRLLAIFFALFDPLQGPIVACEAPAGSVTNVDGGKNCLLPFETISDYVIPKRELCNKTITVCTNHYQVIGHPISIIGSNYERNALIFNMCMIFHEEEDSACYIPLVKRLARNLEVLEKQIHYISDLNKRPVIFSVIEQILEDMNNFCECMIQLDDQNSINIKLFPVFPSPPTVKSFHVPILTAQLDLLMDKNWDMTVQKVYPFINGINSVQRIAELANVSYRSCQKCMEHFLYYGCLIIADIFQFHNIYAMTTNAPNLLQDPDFQRECTAYVSTNSSNAKNVTFATIFKLYCSLRQGLRVKDWMNENKEIFKGLDVRRLISFGTIKGLIYRVHKYPYLERRTMRNNLTEEEKKLLGLLDGKHHFDELCVTLKKSPKVVNEMIAGLGDACFIYV
Protein: Histone H2A type 3 (H2A-clustered histone 25) (Q7L7L0)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2B type 2-E
- Histone H2B type 3-B
- Histone H4
- Histone H1.1
- Histone H2B type 1-A
- Ubiquitin-ribosomal protein eS31 fusion protein
- Histone H3.1
- Histone H2B type 1-J
- Histone H2B type 1-K
- Histone H2B type 1-D
Sequence:
MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
Protein: Tyrosine-protein phosphatase non-receptor type (EC 3.1.3.48) (A8K3M3)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYGIESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLTAGAYLCYRFLFNSNT
Protein: Uncharacterized protein (Q585M8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- C3H1-type domain-containing protein
- Cleavage and polyadenylation specificity factor-like protein, putative
- Cleavage and polyadenylation specificity factor subunit, putative
- Nucleic acid binding protein, putative
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Uncharacterized protein
- Methyltransferase, putative
- Suppressor of forked domain-containing protein
- RNA-binding protein, putative
Sequence:
MEFETERSTTRTQQQPRQKFRGQEYDDYVPRRKTHGQRSVDFYSSAIQYVTTRLQHRNTPYGYHVDPHPYCSKDMLPAFRTPFNPSTALCTQWVSTSYHPDSRGGLSRQGLLNLKWAPNGRRLLCSTGRGEFLLFNGHSFGVEVKTVAHEDHRPCRAITWGNNSDLIISGDDAGMVKLWLSNFVLVAEFNSHHRAVRELTWAPLEGKFCSCGQDGSARVWDTNAVGTNPQQAREEMKLEGHGGDVVSVDWHPYHSLILTGSQDRDCRLWDPRTASRGSIAALQGHAQSVNCVRWNPSGTMLLSASKDCTLKLWDIRMVQEVASYEAHSKSVERVEWHPHVPDLFVSAGADGSIMYWMVDGCEGTARQDGVLVVIHNAALVESAHDRFRDVANPINAIAWSPLGNLLASCSSEVKYWHRNIPGAMEEKERGEEDDVFEMNRQQ
Protein: BTB/POZ domain-containing protein KCTD5 (Q9NXV2)
Organism: Homo sapiens (Human)
Function: Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex. Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17239418}. Cytoplasm {ECO:0000269|PubMed:18573101}. Nucleus. Note=Predominantly cytoplasmic, translocated to the nucleus upon interaction with Rep proteins. {ECO:0000269|PubMed:18573101}.
Interaction partners:
- Cullin-3
- BTB/POZ domain-containing protein KCTD17
- A-type voltage-gated potassium channel KCND2
- BTB/POZ domain-containing protein KCTD2
- BTB/POZ domain-containing protein KCTD11
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- E3 ubiquitin-protein ligase RBX1
Sequence:
MAENHCELLSPARGGIGAGLGGGLCRRCSAGLGALAQRPGSVSKWVRLNVGGTYFLTTRQTLCRDPKSFLYRLCQADPDLDSDKDETGAYLIDRDPTYFGPVLNYLRHGKLVINKDLAEEGVLEEAEFYNITSLIKLVKDKIRERDSKTSQVPVKHVYRVLQCQEEELTQMVSTMSDGWKFEQLVSIGSSYNYGNEDQAEFLCVVSKELHNTPYGTASEPSEKAKILQERGSRM
Protein: DAZ interacting zinc finger protein 1 L homeolog (Dzip1-prov protein) (Q6DCV2)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
Interaction partners:
Sequence:
MPFYENVYYPFDSDNASSTPSILSSPCLLPSATRKRPSSAGAMFKFRTRHESMDWRRIGAIDVDRVANELDFITLQENVMSITFCNLEDEKCPHCKNSLDPILLKLFRLSQFTIEYLLHSQEYLTSSLRSMEEEVQAATKEAEQIKLKMVKQSEEIKSLKEECKRRKKMIASQQMMISASAGSYHKCNFCDKAFVNYSYLQSHMHRRHPQSADSEKSKHTSEVLQNEISKLKNELQNTKCQLEAEKCAQIEKLSKIQEMECQKAFEQELINKFKSWKEEEKEKHAEEIAKVKGMFSKELKELTMKNASLEQIHEMEQHKTFEQDMLKKFNSWKNEEKGKHAEEMVKVKDMFQKDIKELTMKIAVLEKFHETGRRKTYEQEMQKMFHSWKEEEKEKHAEEIAKLKNMFQKEVKELTVKNASLEKVKEQSVKLPAPVTPYSEIVQAPAPLSSHHSEIKPIASSLSDVEADVSSSQKPHGWKKNQLLAKELRAVFEEGLAEKLESLGVKPGARGIPSDHCKKILESSKHVREERDKQMPLYRQMRQNLTSSLNCKAEERTSPAAGSRSSTLHSKSEVSVLKSSQRSHLSDQRSSASMKPTKAKVKAVLSKDTFAKKPPSIKTPPFSSDDESCADAGPLPSCNTTDSLKLRLPLKTKGNVGFVESESDSEGSFLEELQPQWVSKHNVQKQTPATTAPATLVKERCEQIEKQPMLPSVKNKPVGGVNVGYGFASSKDEVMELKVADIDENEFDNSTTDEESFEVPRSVKSRPLAKKVKNGYAAAPVRNTFVSRTAKEDVVDTSSTLVSSLVTVSDFSDSSDT
Protein: Scx protein (B5DFF0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSFAMLRSAPPPGRYLYPEVSPLSEDEDRGSESSGSDEKPCRVHAARCGLQGARRRAGGRRAAGSGPGPGGRPGREPRQRHTANARERDRTNSVNTAFTALRTLIPTEPADRKLSKIETLRLASSYISHLGNVLLVGEACGDGQPCHSGPAFFHSGRAGSPLPPPPPPPPLPLARDGGENTQPKQICTFCLSNQRKLVSRAGSTEGPKCTHQPTPARQREVQGRGSIP
Protein: Large ribosomal subunit protein mL41 (39S ribosomal protein L41, mitochondrial) (L41mt) (MRP-L41) (Q7JZM8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q8IXM3}.
Interaction partners:
- Small ribosomal subunit protein uS12m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein uL13m
- Ribosomal protein
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL30m
- Small ribosomal subunit protein mS29
Sequence:
MNNCIKVVPIALRCQQRTISTSSVLEGKRNFRKFNAYNKRGTRVVKEAQKTLANPPVAIHKRGVRDTGILVDGQYVEIPEKIPDIIVPDLTGCKLKPYVSYKAPDVVQSEFTSLDLFNAVYSQKIIEDFKAGKLQKDGSAKEPSVNEQLTPEEALQRARKTGSDIF
Protein: Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (Differentially expressed in chondrocytes protein 1) (DEC1) (Enhancer-of-split and hairy-related protein 2) (SHARP-2) (Stimulated by retinoic acid gene 13 protein) (O14503)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1|BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity. May be involved in the regulation of chondrocyte differentiation via the cAMP pathway. Represses the transcription of NR0B2 and attentuates the transactivation of NR0B2 by the CLOCK-BMAL1 complex. Drives the circadian rhythm of blood pressure through transcriptional repression of ATP1B1 in the cardiovascular system.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21829689}. Nucleus {ECO:0000269|PubMed:11278694, ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:28797635}. Note=Predominantly localized in the nucleus (PubMed:11278694). {ECO:0000269|PubMed:11278694}.
Interaction partners:
- Basic helix-loop-helix ARNT-like protein 1
- Neuronal PAS domain-containing protein 2
- Class E basic helix-loop-helix protein 41
- Cryptochrome-1
- Period circadian protein homolog 2
- Circadian locomoter output cycles protein kaput
- Nuclear factor interleukin-3-regulated protein
- Period circadian protein homolog 3
- Nuclear receptor subfamily 1 group D member 1
- Nuclear receptor subfamily 1 group D member 2
Sequence:
MERIPSAQPPPACLPKAPGLEHGDLPGMYPAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGELSGRNVETGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGTSRKPSDPAPKVMDFKEKPSSPAKGSEGPGKNCVPVIQRTFAHSSGEQSGSDTDTDSGYGGESEKGDLRSEQPCFKSDHGRRFTMGERIGAIKQESEEPPTKKNRMQLSDDEGHFTSSDLISSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNASAAALSSFMNPDKISAPLLMPQRLPSPLPAHPSVDSSVLLQALKPIPPLNLETKD
Protein: Flavohemoprotein (EC 1.14.12.17) (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (Q59MV9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Nitric oxide dioxygenase involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Plays a role in virulence since nitric oxide is generated by macrophages of the host immune system.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MTVEYETKQLTPAQIKIILDTVPILEEAGETLTQKFYQRMIGNYDEVKPFFNTTDQKLLRQPKILAFALLNYAKNIEDLTPLTDFVKQIVVKHIGLQVLPEHYPIVGTCLIQTMVELLPPEIANKDFLEAWTIAYGNLAKLLIDLEAAEYAKQPWRWFKDFKVTRIVQECKDVKSVYFTPVDKDLLPLPKPERGQYLCFRWKLPGEEFEISREYSVSEFPKENEYRISVRHVPGGKISGYIHNNLKVGDILKVAPPAGNFVYDPATDKELIFVAGGIGITPLLSMIERALEEGKNVKLLYSNRSAETRAFGNLFKEYKSKFGDKFQAIEYFSEDNNTDDKIVIDKAFNRKLTTDDLDFIAPEHDVYLVGPREFMKDIKEHLGKKNVPVKLEYFGPYDP
Protein: Lipopolysaccharide-binding protein (LBP) (P18428)
Organism: Homo sapiens (Human)
Function: Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide.
Subcellular location: Secreted {ECO:0000269|PubMed:2402637, ECO:0000269|PubMed:24120359, ECO:0000269|PubMed:7517398}. Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}. Note=Membrane-associated in polymorphonuclear Leukocytes (PMN) granules. {ECO:0000250|UniProtKB:P17213}.
Interaction partners:
- Monocyte differentiation antigen CD14
- Lymphocyte antigen 96
- Toll-like receptor 4
- Apolipoprotein A-I
- Interleukin-6
- Bactericidal permeability-increasing protein
- C-reactive protein
- Haptoglobin
- Toll-like receptor 2
- Serum amyloid A-1 protein
Sequence:
MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLPDFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRKSFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNLFHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATAQMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLNFSITDDMIPPDSNIRLTTKSFRPFVPRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDPYMEIDAFVLLPSSSKEPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFNAELLEALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGANVQYMRV