wanglab/gogpt-training-data huggingface dataset:
Protein: TTAGGG repeat binding factor 1 (Q7T1R9)
Organism: Gallus gallus (Chicken)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}.
Interaction partners:
Sequence:
VGAGGAVAARLKMSEAGREREGGLVPFLPSALAEAVAADWVLEFSCCCLCRYFVEECEAEFRRWRDVAQAVSNGFSKVTMHQKKMVYLCQLLIRIAEGKRLECHFENDTTISPLESALSFWTLLEREESKLNTLHEEIRRLIQIQVVAVYMEKGYYKEAAEVLERLFTDSESHKPLRMKLAAIVKSKDPYVPLLQSFSYSLLLSKVKSYVKLFLKENRTNFLLQAATKQVESEGGEVRVLQNKTLNVKEERENNLEAKQRPPSKKGCRTSSAQRLKDLKNVEERGDDLPCSRRRQPWTYEEDKKLKSGVREFGVGNWTKILIHGDFNNRTSVMLKDRWRTLCKIK
Protein: Delta-like protein (Q1ECY3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU280815}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU280815}.
Interaction partners:
Sequence:
MAAWLTFLIAFFTTVLTQIFGSGVFELDLHEFKNFKGLLANGNSCTPDCRTFFRVCLKNYQVVVSPGDCIFGSALTPVLGTNSFRIMGGGSFSTPIRLPFNFGWPGSFSLIIEAWHSPYSDLPVDAYNPNMQISFFAIQRKLEVGAEWSQDVQSGKQTELRYSYRFICNENYYGDSCSKKCTPRDDRFGHYTCNPDGQLSCLPGWKGEYCEEPICLEGCSEANGNCSKPGECVCREGWQGKFCTECKTYPACKHGTCHLPGQCNCKEGWGGLFCDQDLNFCTHHKPCVNGATCMNTGQGSYTCICRPGYTGVNCELQVRECDSSPRKNGGLCTDHDKSYTCTCLPDFEGTHCEHSLLTCADSPCFHKGRCHEKDNGRSYACECPLGYTGLNCERRMDKCTSMLCANDGLCLILGGKRICSCRAGFTGQRCEININDCANNPCANGGTCYDRINEYVCSCPPGYKGRNCDRPSCLSTPCLNGGSCVGITGNPPACFCPSGFTGPLCEYYAVTAPVTRGETQDRFQWAAVSLAVGLVALVVLLCMVVIALRHIHRQASGERTRGEAMNNLSESQRDNLIPTSQLKNTNKQVSLEVDCTPDKSNYIHKNCHLDYNSSKEFKDIVSQEDKSSHKYEKCLEEKIPLSRMYREKPECRISTICSPRDSVYQSVFVIAEERSECVIATEV
Protein: Cytoskeleton-associated protein 4 (63-kDa cytoskeleton-linking membrane protein) (Climp-63) (p63) (Q07065)
Organism: Homo sapiens (Human)
Function: Mediates the anchoring of the endoplasmic reticulum to microtubules.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18296695, ECO:0000269|PubMed:19144824}; Single-pass type II membrane protein. Cell membrane {ECO:0000269|PubMed:18296695, ECO:0000269|PubMed:19144824}; Single-pass type II membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Note=Translocates to the perinuclear region upon APF-stimulation.
Interaction partners:
- Dickkopf-related protein 1
- Palmitoyltransferase ZDHHC2
Sequence:
MPSAKQRGSKGGHGAASPSEKGAHPSGGADDVAKKPPPAPQQPPPPPAPHPQQHPQQHPQNQAHGKGGHRGGGGGGGKSSSSSSASAAAAAAAASSSASCSRRLGRALNFLFYLALVAAAAFSGWCVHHVLEEVQQVRRSHQDFSRQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQLVLYGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLDNLKASVSQVEADLKMLRTAVDSLVAYSVKIETNENNLESAKGLLDDLRNDLDRLFVKVEKIHEKV
Protein: Pou domain motif 3, isoform C (B7YZU0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MAEGCEDSAGAAESTTSQSQYTTLDKMLGTVLPCEAAIGATPGGGSSSGNSSSNIGGNTTNSSNNGSNIVKREFCDGSLMPGAGASVNNNNANAANNNNNNSSSSNNNNNNNNTKMQAMICNKSSSTNNSSSSSSSSSSCSSSSSSSSSATSTLTSCTTAAVVPSNCSTNANKSPVSPYSQSLGMAIGIGAGAGSSPLREASPLPSSRSPLNAIASTIAAKSPCSGAAPASPPSASSNSSSHVLALNIKTESDFDKEISCHKIHSPSSSSHAHSLHHHHHHHHHPHHSSRSNNNDDEMEITDGHALLSPPPPSHSHSHSPFDSKDHVKELEFYKNLAAKAASLANQHSPPPMPLPLPLPMQIDGEEDENEGEGEGEGEAEEQSAEVMRLRREEQAQAKAFAAHLNGTMQDMINLQKLQNLATLQQQQQQQQQHPHPHHGHQHHHHHPATAAALASLQGLAASVFNSPLNLSVGGEPVATTGPSVAPTSPTHNGGKSKTAKGGSSGNGSGGSSANSGTSSAQQQQQPDNPSSSSSPHHPLSASSLANVLAAATASPPPSLQAPPASAQMPQLILASGQLVQGVQGAQLLIPTAQGIAVQTILTIPVSPQIPTTEQFLPNAFGAFASYQQQQQQQQQQRDLLPPSLAALQHATALPQLAQTPTNLLKPNLFSTGVQQLLTALHPELFAAAAATHQQQQQQQQQQVQQQREREREREREREREREREREQHLGIGHLPHSHLAADLRRSAERSPTAGSPTGGSPGLAAKGPQPPPPGAAFLLQQQLHIKPETQTHLHHHLQTQSTSAVSSTLPQISLRHPDELTAPQMDLKPLELSASTSPPAPPPRHHFGHSLRGSSTVSPKHSPQGRMGGSGGSTTTGMNLSQHHERHDRLERLERQERHERRSHTPTATATRASVSSSSSAGHHGGSLPSGRLSPPSSAPSNSAANSISDRGYTSPLFRTHSPQGHALSLGGSPRLERDYLGNGPSSGTATSTSSCGAPTAAGSSATANVLSSINRLNASNGELTITKSLGAPTATATRASSASPRDDSPGPGPSTSSVSHMQPLKLSPSSRSEPPHLSPNGNDNDNDLLMDSPNEPTINQATTNVVDGIDLDEIKEFAKAFKLRRLSLGLTQTQVGQALSVTEGPAYSQSAICSALAAQMYAAQLSTQQQNMFEKLDITPKSAQKIKPVLERWMKEAEESHWNRYKSGQNHLTDYIGVEPSKKRKRRTSFTPQALELLNAHFERNTHPSGTEITGLAHQLGYEREVIRIWFCNKRQALKNTVRMMSKGMV
Protein: Asnovolin J 5',6'-dehydrogenase nvfM (EC 1.3.99.-) (Novofumigatonin biosynthesis cluster protein M) (A0A2I1BSW0)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: Asnovolin J 5',6'-dehydrogenase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAITDTINVAIVGASGVTGGSIVNGLLALTGLTVKITALTRPESLNKPANIQLKERGVQVVAANLRGPLEKLVDLLSSIDVVISAIYWGSLDDEIPLANAAKAAGVKRFVQSAYNIPAAARGVTHLRDKKEVILSHIQQLRLPYTYIDVGWWYHVVLPRVASGRTEHALPFGMPDLPIALDGNIPSGLTHIRDIGRYIARIILDPRTVNKKVFVYNELYTQNQLCDLVERLTGEMPQRRYISEKCVQSWLQEALDELERNPSSDIALGVVSLREVFLASNVHGTNTPEYAKYLGYLDGKELYPDFTFLTYEDYVEEVLDGMHSQTVA
Protein: Inner membrane protein YecN (P64515)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Single-pass membrane protein.
Interaction partners:
- UPF0759 protein YecE
- Isochorismatase family protein YecD
- Carboxy-S-adenosyl-L-methionine synthase
Sequence:
MVSALYAVLSALLLMKFSFDVVRLRMQYRVAYGDGGFSELQSAIRIHGNAVEYIPIAIVLMLFMEMNGAETWMVHICGIVLLAGRLMHYYGFHHRLFRWRRSGMSATWCALLLMVLANLWYMPWELVFSLR
Protein: Selenocysteine lyase (EC 4.4.1.16) (Q68FT9)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JLI6}.
Interaction partners:
- Iron-sulfur cluster assembly enzyme ISCU
- Selenide, water dikinase 1
- Thioredoxin reductase 1, cytoplasmic
- Thioredoxin reductase 2, mitochondrial
- thioredoxin-disulfide reductase
- Frataxin, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Selenoprotein M
- O-phosphoseryl-tRNA
- Phosphoseryl-tRNA kinase
Sequence:
MDVARNGARGSVESPPNRKVYMDYNATTPLEPEVIQAVTEAMKEAWGNPSSSYVAGRKAKDIINTARASLAKMIGGKPQDIIFTSGGTESNNLVIHSTVRCFHEQQTLQGRTVDQISPEEGTRPHFITCTVEHDSIRLPLEHLVEDQVAEVTFVPVSKVNGQVEVEDILAAVRPTTCLVTIMLANNETGVIMPISEISRRIKALNQIRAASGLPRVLVHTDAAQALGKRRVDVEDLGVDFLTIVGHKFYGPRIGALYVRGVGKLTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAADLVSENCETYEAHMRDIRDYLEERLEAEFGKRIHLNSRFPGVERLPNTCNFSIQGSQLRGYMVLAQCQTLLASVGASCHSDHEDRPSPVLLSCGIPVDVARNAVRLSVGRSTTRAEVDLIVQDLKQAVNQLEGPV
Protein: ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Q382C3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Choline/ethanolamine kinase, putative
- ethanolamine kinase
- Ethanolaminephosphotransferase, putative
Sequence:
MKRSVSKVWLNEDTPNDPYPLYAPSPLPPKRPGTIRVWVDGCFDMLHFGHANALRQARSMGDELFVGCHTDEEIIRHKGPPSMRQEERYEALRACKWVDAVIEGYPYVTRVEDMKRFEVDFVVHGDDISVDLNGRNSYQAIIDAGMFKAVRRTECISTTDLVGRMLLCVPSELLSDADKKLLDSEVARKRGPHYLTTSRKIAQFSNKLAPPVGATVVYVDGAFDLFHAGHIRFLQKARALGDYLIVGIHDDQLVRESKGEHFPIMSLNERALGVLSCRYVDDVVFGAPRGVTQEMIKILDIKIVACGTSSETRNCKGAFDVYEVPKSLNLFKVVESGSDLSTDMIVERVVKNHVVLLERQFLKHMKDSEAELRKPDVYRNVREV
Protein: Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 2 (AthCYSTM2) (Protein CADMIUM TOLERANCE 1) (AtCDT1) (Cd tolerant 1) (Q3ECR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance to abiotic stress.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:29272523}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:29272523}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000250|UniProtKB:Q5VSB5}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000250|UniProtKB:Q5VSB5}.
Interaction partners:
- Cell division control protein 6 homolog
- CDT1-like protein a, chloroplastic
- DNA replication licensing factor MCM2
- DNA polymerase epsilon subunit B
- CDT1-like protein b
- Origin of replication complex subunit 2
- Origin of replication complex subunit 1B
- Cell division control protein 6 homolog B
- ARMADILLO BTB ARABIDOPSIS PROTEIN 1
- Origin of replication complex subunit 5
Sequence:
MTMSRNGKTNKAAYSQRFTRCSVAVAATRSASVVAAAFDFYICIIISTLLSLIVSLASQLLF
Protein: Profilin-2 (Profilin II) (Q9EPC6)
Organism: Rattus norvegicus (Rat)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Toll-like receptor 11
- Actin, cytoplasmic 1
- Vasodilator-stimulated phosphoprotein
- Protein diaphanous homolog 1
- Actin, cytoplasmic 2
- Diaphanous-related formin 2
- Toll-like receptor 12
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Transforming protein RhoA
- Cofilin 2
Sequence:
MAGWQSYVDNLMCDGCCQEAAIVGYCDAKYVWAATAGGVFQSITPAEIDVIIGKDREGFFTNGLTLGGKKCSVIRDSLYVDSDCTMDIRTKSQGGEPTYNVAVGRAGRVLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF
Protein: Monooxygenase 1 (AtMO1) (EC 1.14.13.-) (O81815)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Eukaryotic translation initiation factor 4E-1
- Cytochrome P450 71A26
- Eukaryotic translation initiation factor 4G
- Putative glucuronosyltransferase PGSIP7
- Eukaryotic translation initiation factor isoform 4E
- Probable flavin-containing monooxygenase 1
Sequence:
MEEIGIVIVGGGIAGLATSIALHRKGIKSVVLERAEKVRSEGAGIGTLSNGWRALDQLGVGDRLRLNSSLIHKARTMLIENGKKREFVSNIVDEARCIKRNDLVEALSDALPKGTIRFGSHIVSIEQDKTTLFPVVHLANGNSIKAKVLIGCDGANSIVSDYLQLNPKKAFACRAVRGFTKYPNGHGFPQEVLRIKQGNVLIGRLPLTDNQVFWFLVHMQDNNHNGKDQESIANLCRKWADDLSEDWKEMVKICNVESLTLTHLRYRAPSEIMLGKFRRGTVTVAGDAMHVMGPFLAQGGSAALEDAVVLARCLARKVGPDHGDLLKDCSMKNIEEAIDEYVDERRMRLLGLSVQTYLTGRSLQTSSKVLRLMFIALLLLLFGRDQIRHTRYDCGRL
Protein: Heme oxygenase 3, chloroplastic (EC 1.14.14.18) (Q9C9L4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19860740}.
Interaction partners:
- Ferrochelatase-2, chloroplastic
- Ferrochelatase-1, chloroplastic/mitochondrial
- Phytochromobilin:ferredoxin oxidoreductase, chloroplastic
- Frataxin, mitochondrial
- Heme oxygenase 4, chloroplastic
- Heme oxygenase 1, chloroplastic
- Protoheme IX farnesyltransferase, mitochondrial
- ELM2 domain-containing protein
- S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase, chloroplastic
Sequence:
MATTRLNPSCHFPASTRLSCESYLGLRTTGRISYARTLTAPRGYLAVKANGGQASVVTAAAITEKQQKKYPGESKGFVEEMRFVAMRLHTKDQAREGEKESRSPEEGPVAKWEPTVEGYLHFLVDSKLVYDTLEGIIDGSNFPTYAGFKNTGLERAESLRKDLEWFKEQGYEIPEPMAPGKTYSEYLKDLAENDPQAFICHFYNIYFAHSAGGQMIGTKVSKKILDNKELEFYKWDGQLSQLLQNVRQKLNKVAEWWTREEKSHCLEETEKSFKFSGEILRLILS
Protein: Transcription regulator (Q5ADP3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcriptional repressor TUP1
- Transcriptional regulator SKO1
- Serine/threonine protein kinase
- Large ribosomal subunit protein uL3
- Kinesin-like protein
- Rgt1p
- histone deacetylase
- NADH-ubiquinone oxidoreductase chain 4
- Very long-chain fatty acid transport protein
- Transcriptional regulator NRG1
Sequence:
MYATAHTIKQQQQQQQQHPPPPLNGGLHASGAPPNSHEAAAIAQQQQQQQQHHNGPGMIVAAAAASANQQAVQARAQQQQQQQQQRLPSSAALNETTVSTWLAIGSLAESLGDIERATASYNSALRHSPNNPDILVKIANTYRSKDQFLKAAELYEQALNFHVENGETWGLLGHCYLMLDNLQRAYAAYQRALFYLENPNVPKLWHGIGILYDRYGSLEYAEEAFVRVLDLDPNFDKANEIYFRLGIIYKHQGKLQPALECFQYILNNPPHPLTQPDVWFQIGSVYEQQKDWNGAKDAYEKVLQINPHHAKVLQQLGCLYSQAESNPSTPANGAAPPHKPFQQDLTIALKYLKQSLEVDQSDAHSWYYLGRVEMIRGDFTAAYEAFQQAVNRDARNPTFWCSIGVLYYQISQYRDALDAYTRAIRLNPYISEVWYDLGTLYETCNNQISDALDAYRQAERLDPNNPHIKARLEQLTKYQQEGNTHPPQPPPSSQQPRLPQGMVLESTQQQQQQQPPPPPQQQQQQLQHQSQSQPQPQQPPQTQSQPSLLQHQSSLPPQQIQPLHQQAAKPLVNQQQSPPPPHLMNLGQPGQQPQQLPPHLPPHTQQPSQIQEKPPTQEQPHYQPPPPPQHQQQSQSQPQPPHQPQHTQNQSPQLAQLPPHHSNPPAKPHGAPQQRTGLPDLLHNSANIISAPSQVPQPQQQYQQPHIAPVRQEQVNHVPSIYSAPRPTETTLPQINNPNESTTTQVPQLKKEEPKPEATVSAPVPEAIKVQDQVTIQESAPAAAAAVSAPASAPVGDIKTDTVSTTTPATSTTADAVPVSVSQVGEAPNVVQEKKVPDTEQIVSQVEKPVESQPEVTPAPTPAPALATAPTEPAPTDKDVVMAPSKSATPVPQSIVEQNTRVSEATKAPESNGKHDLEDKNDEEKILKRPTVETTTESVPVNQPVEKENEKVEVPPPSEQPSSEKREKEVNGSIKKPLENESKVDIPQFSSNITAQNEEAKSGEETKKDTTKTSPAKQGEVKEVIPSSTETVSKPDVEKDNKEKDKDEDEVMADEDDVKKDENPEPPMRKIEEDENYDDE
Protein: Dihydrosphingosine 1-phosphate phosphatase YSR3 (EC 3.1.3.-) (Long-chain base protein 2) (Sphingolipid resistance protein 3) (P23501)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Dihydrosphingosine 1-phosphate phosphatase required for efficient ceramide synthesis from exogenous sphingoid bases. Involved in endocytosis and calcium-mediated signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10477278, ECO:0000269|PubMed:10563329, ECO:0000269|PubMed:9353337}; Multi-pass membrane protein {ECO:0000269|PubMed:10477278, ECO:0000269|PubMed:10563329, ECO:0000269|PubMed:9353337}.
Interaction partners:
- Sphingoid long chain base kinase 5
- Sphingoid long chain base kinase 4
- Dihydrosphingosine 1-phosphate phosphatase LCB3
- Alkaline ceramidase YDC1
- Sphingosine-1-phosphate lyase
- Ceramide synthase LAG1
- Ceramide synthase LAC1
- Sphingolipid C4-hydroxylase SUR2
- 3-ketodihydrosphingosine reductase TSC10
- Alkaline ceramidase YPC1
Sequence:
MTIIQTVTELGVTEDTIKVQMAPSGGKHLLADPGNHPAEHFESQMSWLRFQTRQYLTRFTDNQSDFVHSLQKKHRTPFRDVYFKYTSLMGSHMFYVIVLPMPVWLGYRDLTRDMIYVLGYSIYLSGYLKDYWCLPRPKSPPVDRITLSEYTTKEYGAPSSHSANATAVSLLFFWRICLSDTLVWPTKLLLLSLVIFYYLTLVFGRVYCGMHGMLDLFSGAAVGAICFFIRIWVVHALRNFQIGEHLWFPLLSVAWGLFILFNHVRPIDECPCFEDSVAFIGVVSGLDCSDWLTERYGWNLVCSRYASCGSKVFLRPLVGVASVIVWKDVISKTAVYTLLIKLLRFHDDRSEKVHFHNETSEEEECLLYSGVSKVEIVGRFLIYAGIPTTVFLLCPVFFTWTNLR
Protein: Keratin, type I cytoskeletal 26 (Cytokeratin-26) (CK-26) (Keratin-25B) (K25B) (Keratin-26) (K26) (Type I inner root sheath-specific keratin-K25irs2) (Q7Z3Y9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSFRLSGGSRRICSRTGSGRLSGGGTGFVAGNVCVGSGARSSFSCTLEGISSGGSFCNSGGGLGSGACAGFLGNEHSLLSGNEKVTMQNLNDRLASYLDHVHALEEANADLEQKIKGWYEKCEPGSSREHDHDYSRYFSVIEDLKRQIISATICNASIVLQNDNARLTADDFRLKYENELALHHSVEADTSGLRRVLDELTLCTTDLEIQCETLSEELTYLKKSHEEEMEVLQYTAGGNVNVEMNATPGVDLTVLLNNMRAEYEDLAEQNRKDAEAWFNERSATLQQQISDHEGAATAARNELTELKRNLQTLEIELQSLMAVKHSYECSLAETEGNYCNQLQQIQDQIGVMEEQLQQIRTETEGQKLEYEQLLDVKIFLEKEIDIYCNLLDGEERKSKSTCYKSKGYRPVNSGNQAKDSTEETIVKTVVEELDQIGNLLSLRVHSVEEKSSKISNITVEQRVPSKAP
Protein: Probable sulfate transporter Rv1739c (P9WGF7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Expression in E.coli induces sulfate uptake during early- to mid-log phase growth. Uptake is maximal at pH 6.0, is sulfate-specific, requires E.coli CysA and the transmembrane segment but not the STAS domain of the protein.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phthioceranic/hydroxyphthioceranic acid synthase
- Mycocerosic acid synthase-like polyketide synthase
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Mycoketide-CoA synthase
- Probable polyketide synthase Pks17
- Cytochrome bc1 complex cytochrome b subunit
- Triple specificity protein phosphatase PtpB
Sequence:
MIPTMTSAGWAPGVVQFREYQRRWLRGDVLAGLTVAAYLIPQAMAYATVAGLPPAAGLWASIAPLAIYALLGSSRQLSIGPESATALMTAAVLAPMAAGDLRRYAVLAATLGLLVGLICLLAGTARLGFLASLRSRPVLVGYMAGIALVMISSQLGTITGTSVEGNEFFSEVHSFATSVTRVHWPTFVLAMSVLALLTMLTRWAPRAPGPIIAVLAATMLVAVMSLDAKGIAIVGRIPSGLPTPGVPPVSVEDLRALIIPAAGIAIVTFTDGVLTARAFAARRGQEVNANAELRAVGACNIAAGLTHGFPVSSSSSRTALADVVGGRTQLYSLIALGLVVIVMVFASGLLAMFPIAALGALVVYAALRLIDLSEFRRLARFRRSELMLALATTAAVLGLGVFYGVLAAVALSILELLRRVAHPHDSVLGFVPGIAGMHDIDDYPQAKRVPGLVVYRYDAPLCFANAEDFRRRALTVVDQDPGQVEWFVLNAESNVEVDLTALDALDQLRTELLRRGIVFAMARVKQDLRESLRAASLLDKIGEDHIFMTLPTAVQAFRRR
Protein: Myb-like HTH transcriptional regulator family protein (Q8GYE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIPSMEGGGKTNREEEEEEEEEEEEGEESKVSSNSTVEESDKKTKVRPYVRSKVPRLRWTPDLHLRFVRAVERLGGQERATPKLVRQMMNIKGLSIAHVKSHLQMYRSKKIDDQGQAIAGHKHLFETSTDRNIYKLSQLPMFRGYNHNHDSPFRYGSKISNASLWNSSSQGTERSLIDQIRPGLIRNASVSNNIRGSDYWTNNKSFQNIYSSSISNHFPKLRHDHHERTNSVTFNSIQGHSRTFQKFHNGVEENTNHSYCSKTNGKRDASRSIDLDLSLKLRQPEKTILEETETAATTTDQTLSLSLCPGSSSWKKSRLMKDEEDRTVKIGQESTLDLTL
Protein: Unpaired 2 (Q9VWX2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cytokine receptor
- FI03911p
- Outstretched
- Tyrosine-protein kinase hopscotch
- Signal transducer and transcription activator
- Suppressor of cytokine signaling at 36E, isoform D
- Death-associated inhibitor of apoptosis 2
- Insulin-like peptide 6
- Insulin-like peptide 3
- Insulin-like peptide 5
Sequence:
MPAFTLNASQQSQSSRSSRSAHSSWSCHSRQVLLVIMILSVVMPFTKARHLRDQVALDYAYDEDNSGRSSSSSSSSSSSGGDILPAFDVNPYRGLADSFGEGSYDSDMSLSESSYEEIAQAAIRAARREMRRQRTRHARSHNLRLFSGKSEIPEWENPCGGTYTPDESLSDSSASQGRVIKRKHLENLRNITMSEYQDITHRATLEYGNLQHWQREYKFLPNMTRPTSAVKLKTWYRHMQTFVGSFSYLGRAQYKFRKDQQKSLNEAVTKELHDLLVSARYMLCEIELTINASYPNSNGAKLSRVSRQAMEERLNFHTPANGSMEADQRDLKVSKELYFQYLNNVWKTLHRVLRRPRRNSAERRHLAAIHGTGASGLRAGSSEMLDVGSSNGSGGSSGSDGGSNES
Protein: RNA polymerase II subunit A C-terminal domain phosphatase ssu72 (CTD phosphatase ssu72) (EC 3.1.3.16) (Suppressor of SUA7 protein 2 homolog) (O42868)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (rpb1).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Polyadenylation factor subunit 2
- Protein cft1
- mRNA cleavage and polyadenylation specificity factor complex subunit pta1
- Serine/threonine-protein phosphatase PP1-1
- Cleavage factor two protein 2
- Endoribonuclease ysh1
- mRNA 3'-end-processing protein yth1
- Uncharacterized WD repeat-containing protein C824.04
- Uncharacterized protein C4G9.04c
- Pre-mRNA polyadenylation factor fip1
Sequence:
MAPKTNLQISVICASNQNRSMEAHNVLKNAGYQVDSFGTGSAVRLPGPSIDKPNIYQFGYPYDEIYKELEAQDSRLYTANGLLKMLDRNRRIKRAPCRWQDQDSIYNIVITCEERCYDAICEDLYRRGETLNRPVYLINVDIKDNHEEASVGGKAILDLVNKLTEAQDKLEELFPSIMADFQSNHPKLPVLYTIHFF
Protein: glycerol kinase (EC 2.7.1.30) (Q9W095)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- glycerol kinase
- BcDNA.GH07066
- Glycerol-3-phosphate acyltransferase 4, isoform D
- Phospholipid/glycerol acyltransferase domain-containing protein
- LD24679p
- glycerol kinase
- AT10158p
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase
- BcDNA.GH10614
Sequence:
MTEGKNLPHSSADVPFRSKELRKQSLIQHTGLVGVIDEGTKTIGFSIYTTPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPEQGFSASDIVTVGITNQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRERRCKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRGMTLSGIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGPQAPTIYAIEGAVSVAGHALSWLQNKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMHQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVNLCQFEPEKRYYENVHYDTFLATTTDVERKERYGKWKRAVERSLGWVIKQKKTREYTEENYRMLSSLPASIFLISSFAMLVHSLAASGQ
Protein: Bilin biosynthesis protein PecE (P29729)
Organism: Mastigocladus laminosus (Fischerella sp.)
Function: An enzyme involved in the biosynthesis of bilin.
Interaction partners:
Sequence:
MTAACCAQPILSPEAAIAALAGEDNQIRYYAAWWLGKHQVQAGCAALCEALFDERYRIPSGGYPLRRQAARALGQLKNPQAVPALIAALACEEDLGLREAVIQALAMIGDRRAVHPLVQLLQSQQPQPYEALIEALATLQVWSARPQIEPFLYHSSERVQCAAARYLYLLTKQPQYLERIVQNLNHDNMYLRWAAIFDLAALGHRQAVDAILAAKVPNSLKLLNLKRILETLLDGDRSQLNNGEFCQNQSDRETIELLFQAIDDLLIQL
Protein: Metallo-beta-lactamase subclass B3 (Subclass B3 metallo-beta-lactamase BJP-1) (Subclass B3 metallo-beta-lactamase POM-1) (E6Y3G9)
Organism: Metapseudomonas otitidis
Interaction partners:
Sequence:
MRTLTTLGLALLLAQPAVAAQAVLPQLQPYTAPAAWLTPVAPLRIADNTWHIGTASITALLVKTPEGAVLLDGGMPQVADHLLANMRELGVAPGDLKLILHSHAHIDHVGPLAAIKKATGAQLVSNAESAVLLQRGDSQDIHFGDDMVFAPVQVDRLVQDGETVELGGMTFTAHFTPGHTPGSLSWTWTDRRDGKPLRIAYSDSLSAPGYSLWMNPRFPKIAEAFRSGFAAVRALPCDLLITPHAEASGWDYTNAEHPNPSPMSCKAYADKAEAAFDAQLKKQRGG
Protein: GH13213p (Radial spoke head protein 3, isoform B) (Q9VRY7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
- Dystrobrevin, isoform F
- cAMP-dependent protein kinase type I regulatory subunit
- Pre-mRNA-splicing regulator female-lethal
- Kelch-like protein diablo
- Uncharacterized protein, isoform B
- Stretchin-Mlck, isoform U
- Protein bowel
- LD15807p)
- Inhibitor of growth protein
- Combover, isoform A
Sequence:
MPETEQQQHPAHSHPELKPDPQPVPELEHLTDNRPNRVQNFSFASSYPYAPGRVSSSSNSNTNYSSTNYNAGGFNVQRYQSPYNFQHVVTNAFSVLRHQPSEEPEFDSYPTRPQQAIVRPIRREAGIADNRDNHVGNPPQRSHFSRSNQEVRSFADELSQKLRFLAPEEQNYGGRQSANSGAWMDPAMSQRPRFETTVPQGIFLPPPHEVQMIPATMLRRHVYAYSSYPMILQGYLTKETGSESKEQKVTATRLNGLRATAAVAAATAAASKSSRNDTQSLAGGLHITKAQFQQQLQQRRSTSNNNNNSSSNISDKRPVVPPPEPYKNVMYDRRVIKGSNFGNASLVTDVDPFDKAAELRRRNMLRKRTMQCRNQRNVLGTPPPVKGRKHETIQTEKYLEKLVQRPPEFTIDTQTDLFLEKPPTPPFIPAKVGVDVATEIGEGELFHFDAEAQPIIDVLVDACIEQSMLEVAHEMELSSLRRKQEEFLAQREAELAELRRLEAEELRLQAEKERRLRQDAIAKELDAEMQKSVTAAKLLQGHIASLVPEVLENIEPASDAVKKEQLMKSVCPWLSAEVAEEVGHIVDSREILTAIIQEIIKQRAEIYAGYKEPESEPSGPDAGVCEEEGCAIDEMEACPCESETEMEECPEPPPPAPHL