wanglab/gogpt-training-data huggingface dataset:
Protein: Calcyon neuron specific vesicular protein (Neuron-specific vesicular protein calcyon) (F6VEL3)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- D
Sequence:
MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDVSQLQPPLPDQVVIKTQTEYQLSSLDQQKKFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPTQAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPVQ
Protein: Quinohemoprotein alcohol dehydrogenase ADH IIB (ADH IIB) (EC 1.1.9.1) (Alcohol dehydrogenase (azurin)) (Q8GR64)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Catalyzes the dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Exhibits activity with longer mono-alcohols (C-4 to C-7) but not with methanol or glycerol. Reacts with 1,2-propanediol and 1,3-propanediol but not with sugar alcohols such as D-sorbitol.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MKKPLRTSLLMLCLATPLAALAAGVDEAAIRATEQAGGEWLSHGRTYAEQRFSPLKQIDASNVRSLGLAWYMDLDNTRGLEATPLFHDGVIYTSMSWSRVIAVDAASGKELWRYDPEVAKVKARTSCCDAVNRGVALWGDKVYVGTLDGRLIALDAKTGKAIWSQQTTDPAKPYSITGAPRVVKGKVIIGNGGAEYGVRGFVSAYDADTGKLAWRFYTVPGDPALPYEHPELREAAKTWQGDQYWKLGGGGTVWDSMAYDPELDLLYVGTGNGSPWNREVRSPGGGDNLYLSSILAIRPDTGKLAWHYQVTPGDSWDFTATQQITLAELNIDGKPRKVLMQAPKNGFFYVLDRTNGKLISAEKFGKVTWAEKVDLATGRPVEAPGVRYEKEPIVMWPSPFGAHNWHSMSFNPGTGLVYIPYQEVPGVYRNEGKDFVTRKAFNTAAGFADATDVPAAVVSGALLAWDPVKQKAAWKVPYPTHWNGGTLSTAGNLVFQGTAAGQMHAYSADKGEALWQFEAQSGIVAAPMTFELAGRQYVAIMAGWGGVATLTGGESMNLPGMKNRSRLLVFALDGKAQLPPPAPAPAKVERVPQPVTAAPEQVQAGKQLYGQFCSVCHGMGTISGGLIPDLRQSSDATREHFQQIVLQGALKPLGMPSFDDSLKPEEVEQIKLYVMSREYEDYMARHKAAP
Protein: Protein phosphatase 1A (EC 3.1.3.16) (Protein phosphatase 2C isoform alpha) (PP2C-alpha) (Protein phosphatase IA) (P20650)
Organism: Rattus norvegicus (Rat)
Function: Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling (By similarity). Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P35813}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35813}. Membrane {ECO:0000250|UniProtKB:P35813}; Lipid-anchor {ECO:0000250|UniProtKB:P35813}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000250|UniProtKB:P49443}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 4
- mitogen-activated protein kinase kinase
- Dual specificity mitogen-activated protein kinase kinase 7
- mitogen-activated protein kinase kinase
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- E3 ubiquitin-protein ligase KCMF1
Sequence:
MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLETWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSAEAVKKEAELDKYLENRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSASTDDMW
Protein: Uncharacterized transporter mfs2 (Q10084)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDLLSLITGKKFEKHYSKVGSRFSDESLNGLEKQLSNGADAAIDTTADDRGSVVSLGASLPLSQGRPAKSKNILNDTLLAEDQYLVTWDGPDDPLNPRNWSHSYKWWIVIQVSVITIVVTFASSVYSSGIIDIASELHSSIPVSTLGSCTFLVGFGVGSLPFAPLSDIYGRFIIYFVTLLIFTIFQVGGGCAHNVWTLAIVRFFQGVFGSTPLANAGGTISDLFTPVQRTYVLPGFCTFPYLGPIIGPIIGDFITQSYLEWRWTFWINMIWAAAVIVFVFIFFPETHEDTILDYKAKYLRKTTGNTAYYTIHERERDPKNAMIQAATQAVSLIFTEPIVVCFTLYLTVVYIINYINFEGYPIVFAKYGFNKGEQGLSFIGVGVGIVCAGLCTPFIYWHYLKVNKKRNGVICPEDRLYPLFIGCFLLPISMFWFAWTCYPHHIHWIVPIIASAFFGFSLLIVFFVSYNYIIDSYQHMAPSALAAATLVRYSASGGISMVARPMYLNLGDHWATSVLGFISVAMVPIPFIFYRFGKSIRAWSKNAYKL
Protein: Amidase 1 (OsAMI1) (EC 3.5.1.4) (Q7XTK3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Amidase involved in auxin biosynthesis (Probable). Converts indole-3-acetamide (IAM) to indole-3-acetate, and phenyl-2-acetamide (PAM) to phenyl-2-acetate. Substrate preference is PAM > IAM.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27135507}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27135507}.
Interaction partners:
- Glutamyl-tRNA
- Indole-3-pyruvate monooxygenase YUCCA1
- Probable aldehyde oxidase 3
- Os01g0153400 protein
- Flavin-containing monooxygenase
- Probable aldehyde oxidase 1
- Probable aldehyde oxidase 2
- indole-3-pyruvate monooxygenase
- Indole-3-pyruvate monooxygenase YUCCA4
- aldehyde dehydrogenase
Sequence:
MAMAGGGRGDYGAFMERFVLPPPPSQQLPLHGLTFAIKDIFDIAGRVTGFGNPDWARTHAPAAATSPVVLAALAAGATSLGTTIMDEMAYSINGENTHYGTPTNPCAPGRVPGGSSSGSAVAVAANLVDFSLGTDTGGSVRVPAAYCGIFGLRPSHGLVSAENVIPMAQMFDTVGWFSRDLSTLSRVTKVLLPLPDDIVKQPTQVTIPMDCFQILGSLDDRTYQIINASVAKRFDSQILDNRNLGDFISDNVPSIGKFITDFSESELPSVPALSVISHVMRGLQRSQFKANHAEWVNTVKPNLGPGLRERILEAIASGDNESLEDFQAIRAEFKSALAALLKDHGILAIPTVPGPPPKVGMEAAPLENFRARAFSLLSIAGLSGFCQVSIPLGMRNGLPVSVSLVARHGADHFLLNVVEELYQTLIDEATKTWSS
Protein: Intermembrane phospholipid transport system permease protein MlaE (P64606)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:19383799}; Multi-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:19383799}.
Interaction partners:
- Intermembrane phospholipid transport system binding protein MlaB
- Intermembrane phospholipid transport system ATP-binding protein MlaF
- Intermembrane phospholipid transport system binding protein MlaD
- Intermembrane phospholipid transport system binding protein MlaC
- Intermembrane phospholipid transport system lipoprotein MlaA
- Acid stress protein IbaG
- Lipopolysaccharide export system ATP-binding protein LptB
Sequence:
MLLNALASLGHKGIKTLRTFGRAGLMLFNALVGKPEFRKHAPLLVRQLYNVGVLSMLIIVVSGVFIGMVLGLQGYLVLTTYSAETSLGMLVALSLLRELGPVVAALLFAGRAGSALTAEIGLMRATEQLSSMEMMAVDPLRRVISPRFWAGVISLPLLTVIFVAVGIWGGSLVGVSWKGIDSGFFWSAMQNAVDWRMDLVNCLIKSVVFAITVTWISLFNGYDAIPTSAGISRATTRTVVHSSLAVLGLDFVLTALMFGN
Protein: Calponin-homology (CH) domain-containing protein (Q3TR59)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSLAATTFRWKKWRLDLPGQVPLQACRRSPDEHNDVQKKTFTKWINARFSKSGKPPISDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVDLVNIGGTDIVDGNPKLTLGLLWSIILHWQVKDVMKDIMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPIERLEHAFSKAHTYLGIEKLLDPEDVAVHLPDKKSIIMYLTSLFEVLPQQVTIDAIREVETLPRKYKKECEEEEIHIQSAVLAEEGQSPRAETPSTVTEVDMDLDSYQIALEEVLTWLLSAEDTFQEQDDISDDVEEVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGTLSEEEEFEIQEQMTLLNARWEALRVESMERQSRLHDALMELQKKQLQQLSSWLALTEERIQKMESLPLGDDLPSLQKLLQEHKSLQNDLEAEQVKVNSLTHMVVIVDENSGESATALLEDQLQKLGERWTAVCRWTEERWNRLQEISILWQELLEEQCLLEAWLTEKEEALNKVQTSNFKDQKELSVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQLLSNPKASKKMNSDSEELTQRWDSLVQRLEDSSNQVTQAVAKLGMSQIPQKDLLETVHVREQGMVKKPKQELPPPPPPKKRQIHVDVEAKKKFDAISTELLNWILKSKTAIQNT
Protein: Zinc finger protein unc-98 (Uncoordinated protein 98) (Q19203)
Organism: Caenorhabditis elegans
Function: Probable transcription factor required for muscle structure. Its dual subcellular localization suggests that it may function both as a muscle adhesion complex protein and as a transcription factor, or work together with transcription factors, to influence gene expression. Thought to act as a molecular bridge between unc-97 and myo-3 at the M-line of muscles, possibly in a signaling role. Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord.
Subcellular location: Nucleus {ECO:0000269|PubMed:12808046}. Cytoplasm {ECO:0000269|PubMed:12808046}. Note=Localized in body wall muscle M-lines, dense bodies and muscle nuclei.
Interaction partners:
- CRE-UNC-96 protein
- LIM domain-containing protein unc-95
- LIM domain-containing protein unc-97
- Muscle M-line assembly protein unc-89
- Paramyosin
- COP9 signalosome complex subunit 5
- Protein espinas
- Paralyzed arrest at two-fold protein 6
- PDZ and LIM domain protein Zasp
- PDZ domain-containing protein
Sequence:
MDDDIFKEARKERDDFEELMNACDLAKMSVKNNEMVHGLETFGINGESSENGNKEKPKEIMKVVAPTVEAYVGSSSAQTPTKSSGGALDGSDQQEVRQDGTSVQKDDNGFVFYKCRFCGLTFNFMNTLRAHERIHDVSQPYVCGKCGDSFEFACQLEYHAAQHSEIDGYKCECGRTFFSYTEMLYHKHTDDPLELIGAPETTTIKVSKKRVLPVSEQDLPQPAFVTEGYEPKHPLRVYNDVRSKPYICEYCSKSYSDSRGLAYHMYSHRGEKYFNPRASRYMMGREGVGYTDSRSYYLFPRTSGYVTPRF
Protein: Pannexin-2 (Q6IMP4)
Organism: Mus musculus (Mouse)
Function: Structural component of the gap junctions and the hemichannels.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20529862}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Golgi apparatus membrane {ECO:0000269|PubMed:20529862}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20529862}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Note=Localizes to Golgi apparatus and endoplasmic reticulum in multipotential neural stem and progenitor cells and to plasma membrane in terminally differentiated neurons. {ECO:0000269|PubMed:20529862}.
Interaction partners:
- Pannexin-1
Sequence:
MHHLLEQSADMATALLAGEKLRELILPGSQDDKAGALAALLLQLKLELPFDRVVTIGTVLVPILLVTLVFTKNFAEEPIYCYTPHNFTRDQALYARGYCWTELRDALPGVDASLWPSLFEHKFLPYALLAFAAIMYVPALGWEFLASTRLTSELNFLLQEIDNCYHRAAEGRAPKIEKQIQSKGPGITEREKREIIENAEKEKSPEQNLFEKYLERRGRSNFLAKLYLARHVLILLLSVVPISYLCTYYATQKQNEFTCALGASPDGPVGSAGPTVRVSCKLPSVQLQRIIAGVDIVLLCFMNLIILVNLIHLFIFRKSNFIFDKLNKVGIKTRRQWRRSQFCDINILAMFCNENRDHIKSLNRLDFITNESDLMYDNVVRQLLAALAQSNHDTTPTVRDSGIQTVDPSINPAEPDGSAEPPVVKRPRKKMKWIPTSNPLPQPFKEQLAIMRVENSKTEKPKPVRRKTATDTLIAPLLDAGARAAHHYKGSGGDSGPSSAPPAASEKKHTRHFSLDVHPYILGTKKAKTEAVPPALPASRSQEGGFLSQTEECGLGLAAAPTKDAPLPEKEIPYPTEPALPGLPSGGSFHVCSPPAAPAAASLSPGSLGKADPLTILSRNATHPLLHISTLYEAREEEEGGPCAPSDMGDLLSIPPPQQILIATFEEPRTVVSTVEF
Protein: Response regulatory protein (O30989)
Organism: Pseudomonas fluorescens
Interaction partners:
Sequence:
MTAKPTVFVVDDDMSVREGLRNLLRSAGFEVETFDCASTFLEHRRPEQHGCLVLDMRMPGMSGIELQEQLTAISDGIPIVFITAHGDIPMTVRAMKAGAIEFLPKPFEEQALLDAIEQGLQLNAERRQARETQDQLEQLFSSLTGREQQVLQLTIRGLMNKQIAGELGIAEVTVKVHRHNIMQKLNVRSLANLVHLVEKYESFERGVS
Protein: Optic atrophy 3 protein (OPA3) (Q384Y5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPAPVYRFALLAIRQMSKPMVSRTVKKAQHGASITRTVCLRLGHLSAAISSVMARWHVEEKHKPSPVNSSKQDSATGEGSTSTFGKSKEDRAVTVAPRVRSLLGSTPSSRGGRSRSGRIFFSSRPMRTVWQTFREGYSASLSEEHLVAAGAELLIELLVYFILAFVLYAEITSSAKASEAKERRLLQRIDALEQKVNELVEANKHMDLAALEVAVHVEEPRGLRWVCHKFNDVAKKALGT
Protein: Rho GTPase Rho1 (A0A068C8U8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
Sequence:
MAEIRRKLVIVGDGACGKTCLLIVFSKGTFPEVYVPTVFENYVADVEVDGKHVELALWDTAGQEDYDRLRPLSYPDSHVILICFAIDSPDSLDNVQEKWISEVLHFCQGLPIILVGCKKDLRHDPKTIEELHKTSQKPVTPEQGEEVRKKIGAYKYLECSARTNEGVREVFEAATRAALLTKTHKKKGKCTIL
Protein: S-adenosyl-L-methionine-dependent methyltransferase (C8V1Z0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MTQYSDDDIDSAYGDDSLIGDDTQTLSTYITDYRYEFGRRYHSYRDGAYWEILDVGTGTGIWAIDAADEYPSARVTGVDLSPIQPSFVPPNCIFEIDDITLPWTYSANQFDFIHIRELFGCIPDWDQFFGHCWHCLKPGGYIEVVEHSVQPIADDGSMGPDHFYHEWGRVVVESGERSGKTFKIWQESAERLKRAGFVDVVEQRFKWPMNGWSSDPKLHELGRWNQFRLNGGIEGFMLRLLTTTLGWSYERSQVHLAQMRTALRDYRTHAYLPGTVVYARKPGSGISSPPR
Protein: Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (O58035)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Edits incorrectly charged Ser-tRNA(Ala). Incorrectly charged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Gly and Ser) in the charging step.
Subcellular location: Cytoplasm.
Interaction partners:
- Leucine--tRNA ligase
- Valine--tRNA ligase
- Isoleucine--tRNA ligase
- Inorganic pyrophosphatase
Sequence:
MEFIMKTRMFEEEGWIRKKCKVCGKPFWTLDPDRETCGDPPCDEYQFIGKPGIPRKYTLDEMREKFLRFFEKHEIYPHGRVKRYPVLPRWRDDVLLVGASIMDFQPWVISGEADPPANPLVISQPSIRFTDIDNVGITGRHFTIFEMMAHHAFNYPGKPIYWMDETVELAFEFFTKELKMKPEDITFKENPWAGGGNAGPAFEVLYRGLEVATLVFMQYKKAPENAPQDQVVVIKGEKYIPMETKVVDTGYGLERLVWMSQGTPTAYDAVLGYVVEPLKKMAGIEKIDEKILMENSRLAGMFDIEDLGDLRYLREQVAKRVGITVEELEKAIRPYELIYAIADHTKALTFMLADGVVPSNVKAGYLARLLIRKSIRHLRELGLEVPLSEIVALHIKELHKTFPEFKEMEDIILEMIELEEKKYAETLRRGSDLVRREIAKLKKKGIKEIPVEKLVTFYESHGLTPEIVKEIAEKEGVKVNIPDNFYSMVAKEAERTKEEKGEELVDFELLKDLPDTRRLYYEDPFMKEFDAKVLRVIKDWVILDATAFYPEGGGQPYDTGVLIVNGREVKVTNVQKVGKVIIHKVEDPGAFKEGMIVHGKIDWKRRIQHMRHHTGTHVLMGALVRVLGRHVWQAGSQLTTDWARLDISHYKRISEEELKEIEMLANRIVMEDRKVTWEWLPRTTAEQKYGFRLYQGGVVPGREIRVVKIEDWDVQACGGTHLPSTGLVGPIKILRTERIQDGVERIIFACGEAAIREWQKERDLLKKASNVLRVPPEKLPETAERFFNEWKEARKEVDKLKKELARLLVYELESKMQKIGSIEFIGEVVEGSMEDLRELVEKLKKPKRVVVLISRDGYFAVSVGSEVGVEANELAKKITLIAGGGGGGRRDIAQGKVKDISKAKDVIESIKSMFS
Protein: MLO-like protein 1 (AtMlo1) (MLO protein homolog 1) (AtMlo-H1) (O49621)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- At5g51840
- Putative F-box protein At3g25750
- Alpha/beta-Hydrolases superfamily protein
- F-box protein At3g54460
- MACPF domain-containing protein At4g24290
- Protein DOWNY MILDEW RESISTANCE 6
Sequence:
MGHGGEGMSLEFTPTWVVAGVCTVIVAISLAVERLLHYFGTVLKKKKQKPLYEALQKVKEELMLLGFISLLLTVFQGLISKFCVKENVLMHMLPCSLDSRREAGASEHKNVTAKEHFQTFLPIVGTTRRLLAEHAAVQVGYCSEKGKVPLLSLEALHHLHIFIFVLAISHVTFCVLTVIFGSTRIHQWKKWEDSIADEKFDPETALRKRRVTHVHNHAFIKEHFLGIGKDSVILGWTQSFLKQFYDSVTKSDYVTLRLGFIMTHCKGNPKLNFHKYMMRALEDDFKQVVGISWYLWIFVVIFLLLNVNGWHTYFWIAFIPFALLLAVGTKLEHVIAQLAHEVAEKHVAIEGDLVVKPSDEHFWFSKPQIVLYLIHFILFQNAFEIAFFFWIWVTYGFDSCIMGQVRYIVPRLVIGVFIQVLCSYSTLPLYAIVSQMGSSFKKAIFEENVQVGLVGWAQKVKQKRDLKAAASNGDEGSSQAGPGPDSGSGSAPAAGPGAGFAGIQLSRVTRNNAGDTNNEITPDHNN
Protein: NAD-dependent L-serine dehydrogenase (EC 1.1.1.387) (L-serine 3-dehydrogenase (NAD(+))) (Q9I5I6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: NAD-dependent L-serine dehydrogenase that catalyzes the oxidation of L-serine and methyl-L-serine and is possibly involved in serine catabolism. Has low activity toward beta-hydroxyisobutyrate.
Interaction partners:
- methylmalonate-semialdehyde dehydrogenase
- 3-hydroxyisobutyryl-CoA hydrolase
- Probable FMN oxidoreductase
- Methylmalonate-semialdehyde dehydrogenase [acylating]
- Immunity protein Imm33 domain-containing protein
- Probable chemotaxis transducer
- UPF0229 protein PA0587
- Ferredoxin-type protein NapF
Sequence:
MKQIAFIGLGHMGAPMATNLLKAGYLLNVFDLVQSAVDGLVAAGASAARSARDAVQGADVVISMLPASQHVEGLYLDDDGLLAHIAPGTLVLECSTIAPTSARKIHAAARERGLAMLDAPVSGGTAGAAAGTLTFMVGGDAEALEKARPLFEAMGRNIFHAGPDGAGQVAKVCNNQLLAVLMIGTAEAMALGVANGLEAKVLAEIMRRSSGGNWALEVYNPWPGVMENAPASRDYSGGFMAQLMAKDLGLAQEAAQASASSTPMGSLALSLYRLLLKQGYAERDFSVVQKLFDPTQGQ
Protein: IQ motif containing GTPase activating protein 3 (F8VQ29)
Organism: Mus musculus (Mouse)
Interaction partners:
- Cell division control protein 42 homolog
- Ras GTPase-activating-like protein IQGAP1
- Ras GTPase-activating-like protein IQGAP2
- Ras-related C3 botulinum toxin substrate 3
- Ras-related C3 botulinum toxin substrate 2
- Calmodulin-1
- Proline-rich protein 11
- Kinesin-like protein KIF20A
- Kinesin-like protein KIF2C
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MEPCAAGRARTAYERLTAEEMDEQRRQNVAYQYLCRLEEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRYQATGLHFRHTDNINFWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELGNIASELAKYGLQLPAFSKIGGILANEFSADEAAVHAAILAINDAVERGVVEDTLVTLQNPNALLGNLREPLAAVYQELLALAKMEKAANARNHDDGQEQDIYESCLTQAEIQGHINLANVQGALEVVDDALERQNPGALLEALHDPVLALQGVRGTFADWYLEQLTSDREQKSQELGLVRLLEKEEIQAGVAVANEKGDEEQTMLQAVWRINKAIRRGVAADTVKELMCPEAQLPRVYPFASAFYQQELALLQKQQQGELGQEELFVAVEMLSAVVLINRALEAGDVCAFWDNLVNPATGLAQVEEENAQRYFDALVKVQQFQGTHRGILSWNDLQAAVSQVNEQVQEETDQVLAISLINEALDQGCPEKTLSALLLPAAGLEDVSLHVAPRYHLLLVAAKRQKARVTGDPGAVLWLEEIRQGVARANEDTSTAQRIALGVAAINQAIKEGKAAQTERVLRNPNVALRGIVPDCAKSYQQALEGAAAKKQCPGDTAFWVQHDMKDGTAYYLHLQTFQGTWEHPSGCHLNTSHLTWEEIQSVITKVTAAHDRQLLWKANVGFVIKLQARLRGFLVRQKFAESSHVFRTLLPAVIKIQAHWRGYRQRKAYQERLQHFKANLDAIIKIQAWARMWAARRRYLRRLRYFQKNVDSVVKIQAFFRARKARDDYRMLVHARHPPLCVVRKFAHLLNQSQEDFSAESELLKLQEEVVRKIRSNQQLEQDLNLMDIKIGLLVKNRITLQEVVSHCKKLTKKNKEQLSDMMILDKQKGLKSLSREKRQKLEAYQHLFYLLQTQPIYLAKLIFQMPQNKTTKFMEGVIFSLYNYASNRREAYLLLQLFRTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDRSVSIHTDPVHIYKSWINQEEAQTGQRSHLPYDVTPEQALSHSEVQRRLDISLRSLLTLTEKFFVAISSSVDHIPYGMRYMAKVLKTTLEKKFPNATERDIYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGSTLAAPQRHALGAVAQLLQHAAAGQIFSGESRHLRVLNDYLEDLHLKFRKFICRACRVPEPEERFAIDEYSDMVAVAKPMVYITVGELIGTHRLLLEHQDQLAPGHQDPLHQLLEDLGEPPTISDLIGDNIATDGHVDLSRLEVSLTLTNKFEGLETDADHNSNQSLLLSTKQMLADLIQFHPGESLEEILTSSAPREHEEAHRRLMCWRQACDTQKPEPLRRHHSLMAHSLLSLSEKQQRVLRNLRRLQGLGLVRASDCYQGLVDELAKDICNQRRHRQRRKAEMLRLRTTLQGLDAKTIFYEEQGDYYNQYIQACLDHLAPKPKSSGKGKKQPSLHYTAAQLLEKGVLVEIEDLPVSHFRNVIFDITPGDEAGRFFVNAKFLGVDMEKFQLHYQDLLQLQYEGVAVMKLFNKAKVNVNLLIFLLNKKFLRK
Protein: Circadian input-output histidine kinase CikA (EC 2.7.13.3) (Q9KHI5)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Functions in an input pathway to the Kai circadian clock. Senses oxidized quinones via its C-terminal pseudo-receiver domain, providing a link between cell metabolism and the clock. Affects the ratio of phosphorylated to unphosphorylated KaiC, binds quinones via its pseudo-receptor domain. Quinone-binding destabilizes the protein rapidly. Autophosphorylates, does not transfer the phosphate to its pseudo-receiver (PsR) domain. May play a role in cell division, as suggested by its polar location and increased cell length in a deletion strain (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17088557}. Membrane {ECO:0000269|PubMed:17088557}. Note=Localized in tight foci at one or both cell poles (PubMed:16629668). Both soluble and membrane-associated (PubMed:17088557). {ECO:0000269|PubMed:16629668, ECO:0000269|PubMed:17088557}.
Interaction partners:
- Response regulator receiver domain protein
- Circadian clock oscillator protein KaiB
- Diguanylate cyclase with GAF sensor
- Light dependent period A
- Circadian clock oscillator protein KaiC
- Two component transcriptional regulator, LuxR family
- Potassium-transporting ATPase D chain
- Low amplitude and bright protein LabA
- Circadian clock oscillator protein KaiA
- histidine kinase
Sequence:
MLAPSSNCSLASQRLTPEGFAQLQSALQDFVATLPQAFYWDSRSLHTHLRTQTGDCAIAIAAGFQLLLLGRTAAEYCQPHPLSEPHHVSVQFGADSIQRYCQATNLPVEYQPALAQLGDLSLNPDLISQFSNLLIAAIAADRAPLAAQYPAVSVCQPLEQALHWQEEQDRLISQVSAQIRLSLDLSEILTTTIREIRQLLNADRAIIYQFKPQCLDAGLDQRWPLYIPSQSYITYEDRRNEALLSVIDPLVQPGLLITTEEWQRFQQGETLLIDSVGFYKERLPEQYSFYERVQVRSVCKIPILVQGRIWGLLVAHQCQQDHRWQPRERDILQHLAEHLSIAIYQAQLYGQLQDQTQTLENRVLERTQELIDALALAQAANAAKGEFLATMSHELRTPLTCVIGMSSTLLRWAFGPLTERQREYIKAIHDSGEHLLELINDILDLSQIEAGKAALQVRPFSLSRLATQTLNTLQEKARLGEIQLMLDLQLNNRVDVFRADPKRLRQILINLLSNAVKFTEPQGTVFLRVWREGDRAIFQVSDTGIGIPESEQAQLFQKFQQLDTSIRRQYGGTGLGLALTKQLVELHGGHIQIESTVGQGSTFTVWIPEQTLIEPVEPRPSIDNLPAGHILLLEEEDEAATVVCEMLTAAGFKVIWLVDGSTALDQLDLLQPIVILMAWPPPDQSCLLLLQHLREHQADPHPPLVLFLGEPPVDPLLTAQASAILSKPLDPQLLLTTLQGLCPPNLSEGDRPSS
Protein: Pre-mRNA-processing factor 19 (EC 2.3.2.27) (Q7KLW9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
- Puff-specific protein Bx42
- Pre-mRNA-splicing factor syf1 homolog
- RNA helicase aquarius
- Peptidyl-prolyl cis-trans isomerase E
- Cell division cycle 5, isoform A
- Pleiotropic regulator 1
- Pre-mRNA-splicing factor SPF27
- RE31520p
- Protein CWC15 homolog
- Protein crooked neck
Sequence:
MALVCALTNEVPETPVVSPHSGAVFEKRVIEKYLLENGCDPISGKELKPEELIEIKTPAVVKPKPPSATSIPATLKTMQDEWDALMIHSFTQRQQLQTTRQELSHALYQHDAACRVIARLNKEVAAAREALATLKPQAGIANAPTAIPQPALASEAGGAAAHPMEQAGMSAEVIQKLQDKATVLTQERKKRGRTVPEDLVTTDQVKNFLTVASHPGLHSASVPGILALDINSADHSKILTGGNDKNATVFNKDTEQMVAILKGHTKKITKVIYHPNEDTVITGSPDMNIRIWHVPTSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSSDKHWAFSDIRTGRLLTKVIDTAEVGLTTAQFHPDGLIFGTGTVDSQVKIWDLKEQSNVANFPGHTGPISAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGYEVKDLCFDQSGTYLAIAGSDVRVYLCKQWQELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLYAIE
Protein: Beta-catenin-like protein 1 (Nuclear-associated protein) (NAP) (Testis development protein NYD-SP19) (Q8WYA6)
Organism: Homo sapiens (Human)
Function: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated somatic hypermutation (SHM) and class-switch recombination (CSR), 2 processes resulting in the production of high-affinity, mutated isotype-switched antibodies.
Subcellular location: [Isoform 1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
Interaction partners:
- Cell division cycle 5-like protein
- Spliceosome-associated protein CWC15 homolog
- Pre-mRNA-processing factor 19
- Pleiotropic regulator 1
- Pre-mRNA-splicing factor SPF27
- Heat shock cognate 71 kDa protein
- Pre-mRNA-splicing factor SYF1
- Crooked neck-like protein 1
- Protein BUD31 homolog
- SNW domain-containing protein 1
Sequence:
MDVGELLSYQPNRGTKRPRDDEEEEQKMRRKQTGTRERGRYREEEMTVVEEADDDKKRLLQIIDRDGEEEEEEEEPLDESSVKKMILTFEKRSYKNQELRIKFPDNPEKFMESELDLNDIIQEMHVVATMPDLYHLLVELNAVQSLLGLLGHDNTDVSIAVVDLLQELTDIDTLHESEEGAEVLIDALVDGQVVALLVQNLERLDESVKEEADGVHNTLAIVENMAEFRPEMCTEGAQQGLLQWLLKRLKAKMPFDANKLYCSEVLAILLQDNDENRELLGELDGIDVLLQQLSVFKRHNPSTAEEQEMMENLFDSLCSCLMLSSNRERFLKGEGLQLMNLMLREKKISRSSALKVLDHAMIGPEGTDNCHKFVDILGLRTIFPLFMKSPRKIKKVGTTEKEHEEHVCSILASLLRNLRGQQRTRLLNKFTENDSEKVDRLMELHFKYLGAMQVADKKIEGEKHDMVRRGEIIDNDTEEEFYLRRLDAGLFVLQHICYIMAEICNANVPQIRQRVHQILNMRGSSIKIVRHIIKEYAENIGDGRSPEFRENEQKRILGLLENF
Protein: Gremlin-1 (Cysteine knot superfamily 1, BMP antagonist 1) (O73754)
Organism: Xenopus laevis (African clawed frog)
Function: Cytokine that has an axial patterning activity. Acts like BMP antagonist in embryonic explants. Blocks the BMP2 activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MNCLVYALGSLFLLSGLLLPSSEGKKKVSGSQGAIPPPDKGQPNDSEQGQAQPGDRVRGKGKGQALAAEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEDGCNSRTIINRFCYGQCNSFYIPRHIRREEGSFQSCSFCKPKKFTTMVVTLNCPELQPPTKKKRITRVKQCRCISIDLD