wanglab/gogpt-training-data huggingface dataset:
Protein: Tetraspanin-3 (Tspan-3) (Tetraspanin TM4-A) (Transmembrane 4 superfamily member 8) (O60637)
Organism: Homo sapiens (Human)
Function: Regulates the proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Integrin beta-1
Sequence:
MGQCGITSSKTVLVFLNLIFWGAAGILCYVGAYVFITYDDYDHFFEDVYTLIPAVVIIAVGALLFIIGLIGCCATIRESRCGLATFVIILLLVFVTEVVVVVLGYVYRAKVENEVDRSIQKVYKTYNGTNPDAASRAIDYVQRQLHCCGIHNYSDWENTDWFKETKNQSVPLSCCRETASNCNGSLAHPSDLYAEGCEALVVKKLQEIMMHVIWAALAFAAIQLLGMLCACIVLCRRSRDPAYELLITGGTYA
Protein: Grancalcin (Q8VC88)
Organism: Mus musculus (Mouse)
Function: Calcium-binding protein that may play a role in the adhesion of neutrophils to fibronectin. May play a role in the formation of focal adhesions.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P28676}. Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P28676}; Peripheral membrane protein {ECO:0000250|UniProtKB:P28676}; Cytoplasmic side {ECO:0000250|UniProtKB:P28676}. Note=Primarily cytosolic in the absence of calcium or magnesium ions. Relocates to granules and other membranes in response to elevated calcium and magnesium levels. {ECO:0000250|UniProtKB:P28676}.
Interaction partners:
Sequence:
MAYPGYGGAFGNFSGQIPGMQMQMGQPMPGAGPNMFSGGYPGYLGYSDSYSPADDSMWTYFTAVAGQDGEVDAEELQRCLTQSGISGTYAPFSLETCRIMIAMLDRDYTGKMGFNEFKELWAALNAWKQNFMTIDQDQSGTVEHHELSQAIALMGYRLSPQTLAAIVRRYSKNGRIFFDDYVACCVKLRALTDFFRRRDHLQQGIVNFMYEDFLQGTMTI
Protein: Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta) (P9WGC5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Interaction partners:
- Succinate--CoA ligase subunit alpha
- Multifunctional 2-oxoglutarate metabolism enzyme
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- succinate dehydrogenase
- Succinate dehydrogenase 2 membrane subunit SdhC
- Succinate dehydrogenase flavoprotein subunit
- Probable succinate dehydrogenase [iron-sulfur subunit]
- Probable succinate dehydrogenase [iron-sulfur subunit]
- Probable succinate dehydrogenase SdhD
- 2-oxoglutarate oxidoreductase subunit KorA
Sequence:
MDLFEYQAKELFAKHNVPSTPGRVTDTAEGAKAIATEIGRPVMVKAQVKIGGRGKAGGVKYAATPQDAYEHAKNILGLDIKGHIVKKLLVAEASDIAEEYYLSFLLDRANRTYLAMCSVEGGMEIEEVAATKPERLAKVPVNAVKGVDLDFARSIAEQGHLPAEVLDTAAVTIAKLWELFVAEDATLVEVNPLVRTPDHKILALDAKITLDGNADFRQPGHAEFEDRAATDPLELKAKEHDLNYVKLDGQVGIIGNGAGLVMSTLDVVAYAGEKHGGVKPANFLDIGGGASAEVMAAGLDVVLGDQQVKSVFVNVFGGITSCDAVATGIVKALGMLGDEANKPLVVRLDGNNVEEGRRILTEANHPLVTLVATMDEAADKAAELASA
Protein: Aminomethyltransferase, mitochondrial (EC 2.1.2.10) (Glycine cleavage system T protein) (GCVT) (P48728)
Organism: Homo sapiens (Human)
Function: The glycine cleavage system catalyzes the degradation of glycine.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:16051266}.
Interaction partners:
- Glycine cleavage system H protein, mitochondrial
- Glycine dehydrogenase
- Dihydrolipoyl dehydrogenase, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- P protein
- Myosin-binding protein H
- Methylenetetrahydrofolate reductase
Sequence:
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQYRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFTNEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALLALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGAVHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAMDFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNVAMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
Protein: Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1) (Q62073)
Organism: Mus musculus (Mouse)
Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity (By similarity). Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane. {ECO:0000250}.
Interaction partners:
- TNF receptor-associated factor 6
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
- NF-kappa-B essential modulator
- Myeloid differentiation primary response protein MyD88
- Ubiquitin-conjugating enzyme E2 N
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- Dual specificity mitogen-activated protein kinase kinase 4
- Toll-like receptor 4
- Baculoviral IAP repeat-containing protein 3
Sequence:
MSTASAASSSSSSSASEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIVATAGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPARSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS
Protein: Epsilon-sarcoglycan (Epsilon-SG) (Q6YAT4)
Organism: Rattus norvegicus (Rat)
Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Subcellular location: Cell membrane, sarcolemma {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P82350}. Cell projection, dendrite {ECO:0000250}. Golgi apparatus {ECO:0000250}.
Interaction partners:
- Sarcoglycan, delta
- Sarcoglycan zeta
- Gamma-sarcoglycan
- Dystroglycan 1
- Sarcospan
- Beta-sarcoglycan
- Dystrophin
- Utrophin
- Caveolin-3
- Neuronatin
Sequence:
MLLFWWWELGDPCAWTGKGRGTLKMSPATTGTFLLTVYTLFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEVSNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEEFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPIKDMKEGVYVMVGADVAFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTQFYIDWCKISLVDKTKQVSTYQEVVRGEGILPDGGEYKPPSDSLKSRDYYTDFLVTLAVPSAVALVLFLILAYIMCCRREGVEKRNMQTPDIQLVHHSSIQKSTKELRDMSKNREIAWPLSTLPVFHPVTGEIIPPMHTDNYDSTNMPLMQTQPNLPHQTQIPQQQTTGKWYP
Protein: Tumor necrosis factor receptor superfamily member 27 (X-linked ectodysplasin-A2 receptor) (EDA-A2 receptor) (Q8BX35)
Organism: Mus musculus (Mouse)
Function: Receptor for EDA isoform A2, but not for EDA isoform A1. Mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated by binding to TRAF3 and TRAF6 (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- Ectodysplasin-A
- TNF receptor-associated factor 6
- TNF receptor-associated factor 3
Sequence:
MDCQENEYRDQWGRCVTCQQCGPGQELSKDCGYGEGGDAHCIVCPPRKYKSTWGHHRCQTCITCAVINRVQKANCTNTSNAICGDCLPRFYRKTRIGGLQDQECIPCTKQTPSSEVQCTFQLSLVKVDAHTVPPREATLVALVGSLLVVFALAFLGLFFLYCKQIFNRHCQCRDSLQYEAEKTVEEDSLFPVPPGQETSPEFPANEGILEIKPLNSILDDDCSSTRGFPTQESFTMASCASESHSQWVHTPIECTELDLQKFSSSIPSTGPETLRENTAEHSGDRLELYVPFEVPSL
Protein: Cell membrane protein YLR413W (Q06689)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MNFKILLPICALLTLTTFLLTIIATAGSTSNYKPITNIYIGDADISKINVTKVMPQVGPILTVLGSALTAPNTTVDTIFGALKAIASTEALSPLLHLLSNAANTSATLSSLTQLAPMALLGTNTATTTTFSALDELLTTSKNTTELLDGFSTLMSSMSTNTSSTSASLENTVLTLLVDSTNPIGTTESLITLNNMTTEEKTKLSPVFELFASSKNITATCDALETIMNSTIPTSTVSSLFSSLKTSLAEGGNATETIMQLGSLVPSSLKPAVQAVVTLFDETTSQNVTLSVLSTMIAENITQSSSAKAAMGALTDLLNYTTNQTELLTSVESLALSKEAASSTNQLVALDEILSASANASTVVSIIPTLESQLANNTVLLKYVPYLFSLLAASSDPVSSFSSLVNITKWAETNAATFMPMLKILNSAVNMTTITPEQLKEMTPSILEYLHIPVIYRLSIFTMCRAHLNRTMYSCSKSHAVQNMDFRSIVYNNIEGSDFKPYMDALNIGKDDLHLDGELQDRQHMYVPAVKAALAMNLMCIITSFFLMVFLLLLSRRSVVSQKLWLALGFISCWICIFSGLGSTIFSVILNMMKSGSKKDNYDVIISGSSPFYGLMWSGFVFAVLVFLCIAYCWWSSRKGAAIVEAEKAVQESDSTTSRIIEEHESPIDAEKNFAR
Protein: Transcription factor PU.1 (31 kDa-transforming protein) (P17947)
Organism: Homo sapiens (Human)
Function: Pioneer transcription factor, which controls hematopoietic cell fate by decompacting stem cell heterochromatin and allowing other transcription factors to enter otherwise inaccessible genomic sites. Once in open chromatin, can directly control gene expression by binding genetic regulatory elements and can also more broadly influence transcription by recruiting transcription factors, such as interferon regulatory factors (IRFs), to otherwise inaccessible genomic regions. Transcriptionally activates genes important for myeloid and lymphoid lineages, such as CSF1R (By similarity). Transcriptional activation from certain promoters, possibly containing low affinity binding sites, is achieved cooperatively with other transcription factors. FCER1A transactivation is achieved in cooperation with GATA1 (By similarity). May be particularly important for the pro- to pre-B cell transition. Binds (via the ETS domain) onto the purine-rich DNA core sequence 5'-GAGGAA-3', also known as the PU-box. In vitro can bind RNA and interfere with pre-mRNA splicing (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:33951726}.
Interaction partners:
- Interferon regulatory factor 8
- Interferon regulatory factor 4
- Erythroid transcription factor
- Endothelial transcription factor GATA-2
- Transcription factor Jun
- Runt-related transcription factor 1
- Macrophage colony-stimulating factor 1 receptor
- CCAAT/enhancer-binding protein alpha
- Retinoic acid receptor alpha
- Integrin alpha-M
Sequence:
MLQACKMEGFPLVPPPSEDLVPYDTDLYQRQTHEYYPYLSSDGESHSDHYWDFHPHHVHSEFESFAENNFTELQSVQPPQLQQLYRHMELEQMHVLDTPMVPPHPSLGHQVSYLPRMCLQYPSLSPAQPSSDEEEGERQSPPLEVSDGEADGLEPGPGLLPGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRHPPH
Protein: Chloroplastic lipocalin (AtCHL) (Q9STS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipocalin that prevents thylakoidal membrane lipids peroxidation and confers protection against oxidative stress, especially mediated by singlet oxygen in response to high light and other stress (e.g. heat shocks). Required for seed longevity by insuring polyunsaturated lipids integrity.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:19674405}.
Interaction partners:
- Temperature-induced lipocalin-1
- NAD
- Protein SUPPRESSOR OF QUENCHING 1, chloroplastic
- Ankyrin repeat family protein
- Ankyrin repeat family protein
- NADPH-dependent aldehyde reductase 1, chloroplastic
- Probable aldo-keto reductase 1
Sequence:
MILLSSSISLSRPVSSQSFSPPAATSTRRSHSSVTVKCCCSSRRLLKNPELKCSLENLFEIQALRKCFVSGFAAILLLSQAGQGIALDLSSGYQNICQLGSAAAVGENKLTLPSDGDSESMMMMMMRGMTAKNFDPVRYSGRWFEVASLKRGFAGQGQEDCHCTQGVYTFDMKESAIRVDTFCVHGSPDGYITGIRGKVQCVGAEDLEKSETDLEKQEMIKEKCFLRFPTIPFIPKLPYDVIATDYDNYALVSGAKDKGFVQVYSRTPNPGPEFIAKYKNYLAQFGYDPEKIKDTPQDCEVTDAELAAMMSMPGMEQTLTNQFPDLGLRKSVQFDPFTSVFETLKKLVPLYFK
Protein: Cecropin-A2 (C0HKQ8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARG
Protein: 2',5'-phosphodiesterase 12 (2'-PDE) (2-PDE) (EC 3.1.4.-) (Mitochondrial deadenylase) (EC 3.1.13.4) (Q3TIU4)
Organism: Mus musculus (Mouse)
Function: Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. Degrades triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme increases cellular 2-5A levels and decreases viral replication in cultured small-airway epithelial cells.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q6L8Q7}.
Interaction partners:
- Probable ATP-dependent RNA helicase DDX6
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 9
Sequence:
MWRLPGRSALRGVRSVVERRSRAEAGTHEAVRAMERAVVRCVPSEPKLSLSFALADGSHKNMQRDQSEPLGRALSRIATNALKGHAKVAAAKKSRKNRAHSSGGAACEATGPEPVATCEPVVKLYYREEAVAEDVLNVDAWQDGAVLQIGDVKYKVERNPPTFTELQLPRYIMAGFPVCPKLGVEFGDPASSVFRWYKEVKPGAAEPGDSGPASSSHSSQPSAWIETGVDERVYTPCNADIGLRLRLHCTPGNGQRFGPSRELESLCPVEAGPGTCTFDHRHLYTKKVTEDSFIRTVSYNILADTYAQTEFSRTVLYPYCAPYALELDYRQNLIQKELTGYNADLICLQEVDRAVFSDSLVPALEAFGLEGVFRIKQHEGLATFYRKSKFRLLSQHDISFQEALKSDPLHKELLEKLALNPLAQEKVLQRSSVLQISVLQSTTDSSKKICVANTHLYWHPKGGYIRLIQMEVALVHIRHVSRDLYPGIPVIFCGDFNSTPSTGMYHFVISGSIAEDHEDWASNGEEERCSMPLSHCFKLKSACGEPAYTNYVGGFHGCLDYIFIDLNTLEVEQVIPLPSHEEVTTHQALPSVSHPSDHIALVCDLKWK
Protein: Carbonic anhydrase 3 (EC 4.2.1.1) (Carbonate dehydratase III) (Carbonic anhydrase III) (CA-III) (P14141)
Organism: Rattus norvegicus (Rat)
Function: Reversible hydration of carbon dioxide.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P07451}.
Interaction partners:
Sequence:
MAKEWGYASHNGPEHWHELYPIAKGDNQSPIELHTKDIRHDPSLQPWSVSYDPGSAKTILNNGKTCRVVFDDTFDRSMLRGGPLSGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFGEALKQPDGIAVVGIFLKIGREKGEFQILLDALDKIKTKGKEAPFNHFDPSCLFPACRDYWTYHGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLFASAENEPPVPLVGNWRPPQPIKGRVVRASFK
Protein: Transmembrane protein 132E (Q6IEE7)
Organism: Homo sapiens (Human)
Function: Required for normal inner ear hair cell function and hearing.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAPGMSGRGGAALLCLSALLAHASGRSHPASPSPPGPQASPVLPVSYRLSHTRLAFFLREARPPSPAVANSSLQRSEPFVVFQTKELPVLNVSLGPFSTSQVVARELLQPSSTLDIPERLTVNWKVRAFIVRSHVPASQPVVQVLFYVAGRDWDDFGVTERLPCVRLHAFRDAREVKSSCRLSGGLATCLVRAELPLAWFGPPAPAAPPTARRKSPDGLEPEATGESQQAELYYTLHAPDASGGCGGSRRGAGPGVGARAESPTQHPLLRIGSISLFRPPPRRTLQEHRLDSNLMIRLPDRPLKPGEVLSILLYLAPNSSSPSSPSVEHFTLRVKAKKGVTLLGTKSRSGQWHVTSELLTGAKHSTATVDVAWAQSTPLPPREGQGPLEILQLDFEMENFTSQSVKRRIMWHIDYRGHGALPDLERAVTELTVIQRDVQAILPLAMDTEIINTAILTGRTVAIPVKVIAIEVNGLVLDISALVECESDNEDIIKVSSSCDYVFVSGKESRGSMNARVTFRYDVLNAPLEMTVWVPKLPLHIELSDARLSQVKGWRVPILPDRRSVRESEDEDEEEEERRQSASRGCTLQYQHATLQVFTQFHTTSSEGTDQVVTMLGPDWLVEVTDLVSDFMRVGDPRVAHMVDSSTLAGLEPGTTPFKVVSPLTEAVLGETLLTVTEEKVSITQLQAQVVASLALSLRPSPGSSHTILATTAAQQTLSFLKQEALLSLWLSYSDGTTAPLSLYSPRDYGLLVSSLDEHVATVTQDRAFPLVVAEAEGSGELLRAELTIAESCQKTKRKSVLATTPVGLRVHFGRDEEDPTYDYPGPSQPGPGGGEDEARGAGPPGSALPAPEAPGPGTASPVVPPTEDFLPLPTGFLQVPRGLTDLEIGMYALLGVFCLAILVFLINCIVFVLRYRHKRIPPEGQTSMDHSHHWVFLGNGQPLRVQGELSPPAGNPLETVPAFCHGDHHSSGSSQTSVQSQVHGRGDGSSGGSARDQAEDPASSPTSKRKRVKFTTFTTLPSEELAYDSVPAGEEDEEEEEDLGWGCPDVAGPTRPTAPPDLHNYMRRIKEIA
Protein: Ribonuclease K6 (RNase K6) (EC 3.1.27.-) (Q93091)
Organism: Homo sapiens (Human)
Function: Ribonuclease which shows a preference for the pyrimidines uridine and cytosine. Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli. Causes loss of bacterial membrane integrity, and also promotes agglutination of Gram-negative bacteria. Probably contributes to urinary tract sterility. Bactericidal activity is independent of RNase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:25075772}. Lysosome {ECO:0000305|PubMed:25075772}. Cytoplasmic granule {ECO:0000269|PubMed:25075772}.
Interaction partners:
- Ribonuclease T2
- Lymphocyte antigen 86
Sequence:
MVLCFPLLLLLLVLWGPVCPLHAWPKRLTKAHWFEIQHIQPSPLQCNRAMSGINNYTQHCKHQNTFLHDSFQNVAAVCDLLSIVCKNRRHNCHQSSKPVNMTDCRLTSGKYPQCRYSAAAQYKFFIVACDPPQKSDPPYKLVPVHLDSIL
Protein: Indole-3-acetaldehyde oxidase (IAA oxidase) (EC 1.2.3.7) (Aldehyde oxidase) (ZmAO-1) (O23887)
Organism: Zea mays (Maize)
Function: In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. Involved in the biosynthesis of auxin from (indol-3-yl)acetaldehyde. Can also use indole-3-aldehyde and benzaldehyde as substrate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Indole-3-acetaldehyde oxidase
- Amidase 1
- Aldehyde dehydrogenase2
- aldehyde dehydrogenase
- Amidase family protein
- indole-3-acetaldehyde oxidase
- 2-oxoglutarate-dependent dioxygenase DAO
Sequence:
MGKEAGAAESSTVVLAVNGKRYEAAGVAPSTSLLEFLRTQTPVRGPKLGCGEGGCGACVVLVSKYDPATDEVTEFSASSCLTLLHSVDRCSVTTSEGIGNTRDGYHPVQQRLSGFHASQCGFCTPGMCMSIFSALVKADNKSDRPDPPAGFSKITTSEAEKAVSGNLCRCTGYRPIVDTCKSFASDVDLEDLGLNCFWKKGEEPAEVSRLPGYNSGAVCTFPEFLKSEIKSTMKQVNDVPIAASGDGWYHPKSIEELHRLFDSSWFDDSSVKIVASNTGSGVYKDQDLYDKYIDIKGIPELSVINKNDKAIELGSVVSISKAIEVLSDGNLVFRKIADHLNKVASPFVRNTATIGGNIMMAQRLPFESDVATVLLAAGSTVTVQVASKRLCFTLEEFLEQPPCDSRTLLLSIFIPEWGSDYVTFETFRAAPRPFGNAVSYVNSAFLARTSGSLLIEDICLAFGAYGVDHAIRAKKVEDFLKGKSLSSFVILEAIKLLKDTVSPSEGTTHHEYRVSLAVSFLFSFLSSLANSSSAPSNIDTPNGSYTHETGSNVDSPERHIKVDSNDLPIRSRQEMVFSDEYKPVGKPIKKVGAEIQASGEAVYVDDIPAPKDCLYGAFIYSTHPHAHVRSINFKSSLASQKVITVITAKDIPSGGENIGSSFLMQGEALFADPIAEFAGQNIGVVIAETQRYANMAAKQAVVEYSTENLQPPILTIEDAIQRNSYIQIPPFLAPKPVGDYNKGMAEADHKILSAEVKLESQYYFYMETQAALAIPDEDNCITIYSSTQMPELTQNLIARCLGIPFHNVRVISRRVGGGFGGKAMKATHTACACALAAFKLRRPVRMYLDRKTDMIMAGGRHPMKAKYSVGFKSDGKITALHLDLGINAGISPDVSPLMPRAIIGALKKYNWGTLEFDTKVCKTNVSSKSAMRAPGDVQGSFIAEAIIEHVASALALDTNTVRRKNLHDFESLEVFYGESAGEASTYSLVSMFDKLALSPEYQHRAAMIEQFNSSNKWKKRGISCVPATYEVNLRPTPGKVSIMNDGSIAVEVGGIEIGQGLWTKVKQMTAFGLGQLCPDGGECLLDKVRVIQADTLSLIQGGMTAGSTTSETSCETVRQSCVALVEKLNPIKESLEAKSNTVEWSALIAQASMASVNLSAQPYWTPDPSFKSYLNYGAGTSEVEVDILTGATTILRSDLVYDCGQSLNPAVDLGQIEGCFVQGIGFFTNEDYKTNSDGLVIHDGTWTYKIPTVDNIPKEFNVEMFNSAPDKKRVLSSKASGEPPLVLATSVHCAMREAIRAARKEFSVSTSPAKSAVTFQMDVPATMPVVKELCGLDVVERYLENVSAASAGPNTAKA
Protein: Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic (EC 1.3.1.75) (Protein PALE-GREEN AND CHLOROPHYLL B REDUCED 2) (Q1H537)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of divinyl chlorophyllide to monovinyl chlorophyllide. Reduces the 8-vinyl group of the tetrapyrrole to an ethyl group using NADPH as the reductant. The best substrate is (3,8-divinyl)-chlorophyllide a (DV-Chlidea). Very low activity with (3,8-divinyl)-protochlorophyllide a (DV-Pchlidea) and (3,8-divinyl)-magnesium-protoporphyrin IX monomethyl ester (DV-MPE). No activity with (3,8-divinyl)-chlorophyllide b (DV-Chlideb), (3,8-divinyl)-magnesium-protoporphyrin IX (DV-Mg-Proto) and either (3,8-divinyl)-chlorophyll a (DV-Chla) or b (DV-Chlb).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15695432}.
Interaction partners:
- Chlorophyll synthase, chloroplastic
- Chlorophyllide a oxygenase, chloroplastic
- Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic
- Protochlorophyllide reductase A, chloroplastic
- Protochlorophyllide reductase C, chloroplastic
- Protochlorophyllide reductase B, chloroplastic
- Chlorophyllase-1
- Chlorophyllase-2
- Magnesium dechelatase SGRL, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
Sequence:
MSLCSSFNVFASYSPKPKTIFKDSKFISQFQVKSSPLASTFHTNESSTSLKYKRARLKPISSLDSGISEIATSPSFRNKSPKDINVLVVGSTGYIGRFVVKEMIKRGFNVIAVAREKSGIRGKNDKEETLKQLQGANVCFSDVTELDVLEKSIENLGFGVDVVVSCLASRNGGIKDSWKIDYEATKNSLVAGKKFGAKHFVLLSAICVQKPLLEFQRAKLKFEAELMDLAEQQDSSFTYSIVRPTAFFKSLGGQVEIVKDGKPYVMFGDGKLCACKPISEQDLAAFIADCVLEENKINQVLPIGGPGKALTPLEQGEILFKILGREPKFLKVPIEIMDFVIGVLDSIAKIFPSVGEAAEFGKIGRYYAAESMLILDPETGEYSEEKTPSYGKDTLEDFFAKVIREGMAGQELGEQFF
Protein: CENP-A recruiting complex protein mis19 (Eighteen-interacting centromere protein 1) (Kinetochore protein mis19) (O42995)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the CENP-A recruiting complex that ensures the integrity of mitotic spindles through maintenance of kinetochore factors mis6/CENP-I and cnp1/CENP-A. Links mis16 and mis18 to recruit CENP-A through interacting with non-sense-mediated mRNA decay (NMD) factors and the SWI/SNF complex. Links also mis18 with the CCAN/mis6/ctf19 complex to promote CENP-A assembly.
Subcellular location: Chromosome, centromere {ECO:0000269|PubMed:24774534, ECO:0000269|PubMed:24789708, ECO:0000269|PubMed:25375240}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:25375240}. Note=Localizes at the centromeres during interphase, but not in mitosis (PubMed:24774534, PubMed:25375240). {ECO:0000269|PubMed:24774534, ECO:0000269|PubMed:25375240}.
Interaction partners:
- Histone acetyltransferase type B subunit 2
- CENP-A recruiting complex protein mis20
- Kinetochore protein mis18
- CENP-A histone chaperone scm3
- Histone acetyltransferase type B catalytic subunit
- Histone H3-like centromeric protein cnp1
- Uncharacterized serine-rich protein C2F12.03c
- Inner kinetochore subunit mal2
Sequence:
MDLMPLEKARAIEIAFDNVFHNTKIPDNLQQFDAILKRLERRRFIPTENQKPRVYETELLVLRFREFGVKDNHNHPINLHSLRSKSLIRAQGKKLDLHNRVFLRRNVRAVKM
Protein: Chemokine CK-1 (Q9PT07)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MISCRVCVLAALFSLLIITLIPTTQSADCCLKFTRRPVHCRWLKGYTFQDITSSCDLNAVIFQNLRNKFVCADPSQDWTKRVQRCLRKRQENKSQLKKRV