wanglab/gogpt-training-data huggingface dataset:
Protein: MLP-like protein 28 (Q9SSK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Can bind steroids (in vitro), and may also bind other types of hydrophobic ligands.
Interaction partners:
- Uncharacterized protein At1g24000
- Putative UPF0481 protein At3g02645
- Protein trichome birefringence-like 12
- AT2G45990 protein
- Uncharacterized protein At4g24700
- Uncharacterized protein
- Uncharacterized protein
- Expressed protein
- At3g13230
- At2g45350/F14N22.7
Sequence:
MADVATKHPMEDEVKKTEASSLVGKLETDVEIKASADKFHHMFAGKPHHVSKASPGNIQGCDLHEGDWGTVGSIVFWNYVHDGEAKVAKERIEAVEPDKNLITFRVIEGDLMKEYKSFLLTIQVTPKPGGPGSIVHWHLEYEKISEEVAHPETLLQFCVEVSKEIDEHLLAEEEEVKTPETPSLVGKLETDVEIKASAEKFHHMFAGKPHHVSKASPGNIQGCDLHEGDWGQVGSIVFWNYVHDREAKVAKERIEAVEPNKNLITFRVIDGDLMKEYKSFLLTIQVTPKLGGPGSIVHWHLEYEKISEEVAHPETLLQFCVEVSKEIDEHLLAEE
Protein: NSm (Q8V6X2)
Organism: Iris yellow spot virus
Interaction partners:
Sequence:
MSRITNVLESFKKNDNKELIPAVRTIDSDNKLALGRKVTKKDVDAAIRNKASTFNGNQYISSSDSSVLGSYESGESVENSSDDILSRLIVEKSTHLSNWKDDSLIGNGDEKVSYTINIIPTWDSKRKYMHLSRLIVWVVPTIPDSKGFVKATIIDQNKMTPKEKIIISKQGTLENPLCFVFHLNWSFNKDRNVPKRCMQLNLTSNGKYAKGVSFASVMYSWVKNFCDTAIASDSNTCDVIPINRAKAIRSAALIEACKLMIPKGTTGKAIKNQITSLQKLAEKVAFEEEADENDDVLEIEIDNPKNRFDEL
Protein: Bone morphogenetic protein 2 (BMP-2) (Bone morphogenetic protein 2A) (BMP-2A) (P49001)
Organism: Rattus norvegicus (Rat)
Function: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and bone formation. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical pathways such as ERK/MAP kinase signaling cascade that regulates osteoblast differentiation. Stimulates also the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Bone morphogenetic protein receptor type-1A
- Noggin
- Chordin
- Serine/threonine-protein kinase receptor
- Bone morphogenetic protein receptor type-2
- Activin receptor type-2B
- Activin receptor type-2A
- Neogenin
- Activin receptor type-1
- Hemojuvelin
Sequence:
MVAGTRCLLVLLLPQVLLGGAAGLIPELGRKKFAGASRPLSRPSEDVLSEFELRLLSMFGLKQRPTPSKDVVVPPYMLDLYRRHSGQPGALAPDHRLERAASRANTVLSFHHEEAIEELSEMSGKTSRRFFFNLSSVPTDEFLTSAELQIFREQMQEALGNSSFQHRINIYEIIKPATASSKFPVTRLLDTRLVTQNTSQWESFDVTPAVMRWTAQGHTNHGFVVEVAHLEEKPGVSKRHVRISRSLHQDEHSWSQVRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
Protein: Brevinin-2Ej (P86152)
Organism: Pelophylax ridibundus (Marsh frog) (Rana ridibunda)
Function: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
GIFLDKLKNFAKGVAQSLLNKASCKLSGQC
Protein: C-type lectin domain family 3 member A (C-type lectin superfamily member 1) (Cartilage-derived C-type lectin) (O75596)
Organism: Homo sapiens (Human)
Function: Promotes cell adhesion to laminin-332 and fibronectin.
Subcellular location: Secreted {ECO:0000269|PubMed:19173304}.
Interaction partners:
Sequence:
MAKNGLVICILVITLLLDQTTSHTSRLKARKHSKRRVRDKDGDLKTQIEKLWTEVNALKEIQALQTVCLRGTKVHKKCYLASEGLKHFHEANEDCISKGGILVIPRNSDEINALQDYGKRSLPGVNDFWLGINDMVTEGKFVDVNGIAISFLNWDRAQPNGGKRENCVLFSQSAQGKWSDEACRSSKRYICEFTIPQ
Protein: Oxalate oxidoreductase subunit beta (OOR subunit beta) (EC 1.2.7.10) (Q2RI42)
Organism: Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Function: Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.
Interaction partners:
- Oxalate oxidoreductase subunit alpha
- Oxalate oxidoreductase subunit delta
- Pyruvate:ferredoxin oxidoreductase
- Pyruvate ferredoxin oxidoreductase, alpha subunit
- Pyruvate ferredoxin oxidoreductase, alpha subunit
- Pyruvate ferredoxin oxidoreductase, gamma subunit
- Pyruvate ferredoxin oxidoreductase, gamma subunit
- 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate
- 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate
- 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate
Sequence:
MLDRIASIKKAPDEEYYVPGHRTCAGCGPALTYRLVAKAAGPNTIFIGPTGCMYVANTSYGCGPWRVPWIHAQITNGGAVASGIEAAYKAMIRKKKTDAEFPNIIVMAGDGGAVDIGLQALSAMLYRGHDVLFICYDNESYANTGIQTSPTTPYGANTTFTPPGEVVPEGKKLFPKDNPKVIAHGHPELKYVATASIGWPVDLMNKVRKGLNQEGPAYIHIHAPCPKGWQFPADKTIEMAKLAVQTGMFQLYEYENGEYKLSVKVDKRKPVSEYMKLQKRFAHLKPEHIAKMQAFVDARCAEVGITVPVVASNA
Protein: RE48574p (Q6AWN7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGTKSPGGPQRCRLILQRCLAIQLTKPGHKPEDFWMYDSGYMIFQNFLAANAQCWWNGPLTAATRALKYAGHVAPGMLLVTAEPCALEVLRGAFARSVLKPPATYVISSVGDIDDCIVTPTVQGQFTPLPEALCDVIMDLTAEGQSATIEHVRSKLGSRFPHMTTPATEVIYDSLAQLMQEQKIYQTSKGYFIFTPERRRSRSRPRSNHHQLNGSLAYGHLAEEEQQHGDDVVPQEARTMLMSNSEALHSLYGEISTERDGDLTHQCIQTNLADVICGGNPNDKIIYPRAAKRRSASFPTPRSLERRHSLRLFGSSKRLQRCASTRSLSKTYAQTLNTTDSSSSEYQSTDSSSPKKGSLLSRLFRRSGRAKQRQIETYSAQFPPAEWFNTRAVHLHSVGTQTAEHDMPVAHTLSNSTFYDGSELSQRSSTLPRRHRRHMSSESTFLISSRDCSPIRRRSPVYCSSSLPRSTQSIPATTAKTNHSSRLSHGHGGSVTPTPPKTAQKSVIGKHIFESSPSRSATLKATAAKRHTDGLIINSCLDNKATYRSLQSSGPSSLESCKTTSMLASGPSSIDSGKVSFSQKTSGHSSLDSQCSTNTAVIAPPSNSNNGSSRSILLLNGSPRGTPRHQAMRARVAEAQAQRQRASTPSRIMEEIYPAGGSNGVPTSNSNNSITLQVTTSNGNQSIPSTKIFVQNSPVRSVITLENGKMLENSNVFIINNETMTNEKGEIIKKTLSKQTSAAPAATSTPVKPETVSEQPLSETEANSETCDSISFISECSPESTCAVEPETPVYDGGKYAKNTNNDATMNNSRKLCLQLANGIAYKNNVLKNESQPNSPSADAPLKMAALAKQDFEIAGSVGNLNFYEKSSKDVGASQSNNMMMNSSTDLKNLCYESVCQLQKCSMNGDELALAHLLHKSSSPLGSEPNLALKDLANDKSIDKEAIDRRLSLTKESLEQGMGSVLANGGEELYNFPSLTDLSFNFTSLAARKILQGVSLNSIDTLVELNMAAAAAAAAVANNAQEKQQNNQPATAGPTASVCTDFGMV
Protein: Transcription-repair-coupling factor (TRCF) (EC 3.6.4.-) (P30958)
Organism: Escherichia coli (strain K12)
Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site. Can also dissociate RNAP that is blocked by low concentration of nucleoside triphosphates or by physical obstruction, such as bound proteins. In addition, can rescue arrested complexes by promoting forward translocation. Has ATPase activity, which is required for removal of stalled RNAP, but seems to lack helicase activity. May act through a translocase activity that rewinds upstream DNA, leading either to translocation or to release of RNAP when the enzyme active site cannot continue elongation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}.
Interaction partners:
- UvrABC system protein A
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- UvrABC system protein C
- DNA helicase II
- Transcription elongation factor GreA
- DNA-directed RNA polymerase subunit alpha
- DNA mismatch repair protein MutL
- Transcription elongation factor GreB
- DNA-directed RNA polymerase subunit omega
Sequence:
MPEQYRYTLPVKAGEQRLLGELTGAACATLVAEIAERHAGPVVLIAPDMQNALRLHDEISQFTDQMVMNLADWETLPYDSFSPHQDIISSRLSTLYQLPTMQRGVLIVPVNTLMQRVCPHSFLHGHALVMKKGQRLSRDALRTQLDSAGYRHVDQVMEHGEYATRGALLDLFPMGSELPYRLDFFDDEIDSLRVFDVDSQRTLEEVEAINLLPAHEFPTDKAAIELFRSQWRDTFEVKRDPEHIYQQVSKGTLPAGIEYWQPLFFSEPLPPLFSYFPANTLLVNTGDLETSAERFQADTLARFENRGVDPMRPLLPPQSLWLRVDELFSELKNWPRVQLKTEHLPTKAANANLGFQKLPDLAVQAQQKAPLDALRKFLETFDGPVVFSVESEGRREALGELLARIKIAPQRIMRLDEASDRGRYLMIGAAEHGFVDTVRNLALICESDLLGERVARRRQDSRRTINPDTLIRNLAELHIGQPVVHLEHGVGRYAGMTTLEAGGITGEYLMLTYANDAKLYVPVSSLHLISRYAGGAEENAPLHKLGGDAWSRARQKAAEKVRDVAAELLDIYAQRAAKEGFAFKHDREQYQLFCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVDNHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEMISRFRSAKEQTQILAEVAEGKIDILIGTHKLLQSDVKFKDLGLLIVDEEHRFGVRHKERIKAMRANVDILTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDSMVVREAILREILRGGQVYYLYNDVENIQKAAERLAELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQAYAWLLTPHPKAMTTDAQKRLEAIASLEDLGAGFALATHDLEIRGAGELLGEEQSGSMETIGFSLYMELLENAVDALKAGREPSLEDLTSQQTEVELRMPSLLPDDFIPDVNTRLSFYKRIASAKTENELEEIKVELIDRFGLLPDPARTLLDIARLRQQAQKLGIRKLEGNEKGGVIEFAEKNHVNPAWLIGLLQKQPQHYRLDGPTRLKFIQDLSERKTRIEWVRQFMRELEENAIA
Protein: Scaffold protein ILK (ILK-1) (ILK-2) (Inactive integrin-linked kinase) (p59ILK) (Q13418)
Organism: Homo sapiens (Human)
Function: Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Regulates cell motility by forming a complex with PARVB. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
Subcellular location: Cell junction, focal adhesion {ECO:0000269|PubMed:11402068, ECO:0000269|PubMed:12167643, ECO:0000269|PubMed:12432066, ECO:0000269|PubMed:35259013}. Cell membrane {ECO:0000269|PubMed:11402068}; Peripheral membrane protein {ECO:0000269|PubMed:11402068}; Cytoplasmic side {ECO:0000269|PubMed:11402068}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O55222}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:11402068}. Cytoplasm {ECO:0000269|PubMed:17420447}. Nucleus {ECO:0000269|PubMed:17420447}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18283114}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O55222}.
Interaction partners:
- Integrin beta-1
- Alpha-parvin
- LIM and senescent cell antigen-like-containing domain protein 2
- Beta-parvin
- LIM and senescent cell antigen-like-containing domain protein 1
- Paxillin
- Gamma-parvin
- RAC-alpha serine/threonine-protein kinase
- Fermitin family homolog 2
- Talin-1
Sequence:
MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQSPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK
Protein: ATP synthase delta subunit 1 (ATP synthase subunit delta', mitochondrial-like) (C6GFP2)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit a, chloroplastic
- F-ATPase protein 6
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit alpha
- ATP synthase subunit delta, chloroplastic-like
- ATP synthase subunit O, mitochondrial-like
- ATP synthase subunit O, mitochondrial-like
- ATP synthase delta chain, chloroplastic-like
Sequence:
MLRRALGLLPRPIAAARARSFSTDLPAAHTADATFMEAWNKVMPNTDPPKTPLSFMHPRPPTPSSIPPKLTVNFVLPYASELSTKEVDMVIVPATTGQMGVLPGHVATIAELKPGVLSVHEGSETTKYFVSSGFVFIHANSFADIIAVEAVPLDQIDANLVQKGLADFTQKLSSATTELEKAEAQIGIDVHSALNSALTG
Protein: Glutathione S-transferase theta-1 (EC 2.5.1.18) (GST class-theta-1) (Glutathione transferase T1-1) (P30711)
Organism: Homo sapiens (Human)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2-epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MGLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGAGCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR
Protein: NADPH dehydrogenase 2 (EC 1.6.99.1) (Old yellow enzyme 2) (Q03558)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Flavin-dependent enoate reductase that catalyzes the chemo- and stereoslective hydrogenation of electron-poor alkenes. The enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta-unsaturated aldehydes and ketones can act as electron acceptors to complete catalytic turnover. The physiological oxidant remains elusive (By similarity). Has an antioxidant activity, reducing reactive oxygen species (ROS) levels when overexpressed. Formation of OYE2-OYE3 heterodimers contribute to the induction of programmed cell death upon oxidative stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:17897954}.
Interaction partners:
- Fumarate reductase 1
- Probable electron transfer flavoprotein subunit beta
Sequence:
MPFVKDFKPQALGDTNLFKPIKIGNNELLHRAVIPPLTRMRAQHPGNIPNRDWAVEYYAQRAQRPGTLIITEGTFPSPQSGGYDNAPGIWSEEQIKEWTKIFKAIHENKSFAWVQLWVLGWAAFPDTLARDGLRYDSASDNVYMNAEQEEKAKKANNPQHSITKDEIKQYVKEYVQAAKNSIAAGADGVEIHSANGYLLNQFLDPHSNNRTDEYGGSIENRARFTLEVVDAVVDAIGPEKVGLRLSPYGVFNSMSGGAETGIVAQYAYVLGELERRAKAGKRLAFVHLVEPRVTNPFLTEGEGEYNGGSNKFAYSIWKGPIIRAGNFALHPEVVREEVKDPRTLIGYGRFFISNPDLVDRLEKGLPLNKYDRDTFYKMSAEGYIDYPTYEEALKLGWDKN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (X1WD79)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 6
- PAXIP1-associated glutamate-rich protein 1
- TLC domain-containing 3Ba.
- Aspartate beta-hydroxylase domain-containing protein 2
- Seizure-related 6 homolog
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- HIRA-interacting protein 3.
- Double C2-like domain-containing protein alpha isoform X2
- Proline-rich transmembrane protein 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase.
Sequence:
MPASVRTGTLKDSEVSELFYRDDPEKLFTDLREIGHGSFGAVYFAHDVRSNEVVAIKKMSFSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEMEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGQVKLGDFGSASIVSPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITSIELAERKPPLFNMNAMSALYHIAQNESPVLASNHWSDYFRNFVDSCLQKIPQDRPTSDVLLNHHFLCRERPHSVVMDLITRTKDAVRELDNLQYRKMKKILFQETHNGPVQEGGEEEEEGEQYLLQTGTVNSMESSQSVPSMSISASSQSSSVNSLADGSDDSAEMAMMQEGEQTVTSNSSIIHRPSARDNIYDDPYQPEMESQQPASSAARRRIHRNRDHFATIRTASVVTRQIQEHEQGSALREQMSGYKRMRRQHQKQLLALENKLKSEMDEHQLRLDKELETQRNNFGSEADKLGKKHLAILEKEIKGAQTEEKKFQQHILNQQKKELNSLLDNQKRQYRQRKDQLKEELSENQSTPKREKQEWLVRQKECLQQIQAEEEASLLRRQRQYYELQCRQYKRKMLLARHNLEQDLLREDLNKRQTQKDLECAMLLRHHESTQELEFRQLALVQRTRADLIRTQHQSELANQMEYNKRREQELRQKHAVEVRQQPKSLKTKELQIKRQFQDTCKIQTRQYKALRNHLLETTPKSEHKTVLKRLKEEQTRKLAILAEQYDHSIKDMLSTQALRLDETQEDEYRALRMQLQQELELLNAYQSKIKMHTDTQHEREVKDLEQRVSIRRALLEQRIEEEMLSLQNERSERIRALLEQQAREIESFDSESMRLGFSNMALSGIPAEAYNQGYSNPPSSGPGGWPSRPVPRSGSQWSHGVQNSAAPPSWRSQNSTAGFSRAEQMSSRERDRDRELESMAARAYPGSRSSASSASSSSSSSSHHHLRYIPQQYHHQSTPHLYRDSREREWGSGGGGHHSSSSSSHGHSHHISAQSLALLPPPPPPPPISLSSSSPPSSSSSSSSQSGYGGRGEGLVVRGPSLMALRNSPGPLRRTASGGGAGGSGGDGGLSRSTSVTSHISNGSHLSYS
Protein: Ribonucleases P/MRP protein subunit POP7 (EC 3.1.26.5) (RNA-processing protein POP7) (RNases P/MRP 15.8 kDa subunit) (P38291)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribonuclease MRP protein subunit SNM1
- RNases MRP/P 32.9 kDa subunit
- Ribonucleases P/MRP protein subunit POP8
- Ribonuclease P/MRP protein subunit RPP1
- Ribonucleases P/MRP protein subunit POP1
- Ribonuclease MRP protein subunit RMP1
- Ribonucleases P/MRP protein subunit POP3
- Ribonucleases P/MRP protein subunit POP6
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease P protein subunit RPR2
Sequence:
MALKKNTHNKSTKRVTKHPSLKTLTHKQIHTTIFVKSTTPYVSALKRINKFLDSVHKQGSSYVAVLGMGKAVEKTLALGCHFQDQKNKKIEVYTKTIEVLDEVITEGQADIDMESDVEDDDKETQLKKRAVSGVELRIYV
Protein: Acetylcholine receptor subunit alpha (P02711)
Organism: Torpedo marmorata (Marbled electric ray)
Function: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLINVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTVLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIVTVVVINTHHRSPSTHTMPQWVRKIFINTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG
Protein: CD86 molecule (O35531)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- T-cell-specific surface glycoprotein CD28
- Cytotoxic T-lymphocyte protein 4
- T-lymphocyte activation antigen CD80
- CD40 ligand
- Inducible T-cell costimulator
- Tumor necrosis factor receptor superfamily, member 5, isoform CRA_a.
- T-cell surface glycoprotein CD4
- Intercellular adhesion molecule 1
- Tumor necrosis factor receptor superfamily member 4
- CD276 antigen
Sequence:
MYVVKTCVTCTMYLGILFSVLAYLLSDAVPVKRQAYFNSTAYLPCPFTKAQNISPSELVVFWQDRKKSVLYEHYLGAEKLDNVNAKYLGRTSFDRDNQALRLHNVQIKDTGLYDCFIQQKTPTGSIILQQWETELSVIANFSEPEIEEAQNETRNTGINLTCSSKQGYPKPTKMYFLITNSTNEYGDNMQISQDNVTKLFSVSISLSLPFPDGVYNMTIVCILETESMNISSKPHNMVFSQPQFDRKTWIQIAGPSSLLCCLFLLVVYKAVKKCLKMQNQPGRPSRKTCESKQDSGVDESINLEEVEPQLHQQ
Protein: Serine/threonine-protein kinase D6PKL1 (EC 2.7.11.1) (Serine/threonine-protein kinase AGC1-2) (Q9SUA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein kinase that regulates the auxin transport activity of PIN auxin efflux facilitators by direct phosphorylation. D6PK-mediated PIN phosphorylation promotes auxin transport in the hypocotyl and this is a prerequisite for PHOT1-dependent hypocotyl bending.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with PIN1 to the basal (lower) membrane of root cells. {ECO:0000250}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase Pin1
- Protein DUF642 L-GALACTONO-1,4-LACTONE-RESPONSIVE GENE 1
- Protein DETOXIFICATION 40
- Protein PELOTA 1
Sequence:
MASKYGSGVLPENKKEKGDKETPETSYSSQSVSVNTLADQVSSTLSFAPSSDSKTGGEVKFNEKSDQSGKSNTCRPSTSSDISDESTCSSFSGNNKPHKANDVRWEAIQAVRTKHGVLGLNHFRLLKRLGCGDIGTVHLAELHGTRCFFAMKVMDKGALASRKKLLRAQTEREILQCLDHPFLPTLYSHFETEKFSCLVMEFCPGGDLHTLRQRQPGKRFSEQAAKFYVAEVLLAMEYLHMLGIIYRDLKPENVLVRDDGHVMLSDFDLSLRCTVSPTVVRSTVLASEGQKNSGYCAQPACIQQPSCISAPTTCFSPRYFSSKSKKDKKMKNETGNQVSPLPELVAEPTSARSMSFVGTHEYLAPEIIKGEGHGSAVDWWTFGIFLYELLFGKTPFKGSGNRATLFNVVGQPLRFPESPVVSFAARDLIRSLLVKEPQHRLAYKRGATEMKQHPFFEGVNWALVRCASPPEIPKPVDYESAPATPAAATSTSVKSDQSNYLEFDFF
Protein: COP9 signalosome complex subunit 3 (Signalosome subunit 3) (Q5B0Y2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex seems to link protein degradation to sexual development.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 1
- Uncharacterized protein
- COP9 signalosome complex subunit 8
- Ubiquitin-like domain-containing protein
- RING-box protein 1
Sequence:
MSDFLAYLTSAPSRPHGSANITDKCYDHQLRDLIAYLKQPGVAPSTADINGYLEAISPAVHSLSYLYLLRIRIQQLQEKTAVGVPNDLQPGGTLWNQTVKFLRSFDPIQIRYVGHEWRELVDSVANAALSVSKPILAVKMIRDALERLNTAGVFTSLHLMLVKLALLSSSYTYVLPVLDKLLCHFPSDTQNAHAGILLCSEHEPSTVFFTDSSGFSANLTYRDHLQFYMYSGMVYMALKKWDQASHCLGIVISAPTANSVSKIMVEAYKKWVLANLLGHGKLFSVPNLVAPHVTRVYQSLSKPYISLAEAFEKRDFQRLRTEISLGQTIWRADKNSGLVYQVFEAYDKFLIIKLGKTFSALTMPDVLQRASSCSKGSRDIEEFVVSLVMTKELRAKLSHSPGNETTTMLRFPLSSQSHALREEHIRFRLIQKEAALNTISRAITQTKITLETSHENLQVIAKNQKLAGSSERSGVVGSTEADGGGDLDEDLMGDGR
Protein: Crustapain (EC 3.4.22.-) (NsCys) (Q86GF7)
Organism: Pandalus borealis (Northern red shrimp)
Function: Cysteine protease which may be involved in digestion. Shows highest affinity for proline at the P2 position. Cleaves valine more efficiently than leucine and exhibits 10-fold lower affinity for phenylalanine than proline. Can cleave type I collagen.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MRSLFLILLGLAAVSAIGEWENFKTKFGKKYANSEEESHRMSVFMDKLKFIQEHNERYDKGEVTYWLKINNFSDLTHEEVLATKTGMTRRRHPLSVLPKSAPTTPMAADVDWRNKGAVTPVKDQGQCGSCWAFSAVAALEGAHFLKTGDLVSLSEQNLVDCSSSYGNQGCNGGWPYQAYQYIIANRGIDTESSYPYKAIDDNCRYDAGNIGATVSSYVEPASGDESALQHAVQNEGPVSVCIDAGQSSFGSYGGGVYYEPNCDSWYANHAVTAVGYGTDANGGDYWIVKNSWGAWWGESGYIKMARNRDNNCAIATYSVYPVV
Protein: Ataxin-3 homolog (EC 3.4.19.12) (MJD1a-like) (Machado-Joseph disease-like protein) (Q9M391)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Interacts with key regulators of transcription and represses transcription. Acts as a histone-binding protein that regulates transcription. Acts as a deubiquitinating enzyme (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cell division control protein 48 homolog A
- Josephin protein-like protein
- Cell division control protein 48 homolog E
- Cell division control protein 48 homolog D
- AAA-type ATPase family protein / ankyrin repeat family protein
- Cell division control protein 48 homolog B
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin-ribosomal protein eL40z fusion protein
- Ubiquitin-ribosomal protein eS31z fusion protein
Sequence:
MERTSNGGMLYHEVQESNLCAVHCVNTVLQGPFFSEFDLAAVAADLDGKERQVMLEGAAVGGFAPGDFLAEESHNVSLGGDFSIQVLQKALEVWDLQVIPLNCPDAEPAQIDPELESAFICHLHDHWFCIRKVNGEWYNFDSLLAAPQHLSKFYLSAFLDSLKGAGWSIFIVKGNFPQECPMSSSSEASNSFGQWLSPEDAERIRKNTSSGSSARNKRSNDNVNQQRRNQALSREEVQAFSEMEDDDLKAAIAASLLDASAAEANLGAVGTSEKETEKQK