wanglab/gogpt-training-data huggingface dataset:
Protein: Metalloproteinase inhibitor 3 (Tissue inhibitor of metalloproteinases 3) (TIMP-3) (P48032)
Organism: Rattus norvegicus (Rat)
Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P35625}.
Interaction partners:
- Matrix metalloproteinase-9
- 72 kDa type IV collagenase
- Disintegrin and metalloproteinase domain-containing protein 17
- EGF-containing fibulin-like extracellular matrix protein 1
- Matrilysin
- Stromelysin-1
- Vascular endothelial growth factor receptor 2
- A disintegrin and metalloproteinase with thrombospondin motifs 5
- Collagenase 3
- Matrix metalloproteinase-14
Sequence:
MTPWLGLVVLLSCWSLGHWGTEACTCSPSHPQDAFCNSDIVIRAKVVGKKLVKEGPFGTLVYTIKQMKMYRGFSKMPHVQYIHTEASESLCGLKLEVNKYQYLLTGRVYEGKMYTGLCNFVERWDHLTLSQRKGLNYRYHLGCNCKIKSCYYLPCFVTSKKECLWTDMLSNFGYPGYQSKHYACIRQKGGYCSWYRGWAPPDKSISNATDP
Protein: Proline-rich nuclear receptor coactivator 2 (Q9NPJ4)
Organism: Homo sapiens (Human)
Function: Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery. May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs. Required for UPF1/RENT1 localization to the P-body. Plays a role in glucocorticoid receptor-mediated mRNA degradation by interacting with the glucocorticoid receptor NR3C1 in a ligand-dependent manner when it is bound to the 5' UTR of target mRNAs and recruiting the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Also acts as a nuclear receptor coactivator. May play a role in controlling the energy balance between energy storage and energy expenditure (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19150429}. Cytoplasm, P-body {ECO:0000269|PubMed:19150429}.
Interaction partners:
- mRNA-decapping enzyme 1A
- Regulator of nonsense transcripts 1
- Nonsense-mediated mRNA decay factor SMG5
- m7GpppN-mRNA hydrolase
- Estrogen-related receptor gamma
- Nonsense-mediated mRNA decay factor SMG7
- Telomerase-binding protein EST1A
- Nonsense-mediated mRNA decay factor SMG8
- COMM domain-containing protein 7
- Regulator of nonsense transcripts 2
Sequence:
MGGGERYNIPAPQSRNVSKNQQQLNRQKTKEQNSQMKIVHKKKERGHGYNSSAAAWQAMQNGGKNKNFPNNQSWNSSLSGPRLLFKSQANQNYAGAKFSEPPSPSVLPKPPSHWVPVSFNPSDKEIMTFQLKTLLKVQV
Protein: Ribonucleoside-diphosphate reductase small subunit (EC 1.17.4.1) (Ribonucleotide reductase small subunit) (P0C701)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Subcellular location: Host membrane {ECO:0000255|HAMAP-Rule:MF_04028}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04028}.
Interaction partners:
Sequence:
MSKLLYVRDHEGFACLTVETHRNRWFAAHIVLTKDCGCLKLLNERDLEFYKFLFTFLAMAEKLVNFNIDELVTSFESHDIDHYYTEQKAMENVHGETYANILNMLFDGDRAAMNAYAEAIMADEALQAKISWLRDKVAAAVTLPEKILVFLLIEGIFFISSFYSIALLRVRGLMPGICLANNYISRDELLHTRAASLLYNSMTAKADRPRATWIQELFRTAVEVETAFIEARGEGVTLVDVRAIKQFLEATADRILGDIGQAPLYGTPPPKDCPLTYMTSIKQTNFFEQESSDYTMLVVDDL
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10-B (Q94C12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase iron-sulfur protein 8-A, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- NADH dehydrogenase iron-sulfur protein 6
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 13-A
Sequence:
MGRKKGLPEFEESAPDGFDPENPYKDPVAMVEMREHIVREKWIQIEKAKILREKVKWCYRVEGVNHYQKCRHLVQQYLDSTRGVGWGKDHRPISLHGPKPEAVEAE
Protein: Cyclic nucleotide gated channel subunit alpha 3 (A0A0G2JVT7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
GHQYLLSPSRVSRFIISIRAWAARHLHHEDPTPDSFLDRFHGAELKEVSSQERNAQPNPGGQEPPEGGKGRKKDPIVVDPSSNIYYRWLTAIALPVFYNWCLLVCRACFDELQSEHLTLWLVLDYSADALYVVDMLVRARTGFLEQGLMVRDTKRLWKHYTKTLHFKLDILSLIPTDLAYLKLGMNYPELRFNRLLRFSRLFEFFDRTETRTNYPNVFRIGNLVLYTLIIIHWNACIYFAISKFIGFGTDSWVYPNTSKPEYGRLSRKYIYSLYWSTLTLTTIGETPPPVKDEEYLFVVIDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSIKQYMQFRKVTKDLETRVIRWFDYLWANRKTVDEKEVLKNLPDKLKAEIAINVHLDTLKKVRIFQDCEAGLLVELVLKLRPAVFSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMETLTEYPDAKRALEEKGRQILMKDNLIDDDLVTARADARNIEEKVEYLESSLDGLQTRFARLLAEYSASQMKLKQRLSQLESQMTRRGHGFSPDRENSEDASKAD
Protein: VIRF-1 (F5HF68)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Plays a role in the inhibition of host innate response by repressing the expression of interferon-inducible genes and blocking host IRF1- and IRF3-mediated transcription. Blocks the interaction between host IRF3 and CREBBP. Regulates the host cellular metabolism by increasing glucose uptake, ATP production and lactate secretion through down-regulation of heterogeneous nuclear ribonuclear protein Q1/SYNCRIP. Mechanistically, induces ubiquitination and degradation of SYNCRIP through the ubiquitin-proteasome pathway by recruiting KLHL3/CUL3 ubiquitin ligase complex. Disrupts host TP53 signaling pathway during viral infection by interacting with host USP7 and thereby decreasing the availability of USP7 for deubiquitinating and stabilizing TP53.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:35538151, ECO:0000269|PubMed:37459327}.
Interaction partners:
Sequence:
MDPGQRPNPFGAPGAIPKKPCLSQGSPGTSGSGAPCDEPSRSESPGEGPSGTGGSAAAGDITRQAVVAAITEWSRTRQLRISTGASEGKASIKDWIVCQVNSGKFPGVEWEDEERTRFRIPVTPLADPCFEWRRDGELGVVYIRERGNMPVDASFKGTRGRRRMLAALRRTRGLQEIGKGISQDGHHFLVFRVRKPEEEQCVECGVVAGAVHDFNNMARLLQEGFFSPGQCLPGEIVTPVPSCTTAEGQEAVIDWGRLFIRMYYNGEQVHELLTTSQSGCRISSALRRDPAVHYCAVGSPGQVWLPNVPNLACEIAKRELCDTLDACAKGILLTSSCNGIFCVCYHNGPVHFIGNTVPPDSGPLLLPQGKPTRIFNPNTFLVGLANSPLPAPSHVTCPLVKLWLGKPVAVGKLEPHAPSPRDFAARCSNFSDACVVLEIMPKPLWDAMQ
Protein: Probable glycine dehydrogenase (decarboxylating) (EC 1.4.4.2) (Glycine cleavage system P-protein) (Glycine decarboxylase) (Glycine dehydrogenase (aminomethyl-transferring)) (P9WN53)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity).
Interaction partners:
- Glycine cleavage system H protein
- Aminomethyltransferase
- Serine hydroxymethyltransferase 1
- Serine hydroxymethyltransferase 2
- Multifunctional 2-oxoglutarate metabolism enzyme
- Phosphoribosylamine--glycine ligase
- Glutamate synthase large chain
- Dihydrolipoyl dehydrogenase
- D-amino-acid oxidase
- NAD-specific glutamate dehydrogenase
Sequence:
MSDHSTFADRHIGLDSQAVATMLAVIGVDSLDDLAVKAVPAGILDTLTDTGAAPGLDSLPPAASEAEALAELRALADANTVAVSMIGQGYYDTHTPPVLLRNIIENPAWYTAYTPYQPEISQGRLEALLNFQTLVTDLTGLEIANASMLDEGTAAAEAMTLMHRAARGPVKRVVVDADVFTQTAAVLATRAKPLGIEIVTADLRAGLPDGEFFGVIAQLPGASGRITDWSALVQQAHDRGALVAVGADLLALTLIAPPGEIGADVAFGTTQRFGVPMGFGGPHAGYLAVHAKHARQLPGRLVGVSVDSDGTPAYRLALQTREQHIRRDKATSNICTAQVLLAVLAAMYASYHGAGGLTAIARRVHAHAEAIAGALGDALVHDKYFDTVLARVPGRADEVLARAKANGINLWRVDADHVSVACDEATTDTHVAVVLDAFGVAAAAPAHTDIATRTSEFLTHPAFTQYRTETSMMRYLRALADKDIALDRSMIPLGSCTMKLNAAAEMESITWPEFGRQHPFAPASDTAGLRQLVADLQSWLVLITGYDAVSLQPNAGSQGEYAGLLAIHEYHASRGEPHRDICLIPSSAHGTNAASAALAGMRVVVVDCHDNGDVDLDDLRAKVGEHAERLSALMITYPSTHGVYEHDIAEICAAVHDAGGQVYVDGANLNALVGLARPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPVAVRAHLAPFLPGHPFAPELPKGYPVSSAPYGSASILPITWAYIRMMGAEGLRAASLTAITSANYIARRLDEYYPVLYTGENGMVAHECILDLRGITKLTGITVDDVAKRLADYGFHAPTMSFPVAGTLMVEPTESESLAEVDAFCEAMIGIRAEIDKVGAGEWPVDDNPLRGAPHTAQCLLASDWDHPYTREQAAYPLGTAFRPKVWPAVRRIDGAYGDRNLVCSCPPVEAFA
Protein: Putative ribosomal recycling factor, mitochondrial (O74734)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Necessary for protein synthesis in mitochondria. Functions as a ribosome recycling factor in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein uL24
- Elongation factor Ts, mitochondrial
Sequence:
MFRIISKATLFQDSQRFHTSILSPRCAFHNGGILHKKAKDKDVKHDHDPEFANSFNKMLKSFEAKMQLVHEKLAKRFQEAVVLPSQGNFTQLEALFIPSKSIKAPTPSRLLREIAAVSQKGSQQIIIRPFEDVDIKNILKAIEDSRYPFVANKLNASTIEVKPQRTTLESRQQLAKVLEGYAKDSREQLSAMRTELKKEIAKNKKSKAWTSDDCYKAEAEMQTAFKNAINLLDSGLKSALKKVI
Protein: Asparagine synthetase domain-containing protein YML096W (Q04489)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MCGILLHYCPNNNYLNDELIEFPEGTEFGDTTCTNESSIFNKIIPYIAARGPNYSSLRAVKAYRISWFSSVLSLRQPFTKQSINVDDRYFLQFNGELYNKEISQGDNDSLYIASMLQNLKEGMGVIDVIKSLEGEYAYTIYDVNSSKLYFGRDPIGRRSLSYSVTPDNELYVASVTGSAGSFQDCIGGVIYEYDTRTKLLNSNQRSHLPYEVTSEIDLNFTSLSEVSKNLYAVLRDSVKKRVESIHPRHIENSPIAVLFSGGIDCSVIVALICEVLQENDYKCGKPVIELLNVSFENPRTGLFPSDTPDRKLSINSAKTLQNLYPNVDIKLVEVDVPYDEYLKWKPFVINLMYPKQTEMDLSIAIAFFFASRGRGFLTSLNGERTPYQRHGIVLFSGLGADELYGGYHKFANKPPHELVEELTRQINNIYDRNLNRDDKVIAHNGVEVRYPFLDEYVIKLSTAEIPINFKVNKLILRKVASQYLKLDGISSEPKRAIQFGAKSAKMTKDGNKHGTDLLKENRNCS
Protein: Cytochrome b-c1 complex subunit 8 (Complex III subunit 8) (Complex III subunit VIII) (Ubiquinol-cytochrome c reductase complex 9.5 kDa protein) (Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C) (O14949)
Organism: Homo sapiens (Human)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08525}.
Interaction partners:
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Cytochrome b-c1 complex subunit 10
- Cytochrome c oxidase subunit 6B1
Sequence:
MGREFGNLTRMRHVISYSLSPFEQRAYPHVFTKGIPNVLRRIRESFFRVVPQFVVFYLIYTWGTEEFERSKRKNPAAYENDK
Protein: LD15927p (Wings apart, isoform A) (Wings apart, isoform B) (Wings apart, isoform C) (Wings apart, isoform D) (Q9VR53)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein kinase minibrain
- non-specific serine/threonine protein kinase
- DNA damage-binding protein 1
- Cullin-4A
- Putative dual specificity tyrosine-phosphorylation-regulated kinase 3 homolog
- Dual specificity tyrosine-phosphorylation-regulated kinase 2
- Chromatin assembly factor 1 p55 subunit
- GH05923p
Sequence:
MSSTAGKRKEIYKYLAPWPLYSMNWSVRPDKRFRLALGSFIEEYNNKVQIISLDEDTSEFSAKSTFDHPYPTTKIMWIPDSKGVYPDLLATSGDYLRVWRAGEPDTRLECVLNNNKNSDFCAPLTSFDWNEVDPNLVGTSSIDTTCTIWGLETGQPHARVYVAGHVKTQLIAHDKEVYDIAFSRAGGGRDMFASVGADGSVRMFDLRHLEHSTIIYEDPAHTALLRLAWNKQDPNYLATVAMDSCEVIILDVRVPCTPVARLSNHRACVNGIAWAPHSSCHICTAGDDHQALIWDIQQMPRAIEDPILAYTAAEGEVNQIQWGATQPDWIAICYNKACEILRV
Protein: Gustatory and pheromone receptor 32a (Q9VKJ7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Required for the response to N,N-Diethyl-meta-toluamide (DEET), the most widely used insect repellent worldwide. Functions as a pheromone receptor for a male inhibitory pheromone and promotes male-male aggression and suppresses male-male courtship. Also promotes preferentially virgin females courting over mated females.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Gustatory receptor for bitter taste 66a
- Gustatory and pheromone receptor 33a
- Putative gustatory receptor 59c
- Gustatory receptor for bitter taste 22e
- Phenoloxidase-activating factor 2
- Dynein axonemal assembly factor 1 homolog
- Uncharacterized protein, isoform C
- FI08446p
- AT29763p
- GH08353p
Sequence:
MSPNTWVIEMPTQKTRSHPYPRRISPYRPPVLNRDAFSRDAPPMPARNHDHPVFEDIRTILSVLKASGLMPIYEQVSDYEVGPPTKTNEFYSFFVRGVVHALTIFNVYSLFTPISAQLFFSYRETDNVNQWIELLLCILTYTLTVFVCAHNTTSMLRIMNEILQLDEEVRRQFGANLSQNFGFLVKFLVGITACQAYIIVLKIYAVQGEITPTSYILLAFYGIQNGLTATYIVFASALLRIVYIRFHFINQLLNGYTYGQQHRRKEGGARARRQRGDVNPNVNPALMEHFPEDSLFIYRMHNKLLRIYKGINDCCNLILVSFLGYSFYTVTTNCYNLFVQITGKGMVSPNILQWCFAWLCLHVSLLALLSRSCGLTTTEANATSQILARVYAKSKEYQNIIDKFLTKSIKQEVQFTAYGFFAIDNSTLFKIFSAVTTYLVILIQFKQLEDSKVEDPVPEQT
Protein: Alpha-amylase MalA (EC 3.2.1.1) (L8B068)
Organism: Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1)
Function: Alpha-amylase that cleaves starch into oligosaccharides, the first step in starch degradation (By similarity). Endo-acting enzyme which prefers a linear polysaccharide to branched polysaccharides hydrolyzing alpha-1,4 glucosidic bonds efficiently. Has also transglycosylation activity, but does not act on alpha-1,6 bonds. Higher activities of 100%, 79% and 67.8% against amylose, soluble starch and amylopectin, respectively. Lower activity of 22% against glycogen and faint or no activity against alpha-, beta- and gamma-cyclodextrin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23391916}.
Interaction partners:
Sequence:
MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYERFIEAAHDRGFKVLFDLVCNHSARTHPYFESAVEGPDADYREWYEWRSDTEPETYFEWEHIANFNFDHLPVRRHLLDAVAQWADLVDGFRCDMAWAVPNGFWREIHDYCKDRDSEFLLLDETIPYIPDFQAGLFDMHFDSTTYAALRQVGGGGDAEAILGAIEGRAEIGFPEHASFMLYAENHDETRYIVDYGREAAEAAAGALFTLPGAPLLYAGQEFGQRGRRDDLAWDHADETLQSFVSDLASARHDQPALSADADLVRIPYEVRDGPSDRVVAYARTTENDAAVVVLNFGSEPTTVGLPAGTDGTDLVSGEYRGAAGDGDATVTVDSVSVFPADENDLRQ
Protein: Microcephalin (Q8NEM0)
Organism: Homo sapiens (Human)
Function: Implicated in chromosome condensation and DNA damage induced cellular responses. May play a role in neurogenesis and regulation of the size of the cerebral cortex.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16479174}.
Interaction partners:
- Abnormal spindle-like microcephaly-associated protein
- CDK5 regulatory subunit-associated protein 2
- SCL-interrupting locus protein
- Telomeric repeat-binding factor 2
- Centrosomal P4.1-associated protein
- Condensin-2 complex subunit D3
- Centrosomal protein of 152 kDa
- Condensin-2 complex subunit G2
- Breast cancer type 2 susceptibility protein
- Mediator of DNA damage checkpoint protein 1
Sequence:
MAAPILKDVVAYVEVWSSNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHIDESLFPAANMNEHLSSLIKKKRKCMQPKDFNFKTPENDKRFQKKFEKMAKELQRQKTNLDDDVPILLFESNGSLIYTPTIEINSRHHSAMEKRLQEMKEKRENLSPTSSQMIQQSHDNPSNSLCEAPLNISRDTLCSDEYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQRNIAGKVVTPDQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPRLQLCRSEDRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCVGKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTSAPEEALRCCRQAGKEDACPEGNGFSYTIEDPALPKGHDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYSGSVKNRPTRHDVLDDSCDGFKDLIKPHEELKKSGRGKKPTRTLVMTSMPSEKQNVVIQVVDKLKGFSIAPDVCETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELGHWISEEPFELSHHFPAAPLCRSECHLSAGPYRGTLFADQPAMFVSPASSPPVAKLCELVHLCGGRVSQVPRQASIVIGPYSGKKKATVKYLSEKWVLDSITQHKVCAPENYLLSQ
Protein: Glycoprotein 24B (gp24B) (Contact site B protein B) (P16643)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Cell-cell adhesion during early development.
Subcellular location: Cell surface.
Interaction partners:
Sequence:
MTDLKITLVNEDGESTISGKGHPLPAPLIFPPIYCFCFIQYKTEGKLWDKNDFQIKSGKIEFGGEEYDITESKGTWSKDDEENHIKVSLHLIVPPKKIFQKNF
Protein: Ski protein homolog (Abnormal dauer formation protein 5) (G5EDM7)
Organism: Caenorhabditis elegans
Function: Probable component of transcriptional regulatory complex with SMAD protein daf-3. Required to regulate entry into a developmentally arrested larval state known as dauer, in response to harsh environmental conditions. Involved in larvae undergoing cell-cycle arrest during the dauer stage.
Subcellular location: Nucleus {ECO:0000269|PubMed:14681186}.
Interaction partners:
- Dwarfin sma.
- Smad protein daf-8
- Cell surface receptor daf-1
- Smad-related protein daf-14
- Dauer larva development regulatory growth factor daf-7
- Dwarfin sma-4
- Cell surface receptor daf-4
- Nuclear hormone receptor family member daf-12
- Dwarfin sma-3
- INTegrator complex Subunit homolog
Sequence:
MSDSPIGSSQQVEPEHRTPDLMDIDPLIANLKALHEETRSDDDDDGQPSTSAKRKDSRADGIVIHQKKYSDPGRFLWIWLLGVRVPALSIDGEPHLPIEILDDMLTKKDKKDQMSFQNLLRYKNVYIRMASPSQFRAVMEKSKECENLNITSLSLMSRSDIERIMGELRLESMLTLAEHDNWDISDRVHVVHVNFIDYCSEWLESDDLEEDVMQSGTHGYWYKNRRNMRCIECQHCEGKFTPTDFIMHHHYPIKPSGFVHTGCNSFQWIRLIEVFDKSNENLEAWNKFVLNSHRAGKREYDEAAPHQAPPKRPAMETPVPVAADNGWEADEEEEGEEIVDRDADIEKCKLRNKKKMENLHIADFLGPSGSKGLKPRNKFEAVIIEQLNKMDDAALEALFLKSPEEYNLWVKESDFTHKVVTQQQEWKAKMKDPNFKSRASANFDVSKGEFDNMRHFDNASKATRQEIQQLAEQFANLDRDAKLLTPMEFVLREHALLKNVSADAIRVLCNRPPLPPLPPPPPPPKPKPAPVQPISLGNINFVALAQQLIASGIKLPLPIVTPPVVSTPAPVITPIPAALPISPNSDFLKQQLSTAMSSPALLSLYPKLTAGAYEQLAQFIKTTTVKN
Protein: 65 kDa invariant surface glycoprotein (Q587F4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMKYLLVFAIIATRISVLLATNGGDKHVKANKKLTKEGAAALCKMKHLADKVAEERSQELKDRTQNFAGYIEFELYRIDYWLEKLNGPKGRKDGYAKLSDSDIEKVKEIFNKAKDGITKQLPEAKKAGEEAEKLHTEVKKAAKNARGVRLSEGTNSSGLYRILDWYCFKEGENAGKSDNCDGVKFSVHYETHRRRNVIDCSSTGYEENYDWSANALQVALNSWENVKPKKLESAGSDMNCNIGQSSESHPCTMTEEWQTPYKETVEKLRELEDAYQRGKKAHDAMLGYANTAYAVNTKVEQEKPLTEVIAAAKEAGKKGAKIIIPAAAPATPTNSTKNEDSASTEHVDRGIATNETQVEVGIDADFDSLLDATEAAEVTRRHQRTAMIILAVLVPAIILVVTAFAFFIMVKRRRNSSKDVDTGKAEGGVSSVKVVM
Protein: 3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase) (Beta-Ketoacyl-acyl carrier protein reductase) (Beta-ketoacyl-ACP reductase) (P0AEK2)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Acyl carrier protein
- Enoyl-[acyl-carrier-protein] reductase FabI
- Phosphate acyltransferase
- Large ribosomal RNA subunit accumulation protein YceD
Sequence:
MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV
Protein: Estrogen-related receptor gamma b (B3DIZ0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MSFSGHCPPYIKTEPSSPSSLSDSLTQHSPGASSDAGSSYSSGPKGNLAGLDSPASYLRSAPCRLLEEAQAKGEYGLSSGPKRLCLVCGDVASGFHYGVASCEACKAFFKRTIQGNIEYSCSVSRDCEITKRRRKSCQACRFTKCLSVGMLREGVRLDRVRGGRQKYKRRIDSDSSVYLSVPLPHRKPVSCSAHAENKVVTLLLGAEPEKVCAMPDPALPDSDIKALTTLCDLADRELVLNISWAKHIPGFSSLSLSDQMSLLQSAWMEILVLRVAFRSLPCDDRLLFADDYIMDAEQAKCAGLLELHTAILQLVRRYRCMSLEREEFVTLKAIALANSDSMHIEDVEAVQGLQDALHEALLDYECVHHSEDPRRAGKLIMTLPLLRQTSAKAVRHFCSIKQDGRVPMHKLFLELLEANI
Protein: Calcium uniporter protein, mitochondrial (cMCU) (Q21121)
Organism: Caenorhabditis elegans
Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit (By similarity). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways (By similarity). Required for rapid mitochondrial calcium uptake and mitochondrial reactive oxygen species (mtROS) production after wounding. In addition, together with mitochondrial calcium regulator micu-1, required for mitochondrial calcium uptake following axon injury in PLM touch receptor neurons.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8NE86}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NE86}.
Interaction partners:
- Calcium uptake protein 1 homolog
- Essential MCU regulator
- EF-hand domain-containing protein
- Inositol 1,4,5-trisphosphate receptor itr-1
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
Sequence:
MRNGRCLVTPFVTAQRLANLRNTLWNRQQIAFSTTTASSSTSPIQESSSPLSIRFEYGLPLLDVPLPSRNEPCQFTMRPLSDTIGSLCEFLRQEDRGIDYVAVYGTNGVKLATCTSIEHLLQFGSFRLRLNDKFFDVTVPKTGTMPYDSDKLRQLDDLRATVASLHAALCVDEYKLSREKKLLLQLENAETLLAPLHDAKRKIEQECEAHTDRVMWAGFAAMGVQTGLFARLTWWEYSWDIMEPVTYFATYSTVCATFGYYLYTQQSFEYPSARERVYTKQFYRRAQKQNFDIEKYNRLVTEVDELRNQLKRMRDPLFQHLPVSYLSNLEAEK