wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase RIO2 (EC 2.7.11.1) (Q95Q34)
Organism: Caenorhabditis elegans
Function: Required for larval development.
Interaction partners:
- Protein LTV1 homolog
- RNA-binding protein NOB1
- Pre-rRNA-processing protein TSR1 homolog
- KRR1 small subunit processome component
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Uncharacterized protein byn-1
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS10
Sequence:
MGRMNVSMMRYLEGDHFRVLIAVEMGMKNHEVVPLALVSAIAGIHRGGVARTLNDLCKHSLVAFERSKKFDGYRLTIRGYDYLALRALCSREVVGSVGNQIGIGKESDVYVGGDPELNDLCLKFHRLGRTSFRKIKEKRDYHKKRKSASWLYLSRLAAAKEFAFLKALQERGFPVPKAVDVCRHLVVMQLVVGQTLCNVTHVEDAGALYDRLMALIVKMARHGVIHGDFNEFNLIMLEDERIVMIDFPQMVSIDHPNAEYYFDRDVTCVRTFFKRKFDYESEDWPKFDEVERKGNMDVLLEASGFTKKMALDLNKAYDEGDFLAHCEQELRNRQEEDLGEDEDDSDDSKSMEDIQEEPEDLEKDHEELQAQENTVKQQKIVLSQTTRFTDWLSDATNQLEAVDLDALKSEEGYKDIELPPEDFKRPADSENDDENDEDEEEGEEEDADGHVAVEEQVAKVVKKKRVPSGARSVASSAATFTAEDVKRRLALDRKRNKEKIRLKVKGKQSAVGRNRKDNKDVIAEYAGWI
Protein: Ras-related protein Rab5 (Drab5) (EC 3.6.5.2) (Small monomeric GTPase Rab5) (Q9V3I2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Perikaryon {ECO:0000269|PubMed:12876219}. Early endosome {ECO:0000269|PubMed:12743108, ECO:0000269|PubMed:12876219}. Endosome, multivesicular body {ECO:0000269|PubMed:12876219}. Presynapse {ECO:0000269|PubMed:12743108}. Presynaptic endosome {ECO:0000269|PubMed:12743108}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:12743108, ECO:0000269|PubMed:12876219}. Cytoplasm, cytosol {ECO:0000269|PubMed:12743108}. Cytoplasm {ECO:0000269|PubMed:19050045}. Cytoplasm, cell cortex {ECO:0000269|PubMed:19050045, ECO:0000269|PubMed:23418349}. Note=The GDP-bound form localizes mainly to the cytosol and does not associate with vesicles (PubMed:12743108). During early oogenesis localizes homogenously to the cytoplasm of germline cells (PubMed:19050045). From stage 8, corresponding to yolk-protein uptake, accumulates at the cell cortex in a phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) dependent process, particularly in the oocyte (PubMed:19050045). {ECO:0000269|PubMed:12743108, ECO:0000269|PubMed:19050045}.
Interaction partners:
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Rabaptin-5-associated exchange factor for Rab5
- LD29542p
- LD23155p
- Rab GDP dissociation inhibitor
- Vacuolar fusion protein MON1 homolog
- FI04419p
- Vacuolar protein sorting-associated protein 8 homolog
- Vacuolar fusion protein CCZ1 homolog
- Uncharacterized protein, isoform C
Sequence:
MATTPRSGGASGTGTAQRPNGTSQNKSCQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTICIEDTVVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDIQNQDSFQRAKTWVKELHKQASPNIVIALAGNKADLSNIRVVEFDEAKQYAEENGLLFMETSAKTGMNVNDIFLAIAKKLPKNDGANNQGTSIRPTGTETNRPTNNCCK
Protein: Caspase-1 (A0A060XPX2)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- CARD domain-containing protein
- Apoptosis-associated speck-like protein containing a CARD
- Apoptosis-associated speck-like protein containing a CARD
- CARD domain-containing protein
- Interleukin-1
- Interleukin-1
- Uncharacterized protein
- Apoptotic protease-activating factor 1 winged-helix domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MADKLLSKARKTFIDSVTKPVIKQLLDDLLEDKVLNDEETESVTEENSTRAEQARCLIDMVRKKGSKASDKMIARVQERDPGLYDKMGLAPTPSSPQLSQQEEQPVSSVLTPSTNDFKKDILQRKGSEIYPPMDKSGRKRLALLINNVEFDDKNMLRRGAEKDEEDVERLLRDLGYDVVKHRNLSGQEMDEAVKAFSKREEHLLSDSVFVVMMSHGELGAIMGVHYKKGDPNLDIFPINNIFTHLNTENCKALINKPKVILIQACRGGKDGSVWVSDTVPGSSLDLGLESDSFRREHKEKDFISLLSCTPDTVSYRDPEMGTLFVQRIMETFNTYACDDHIEELFRKASHGTL
Protein: CTP synthase 2 (EC 6.3.4.2) (CTP synthetase 2) (UTP--ammonia ligase 2) (P38627)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Plays an important role in the regulation of phospholipid synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- CTP synthase 1
- Nucleoside diphosphate kinase
- Golgi apyrase
- Adenylosuccinate synthetase
- Inosine-5'-monophosphate dehydrogenase 2
- GMP synthase
- Glutamine synthetase
- Multifunctional protein URA2
- Glutamate synthase
- Inosine-5'-monophosphate dehydrogenase 3
Sequence:
MKYVVVSGGVISGIGKGVLASSTGMLLKTLGLKVTSIKIDPYMNIDAGTMSPLEHGECFVLDDGGETDLDLGNYERYLGITLSRDHNITTGKIYSHVISRERRGDYLGKTVQIVPHLTNAIQDWIQRVSKIPVDDTGLEPDVCIIELGGTVGDIESAPFVEALRQFQFEVGRENFALIHVSLVPVIHGEQKTKPTQAAIKDLRSLGLIPDMIACRCSEELNRSTIDKIAMFCHVGPEQVVNVHDVNSTYHVPLLLLKQHMIDYLHSRLKLGEVPLTLEDKERGSQLLTNWENMTKNLDDSDDVVKIALVGKYTNLKDSYLSVTKSLEHASMKCRRQLEILWVEASNLEPETQEVDKNKFHDSWNKLSSADGILVPGGFGTRGIEGMILAAKWARESGVPFLGVCLGLQVAAIEFARNVIGRPNSSSTEFLDETLLAPEDQVVIYMPEIDKEHMGGTMRLGLRPTIFQPNSEWSNIRKLYGEVNEVHERHRHRYEINPKIVNDMESRGFIFVGKDETGQRCEIFELKGHPYYVGTQYHPEYTSKVLEPSRPFWGLVAAASGTLGEVIKDINLSEGNENE
Protein: Protein transport protein gos1 (Golgi SNAP receptor complex member 1) (Golgi SNARE protein 1) (Q09835)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Nonessential SNARE involved in retrograde transport within the Golgi complex.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Protein transport protein bet1
- Synaptobrevin homolog ykt6
- Integral membrane protein sed5
- Protein transport protein sft1
- Protein transport protein bos1
- Protein transport protein sec22
- Protein sly1
- t-SNARE affecting a late Golgi compartment protein 1
- Syntaxin pep12
- Intracellular protein transport protein uso1
Sequence:
MKSMLLRDSVKKASQFQRSLHSDPNQAKILLEERRKLLEEANSSADENDSHSMATIKSHFERLKRDEQLLNGVLKKYDAKQEVLSPEELRDAQNFLEMQEANSLDNSIRGTNELLERAYATREDFDYQNSVLGNVTNRINGAAMSIPFINQILRKTSIRRRRDSIILALLISVLMLLFLFFH
Protein: Centromere protein mis12 (NMS complex subunit mis12) (Q9Y738)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Required for correct segregation of chromosomes and for maintaining the inner centromere structure.
Subcellular location: Chromosome, centromere {ECO:0000269|PubMed:12773390}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12773390}.
Interaction partners:
- Kinetochore protein nnf1
- Kinetochore protein nuf2
- Kinetochore protein mis13
- Kinetochore protein mis14
- Inner kinetochore subunit mis6
- Kinetochore protein ndc80
- Outer kinetochore KNL1 complex subunit spc7
- Inner kinetochore subunit mis17
- Inner kinetochore subunit fta6
- Inner kinetochore subunit fta7
Sequence:
MLVELLEFTPLSFIDDVINITNQLLYKGVNGVDKAFSQTRFAKKAPQEIEEGLHKFEVLFESVVDRYYDGFEVYTLRNIFSYPPELKGYMRTFGKDVDYSITTEQDAAMDQAIQEAAEKLVVKMQLRRDLRMRLSRKREKKTEIEKHLERISFLNKVPENWQVTLPETTDFLLDQLGNLQHAVKRVVEASPTVHSREVDERITYLEKGYERLSNPIDQQKDFWSHHLSKLESTANTETANNIHKLLLSSEKDVGHTDEP
Protein: Uncharacterized protein YhfK (P45537)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- DNA-binding transcriptional dual regulator CRP
- Protein YhfA
- Chaperone protein YcdY
- Protein AmpE
- Inner membrane protein YeeA
- UPF0231 protein YacL
Sequence:
MFPPMWRRLIYHPDINYALRQTLVLCLPVAVGLMLGELRFGLLFSLVPACCNIAGLDTPHKRFFKRLIIGASLFATCSLLTQLLLAKDVPLPFLLTGLTLVLGVTAELGPLHAKLLPASLLAAIFTLSLAGYMPVWEPLLIYALGTLWYGLFNWFWFWIWREQPLRESLSLLYRELADYCEAKYSLLTQHTDPEKALPPLLVRQQKAVDLITQCYQQMHMLSAQNNTDYKRMLRIFQEALDLQEHISVSLHQPEEVQKLVERSHAEEVIRWNAQTVAARLRVLADDILYHRLPTRFTMEKQIGALEKIARQHPDNPVGQFCYWHFSRIARVLRTQKPLYARDLLADKQRRMPLLPALKSYLSLKSPALRNAGRLSVMLSVASLMGTALHLPKSYWILMTVLLVTQNGYGATRLRIVNRSVGTVVGLIIAGVALHFKIPEGYTLTLMLITTLASYLILRKNYGWATVGFTITAVYTLQLLWLNGEQYILPRLIDTIIGCLIAFGGTVWLWPQWQSGLLRKNAHDALEAYQEAIRLILSEDPQPTPLAWQRMRVNQAHNTLYNSLNQAMQEPAFNSHYLADMKLWVTHSQFIVEHINAMTTLAREHRALPPELAQEYLQSCEIAIQRCQQRLEYDEPGSSGDANIMDAPEMQPHEGAAGTLEQHLQRVIGHLNTMHTISSMAWRQRPHHGIWLSRKLRDSKA
Protein: COG-1B (Homeobox domain-containing protein) (G5EGF2)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MGRLQHSMQLSPNSLNMQKKQSRPTFTGHQIYQLERKFEQTKYLAGADRAQLAQELNMSESQVKVWFQNRRTKWRKKEAADNALVKRGASGDKSPCSLSPFLSAGI
Protein: Baeyer-Villiger monooxygenase 4 (BVMO4) (EC 1.14.13.-) (U5S003)
Organism: Dietzia sp. (strain D5)
Function: Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters or lactones using NADPH as an electron donor. Has a broad substrate scope and oxidizes different compounds including substituted and unsubstituted alicyclic, bicyclic-, aliphatic-ketones, ketones with an aromatic moiety, and sulfides. The highest activities are measured for 2- and 3-methylcyclohexanone, phenylacetone, bicyclo[3.2.0]hept-2-en-6-one and menthone. Cannot use NADH instead of NADPH. Is not active on benzaldehyde.
Interaction partners:
Sequence:
MPFTLPESKIAIDIDFDPDHLRQRFEADKQARERKDQLAQFQGLDDVLEVDDSDPFSEPITREPVTEELDALVLGGGFGGLTAGAYLTQNGVENFRLVEYGGDFGGTWYWNRYPGVQCDIESHIYMPLLEETGYVPSQRYADGSEIFEHAQRIGRHYGLYDRTYFQTRATHARWDEQIQRWEVTTDRGDRFVTRVLLRSNGALTKPQLPKVPGIGDFEGKIFHTSRWDYGYTGGSAAGDLAHLRDKRVAVVGTGATGVQVVPYLAQDAKELVVVQRTPSVVQPRNNRKTDPEWVASLTPGWQYERHDNFNGIISGHEVEGNLVDDGWTHLFPELTGQHLVDVPVGELPEGDQALVAELADMNLLMSAHARVDSIVTDPATADGLKPWFGYMCKRPCFNDEYLEAFNRPNVTLAASPAGIDGITSSGIVVAGTHYEVDCIIFATGFETGSGPAGIYGYDVIGREGHSMQEYFSEGARTFHGFFTHGFPNFVELGMSQTAYYVNFVYMLDRKARHAARLVRHLLDSGIGTFEPTAEAEADWVAEVRRSNEPREAYWGACTPGYYNGQGEVSKAVFRDVYNSSEIDFWNMIEAWWNSGRFEGLVFEPARDAVPVA
Protein: RING finger protein nenya (Q8IMM9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the formation of DNA double-strand breaks together with narya and vilya during the meiotic recombination process. Plays a redundant role with narya in chromosome segregation during female meiosis.
Interaction partners:
- RING finger protein vilya
- BcDNA.GH07066
- LD31543p
Sequence:
MFRIHCNKCFRRRNVEPTLIFHMTQCQHVLCASCLSESSTDKKCPLCKRDLRAIPIDKNLPPNVAQYFEDPLRFQQLYRKISKFQADQRASDNLGFYRQMQEHEKNESRLKGFCKMEAQFNQQIQKEKERIAELRAYIKYHEEEGLKEWPHATGVEKPWSNQARGLRPRTPSVTTSDNTQSDEHMTTFCLDSDIDCLEEDEPRRYVKKTFNGNIKDFHI
Protein: Aldehyde oxidase GLOX (EC 1.2.3.15) (Glyoxal oxidase) (GLOX) (Q01772)
Organism: Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylic acids by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include, methylglyoxal, glycolaldehyde, acetaldehyde, formaldehyde and glyoxal. May act as a source of extracellular hydrogen peroxide required for the oxidation reactions catalyzed by the lignin peroxidases (ligninases) and manganese peroxidases, both involved in lignin degradation.
Subcellular location: Secreted {ECO:0000269|PubMed:7592374}.
Interaction partners:
Sequence:
MLSLLAVVSLAAATLAAPAASDAPGWRFDLKPNLSGIVALEAIVVNSSLVVIFDRATGDQPLKINGESTWGALWDLDTSTVRPLSVLTDSFCASGALLSNGTMVSMGGTPGGTGGDVAAPPGNQAIRIFEPCASPSGDGCTLFEDPATVHLLEERWYPSSVRIFDGSLMIIGGSHVLTPFYNVDPANSFEFFPSKEQTPRPSAFLERSLPANLFPRAFALPDGTVFIVANNQSIIYDIEKNTETILPDIPNGVRVTNPIDGSAILLPLSPPDFIPEVLVCGGSTADTSLPSTSLSSQHPATSQCSRIKLTPEGIKAGWQVEHMLEARMMPELVHVPNGQILITNGAGTGFAALSAVADPVGNSNADHPVLTPSLYTPDAPLGKRISNAGMPTTTIPRMYHSTVTLTQQGNFFIGGNNPNMNFTPPGTPGIKFPSELRIETLDPPFMFRSRPALLTMPEKLKFGQKVTVPITIPSDLKASKVQVALMDLGFSSHAFHSSARLVFMESSISADRKSLTFTAPPNGRVFPPGPAVVFLTIDDVTSPGERVMMGSGNPPPTLE
Protein: DNA-binding protein scr1 (O14335)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in carbon catabolite repression. Represses the transcription of various genes including the inv1 gene.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SNF1-like protein kinase ssp2
- High-affinity glucose transporter ght5
- Glycerol dehydrogenase 1
- Fructose-1,6-bisphosphatase
Sequence:
MSEATTATTTGKPSRSTKNPDAPRPYKCPLCTKAFYRLEHQTRHIRTHTGEKPHVCTFPGCAKRFSRSDELTRHARIHTNANSRRNAAAAAAANNSARSSNSPAGNLEPSTNNAGVHMTNASMNPNVNPSYPVFIPQVGMSVAPPVATAAVSMSYPHHYSASVQQQQATFVSNGQPHNLPAQAQPATIYGIPDALHTTQNGTTIHVTGTPPGAVSQRSEPDSRLSSMNEMQLLASAAANQLDAAPRITPTKSSGVNLMPLSNAPSPPKQMNVVGSLPSSSNTSPNHLASVPNRGLTSNSSTGSFTKYTNGSSNSLYSNSSMQTPYLPSKSNSSTSLHSMYGVGTTAYAPQSLRYAHYNYLPYSRPSVSNGFDDDSSSSDFAHFRYQRRSRPVSPCSTAPSSPTFSTRSFSPTPDVTPLVTPAHSPRLRPMDDPSCVQLPSIRSLSLRPSQVPLIPPLKCDPNAFSASTPASGAVSRTPSSVSLSSLSNVNSSMPHKPASQSNVGPVRISSNRRSRKFSSSSRVSVSNLLAGSPPSPSSSTKSASSSYSTTTPAFSIGPLTPMTKP
Protein: U6 snRNA-associated Sm-like protein LSm7 (P53905)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, spliceosomal U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM7 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM7, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- LSM2-LSM8 complex subunit LSM8
- ATP-dependent RNA helicase DHH1
- LSM complex subunit LSM4
- Small nuclear ribonucleoprotein Sm D3
- 23 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- 13 kDa ribonucleoprotein-associated protein
- LSM1-LSM7 complex subunit LSM1
- LSM complex subunit LSM2
- Deadenylation-dependent mRNA-decapping factor PAT1
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
Sequence:
MHQQHSKSENKPQQQRKKFEGPKREAILDLAKYKDSKIRVKLMGGKLVIGVLKGYDQLMNLVLDDTVEYMSNPDDENNTELISKNARKLGLTVIRGTILVSLSSAEGSDVLYMQK
Protein: Type II inositol 1,4,5-trisphosphate 5-phosphatase (EC 3.1.3.36) (75 kDa inositol polyphosphate-5-phosphatase) (Phosphoinositide 5-phosphatase) (5PTase) (P32019)
Organism: Homo sapiens (Human)
Function: Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:7721860}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:17956944}. Early endosome membrane {ECO:0000269|PubMed:17956944}. Membrane {ECO:0000269|PubMed:7721860}; Peripheral membrane protein {ECO:0000305|PubMed:7721860}; Cytoplasmic side {ECO:0000305|PubMed:7721860}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q8K337}. Golgi apparatus {ECO:0000269|PubMed:17956944}.
Interaction partners:
- Inositol polyphosphate 5-phosphatase OCRL
- Inositol polyphosphate-4-phosphatase type I A
- Sesquipedalian-1
- Inositol polyphosphate 4-phosphatase type II
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Synaptojanin-1
- Synaptojanin-2
Sequence:
MDQSVAIQETLAEGEYCVIAVQGVLCEGDSRQSRLLGLVRYRLEHGGQEHALFLYTHRRMAITGDDVSLDQIVPVSRDFTLEEVSPDGELYILGSDVTVQLDTAELSLVFQLPFGSQTRMFLHEVARACPGFDSATRDPEFLWLSRYRCAELELEMPTPRGCNSALVTWPGYATIGGGRYPSRKKRWGLEEARPQGAGSVLFWGGAMEKTGFRLMERAHGGGFVWGRSARDGRRDEELEEAGREMSAAAGSRERNTAGGSNFDGLRPNGKGVPMDQSSRGQDKPESLQPRQNKSKSEITDMVRSSTITVSDKAHILSMQKFGLRDTIVKSHLLQKEEDYTYIQNFRFFAGTYNVNGQSPKECLRLWLSNGIQAPDVYCVGFQELDLSKEAFFFHDTPKEEEWFKAVSEGLHPDAKYAKVKLIRLVGIMLLLYVKQEHAAYISEVEAETVGTGIMGRMGNKGGVAIRFQFHNTSICVVNSHLAAHIEEYERRNQDYKDICSRMQFCQPDPSLPPLTISNHDVILWLGDLNYRIEELDVEKVKKLIEEKDFQMLYAYDQLKIQVAAKTVFEGFTEGELTFQPTYKYDTGSDDWDTSEKCRAPAWCDRILWKGKNITQLSYQSHMALKTSDHKPVSSVFDIGVRVVNDELYRKTLEEIVRSLDKMENANIPSVSLSKREFCFQNVKYMQLKVESFTIHNGQVPCHFEFINKPDEESYCKQWLNANPSRGFLLPDSDVEIDLELFVNKMTATKLNSGEDKIEDILVLHLDRGKDYFLSVSGNYLPSCFGSPIHTLCYMREPILDLPLETISELTLMPVWTGDDGSQLDSPMEIPKELWMMVDYLYRNAVQQEDLFQQPGLRSEFEHIRDCLDTGMIDNLSASNHSVAEALLLFLESLPEPVICYSTYHNCLECSGNYTASKQVISTLPIFHKNVFHYLMAFLRELLKNSAKNHLDENILASIFGSLLLRNPAGHQKLDMTEKKKAQEFIHQFLCNPL
Protein: Sodium/potassium/calcium exchanger 2 (Na(+)/K(+)/Ca(2+)-exchange protein 2) (Retinal cone Na-Ca+K exchanger) (Solute carrier family 24 member 2) (Q8BUN9)
Organism: Mus musculus (Mouse)
Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) (By similarity). Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UI40}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDLHQSPTARLLQKWCSHESPFGCRRHYNSRKKLKLIRVIGLVMGLVAVSTVPFSISAFTETDSQSNRGEASDMSGPRVAQGHRQRTLLDLNDKIRDYTPQPPASQEDQAENSTEHTQGDYPKDIFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLLMLITFFLDNVIMWWESLLLLTAYFAYVVFMKFNVQVERWVKQMISRNNVIKVTVPEAQAKSPTAGDKDGPTLPSKPRLQRGGSSASLHNSLMRNSIFQLMIHTLDPLAEELGSYGKLKYYDTMTEEGRFREKASILHKIAKKKCQVDENERQNGAANHVEKIELPNSTSTEVEMTPSSEASEPVQNGNLSHNIEAADAPKATETAEEEDDQPLSLSWPTNTRKQATFLIVFPIVFPLWITLPDVRKPASRKFFPITFFGSITWIAVFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWLLYTIIHRFSPVTVSSNGLFCAIVLLFIMLLFVILSIALCKWRMNKILGFIMFGLYFVFLVVSVLLEDKVLVCPVSI
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (EC 7.1.1.2) (Complex I-30kD) (CI-30kD) (NADH-ubiquinone oxidoreductase 30 kDa subunit) (Q9DCT2)
Organism: Mus musculus (Mouse)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 3
Sequence:
MAAAAARVWCRGLLGAASVGRGAGRPSVLWQHVRRESAAADKRPTVRPRSDVTHKQLSAFGEYVAEILPKYVQQVQVSCLDELEICIHPDGVIPTLTFLRDHTNAQFKSLADLTAVDVPTRQNRFEIVYNLLSLRFNSRIRVKTYADELTPIDSIVSVHIAANWYEREVWDMFGVFFFNHPDLRRILTDYGFEGHPFRKDFPLTGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWEAFPAYRQPPESLKLEAGDKKPETK
Protein: Sentrin-specific protease 3 (EC 3.4.22.-) (SUMO-1-specific protease 3) (Sentrin/SUMO-specific protease SENP3) (Smt3-specific isopeptidase 1) (Smt3ip1) (Q9EP97)
Organism: Mus musculus (Mouse)
Function: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability (By similarity). Deconjugates SUMO2 and SUMO3 from CDCA8 (By similarity). Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300 (By similarity). Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1 (By similarity). Plays a role in the regulation of sumoylation status of ZNF148 (By similarity). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. Deconjugates SUMO2 from KAT5 (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11029585}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:22872859}. Note=Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress (By similarity). Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (PubMed:22872859). {ECO:0000250|UniProtKB:Q9H4L4, ECO:0000269|PubMed:22872859}.
Interaction partners:
- Testis-expressed protein 10
- Ribosomal biogenesis protein LAS1L
- Small ubiquitin-related modifier 1
- Polynucleotide 5'-hydroxyl-kinase NOL9
- WD repeat-containing protein 18
- Proline-, glutamic acid- and leucine-rich protein 1
- Retinoblastoma-binding protein 5
- Small ubiquitin-related modifier 2
- Histone-lysine N-methyltransferase 2A
- Protein dpy-30 homolog
Sequence:
MKETIQGTGSWGPEPPGPGTTYSNPRRERLRWPLPPKPRLKSGGGFGPDPGSGTTVPTRRLPAPRPSFDASASEEEEEEEEEDEEEVAAWRLPPRWGQLGASQRSRALRPSHRKTCSQRRRRAMRAFQMLLYSKSTSLTFHWKLWGRHRGRRRNLAHPKNHLSPQEGGATPQVPSPCCRFDSPRGLPPPRLGLLGALMAEDGMRGSPPVPSGPPMEEDGLRWTPKSPLDPDSGLLSCTLPNGFGGLSGPEGERSLAPPDASILISNVCSIGDHVAQELFQSSDLGIAEEADRTGEKAGQHSPLREEHVTCVQSILDEFLQTYGSLIPLSTDEVVEKLEDIFQQEFSTPSRKSLVLQLIQSYQRMPGNAMVRGFRVSYKRHVLTMDDLGTLYGQNWLNDQVMNMYGDLVMDTVPEKVHFFNSFFYDKLRTKGYDGVKRWTKNVDIFNKELLLIPIHLEVHWSLISVDVRRRTITYFDSQRTLNRRCPKHIAKYLQAEAVKKDRLDFHQGWKGYFKMNVARQNNDSDCGAFVLQYCKHLALSQPFSFTQQDMPKLRRQIYKELCHCKLTV
Protein: Cell division cycle protein 16 homolog (Anaphase-promoting complex subunit 6) (APC6) (CDC16 homolog) (CDC16Hs) (Cyclosome subunit 6) (Q13042)
Organism: Homo sapiens (Human)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:7736578}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:7736578}. Note=Colocalizes with CDC27 to the centrosome at all stages of the cell cycle and to the mitotic spindle. {ECO:0000269|PubMed:7736578}.
Interaction partners:
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 10
- Fizzy-related protein homolog
- Anaphase-promoting complex subunit 13
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 5
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 4
Sequence:
MNLERLRKRVRQYLDQQQYQSALFWADKVASLSREEPQDIYWLAQCLYLTAQYHRAAHALRSRKLDKLYEACRYLAARCHYAAKEHQQALDVLDMEEPINKRLFEKYLKDESGFKDPSSDWEMSQSSIKSSICLLRGKIYDALDNRTLATYSYKEALKLDVYCFEAFDLLTSHHMLTAQEEKELLESLPLSKLCNEEQELLRFLFENKLKKYNKPSETVIPESVDGLQENLDVVVSLAERHYYNCDFKMCYKLTSVVMEKDPFHASCLPVHIGTLVELNKANELFYLSHKLVDLYPSNPVSWFAVGCYYLMVGHKNEHARRYLSKATTLEKTYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAERFFSQALSIAPEDPFVMHEVGVVAFQNGEWKTAEKWFLDALEKIKAIGNEVTVDKWEPLLNNLGHVCRKLKKYAEALDYHRQALVLIPQNASTYSAIGYIHSLMGNFENAVDYFHTALGLRRDDTFSVTMLGHCIEMYIGDSEAYIGADIKDKLKCYDFDVHTMKTLKNIISPPWDFREFEVEKQTAEETGLTPLETSRKTPDSRPSLEETFEIEMNESDMMLETSMSDHST