wanglab/gogpt-training-data huggingface dataset:
Protein: F-BAR domain only protein 1 (Q8K285)
Organism: Mus musculus (Mouse)
Function: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors. Involved in the regulation of T-cell poliferation and activation. Affects TCR clustering upon receptor triggering and modulates its internalisation, playing a role in TCR-dependent T-cell activation.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:O14526}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14526}; Cytoplasmic side {ECO:0000250|UniProtKB:O14526}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2. According to it may also dynamically associate with Golgi/TGN membranes. {ECO:0000250|UniProtKB:O14526}.
Interaction partners:
- Intersectin-1
- Intersectin-2
- Epidermal growth factor receptor substrate 15
- AP-2 complex subunit alpha-2
- Disabled homolog 2
- Epidermal growth factor receptor substrate 15-like 1
- Adaptin ear-binding coat-associated protein 1
- AP-2 complex subunit beta
- Clathrin coat assembly protein AP180
- AP-2 complex subunit mu
Sequence:
MSYFGEHFWGDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLHDLLKDVLRYGEEQLKTHKKCKEEVLGTVDAVQMLSGVGQLLPKSRENYLSRCMDLERLRRENTSQKEMDKAETKSKKAADSLRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQNVENVTVDMLLRKFAESKGTGREKPGPLDFDAYSSAALQEAMKRLRGAKAFRLPGLSRREPRASVDFLESDSGVPPEVDDEGFTVRPDISQNNGAEPPRFSSSDSDFDDEEPRKFYVHIKPAPTRAVACSSEAAAAQLRATAGSLILPPGPGGTMKRHSSRDTSGKPQRPRSAPRTGSCAEKPLASEEPLSKSLFGPPLESAFDHDDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPSPESWVPRPGTPQSPPTCRAQHPEPRGLMPRAPSPGPWGPEGGADSLTPADPTREGLAATLRRPRSRKVSCPLTRSNGDLCRSLSPSPLGSSAPTIPPDRPSFSTQMGHGISRGPSPVVLGSQDALPVATAFTEYVHAYFRGHSPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVNTAPVEHFQPNADLIFSDPSQSDPETKDFWLNMAALTEALQHQAEQNPTASYYNLVLLRYQFSRPGPESVPLQMSAHWQCGPTLTRVSVEYSYRAGATAVSTPLTNVQILLPVGEPVTSVRLQPAATWNTEEKRFTWKLPDVCEAGGSGHLSASWQPQSGPSTPSPVAAQFTSEGATLSGLDLELLGGGYRMSLVKRRFATGMYLVSC
Protein: Ypt/Rab-type GTPase ypt7 (O94655)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (By similarity). Ypt7 is necessary for trafficking from the endosome to the vacuole and for homotypic vacuole fusion. Plays an important role in sporulation.
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P32939}.
Interaction partners:
- Vacuolar morphogenesis protein 6
- Probable vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 33
- Vacuolar protein sorting-associated protein 41
- Vacuolar membrane protein pep3
- E3 ubiquitin-protein ligase pep5
- Vacuolar fusion protein mon1
- GTPase-activating protein gyp7
- Putative lipase atg15
- Ypt/Rab-type GTPase ypt71
Sequence:
MAGKKKHLLKVIILGESGVGKTSIMNQYVNRKFSKDYKATIGADFLTKEVLVDDKVVTLQLWDTAGQERFQSLGVAFYRGADCCVLVYDVNNSKSFETLDSWRDEFLIQASPSNPETFPFILLGNKVDVEEQKRMVSKSKALAFCQARGEIPYFETSAKEAINVQEAFETVAKLALENMDSDDIAADFTDPIHLDMESQKTSCYC
Protein: Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (SMAD family member 5) (SMAD 5) (Smad5) (Q9R1V3)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99717}. Nucleus {ECO:0000250|UniProtKB:Q99717}. Mitochondrion {ECO:0000250|UniProtKB:Q99717}. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. {ECO:0000250|UniProtKB:Q99717}.
Interaction partners:
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 9
- Bone morphogenetic protein receptor type-1A
- Mothers against decapentaplegic homolog 1
- Serine/threonine-protein kinase receptor
- Activin receptor type-1
- Bone morphogenetic protein receptor type-2
- E3 ubiquitin-protein ligase
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog
Sequence:
MTSMASLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSSPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDICEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHNEFNPQHSLLVQFRNLSHNEPHMPQNATFPDSFHQPNSTPFPLSPNSPYPPSPASSTYPNSPASSGPGSPFQLPADTPPPAYMPPDDQMGQDNSQPMDTSNNMIPQIMPSISSRDVQPVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPANNKSRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNFHHGFHPTTVCKIPSSCSLKIFNNQEFAQLLAQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPLNPISSVS
Protein: Tumor necrosis factor receptor superfamily member 1B (Tumor necrosis factor receptor 2) (TNF-R2) (Tumor necrosis factor receptor type II) (TNF-RII) (TNFR-II) (p75) (p80 TNF-alpha receptor) (CD antigen CD120b) (Etanercept) [Cleaved into: Tumor necrosis factor receptor superfamily member 1b, membrane form; Tumor necrosis factor-binding protein 2 (TBP-2) (TBPII)] (P20333)
Organism: Homo sapiens (Human)
Function: Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Tumor necrosis factor-binding protein 2]: Secreted.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 1A
- Lymphotoxin-alpha
- Tumor necrosis factor
- TNF receptor-associated factor 1
- TNF receptor-associated factor 2
- Keratin, type I cytoskeletal 18
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Baculoviral IAP repeat-containing protein 3
- TNF receptor-associated factor 3
- Interleukin-1 beta
Sequence:
MAPVAVWAALAVGLELWAAAHALPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWVPECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSDVVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTSTSPTRSMAPGAVHLPQPVSTRSQHTQPTPEPSTAPSTSFLLPMGPSPPAEGSTGDFALPVGLIVGVTALGLLIIGVVNCVIMTQVKKKPLCLQREAKVPHLPADKARGTQGPEQQHLLITAPSSSSSSLESSASALDRRAPTRNQPQAPGVEASGAGEARASTGSSDSSPGGHGTQVNVTCIVNVCSSSDHSSQCSSQASSTMGDTDSSPSESPKDEQVPFSKEECAFRSQLETPETLLGSTEEKPLPLGVPDAGMKPS
Protein: P2X purinoceptor 1 (P2X1) (ATP receptor) (Purinergic receptor) (RP-2 protein) (P47824)
Organism: Rattus norvegicus (Rat)
Function: Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9606184}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}. Note=Detected at plasma membrane lipid rafts. {ECO:0000250|UniProtKB:P51575}.
Interaction partners:
- P2X purinoceptor 6
- P2X purinoceptor 3
- P2X purinoceptor 2
- P2X purinoceptor 5
- P2Y purinoceptor 2
- P2X purinoceptor 4
- P2X purinoceptor 7
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 2D
Sequence:
MARRLQDELSAFFFEYDTPRMVLVRNKKVGVIFRLIQLVVLVYVIGWVFVYEKGYQTSSDLISSVSVKLKGLAVTQLQGLGPQVWDVADYVFPAHGDSSFVVMTNFIVTPQQTQGHCAENPEGGICQDDSGCTPGKAERKAQGIRTGNCVPFNGTVKTCEIFGWCPVEVDDKIPSPALLREAENFTLFIKNSISFPRFKVNRRNLVEEVNGTYMKKCLYHKIQHPLCPVFNLGYVVRESGQDFRSLAEKGGVVGITIDWKCDLDWHVRHCKPIYQFHGLYGEKNLSPGFNFRFARHFVQNGTNRRHLFKVFGIHFDILVDGKAGKFDIIPTMTTIGSGIGIFGVATVLCDLLLLHILPKRHYYKQKKFKYAEDMGPGEGEHDPVATSSTLGLQENMRTS
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q38BI4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Leucine-rich repeat protein
Sequence:
MSFFRGLNFSNMNDGVDWENAVPPHITAQRNIERAALRNAAPRRAMLMDWPLPEDMGAPTVAERRLVQSTASPGSGAPDVRRATRVPELREVRQESERRSLNRSHPNSHHTQLRPQTSQQLVRADGNIFSALSGIANEMLQAQLSMVSAFNDFFSEGRSDAMNAMGGTASARVLHGNEVTSVTQQRSVQRGPNSGVQVRRVMVAAQSVNGQRPQVAVQVDEWSGPPATRTRNNNRSGSDFDIITGVPRRILYISSSDEGTGRGDPRGGNGNGSRGAGGGWEIDDFSYENLLRLDDNAEKTGLPEAQLRGLKRTTYNAAKRSGATRRGNANPDNAEKCPVCLEQLVDGAEVHEIACGHVSHHSCIIPWLRRSNCCPTCRYEIPRLKKR
Protein: Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] (EC 1.5.1.10) (Saccharopine reductase) (P38999)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Saccharopine dehydrogenase [NAD
- L-2-aminoadipate reductase
- Homoisocitrate dehydrogenase, mitochondrial
- Spermidine synthase SPE3
- Lysine biosynthesis regulatory protein LYS14
- Homoaconitase, mitochondrial
- Homocitrate synthase, cytosolic isozyme
- Spermine synthase SPE4
- Homocitrate synthase, mitochondrial
- Multifunctional methyltransferase subunit TRM112
Sequence:
MGKNVLLLGSGFVAQPVIDTLAANDDINVTVACRTLANAQALAKPSGSKAISLDVTDDSALDKVLADNDVVISLIPYTFHPNVVKSAIRTKTDVVTSSYISPALRELEPEIVKAGITVMNEIGLDPGIDHLYAVKTIDEVHRAGGKLKSFLSYCGGLPAPEDSDNPLGYKFSWSSRGVLLALRNSAKYWKDGKIETVSSEDLMATAKPYFIYPGYAFVCYPNRDSTLFKDLYHIPEAETVIRGTLRYQGFPEFVKALVDMGMLKDDANEIFSKPIAWNEALKQYLGAKSTSKEDLIASIDSKATWKDDEDRERILSGFAWLGLFSDAKITPRGNALDTLCARLEELMQYEDNERDMVVLQHKFGIEWADGTTETRTSTLVDYGKVGGYSSMAATVGYPVAIATKFVLDGTIKGPGLLAPYSPEINDPIMKELKDKYGIYLKEKTVA
Protein: LIM and senescent cell antigen-like-containing domain protein 1 (Particularly interesting new Cys-His protein 1) (PINCH-1) (Q99JW4)
Organism: Mus musculus (Mouse)
Function: Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation.
Subcellular location: Cell junction, focal adhesion {ECO:0000250|UniProtKB:P48059}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Beta-parvin
- Scaffold protein ILK
- Alpha-parvin
- Ras suppressor protein 1
- Gamma-parvin
- Cytoplasmic protein NCK2
- Thymosin beta-4
- Paxillin
- Talin-1
- Vinculin
Sequence:
MANALASATCERCKGGFAPAEKIVNSNGELYHEQCFVCAQCFQQFPEGLFYEFEGRKYCEHDFQMLFAPCCHQCGEFIIGRVIKAMNNSWHPECFRCDLCQEVLADIGFVKNAGRHLCRPCHNREKARGLGKYICQKCHAIIDEQPLIFKNDPYHPDHFNCANCGKELTADARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNAMGKQWHVEHFVCAKCEKPFLGHRHYERKGLAYCETHYNQLFGDVCFHCNRVIEGDVVSALNKAWCVSCFACSTCNTKLTLKNKFVEFDMKPVCKKCYEKFPLELKKRLKKLSETLGRK
Protein: Syndecan-3 (P26261)
Organism: Gallus gallus (Chicken)
Function: Cell surface proteoglycan that may bear both heparan sulfate and chondroitin sulfate. The multiple functional domains provide potential sites for mediating the adhesive cell-matrix interactions and cytoskeletal reorganization involved in limb chondrogenesis. Interaction with other matrix ligands as well as phosphorylation and shedding of the ectodomain might be involved in cell shape changes that occur during chondrogenesis. Furthermore, shedding of the ectodomain might break the adhesive interactions that promoted condensation, thus facilitating the deposition of cartilage matrix molecules.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Pleiotrophin
- Glypican 4
- Glypican 3
Sequence:
MPAELRRLAVLLLLLSARAALAQPWRNENYERPVDLEGSGDDDPFGDDELDDIYSGSGSGYFEQESGLETAVSLTTDTSVPLPTTVAVLPVTLVQPMATPFELFPTEDTSPEQTTSVLYIPKITEAPVIPSWKTTTASTTASDSPSTTSTTTTTAATTTTTTTTISTTVATSKPTTTQRFLPPFVTKAATTRATTLETPTTSIPETSVLTEVTTSRLVPSSTAKPRSLPKPSTSRTAEPTEKSTALPSSPTTLPPTEAPQVEPGELTTVLDSDLEVPTSSGPSGDFEIQEEEETTRPELGNEVVAVVTPPAAPGLGKNAEPGLIDNTIESGSSAAQLPQKNILERKEVLIAVIVGGVVGALFAAFLVMLLIYRMKKKDEGSYTLEEPKQANVTYQKPDKQEEFYA
Protein: Glutaredoxin 1 (Grx1) (P68688)
Organism: Escherichia coli (strain K12)
Function: The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase.
Interaction partners:
- Ribonucleoside-diphosphate reductase 1 subunit alpha
- DNA-binding transcriptional regulator BolA
- Glutaredoxin 4
- Thioredoxin 2
- Glutathione reductase
- Thioredoxin reductase
- Glutaredoxin 2
- DNA-binding transcriptional dual regulator OxyR
- Alkyl hydroperoxide reductase subunit F
- Catalase-peroxidase
Sequence:
MQTVIFGRSGCPYCVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQKAGKPVETVPQIFVDQQHIGGYTDFAAWVKENLDA
Protein: Solute carrier RCH1 (Regulator of calcium homeostasis 1) (Q59UQ7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Solute carrier protein that negatively regulates the cytosolic homeostasis in response to high levels of extracellular calcium.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22530691}; Multi-pass membrane protein {ECO:0000269|PubMed:22530691}. Bud neck {ECO:0000269|PubMed:22530691}. Note=Distributes as multiple foci in the plasma membrane prior to cell division, moves toward and concentrates at the bud neck as the bud grows in size, and disperses again along the plasma membrane immediately prior to cytokinesis. {ECO:0000250|UniProtKB:Q05131}.
Interaction partners:
- GDT1 family protein
Sequence:
MSLETFRESKAYKWTSKVISFLIGQWFFIFLGVFIALAHSYPEFAKQGGTIRAEYSIGYGAVAVIFLISGLSMSTKQLLVNVANWRAHFTVLSMSFLVTSAIIYGIASGIKASHNGQIDDWLLIGLIVTHACPTTVSSNVVMTKQAHGNDILTLCEVFIGNVLGAFITPALLQMYMRGTWEIGNPSHQTQGDSTVQELYAHTMKQLGLSVFVPLFVGQVVQNIFPKQTKWCLTTFKLNKVGSFMLLLIMFQSFSTAFAQHAFTSVSHASIIFLVFFNIGIYLFFTVLTFFYSRPFWILRVFKEEPNESSSKLYRYSYAFFRPFYYNRKDTVAVMLCGPAKTAALGVSLVSSQYGSHNPKLGIILVPLVLYQAEQVMTANVLVSFMRKWIHAEDKVPEDEETSVGSDNDPKK
Protein: Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 4 (Protein ORGAN BOUNDARY 4) (Q9LW68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription regulator that acts as a developmental regulator by promoting cell growth in response to light (By similarity). May suppress organ differentiation in the boundary region.
Subcellular location: Nucleus {ECO:0000269|PubMed:21435050}.
Interaction partners:
- Protein CUP-SHAPED COTYLEDON 1
- Transcription factor MYB117
- Probable E3 ubiquitin-protein ligase EDA40
- Homeobox protein knotted-1-like 6
- Protein CUP-SHAPED COTYLEDON 2
- Protein CUP-SHAPED COTYLEDON 3
Sequence:
MDHIIGFMGTTNMSHNTNLMIAAAATTTTTSSSSSSSSGGSGTNQLSRYENQKRRDWNTFGQYLRNHRPPLSLSRCSGAHVLEFLRYLDQFGKTKVHTHLCPFFGHPNPPAPCACPLRQAWGSLDALIGRLRAAFEENGGSPETNPFGARAVRLYLREVRDSQAKARGISYEKKKRKRPPPPLPPAQPAISSSPN
Protein: Exportin-2 (Exp2) (Cellular apoptosis susceptibility protein homolog) (Chromosome segregation protein 1) (Importin-alpha re-exporter) (Q9XZU1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Export receptor for importin alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates have been released into the nucleoplasm (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Ellipsoid body open, isoform C
- Importin subunit alpha
- Exportin-1
- Importin subunit alpha
- Importin subunit alpha
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran-like
- Importin subunit alpha
- RH51096p
- LD26789p
Sequence:
MEVTEANLQLLAGYLQQTLSADPNVRRPAEKLLESTELQQNYPILLLNLIDKAQMDMTTRVAGAIAFKNYIKRNWAAHLDSDGPDRIHESDRNTIKTLIVTLMLHSPVALQKQLSDAVSIIGKYDFPKKWPQLIDEMVERFASGDFNVINGVLQTAHSLFKRYRYEFKSQALWEEIKFVLDRMAKPLTDLLQAKMQLTKVHENNAGALKVIYGSLVLVNKVFFSLNSQDLPEFFEDNINTWMGAFIQQLAADVPSLRTADDEDAGVLEHLRAQVCENICLYAKKYDEEFKPFMEQFVTAVWELLVKTSLHTKYDSLVSHALQFLSVVADRQHYQSIFENPEILAQICDKVVIPNLDIRPSDEEIFEDSPEEYIRRDIEGSDIDTRRRAACDLVKTLSINFEQKIFGIFGQYLERLLTKYKENPATNWRSKDTAIYLVTSWASRGGTQKHGITQTSELVPLPEFCAQQIIPELERPNINEFPVLKAAAIKYVMVFRSILGPQVLASCLPQLIRHLPAESSVVHSYAACSVEKILSMRDASNAIVFGPQILAPYTTELISGLFATLSLPGSGENEYVMKAIMRSFSVLQSAAMPFMGVALPRLTEILTQVAKNPSRPQFNHYLFETLALCIKIVCHADSSAVSSFEEALFPVFQGILQQDIVEFMPYVFQMLSVLLEMREGTGTIPEPYWALFPCLLSPALWDRTGNVTPLIRLISAFIKQGSAQIQALGKLSGILGIFQKMIASKANDHEGFYLLQNLLSYYPPAEIQTNLRQIFGLLFQRLSLSKTPKYLSGIIIFFSFYVIKFSGSQMAQLIDEIQPNLFGMLLDRVFITEMGKIPKEQDRKMVAVGVTKLLTETPEILQQQYATFWPRLLHSLIDLFERPPEKLMGLEIGETAGVAEDPDAGYQVAFAQLTHAQPNQQDHLAEIKDARQFLATSLSKFAQARAGEFSTLLSPLEPEYKQVLQKYCDQAGVRIA
Protein: Histone acetyltransferase Tip60 (EC 2.3.1.48) (Q960X4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic subunit of the Tip60 chromatin-remodeling complex which is involved in DNA repair. Upon induction of DNA double-strand breaks, acetylates phosphorylated histone H2AV in nucleosomes on 'Lys-4' and exchanges it with unmodified H2AV.
Subcellular location: Nucleus {ECO:0000269|PubMed:15528408}.
Interaction partners:
- NuA4 complex subunit EAF3 homolog
- Enhancer of polycomb-like protein
- Inhibitor of growth protein
- DNA methyltransferase 1-associated protein 1
- YEATS domain-containing protein 4
- Transcription-associated protein 1
- Brahma associated protein 55kD
- Chromatin modification-related protein MEAF6
- RuvB-like helicase 1
- Serine/threonine-protein kinase ATM
Sequence:
MKINHKYEFDDDVASICESTAALTEGCRLPVRMHKTDDWPLAEIVSIKELDGRRQFYVHYVDFNKRLDEWVNEEDLYTRKVQFPRRDGSQTGTSTGVTTPQRHHSLAGSVSRPTSPQHPGSGALAAIPQTPTGASGSVPPPAGIPNSVAPPGTPSSGGELVNGNNLAAALQKRINRKRKNHGGSAHGHHSLTSQQQQSHPHPTTPQTPTATPVHVTGDGLISGAANDDGDGSQDGKTPTPRQSGSMVTHQDDVVTRMKNVEMIELGRHRIKPWYFSPYPQELCQMPCIYICEFCLKYRKSRKCLERHLSKCNLRHPPGNEIYRKHTISFFEIDGRKNKVYAQNLCLLAKLFLDHKTLYYDTDPFLFYVMTEFDSRGFHIVGYFSKEKESTEDYNVACILTMPPYQRKGYGKLLIEFSYELSKFEGKTGSPEKPLSDLGLLSYRSYWAQTILEIFISQNPSTDGEKPTITINDICECTSIKKEDVISTLQNLNLINYYKGQYIVCINRVIIEQHRRAMDKRKIRIDSKCLHWTPKDWSKRSK
Protein: 1-acylglycerol-3-phosphate O-acyltransferase (EC 2.3.1.51) (Lipid droplet-binding protein CGI-58 homolog) (O22975)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis. Is highly specific for lysophosphatidic acid and able to use different acyl-CoA donors. May regulate neutral lipid accumulation and participate in the regulation of lipid turnover in vegetative cells. Possesses additional triacylglycerol lipase and phospholipase A2 activities in vitro. Is not active as esterase or lysophospholipase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20876112}. Note=Does not associate with endogenous lipid droplets.
Interaction partners:
- Phospholipid:diacylglycerol acyltransferase 1
- Wax ester synthase/diacylglycerol acyltransferase 1
Sequence:
MNLSRFASRLRMAEEISKTKVGSSSTASVADSSAAASAATNAAKSRWKILWPNSLRWIPTSTDYIIAAEKRLLSILKTPYVQEQVSIGSGPPGSKIRWFRSTSNESRYINTVTFDAKEGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCRSTEETEAWFIDSFEEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFSAEADAKSEWLTKFRATWKGAVLNHLWESNFTPQKLVRGLGPWGPGLVNRYTTARFGAHSEGTGLTEEEAKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLQSASEWKVPTTFIYGMNDWMNYQGAVEARKSMKVPCEIIRVPQGGHFVFIDNPIGFHSAVLYACRKFISQDSSHDQQLLDGLRLV
Protein: U6 snRNA-associated Sm-like protein LSm1 (Cancer-associated Sm-like) (Small nuclear ribonuclear CaSm) (O15116)
Organism: Homo sapiens (Human)
Function: Plays a role in the degradation of histone mRNAs, the only eukaryotic mRNAs that are not polyadenylated. Probably also part of an LSm subunits-containing complex involved in the general process of mRNA degradation (By similarity).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:18172165}. Cytoplasm, P-body {ECO:0000305|PubMed:18172165}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm3
- Protein PAT1 homolog 2
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm4
- Protein PAT1 homolog 1
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm6
- 5'-3' exoribonuclease 1
- U6 snRNA-associated Sm-like protein LSm2
- Probable ATP-dependent RNA helicase DDX6
Sequence:
MNYMPGTASLIEDIDKKHLVLLRDGRTLIGFLRSIDQFANLVLHQTVERIHVGKKYGDIPRGIFVVRGENVVLLGEIDLEKESDTPLQQVSIEEILEEQRVEQQTKLEAEKLKVQALKDRGLSIPRADTLDEY
Protein: Adenylate kinase 5, chloroplastic (EC 2.7.4.3) (ATP-AMP transphosphorylase 5) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase 5) (AMK5) (Q8VYL1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18162585}.
Interaction partners:
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- Adenosine kinase 2
- Adenosine kinase 1
- AMP deaminase
- At5g66005
- Thiamine pyrophosphokinase 1
- Thiamine pyrophosphokinase 2
- Small ribosomal subunit biogenesis GTPase RsgA 1, mitochondrial
- Alkaline-phosphatase-like family protein
Sequence:
MASLSLSSAHFSSTSSSSRSSISTSSLSPSSTSLPLLQSPIRRRYRSLRRRLSFSVIPRRTSRSFSTSNSQIRCSINEPLKVMISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSSGTDIGKRAKEFMNSGSLVPDEIVIAMVAGRLSREDAKEHGWLLDGFPRSFAQAQSLDKLNVKPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKNYPPESDEIKARLVTRPDDTEEKVKARLQIYKQNSEAIISAYSDVMVKIDANRPKEVVFEETQTLLSQIQLKRMIKTDKASPVQDKWRGIPTRLNNIPHSRDIRAYFYEDVLQATIRSIKDGNTRLRVDINIPELNPEMDVYRIGTLMELVQALALSFADDGKRVKVCVQGSMGEGALAGMPLQLAGTRKILEYMDWGDDETLGTFVKLGAIGGKEVDEEDDMFILVAPQNAVGNCIIDDLQAMTTAAGKRPVVLINPRLKDLPASSGIMQTMGREQRLEYALTFDNCYVFRLLYYLGTQYPIMGALRMSYPYRYELYKRVNEENGKEKYVLLATYAERPTPEQIDDAFSGKSRDQSKKASGIWGFLSSVFS
Protein: GH12891p (Q95SN5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MCAPRNNTCEASKFYCKNGRCISRMWSCDGDDDCGDNSDEDPNYCAYHSCSPNEFRCNNGRCIFKSWKCDHENDCKDGSDELGCVYPPCVDGEFTCANGRCIPQAQVCNGVNDCKDNATSDETHERCPMNTTCPANHLKCEKTNICVEPYWLCDGDNDCGDNSDEDPLHCGQRTCPTNSFRCPNHRCIPATWYCDGDDDCGDGADEPPDYCKSEGRTCFGDLFTCDNGNCIPRIYICDGDNDCLDNSDEDNRHQCNDRKCDEETEFTCVENKSWQRAQCIPKKWICDGDPDCVDGADENTTLHNCATQQPCGEDMFTCGNGRCINKGWICDHDNDCGDGTDEGKFCNSKYKTCSAQEFTCQNFKCIRNQSRCDGEDDCGDHSDEVGCAKENITCPQGQFACTNGQCIDYNLVCNKYPDCADESDEPAHCNVDECAKVEINQCGHKCVDTLTGYYCDCNEGYKLLADGKACADVDECLEQPGACSQHCSNTPGGFYCKCDETYYERQNDEHTCKRKDKIPPWLIFTNKYYVRNMSVDGHQYNLMHQDLMNVVALDFDIREEYMYFCDVTAKTIFRAKYGEADDEMPPEREAVIRHDSHGLEGIAIDWVGRKLYWLDRHSKNLDVSELDGSKRKTLRSGVVDPRAIVVHPGIGYLYFTSWHLQAYIAKMGMDGSNFSRILNWNDGIAWPNALSIDYFTDRIYWADAHLDYIAYADLEGRHRHTVLSGSKVPHVFALSLFDDYIYWSDWNLKAIVRANKFHGANYTVLRNTTHRPYDLHINHPLRQLPYTNPCGTNNGGCSHLCLIAPPPESTYLNIEGYIEEGAPIFKCACPNQFYLARDMKTCVANCTAGQHLCGGRDEKCIPWFWKCDGEKDCKDGSDEPATCAPRHCRAGTFQCKNTNCTPSATICDGVDDCGDRSDEQNCDLPCPLSDFKCKSSGRCILDSWRCDGDADCKDGSDEDPAVCFKRTCDPKTEFSCKNGRCIPQLWMCDFDNDCGDDSDEPAYMCRQRNCTTGWQRCPGQSNYRCIPKWLFCDGKDDCRDNSDELPENCPKCNPETDFKCGNNRCIPKQWMCDFADDCGDASDENEAVCKGRYRECSESEFRCGNGKCISSRWQCDHEDDCGDNSDEMHCEGYQCKNGTFQCASGHCIASYFRCDGDRDCRDMSDEVGCPPRFPGGRYCPESRFQCNNNLCVSLSDLCDGTDDCGDGSDEDPSVCSDFNCDTLRRFQCSNERCVARYQICDGVDNCGDGSDENNMTLCASKQKPCDLYTQYQCANKHCIERSQVCDFSDDCGDASDELGCHHTSSCSEANRGGCQQHCHNLTDGGYICTCYPGYIIAADNKKKCSDVDECLTRQHTCSHQCHNLNGTYSCSCREGFHLTDGASGVCRAEKEDVILLFVNGQEIRGLNWHKSEEFAVIAAEKRIEALDYDAQQQIVFWADSYDKTIKRSYMVNAIDGRAKIGFAQDLNMKGGSKPTAVAVDWLASNLYWTEMDRTGSKPRGRVMVAKTDGRYRRSIVNAGLEVPTSIAVNPQLGRIYWSDAGSAPKIEVSWMDGSKRRPLITEMIRHPAGLTIDYSQDHIIYWVDTKLNAIESMRADGSRRKAIVRGDQLRHPVSLDLFESNMFWMTRDTGELVRQDKFGRGVQVVLHRYIVNPSGLKVYHDKRYNTSLPNPCDNSTCSHLCLLVPGGHRCACPDASGPPPSHRSTAEVICNAAAEHPRPAPRICPCQNGGLCKEDAQGELLCECRTQFVGEHCETSTMGAFGHGDANVTAVVVPIMVILLVMMAAAGAWYVIRKRPFGKLARMPAMTSSQSVTFRHGSNVEFNESGFPGASAPGAGDVAPIEGYNLQTVNANKARDFANPMYDAVQSGTTADPGMGNGSGIYDVPGEPSAKVKSMGHHAGGSFTEPASAIIAPSSITHKASPQLQLRTRELDPSADTGKDTQFLVEEDKSEC