wanglab/gogpt-training-data huggingface dataset:
Protein: Gamma-tubulin complex component 2 homolog (Gamma-ring complex protein 84 kDa) (d84p) (dGrip84) (Q9XYP7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32066907}. Note=In the fat body, localizes to a perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs). {ECO:0000269|PubMed:32066907}.
Interaction partners:
- Gamma-tubulin complex component
- Gamma-tubulin complex component 3
- Grip163
- Gamma-tubulin complex component 4 homolog
- Tubulin gamma-1 chain
- Tubulin gamma-2 chain
- Grip71
- Testis-specific gamma-tubulin ring protein 91
- GEO02508p1
- Testis-specific gamma-tubulin ring protein 128
Sequence:
MYALLVFVERYSECKPVSESSSSTSLSAMGLPHGNKTSDVNSAAGSVPTTLAIASTSTILTTSQNVSGSTRLSLTQSQDFPTSTPVNCKKATESDTTPVVFVRRGPMDRNRGAGKDERNDLSVIKERVLNAVSDQSLSGYRSVTNKTGNSPKSMPNDLVTLTDVPDEYRTHLLWEYYKVDGDKVPRAEIAAMPLLSQESMLLDELLHCLTGIRESLLVPQKPIISAVGLAKYDTDFDIHTHLDRSLTHQVREILPLASYFMGVQKIIAATDGLGQVMNSLNEALQELTHDFYLIIVQAEQELRHNRLTLQKLLYYLQPTMWVMHEVWSSLVIIQLSDSRDAEVLTYLHERIKRLEGNKDAQQLIIGLVRKAAKPYMRMLQMWIQKGVIVDRHREFLVVDNEVIHRDELPEHYSDDYWERRYTLRDEQIPSFLAKYSDKILRTGKYLNVIRQCGKRVMPTQEMNLEFDPTSERHVSVINDAYYFAARMLLDVLLTENDLMGHLQSVKRYLLLNQGDFTMQFMDACEDELTKNVDHVLPMTLENLLGLTLRISSARNDPYKDDLHCELLPYDLVTQMSKIMKKEENWQAQPRLDLSGLECFAFTYEVKWPCSLVLNHISISKYQMLFRQLFYCKHVERQLCKIWKENSIARQFEPQAASLYRAAFTLRQRMMNAIQNLEYYMMIEIIEPNWHIFIEKMKTVENVDNVLRLHQDFLDSCLKNCMLTESSHLNRSIFKLCKICLKYCEFIQITQRYFQDAELRSMVRDSADSSESEQESLHCPQIETPLDPTDTFSERVRRFDLEFTQLLISFLKQINSMAKKNTADCFMNLVHRINFNAFYTDQMDKMCVEDAIG
Protein: Aquaporin NIP2-1 (NOD26-like intrinsic protein 2-1) (AtNIP2;1) (Nodulin-26-like major intrinsic protein 4) (NodLikeMip4) (Protein NLM4) (Q8W037)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low water transport activity in yeast cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16954136}; Multi-pass membrane protein {ECO:0000269|PubMed:16954136}.
Interaction partners:
- Aquaporin SIP1-1
- NEP1-interacting protein 2
- Probable aquaporin SIP2-1
- Probable aquaporin SIP1-2
Sequence:
MDDISVSKSNHGNVVVLNIKASSLADTSLPSNKHESSSPPLLSVHFLQKLLAELVGTYYLIFAGCAAIAVNAQHNHVVTLVGIAVVWGIVIMVLVYCLGHLSAHFNPAVTLALASSQRFPLNQVPAYITVQVIGSTLASATLRLLFDLNNDVCSKKHDVFLGSSPSGSDLQAFVMEFIITGFLMLVVCAVTTTKRTTEELEGLIIGATVTLNVIFAGEVSGASMNPARSIGPALVWGCYKGIWIYLLAPTLGAVSGALIHKMLPSIQNAEPEFSKTGSSHKRVTDLPL
Protein: Retinoic acid-induced protein 3 (G-protein coupled receptor family C group 5 member A) (Retinoic acid-induced gene 1 protein) (RAIG-1) (Q8BHL4)
Organism: Mus musculus (Mouse)
Function: Orphan receptor. Could be involved in modulating differentiation and maintaining homeostasis of epithelial cells. This retinoic acid-inducible GPCR provides evidence for a possible interaction between retinoid and G-protein signaling pathways. Functions as a negative modulator of EGFR signaling. Acts as a lung tumor suppressor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18000218}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTTPTTAPSGCRSDLDSRYHRLCDLAEGWGIALETLAAVGAVATVACMFALVFLICKVQDSNKRKMLPAQFLFLLGVLGVFGLTFAFIIKLDGATGPTRFFLFGVLFAICFSCLLAHAFNLIKLVRGRKPLSWLVILSLAVGFSLVQDVIAIEYLVLTMNRTNVNVFSELPAPRRNEDFVMLLIYVLVLMVLTFFTSFLVFCGSFSGWKRHGFHICFTSFLSIAIWVAWIVLLLIPDIDRKWDDTILSTALVANGWVFLAFYILPEFRQLPRQRSPTDYPVEDAFCKPQLMKQSYGVENRAYSQEEITQGLEMGDTLYAPYSTHFQLQNHQKDFSIPRAQAPASPYNDYEGRKGDS
Protein: Chitinase CLP (OsCLP) (EC 3.2.1.14) (Chitinase-like protein) (Q8S1V1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Chitinase that possesses antifungal activity. Inhibits the growth of the fungal pathogen Rhizoctonia solani by degrading the fungal cell wall. Does not possess inhibiting activity against fungal endo-1,4-beta-D-xylanases belonging to glycoside hydrolase family 10 (GH10) and family 11 (GH11). Involved in the regulation of plant growth by regulating the intracellular calcium ion concentration in roots.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:28401568}.
Interaction partners:
Sequence:
MSLHLLLAVSLCVALASSLPWAAASANGNGNGKPLVAAITKDAATSLYTVPIKDGRPLVLDLAGALVWMSCAAAHPTLECHHHFCMHAHSYHPPGCPHNGYGRADVEDPFRCKCTAHPYNPFSGESATADLTRTRLSANATDGKNPLYPVSFAAVTSCAPDSLLAKLPAGAVGVAGLARTRLALQAQVARSQKVANKFALCLPSGGGGDGVAIFGGGPLFLLPPGRPDVAATLAGETPLHRNKDLPGYFISATKIAVNQEQVQLYTQEPLVVELCTRIPYTALRPDVYRAVVDAFARATAGRKRVTPPPPPAAPFELCYDSRDLGSTRLGYAVPQIDLVLEGGKNWTVFGGNSMAQVSDNTACLAVVKVKGEKGSPPPPAAIIGGFQMENNLVVFDEEKQRLGFSGLLWGRQTTCSNFNFTLAA
Protein: Radial spoke head protein 6 homolog A (Radial spoke head-like protein 1) (Q9H0K4)
Organism: Homo sapiens (Human)
Function: Essential for sperm flagellar assembly and male fertility.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q8CDR2}.
Interaction partners:
- Radial spoke head protein 9 homolog
- Radial spoke head protein 3 homolog
- Dystrophia myotonica WD repeat-containing protein
- Radial spoke head 1 homolog
- E3 SUMO-protein ligase RanBP2
- Ras suppressor protein 1
- Dynein regulatory complex subunit 3
- Adenylate kinase 7
Sequence:
MGDLPPYPERPAQQPPGRRTSQASQRRHSRDQAQALAADPEERQQIPPDAQRNAPGWSQRGSLSQQENLLMPQVFQAEEARLGGMEYPSVNTGFPSEFQPQPYSDESRMQVAELTTSLMLQRLQQGQSSLFQQLDPTFQEPPVNPLGQFNLYQTDQFSEGAQHGPYIRDDPALQFLPSELGFPHYSAQVPEPEPLELAVQNAKAYLLQTSINCDLSLYEHLVNLLTKILNQRPEDPLSVLESLNRTTQWEWFHPKLDTLRDDPEMQPTYKMAEKQKALFTRSGGGTEGEQEMEEEVGETPVPNIMETAFYFEQAGVGLSSDESFRIFLAMKQLVEQQPIHTCRFWGKILGIKRSYLVAEVEFREGEEEAEEEEVEEMTEGGEVMEAHGEEEGEEDEEKAVDIVPKSVWKPPPVIPKEESRSGANKYLYFVCNEPGLPWTRLPHVTPAQIVNARKIKKFFTGYLDTPVVSYPPFPGNEANYLRAQIARISAATQVSPLGFYQFSEEEGDEEEEGGAGRDSYEENPDFEGIPVLELVDSMANWVHHTQHILPQGRCTWVNPLQKTEEEEDLGEEEEKADEGPEEVEQEVGPPLLTPLSEDAEIMHLAPWTTRLSCSLCPQYSVAVVRSNLWPGAYAYASGKKFENIYIGWGHKYSPESFNPALPAPIQQEYPSGPEIMEMSDPTVEEEQALKAAQEQALGATEEEEEGEEEEEGEETDD
Protein: Homocitrate synthase, mitochondrial (HCS) (EC 2.3.3.14) (Q12122)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Homocitrate synthase, cytosolic isozyme
- Homocitrate dehydratase, mitochondrial
- Homoisocitrate dehydrogenase, mitochondrial
- 3-isopropylmalate dehydratase
- Acetyl-coenzyme A synthetase 2
- 2-isopropylmalate synthase
- Acetyl-coenzyme A synthetase 1
- Acetyl-CoA acetyltransferase
- 2-isopropylmalate synthase 2, mitochondrial
- Acetyl-CoA hydrolase
Sequence:
MSENNEFQSVTESTTAPTTSNPYGPNPADYLSNVKNFQLIDSTLREGEQFANAFFDTEKKIEIARALDDFGVDYIELTSPVASEQSRKDCEAICKLGLKAKILTHIRCHMDDARVAVETGVDGVDVVIGTSKFLRQYSHGKDMNYIAKSAVEVIEFVKSKGIEIRFSSEDSFRSDLVDLLNIYKTVDKIGVNRVGIADTVGCANPRQVYELIRTLKSVVSCDIECHFHNDTGCAIANAYTALEGGARLIDVSVLGIGERNGITPLGGLMARMIVAAPDYVRSKYKLHKIRDIENLVADAVEVNIPFNNPITGFCAFTHKAGIHAKAILANPSTYEILDPHDFGMKRYIHFANRLTGWNAIKSRVDQLNLNLTDDQIKEVTAKIKKLGDVRPLNIDDVDSIIKDFHAELSTPLLKPVNKGTDDDNIDISNGHVSKKAKVTK
Protein: Homoserine kinase (HK) (HSK) (EC 2.7.1.39) (P17423)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate in the threonine biosynthesis pathway.
Interaction partners:
- Homoserine dehydrogenase
- Threonine synthase
- Aspartokinase
- Aspartate-semialdehyde dehydrogenase
- Cystathionine beta-synthase
- Cystathionine gamma-synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine gamma-lyase
- Catabolic L-serine/threonine dehydratase
- Bifunctional purine biosynthetic protein ADE5,7
Sequence:
MVRAFKIKVPASSANIGPGYDVLGVGLSLFLELDVTIDSSQAQETNDDPNNCKLSYTKESEGYSTVPLRSDANLITRTALYVLRCNNIRNFPSGTKVHVSNPIPLGRGLGSSGAAVVAGVILGNEVAQLGFSKQRMLDYCLMIERHPDNITAAMMGGFCGSFLRDLTPQEVERREIPLAEVLPEPSGGEDTGLVPPLPPTDIGRHVKYQWNPAIKCIAIIPQFELSTADSRGVLPKAYPTQDLVFNLQRLAVLTTALTMDPPNADLIYPAMQDRVHQPYRKTLIPGLTEILSCVTPSTYPGLLGICLSGAGPTILALATENFEEISQEIINRFAKNGIKCSWKLLEPAYDGASVEQQ
Protein: Solute carrier family 25 member 36 (Q96CQ1)
Organism: Homo sapiens (Human)
Function: Mitochondrial transporter that imports/exports pyrimidine nucleotides into and from mitochondria. Selectively transports cytosine, guanosine, inosine and uridine (deoxy)nucleoside mono-, di-, and triphosphates by antiport mechanism. Catalyzes uniport at much lower rate. May import (deoxy)nucleoside triphosphates in exchange for intramitochondrial (deoxy)nucleoside mono- and diphosphates, thus providing precursors necessary for de novo synthesis of mitochondrial DNA and RNA while exporting products of their catabolism. Participates in mitochondrial genome maintenance, regulation of mitochondrial membrane potential and mitochondrial respiration.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:25320081}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSQRDTLVHLFAGGCGGTVGAILTCPLEVVKTRLQSSSVTLYISEVQLNTMAGASVNRVVSPGPLHCLKVILEKEGPRSLFRGLGPNLVGVAPSRAIYFAAYSNCKEKLNDVFDPDSTQVHMISAAMAGFTAITATNPIWLIKTRLQLDARNRGERRMGAFECVRKVYQTDGLKGFYRGMSASYAGISETVIHFVIYESIKQKLLEYKTASTMENDEESVKEASDFVGMMLAAATSKTCATTIAYPHEVVRTRLREEGTKYRSFFQTLSLLVQEEGYGSLYRGLTTHLVRQIPNTAIMMATYELVVYLLNG
Protein: Peroxisomal ATPase PEX1 (EC 3.6.4.-) (Peroxin-1) (Peroxisomal assembly protein 1) (Peroxisome biogenesis protein PAS1) (P24004)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:14562095}. Peroxisome membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}; Cytoplasmic side {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Peroxisomal ATPase PEX6
- Peroxisomal membrane protein PEX15
- Ubiquitin-conjugating enzyme E2-21 kDa
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal receptor
- Peroxisome assembly protein 22
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX17
Sequence:
MTTTKRLKFENLRIQFSNAIVGNFLRLPHSIINVLESTNYAIQEFGIAVHSHNSDIPIVHLGWDGHDSGSSENVVLINPVLATVYDLNQKSPLVDLYIQRYDHTHLATEVYVTPETSDDWEIIDANAMRFQNGEILHQTRIVTPGETLICYLEGIVTKFKIDRVEPSMKSARITDGSLVVVAPKVNKTRLVKAEYGHSNKTILKNGAIQLLKKVILRSTVCKMDFPKDNLFVVYISDGAQLPSQKGYASIVKCSLRQSKKSDSDNKSVGIPSKKIGVFIKCDSQIPENHIALSSHLWDAFFTHPMNGAKIKLEFLQMNQANIISGRNATVNIKYFGKDVPTKSGDQYSKLLGGSLLTNNLILPTEQIIIEIKKGESEQQLCNLNEISNESVQWKVTQMGKEEVKDIIERHLPKHYHVKETGEVSRTSKDEDDFITVNSIKKEMVNYLTSPIIATPAIILDGKQGIGKTRLLKELINEVEKDHHIFVKYADCETLHETSNLDKTQKLIMEWCSFCYWYGPSLIVLDNVEALFGKPQANDGDPSNNGQWDNASKLLNFFINQVTKIFNKDNKRIRVLFSGKQKTQINPLLFDKHFVSETWSLRAPDKHARAKLLEYFFSKNQIMKLNRDLQFSDLSLETEGFSPLDLEIFTEKIFYDLQLERDCDNVVTRELFSKSLSAFTPSALRGVKLTKETNIKWGDIGALANAKDVLLETLEWPTKYEPIFVNCPLRLRSGILLYGYPGCGKTLLASAVAQQCGLNFISVKGPEILNKFIGASEQNIRELFERAQSVKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQMDGAEGLDGVYILAATSRPDLIDSALLRPGRLDKSVICNIPTESERLDILQAIVNSKDKDTGQKKFALEKNADLKLIAEKTAGFSGADLQGLCYNAYLKSVHRWLSAADQSEVVPGNDNIEYFSINEHGRREENRLRLKTLLQQDVVHETKTSTSAASELTAVVTINDLLEACQETKPSISTSELVKLRGIYDRFQKDRNGEMPNGENSIDIGSRLSLM
Protein: Sodium-coupled neutral amino acid symporter 2 (Amino acid transporter A2) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2) (Q9JHE5)
Organism: Rattus norvegicus (Rat)
Function: Symporter that cotransports neutral amino acids and sodium ions from the extraccellular to the intracellular side of the cell membrane. The trasnport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier. May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate. Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11311116, ECO:0000269|PubMed:11834730, ECO:0000269|PubMed:12054432, ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:19589777, ECO:0000269|PubMed:21158741, ECO:0000269|PubMed:27355203, ECO:0000269|PubMed:29678469, ECO:0000305|PubMed:10859363}; Multi-pass membrane protein {ECO:0000269|PubMed:17488712, ECO:0000269|PubMed:29678469}. Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes (PubMed:11834730). Enriched in the somatodendritic compartment of neurons, it is also detected at the axonal shaft but excluded from the nerve terminal (PubMed:15561425, PubMed:16616430, PubMed:18832333). {ECO:0000269|PubMed:11834730, ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:16616430, ECO:0000269|PubMed:18832333}.
Interaction partners:
- Sodium-coupled neutral amino acid symporter 1
- Amino acid transporter
- Neutral amino acid transporter B
- Serotonin N-acetyltransferase
- Large neutral amino acids transporter small subunit 1
- Large neutral amino acids transporter small subunit 2
Sequence:
MKKTEMGRFNISPDEDSSSYSSNGDFNYSYPTKQAALKSHYVDVDPENQNFLLESNLGKKKYETDFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGHKAYGLAGKLAASGSITMQNIGAMSSYLFIVKYELPLVIKALMNIEDTNGLWYLNGDYLVLLVSFVLILPLSLLRNLGYLGYTSGLSLLCMIFFLIVVICKKFQIPCPVEVALMANETVNGTFTQVALAALASNSTAADTCRPRYFIFNSQTVYAVPILTFSFVCHPAVLPIYEELKSRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLHTYSAIVGTDILLLVVRLAVLVAVTLTVPVVIFPIRSSVTHLLCPTKEFSWFRHSVITVTILAFTNLLVIFVPTIRDIFGFIGASAAAMLIFILPSAFYIKLVKKEPMRSVQKIGALCFLLSGVVVMIGSMGLIVLDWVHDASAGGH
Protein: Amino acid transporter (D7RVR8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}.
Interaction partners:
- Large neutral amino acids transporter small subunit 1
- Neutral amino acid transporter 9
- b
- Monocarboxylate transporter 10
- Transporter
Sequence:
MQKQVEIRMHENHLDPLPEPEESICGSCCDKLMKNLLLTLTVLGVITGSVAGILLRYASPLPADVIMVIAFPGDILMRMLKMVILPLIISSLITGLAGLDAKSSGRLGTRAMIYYMSTTVIAAVLGVILVLLIHPGNPKLKANLGEGKKNDEVSSLDAFFDLIRNLFPENLVQACFQQIQTVTTKVEIAPPPPPTRFGRNATKGAAKYVIKKSLQFKSGMNVLGIIGFFVAFGICMGKMGEKAKLMVDFFNTLNEIVMRLVGMIMWYSPIGIACLICGKIISINDLEMVAKQLGMYMVTVIVGLIIHGGIFLPLIYFVIVRKNPFKFFMGLFQAWVTALGTASSAGTLPVTFRCLEENLGIDKRVTRFVLPVGATINMDGTALYEAVAAIFIAQMNGIELDPGQIVTVSLTATLASVGAASIPSAGLVTMLLILTAVGLPTQDISLLVAVDWLLDRFRTSVNVIGDSYGAGIVYHLSKDELDMFDAQQIRPDDFEMAKTQSYYENNSNHGVYHNSCQPIQIDDCKVTLASNGSPAEFSLVEEEPWIRE
Protein: cAMP-dependent protein kinase inhibitor gamma (PKI-gamma) (Q9Y2B9)
Organism: Homo sapiens (Human)
Function: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
Interaction partners:
- cAMP-dependent protein kinase inhibitor alpha
- Adenosine deaminase
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MMEVESSYSDFISCDRTGRRNAVPDIQGDSEAVSVRKLAGDMGELALEGAEGQVEGSAPDKEAGNQPQSSDGTTSS
Protein: Fas-associated death domain protein (Death domain-containing adapter protein BG4) (FAS-associating death domain-containing protein) (dFADD) (Q9V3B4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the IMD signaling pathway and is required for the host defense against Gram-negative bacteria. Interacts with Dredd, promotes cleavage of Dredd and is necessary and sufficient for enhancing Dredd-induced apoptosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10934188}.
Interaction partners:
- Caspase-8
- Protein immune deficiency
- Peptidoglycan-recognition protein LC
- Nuclear factor NF-kappa-B p110 subunit
- Death-associated inhibitor of apoptosis 2
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- NF-kappa-B essential modulator
- Peptidoglycan-recognition protein LE
- Mitogen-activated protein kinase kinase kinase 7
- Caspase Dronc
Sequence:
MTAGRHWSYDSLKQIAIDGCTENVEQLKLIFVEEIGSRRRSDCIRTIEDLIDCLERADELSEYNVEPLRRISGNMPQLIEALSAYTKPENILGHPVNLYQELRLAEELRQQLRIAPASQNAQPSVSELAAAVPPTAIQNYATPAAFTDHKRTMVFKKISEELGRYWRRLGRSAGIGEGQMDTIEERYPHDLKSQILRLLQLIEEDDCHDPKHFLLRLCRALGDCGRNDLRKRVEQIMSH
Protein: Rho-related GTP-binding protein RhoA-B (Q6DHM9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers.
Subcellular location: Cell membrane {ECO:0000305|PubMed:26190758}; Lipid-anchor {ECO:0000250|UniProtKB:P61586}; Cytoplasmic side {ECO:0000250|UniProtKB:P61586}.
Interaction partners:
- Rho-associated protein kinase
- Rho-associated protein kinase
- Rho-associated protein kinase
- Dishevelled-associated activator of morphogenesis 1a.
- Actin alpha 1, skeletal muscle b.
- Rho guanine nucleotide exchange factor 2
- Rho guanine nucleotide exchange factor 2 isoform X1 2)
- Diaphanous-related formin 2.
- Rho GTPase-activating protein 35
- Rho guanine nucleotide exchange factor
Sequence:
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDSKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELTKMKQEPVKAEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKSNKCCLL
Protein: Telomerase-associated protein of 45 kDa (p45) (Q6JXI5)
Organism: Tetrahymena thermophila (strain SB210)
Function: Component of a CST-like subcomplex of the holoenzyme telomerase ribonucleoprotein complex, which stimulates telomerase complementary-strand synthesis. Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. The CST-like subcomplex (also named 7-4-1) binds telomeric single-stranded DNA and coordinates telomere G-strand and C-strand synthesis.
Subcellular location: Chromosome, telomere {ECO:0000305}.
Interaction partners:
Sequence:
MEDNFELVFLKELPSLPDFSKVCFTGLILSFSNFPSSEQNQQKDVPHKIAIIQDSTGEAELFLDMYKFCQEEISVFKAITGIGVLKKKNIGAGQVCKIIVERFRIIHSADEEMLQYLLIQKYKLSKTLNEQQQIKQKEQQINQQKIDKVVQDKESKEHLLWKQQQIPQIKSNQENINTLKYKELIAGELMRITHKLLIQKLQQQQPANNNKQINEMDVESNELAEKKEVIIKIQEIAKDQQLYDTLSIQYQVDQKEQYYAKIAQSLEDFVSISALKMVSYIYPNISYQVSIGFFQNILDIATKTVKDRGALGCNYKYLKDKLTKALNLQQISYPLISESYISYLVHLFQDFNIIEIENEHKFYYKQAFQYDDS
Protein: tRNA (34-2'-O)-methyltransferase regulator RTT10 (Endosomal recycling protein 2) (Regulator of Ty1 transposition protein 10) (tRNA (guanosine(34)-2'-O)-methyltransferase non-catalytic subunit TRM734) (Q08924)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in regulation of Ty1 transposition. Also plays a role in the regulation of the retromer complex and is required for the recycling from endosomes of plasma membrane proteins like CAN1 and MUP1. Required together with TRM7 for the methylation of the 2'-O-ribose of nucleotides at position 34 of the tRNA anticodon loop of tRNA(Phe) and tRNA(Leu(UAA)).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21880895}. Endosome {ECO:0000269|PubMed:21880895}. Note=Recruited to endosomes in cells in which increased recycling of internalized plasma membrane proteins occurs. {ECO:0000269|PubMed:21880895}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- Diphthine methyltransferase
- tRNA
- tRNA
- tRNA
- U3 small nucleolar RNA-associated protein 15
- tRNA
Sequence:
MKDLSHYGPALCVKFYNDYVLAGYGPFIHVYDYHSATLINKCRLFHYNKVHGLSLSSEGKILAYGARSVTIVELEDVLKKESLVDFERINSDWITGATFSFDNLQIYLLTCYNKVLICDLNCEVLFRKSLGGERSILYSGIIKVFGPDKVYVNAGTVMGGVIIWDLFSETKIHNLLGHEGSIFYVNLSNNGRYVASCSDDRSIRLWDLETGKQLSVGWSHTARIWNLMFFDNDSKLISVSEDCTCRVWNIIESRENVAELSISNVYEVHLIKSIWGVDVKDDEMIAVTSGNDGRLKLIDLLQLKRHGDEETSFSLDDIAKQCGDIFEKNESIKGFQWFSFGVIAITSLGKILKYSDVTKQWKLLLTNEKFNSYPITNGIQTQNIAVFSNNKSDILLIKFSKDSADIIETEEFHLDELSKTNNCLVTEYDDDSFLLTLQSPNPREKFVCLEISLQNLKIKSKHCFNKPENFSSSCLTSFRNHILVGSRFSTLVIYNLLDESEEPFIIRRLSPGDTTTSIEFVEDKDNSAVFSVTNRDGYYVFIELTKNSLEEGPYRLSYKVLHSNKMMKGFLEGAFFNSKGEYITYGFKSSLFYLYNETNCYELASEVCGGSHRLWNLAKITDGHVLMYIKASRFHLRKIYNSIVPETLENGVHGREIRDISICPVSNTNTNDNFKDGHIFCTASEDTTIKLGYFNNRTGKVQNFWTQRKHVSGLQRCQFINHKLMISSSAREELFLWELNDKYNKRPYMTIRQALPVSTNNSDLRIMDFDVKFISQSGDFLLVTVYSDSTIKIWHYRENQNKFDLIMQGRYKTCCLFNVVFIALKEELLVVISPTDGHLVVYNITEYVPFSVDPISGDLVDHKLDATISNLPAPVAQLPVHQSGVKSLDYVANATRTSATILTGGDDNGLGLSNLKLDDSNKVTLKTSDFIAAAASSTITSGMLINGGKEVITTSVDQVIRAWEITAGKLSLVDKKRTTVADTGSLEIISNDEDADSEKTLLIGGVGLSIWKK
Protein: Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1) (P21874)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Interaction partners:
Sequence:
MAQMTMVQAITDALRIELKNDPNVLIFGEDVGVNGGVFRATEGLQAEFGEDRVFDTPLAESGIGGLAIGLALQGFRPVPEIQFFGFVYEVMDSICGQMARIRYRTGGRYHMPITIRSPFGGGVHTPELHSDSLEGLVAQQPGLKVVIPSTPYDAKGLLISAIRDNDPVIFLEHLKLYRSFRQEVPEGEYTIPIGKADIKREGKDITIIAYGAMVHESLKAAAELEKEGISAEVVDLRTVQPLDIETIIGSVEKTGRAIVVQEAQRQAGIAANVVAEINERAILSLEAPVLRVAAPDTVYPFAQAESVWLPNFKDVIETAKKVMNF
Protein: Discoidin-1 subunit B/C (Discoidin I chain C/D) (Discoidin-1 subunit beta/gamma) (P02887)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Galactose- and N-acetylgalactosamine-binding lectin. May play a role in cell-substratum adhesion rather than in cell-cell adhesion. May be necessary for the maintenance of normal elongate morphology during aggregation.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MSTQGLVQLISNAQCHLRTSTNYNDVHTQFNAVLNYKNKGTNTIDGSEAWCSSIVDTNQYIVAGCEVPRTFMCVALQGRGDHDQWVTSYKIRYSLDNVTWSEYRNGAAITGVTDRNTVVNHFFDTPIRARSIAIHPLTWNNHISLRCEFYTQPVQSSVTQVGADIYTGDNCALNTGSGKREVVVPVKFQFEFATLPKVALNFDQIDCTDATNQTRIGVQPRNITTKGFDCVFYTWNANKVYSLRADYIATALE