wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerase I subunit RPA2 (RNA polymerase I subunit 2) (EC 2.7.7.6) (B8JKD7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H9Y6}. Chromosome {ECO:0000250|UniProtKB:P70700}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA43
- RNA polymerase I and III subunit C.
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- RNA polymerase I-specific transcription initiation factor RRN3
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- CD3e molecule, epsilon associated protein
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MDLSKWCNLKTEPSLKHLTEAGFGVPKEKQSVPVQELVKAHIESFDQAVTDGLCRVVEAIPPMEFLYKGDRISLSFVEAIIHTPSVSKGGISRDLRVFPAECRGRRCTYRAKLVADVSWSVNGVPKGIIKQSLGQMPIMVKSKLCNLHGLSPKELLEHHEEAEEMGGYFIVNGIEKVIRLLIMPRRNYPIAVSRPKFKSRGQGYTQYAISMRCVKEEHTAINMNLHYLDNGTVMVNFIYRKELFFLPLGFALKALVDYSDYQIYQELIKGREDNSFYKSCVSEMLRIVMDQGCTTKIKVLNYLGERFRVKLNLPEWFTHEQCAHFLLDECLCIHLKTDVEKFYMLCLMTRKLFSFAKQECMEENPDSPMFHEVLTPGQLYLMFLKEKMEGWLVSVKLALEKKPQRVGGLTPDSMTKLFNMGTDLTKAFEYLLATGNLMSKTGLGMLQNSGLCVVADKLNFIRYLSHFRCVHRGAAFAKMRTTTVRKLLPESWGFLCPVHTPDGEPCGLMNHMTAHCEIVAPVYPTSTLPGLLCSLGVNAADGNPGQAYSDCYPVILDGAMIGWVEKEVAPSVIESLRRFKVLGEKKVPPWTEIVLVPQTGKASLYPGLYLFTTPCRMVRTVRNLSLGKQELIGIFEQVYLNVGIFEKEIEDGVTTHQELFPHSMLSVVAEFIPFSDHNQSPRNMYQCQMSKQTMGFPLHSYQYRSDNKLYRLQTPQSPLVRPAMYDHYDVDNYPIGTNAIVAVISYTGYDMEDAMIVNKSSWERGFAHGSVYKTEIIDLSEKVKGDDSIVFGVKPGDPKVMGKLDADGLPFIGSVLKYGDPFYGYISLNTGQSHVYFYKYQESCVVDNIKVCSNETGTGRFKRICVTSRVPRNPTIGDKFASRHGQKGILSRLWPAEDMPFTESGMSPDILFNPHGFPSRMTIGMLIESMAGKSASLHGLCHDATPFTFSEENSALEHFGELLKAAGYNYYGTERLYSGLSGLELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDKVTNQPMGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAQVCMDCGSLLSPLLEKPPPNWSATRHRKTICLLCNKSDSIETVSVPYVFKYFVAELAAMNIKIKLDVK
Protein: Leucine-rich repeat and transmembrane domain-containing protein 2 (Q8BGX3)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLAPGGGPEQRSKLVLQWRQVSWITCWIALCAVEVIPACPFSCTCDSRSLEVDCSGLGLTTVPPDVPAATQSLLLLNNKLSALPSWAFANLSNLQRLDLSNNFLDQLPRSIFEDLVNLTELQLRNNSIRTLDRDLLQHSPLLRHLDLSINGLAQLPPGLFDGLLALRSLSLRSNRLQSLDRLTFEPLASLQLLQVGDNPWECDCNLREFKHWLEWFSYRGGRLDQLACTLPKELRGKDMRAVPMEMFNYCSQLEDENNSAGLDAPGPPCTKASPEPPKPKPGAEPEPEPSTACPQKQRYRPVSVRRAIGTVIIAGVVCGIVCIMMVVAAAYGCIYASLMAKYHRELKKRQPLMGDPEGEHEDQKQISSVA
Protein: Mitogen-activated protein kinase kinase kinase 14 (EC 2.7.11.25) (NF-kappa-beta-inducing kinase) (HsNIK) (Serine/threonine-protein kinase NIK) (Q99558)
Organism: Homo sapiens (Human)
Function: Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Promotes proteolytic processing of NFKB2/P100, which leads to activation of NF-kappa-B via the non-canonical pathway. Could act in a receptor-selective manner.
Subcellular location: Cytoplasm.
Interaction partners:
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- TNF receptor-associated factor 2
- NF-kappa-B essential modulator
- TNF receptor-associated factor 3
- TNF receptor-associated factor 6
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Tumor necrosis factor receptor superfamily member 3
- Nuclear factor NF-kappa-B p100 subunit
- Mitogen-activated protein kinase kinase kinase 7
- TNF receptor-associated factor 5
Sequence:
MAVMEMACPGAPGSAVGQQKELPKAKEKTPPLGKKQSSVYKLEAVEKSPVFCGKWEILNDVITKGTAKEGSEAGPAAISIIAQAECENSQEFSPTFSERIFIAGSKQYSQSESLDQIPNNVAHATEGKMARVCWKGKRRSKARKKRKKKSSKSLAHAGVALAKPLPRTPEQESCTIPVQEDESPLGAPYVRNTPQFTKPLKEPGLGQLCFKQLGEGLRPALPRSELHKLISPLQCLNHVWKLHHPQDGGPLPLPTHPFPYSRLPHPFPFHPLQPWKPHPLESFLGKLACVDSQKPLPDPHLSKLACVDSPKPLPGPHLEPSCLSRGAHEKFSVEEYLVHALQGSVSSGQAHSLTSLAKTWAARGSRSREPSPKTEDNEGVLLTEKLKPVDYEYREEVHWATHQLRLGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGLTSPRIVPLYGAVREGPWVNIFMELLEGGSLGQLVKEQGCLPEDRALYYLGQALEGLEYLHSRRILHGDVKADNVLLSSDGSHAALCDFGHAVCLQPDGLGKSLLTGDYIPGTETHMAPEVVLGRSCDAKVDVWSSCCMMLHMLNGCHPWTQFFRGPLCLKIASEPPPVREIPPSCAPLTAQAIQEGLRKEPIHRVSAAELGGKVNRALQQVGGLKSPWRGEYKEPRHPPPNQANYHQTLHAQPRELSPRAPGPRPAEETTGRAPKLQPPLPPEPPEPNKSPPLTLSKEESGMWEPLPLSSLEPAPARNPSSPERKATVPEQELQQLEIELFLNSLSQPFSLEEQEQILSCLSIDSLSLSDDSEKNPSKASQSSRDTLSSGVHSWSSQAEARSSSWNMVLARGRPTDTPSYFNGVKVQIQSLNGEHLHIREFHRVKVGDIATGISSQIPAAAFSLVTKDGQPVRYDMEVPDSGIDLQCTLAPDGSFAWSWRVKHGQLENRP
Protein: RHOMBOID-like protein 2 (AtRBL2) (EC 3.4.21.105) (Q9CAN1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Can cleave the Drosophila proteins Spitz and Keren. May function in pollen elongation.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16223493}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- RHOMBOID-like protein 12, mitochondrial
- Rhomboid-like protein 16, chloroplastic
- Protein IQ-DOMAIN 22
- AT2G34560 protein
- non-specific serine/threonine protein kinase
- Metalloendoproteinase 1-MMP
- Metalloendoproteinase 5-MMP
- non-specific serine/threonine protein kinase
- Metalloendoproteinase 4-MMP
- non-specific serine/threonine protein kinase
Sequence:
MANRDVERVGKKNRGANNNYFYEESSGETHWTSWLIPAIVVANLAVFIAVMFVNDCPKKITGPNKECVARFLGRFSFQPLKENPLFGPSSSTLEKMGALEWRKVVHEHQGWRLLSCMWLHAGIIHLLTNMLSLIFIGIRLEQQFGFIRVGLIYLISGLGGSILSSLFLQESISVGASGALFGLLGAMLSELLTNWTIYANKAAALITLLFIIAINLALGMLPRVDNFAHIGGFLTGFCLGFVLLVRPQYGWEASRTNTSRTKRKYSMYQYVLFVVSVVLLVVGLTVALVMLFKGENGNKHCKWCHYLSCFPTSKWTC
Protein: AT02348p (Ubiquinol-cytochrome c reductase core protein 2, isoform A) (Ubiquinol-cytochrome c reductase core protein 2, isoform B) (Q9VV75)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 6
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 5A, mitochondrial
- Mitochondrial-processing peptidase subunit beta
- NADH dehydrogenase iron-sulfur protein 4
Sequence:
MACNASKTSLLRAIAKRGYATCPRPVGDLSAVNVKVLENKLVVATADATLPVSRVSLVLGAGSRNESYDIQGASHLLRLAGGLSTQNSTAFAIARNIQQVGGTLTTWGDRELVGYTVTTTADNAETGLRYLQDLLQPAFKPWELVDNAKTVVNQLNAVSTEERAIELVHKAAFRNGLGNSIYSPRFQLGKLSSESLLHYVAQTFAAGRAAVVGVGIDNNTLAGFAQTLQFPSGGSKAASANWYGGDARKDTSGHRAVVAVAGQGAAASNHKEALAFAILEQALGAKAATKRGTSAGLFGEAVNCAGGVGASVKAVNASYSDAGLFGFVVSADSKDIGKTVEFLVRGLKSASVSDKDVARGKALLKARIISRYSSDGGLIKEIGRQAALTRNVLEADALLGAIDGISQSQVQEAAKKVGSSKLAVGAIGHLANVPYASDLA
Protein: Glyoxylate/hydroxypyruvate reductase B (EC 1.1.1.79) (EC 1.1.1.81) (2-ketoaldonate reductase) (2-ketogluconate reductase) (2KR) (EC 1.1.1.215) (P37666)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2-keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D-fructose and L-sorbose. Activity with NAD is very low.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Malate synthase G
- Isocitrate lyase
- Glycolate oxidase subunit GlcD
- Malate synthase A
- Glyoxylate carboligase
- Glyoxylate/hydroxypyruvate reductase A
- 2-hydroxy-3-oxopropionate reductase
- 2-hydroxy-3-oxopropionate reductase
- Lactaldehyde dehydrogenase
- Phosphoglycolate phosphatase
Sequence:
MKPSVILYKALPDDLLQRLQEHFTVHQVANLSPQTVEQNAAIFAEAEGLLGSNENVNAALLEKMPKLRATSTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTASIGPDWYGTDVHHKTLGIVGMGRIGMALAQRAHFGFNMPILYNARRHHKEAEERFNARYCDLDTLLQESDFVCLILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSMANVVAVPHIGSATHETRYGMAACAVDNLIDALQGKVEKNCVNPHVAD
Protein: Inosine/xanthosine triphosphatase (ITPase/XTPase) (EC 3.6.1.73) (Non-canonical purine NTP phosphatase) (Non-standard purine NTP phosphatase) (Nucleoside-triphosphate phosphatase) (NTPase) (P39411)
Organism: Escherichia coli (strain K12)
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. ITP and XTP are the best substrates, followed by GDP and dITP. Is not active on dATP and dGTP, and exhibits no phosphatase activity toward pyrimidines (CTP, TTP, UTP, dCTP, and dTTP). Seems also implicated in the resistance against the thiamine metabolism inhibitors bacimethrin and CF3-HMP.
Interaction partners:
- Nucleoside diphosphate kinase
- dITP/XTP pyrophosphatase
- dTTP/UTP pyrophosphatase
- Probable phosphoglycerate mutase GpmB
Sequence:
MHQVVCATTNPAKIQAILQAFHEIFGEGSCHIASVAVESGVPEQPFGSEETRAGARNRVANARRLLPEADFWVAIEAGIDGDSTFSWVVIENASQRGEARSATLPLPAVILEKVREGEALGPVMSRYTGIDEIGRKEGAIGVFTAGKLTRASVYHQAVILALSPFHNAVY
Protein: Auxin-responsive protein IAA7 (Indoleacetic acid-induced protein 7) (Q6H543)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 11
- Auxin response factor 9
- Auxin response factor 7
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 3
- Auxin response factor 15
- Auxin response factor 2
- Auxin response factor 14
- Auxin response factor 1
- Auxin response factor 16
Sequence:
MGEASESMKKISRGRLGGSWMGEPSDHHRHGDEQEEEEKTLELSLGLPGGGWRAACRDKGTTTKHSIAAAAAADDDDGDKSSMLSLGYSTLVSHSQGKANKNKGSPEEEEAHPPPATGNNALASNNNGCFQTRSPSTPVVGWPPVRTFRRNLATSSKASLELQNGKKAAKAEEIKRAPFIKINMDGVPIGRKIDLNAFDSYEKLSLAVDKLFRGLLAAQRDPLTAGAKDCQQEDVAISGLLDGTGEYTLVYEDYEGDKVLVGDVPWGMFVSSVKRLRVLKTSDLSSSLITSGRKRTAAEC
Protein: Protein mak16 (Q9UTE6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Brix domain-containing protein C4F8.04
- Ribosome biogenesis protein rlp24
- Ribosome biogenesis protein nsa1
- Ribosomal RNA-processing protein 1 homolog
- Nucleolar complex-associated protein 3
- Probable rRNA-processing protein ebp2
- Ribosome biogenesis protein ytm1
- Uncharacterized RNA-binding protein C1827.05c
- AdoMet-dependent rRNA methyltransferase spb1
- Ribosome biogenesis protein brx1
Sequence:
MQQDEVIWQVVGHEFCSYRIKGEAQNFCRNEYNVTGLCNRQSCPLANSRYATVREDNGKLYLYMKTIERAHFPSKLWQRIKLSKNYAKALEQIDQQLLYWPGRQIHRCKQRLTRLTQYLLKARRLALKHQPALIPIKPKQAHREASRERKALIAAKLEKNIEKELVKRLKSGVYGDQPLNVNEEIWNKVLAAREGLIDEGEEEEEREEAELEFVSDDEDEEEISDLEDWLGSDQSMETSESEEEESSESESDEDEDEDNKGKIRKRKTDDAKKSRKKRAPHIHIEYEQERENEKIPAVQHSW
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (Q95QE2)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
- Cystic Fibrosis Transmembrane conductance regulator homolog
- ABC-type glutathione-S-conjugate transporter
Sequence:
MFPLVRELVCGSDYELLETGWRNNSNIPQVTNCGQHTDFSTIPTLFLVIFSPILFYELYKSRNSYLRSFSAISLRIIFCCLLVVDLTATVIYDFYLLFTKSPLYNAIHFYGDLVQYAGFCLALVLTIACRNRGIITSGVITLYWLLVVVCGVPELRYYITGRLYKEYEIHSCRAALYVFAYVCSALELFLSCFADTPSNGYIGKNSCPEYTASFLNQLTFQWFSGLAYLGNKKSLEKEDLWDLNERDKAENIIPSFIENLIPEVEGYRRKIKKNPEAAIPKNHPSILIPIFKTYKFTLLAGGCYKLMFDLLQFVAPELLRQLISFIEDKNQPMWIGVSIALLMFLSSLLQSMILHQYFHEMFRLGMNIRSVLTSAVYTKTLNLSNEARKGKTTGAIVNLMSVDIQRIQDMTTFIMLFWSAPLQILLSLYFLWKLLGVSVLAGFVILILLIPFNSFISVKMRNCQMEQMKFKDERIKMMSEILNGMKVLKLYSWEKSMEKMVLEVREKEIRVLKKLSYLNAATTLSWACAPFLVAVLTFGLYVLWDPENNVLTPQITFVALALFNILRFPLAVFAMVFSQAVQCSASNTRLKEFFAAEEMSPQTSIAYGGTDSAIKMDGGSFAWGSKEEDRKLHDITFNIKRGQLVAIVGRVGSGKSSLLHALLGEMNKLSGSVQVNGSVAYVPQLAWIQNLSLRNNILFNRPYDAKLYQNVIENCALVQDLESLPAEDRTEIGEKGINLSGGQKQRVSLARAVYQNAEIVLLDDPLSAVDSHVGKHIFENVISTATGCLGTKTRVLLTHGLTYLKHCDQVIVLKDETISEMGTYQELMNSNGAFSEFLEEFLLEESKHKGRSVSFGEDSKEVNELLRDLDQVSPAIRQRIQSQMSQEIEKTDDKNAEIIRNGLHKDEQTAHSSIGKSEEKESLLGAISPKEKTPEPPKQTKTQLIEKEAVETGKVKFEVYMSYFRAIGIKIALVFFLVYVASSMLGVFSNLYLARWSDDAKEIALSGNGSSSETQIRLGIYAVLGMGQATSVCAASIIMALGMVCASRLLHATLLENIMRSPMAFFDVTPLGRILNRFGKDIDVIDYRLPSCIMTFVGAIVQAVTIFAVPIYATPLSSFPITIVLIGYYFLLRFYVSTSRQLKRLESASRSPIYSHFQESIQGASSIRAYGVVDKFIRESQHRVDENLATYYPSIVANRWLAVRLEMVGNLIVLSSAGAAVYFRDSPGLSAGLVGLSVSYALNITQTLNWAVRMTSELETNIVAVERINEYTITPTEGNNSQSLAPKSWPENGEISIKNFSVRYRPGLDLVLHGVTAHISPCEKIGIVGRTGAGKSSLTLALFRIIEADGGCIEIDGTNIADLLLEQLRSRLTIVPQDPVLFSGTMRMNLDPFFAFSDDQIWEALRNAHLDSFVKSLQEGLHHHISEGGENLSVGQRQLICLARALLRKTKVLVLDEAAAAVDVETDSLLQKTIREQFKDCTVLTIAHRLNTVMDSDRLLVLDKGCVAEFDTPKKLLSNPDGIFYSMAKDANVV
Protein: Clathrin heavy chain (P25870)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10848635}; Peripheral membrane protein {ECO:0000269|PubMed:10848635}; Cytoplasmic side {ECO:0000269|PubMed:10848635}. Membrane, coated pit {ECO:0000269|PubMed:10848635}; Peripheral membrane protein {ECO:0000269|PubMed:10848635}; Cytoplasmic side {ECO:0000269|PubMed:10848635}. Note=Cytoplasmic face of coated pits and vesicles. Localized to punctae scattered within the cytoplasm, along the plasma membrane and concentrated in the perinuclear region. Localizes to the posterior plasma membrane in cells which retract their tails when moving forward or changing direction. Recruited to the plasma membrane under the tight cap of cross-linked receptors prior to internalization of the capped ligand. Does not localize to the plasma membrane during phagocytosis.
Interaction partners:
- Clathrin light chain
- I/LWEQ domain-containing protein
- Epidermal growth factor receptor substrate 15 homolog
- AP-1 complex subunit beta
- DNAJ heat shock N-terminal domain-containing protein
- AP-2 complex subunit alpha-2
- ANTH domain-containing protein
- AP-4 complex subunit beta
- AP-2 complex subunit mu
- AP-1 complex subunit gamma
Sequence:
MTNLPIRFQEVLQLTNLGIGSNSIGFSTLTMESEKYICIRETTPDDKNNVVIIDTDNPSQILRKQMKTDAAIMNPKEPILALKIGQVLQLISIEQKMQLKSCQMQEPLEFWKWISPNTLALVTATSVFHWTKEGNSDPVKVFDRHPDLQNTEIINYRSDSTQNWLVLVAIHQRDGRVVGRIQLYSVEKQISQSIEGHAACFANYIVPGATRPSTLFAISSRTQNASKILVLEVSKGDGPNFQKRASDVFYPPEIGASDFPVAMQVSEKYEVIYMVTKLGYIHLFDLGTANLIYRNRISNENIFVTAFEESTNGIIAVNRKGQVLSVSIDDKNIIPYICNTLNNLELAISMACKNNLPGAEGLLTTQFERYFQQGQYKEAAKVAADSPGSILRNLQTIQKFQSIPPIPDQPSALLQYFGMLLEKGKLNKVESLELVRPVLAQGKKPILEKWLTEDKLECSEQLGDEVRPHDRKLALSIYYRANASDKVITLFAETGEFDKIIAYCKKFNYKPDFMFLLQRMANANPMGAADFAVKLVKEEGGPYIDANQVVELFSARNMIQETSNFLFAILDGDRPQDANLQTKLLEINLLHAPQNADAIMGGQKFTHYNRLRIGGLCEKAGLYQRALEHYTDLADIKRVLSHAGHMVNQEFLVSYFGSLNPEDRMECMRDFLRTNPRQNLQLVVAIAVSYSDQITPEAIIAMFESFRLYEGLYLYLTQVVVTSTSPEVHFKYIEAAAKINQFKEVERMCRDSNYYDPEKTRDFLKEAKLPDQLPLIIVCDRYEFISDLTNYLYKNNLSKYIEAYVQKINPVNTPLVVGALLDLDCQEDYLRNLIMSVRNMCPADSLVEQVEKRNRLKLLLPWLEARVAEGNIEPAIHNALAKIYIDSNKNPEAFLLHNQFYDSKVVGKYCEKRDPYLSFVAYKRGLCDYELIEVTNKNTLFKNQARYLVERQDPDLWAYVLSDQNEYKRSLIDQVVQTALPESTNATEVSATVKAFMDANLPNELIELLEKIVLEGKEFKTAKELQNLLILTAIRADKSRVTDYINRLDNFDGSKLAPIAIESQLYEEAFFMYKKFQFNVEAIDVLITHIGSIERAHDFAERCNQTEVYSKLGVAQLKAEMVKECIESFIKANDTEHYQEVVAAAERKDEYEDLVKFLQMCRKKIKEPAIESELIFAYAKVNKLAEMEDFINSPNSAHIQVVGDRCFENGLYEAAKVLYTNISNFSRLTSCLVKLGQYQAAVDAARKANSTKTWKEVSAACIDAKEFRLAQVCGINIIVHGDELEELIRQYEDRGYFNELISLLESGLASERAHVGMFTELAILYSKYKEEKLMEHLKLFYSRLNVPKVIKACQANQQWPQLTYLYIHYDEHDNAIQTMINHSIEAWDHVLFKETIPKVAKLDLYYSAISFYLEEQPLLINDLLSVLSPRIDHTRAVTLIRSLGHLPLVKPYLVSAQDQNVAALNEALNELYVEEEDYESLRSSIDANSNFGTIALAQKLEKHELLEFRRIAAYLYKKNNRWAQSVELSKKDKLYKDAIQSASDSKNPAIGEELLQYFVDQQNNSAFAACLYTCYDFLKPDAVIELAWRNNILNYSFPYLIQYVKEYTTKVDQLVDDFKARQKKTEEEKEQQNIESSQYQPDLTNLSYGYAATGGMLALPPAVGYQQQQQPQQMYNPNQMMGGFQQNYNQYGGF
Protein: Lysosome-associated membrane glycoprotein 1 (LAMP-1) (Lysosome-associated membrane protein 1) (Lysosome membrane glycoprotein LEP100) (P05300)
Organism: Gallus gallus (Chicken)
Function: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, autophagy, and cholesterol homeostasis. Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:2871029, ECO:0000269|PubMed:3107839}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:2871029, ECO:0000269|PubMed:3107839}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:2871029, ECO:0000269|PubMed:3107839}; Single-pass type I membrane protein {ECO:0000255}. Cytolytic granule membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane (PubMed:2871029, PubMed:3107839). Colocalizes with OSBPL1A at the late endosome (PubMed:3107839). {ECO:0000269|PubMed:2871029, ECO:0000269|PubMed:3107839}.
Interaction partners:
- Early endosome antigen 1.
- Lysosome-associated membrane glycoprotein 2
- Serine/threonine-protein kinase TOR
- Uncharacterized protein.
- WD_REPEATS_REGION domain-containing protein
- Regulatory associated protein of MTOR complex 1.
- NPR3 like, GATOR1 complex subunit.
- GATOR2 complex protein WDR24
- DEP domain-containing protein.
- GATOR2 complex protein WDR59
Sequence:
MGGAARAVLLGFLQASSSFDVRDSTGKVCIIANLTVAFSVEYKSSGQKQFAHFFLPQNATSQSHSSCGEGNTSHPILALSFGAGHLISLNFSKTLDKYQVEELTFHYNLSDETLFPNATEGKVMVATQKSVIQARIGTEYRCINSKYVRMKHVNITFSNVTLEAYPTNDTFSANKTECREDMVSTTTVAPTTPKHATSQVPTTSPAPTAAPSSPAVGKYNVTGANGTCVLASMGLQLNITYVKKDEKMGLDLLNFIPHNTSASGMCESTSAFLNLAFEKTKITFHFVLNASSEKFFLQGVNVSTTLPSEAKAPTFEASNDSMSESRATVGNSYKCSAEENFQVTDKALVNVFNVQVQAFKVDGDKFGAMEECQLDENNMLIPIIVGAALAGLVLIVLIAYLIGRKRSHAGYQTI
Protein: GTPase, IMAP family member 4, isoform CRA_b (Immunity associated protein 4) (A0A090N7X0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAQYGSMSFNPSTPGASYGPGRQEPRNSQLRIVLVGKTGAGKSATGNSILGRKVFHSGTAAKSITKKCEKRSSSWKETELVVVDTPGIFDTEVPNAETSKEIIRCILLTSPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARSFMILIFTRKDDLGDTNLHDYLREAPEDIQDLMDIFGDRYCALNNKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQELHRVELEREKARIREEYEEKIRKLEDKVEQEKRKKQMEKKLAEQEAHYAVRQQRARTEVESKDGILELIMTALQIASFILLRLFAED
Protein: Protein phosphatase inhibitor 2 family member C (PPP1R2 family member B) (Protein phosphatase 1, regulatory subunit 2 pseudogene 9) (Type-1 protein phosphatase inhibitor 4) (I-4) (O14990)
Organism: Homo sapiens (Human)
Function: Functions as a protein phosphatase inhibitor. It inhibits activity of the catalytic subunit of PP1 and weakly inhibits the activity of myosin-associated phosphates.
Interaction partners:
Sequence:
MSASTSSHRPIKGILKNKSSSGSSVATSGQQSGGTIQDVKRKKSQKWDESSILAAHRATYRDYDLMKANEPGTSYMSVQDNGEDSVRDVEGEDSVRGVEGKEATDASDHSCEVDEQESSEAYMRKILLHKQEKKRQFEMRRRLHYNEELNIKLARQLMWKELQSEDNENEETPQGTNEEKTAAEESEEAPLTGGLQTQSCDP
Protein: Cysteine and glycine-rich protein 3 (Cysteine-rich protein 3) (CRP3) (LIM domain protein, cardiac) (Muscle LIM protein) (P50463)
Organism: Rattus norvegicus (Rat)
Function: Positive regulator of myogenesis. Acts as cofactor for myogenic bHLH transcription factors such as MYOD1, and probably MYOG and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3 isoform E47 complex and may promote formation of a functional MYOD1:TCF3 isoform E47:MEF2A complex involved in myogenesis. Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation. The role in regulation of cytoskeleton dynamics by association with CFL2 is reported conflictingly. Proposed to contribute to the maintenance of muscle cell integrity through an actin-based mechanism. Can directly bind to actin filaments, cross-link actin filaments into bundles without polarity selectivity and protect them from dilution- and cofilin-mediated depolymerization; the function seems to involve its self-association. In vitro can inhibit PKC/PRKCA activity. Proposed to be involved in cardiac stress signaling by down-regulating excessive PKC/PRKCA signaling (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16963613, ECO:0000269|PubMed:19376126, ECO:0000269|PubMed:9234731}. Cytoplasm {ECO:0000269|PubMed:16963613, ECO:0000269|PubMed:19376126, ECO:0000269|PubMed:9234731}. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P50462}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:P50461}. Note=Nucleocytoplasmic shuttling protein (PubMed:19376126). Mainly cytoplasmic. In the Z line, found associated with GLRX3 (By similarity). {ECO:0000250|UniProtKB:P50462, ECO:0000269|PubMed:19376126}.
Interaction partners:
- Titin
- Uncharacterized protein.
- Myozenin 2
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- F-actin cross-linking protein
- Myosin light chain 3
- Myosin-binding protein C, cardiac-type
- Myosin regulatory light chain 11
- Myopalladin
- Small muscular protein
Sequence:
MPNWGGGAKCGACDKTVYHAEEIQCNGRSFHKTCFHCMACRKALDSTTVAAHESEIYCKVCYGRKYGPKGIGFGQGAGCLSTDTGEHLGLQFQQSPKPARAATTSNPSKFSAKFGESEKCPRCGKSVYAAEKVMGGGKPWHKTCFPCAICGKSLESTNVTDKDGELYCKVCYAKNFGPTGIGFGGLTHQVEKKE