wanglab/gogpt-training-data huggingface dataset:
Protein: Calca protein (Calcitonin/calcitonin-related polypeptide, alpha) (Q6DGJ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Receptor activity-modifying protein 1
- Calcitonin gene-related peptide type 1 receptor
- Calcitonin gene-related peptide type 1 receptor
- G_PROTEIN_RECEP_F2_4 domain-containing protein
- Calcitonin receptor
- Pro-adrenomedullin
- Receptor
- Islet amyloid polypeptide
- Vasoactive intestinal peptide b.
- Si:ch73-193i22.1.
Sequence:
MVMLKISAFLVAYALIICQMYSSNAAPARPALESSPDRTTLSDYEARRLLQAIVKEFMQMTAEDMEQQATEENSVTTQKRACNTATCVTHRLADFLSRSGGIGSSKFVPTNVGSQAFGRRRRLSQE
Protein: GH03577p (No poles, isoform A) (Q7K2X1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLNLNCVICAELFGQADEVFATVCGHMFHHNCLNQWLDRSKTCPQCRNKCTTRNIFRVYFNLANLDVSHIDVGSLQEQLDNAMLSMKMVEKERNKDEQQIRDLKETQKKCLKTIAGLEQKVQKKDFLISSYVEQIGVLKSDAHVVDGLRKENKTLKSQIQSMEGISAILAAGSADADRLLKNEADPHVLANWVSTLKRELRQCESKKTELRNVVKVVQNDLRKEIELKRKLEERVSHLESDLYQAQEKLQAFENKTAYLDSPNASCGLNSNILALKREERRTTISPTVKENIKRIEESTSPYLNIKSSSVGLAHLLNTKGNIGLAKSKISPIKGVGGGVSMTSGTIRKTSSDLSEKYSIFKKPRLLLGSSSSSALTATTGSNFVYNGMGGSEKVDPFAQRAEEEGLSTIRSSTALSRNVNQRLKAGSLRNFNLGK
Protein: Large ribosomal subunit protein eL34B (60S ribosomal protein L34-B) (P40525)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS21B
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL24B
- Large ribosomal subunit protein eL19A
Sequence:
MAQRVTFRRRNPYNTRSNKIKVVKTPGGILRAQHVKKLATRPKCGDCGSALQGISTLRPRQYATVSKTHKTVSRAYGGSRCANCVKERIVRAFLIEEQKIVKKVVKEQTEAAKKSEKKSKK
Protein: Beta-hexosaminidase 1 (EC 3.2.1.52) (Beta-GlcNAcase 1) (Beta-N-acetylhexosaminidase 1) (Beta-hexosaminidase 2) (AtHEX2) (N-acetyl-beta-glucosaminidase 1) (A7WM73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, pyridylaminated chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc-6SO(4)) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and, to a lower extent, of leaves.
Subcellular location: Vacuole {ECO:0000269|PubMed:17644627, ECO:0000269|PubMed:21252225}.
Interaction partners:
- Glycoprotein 3-alpha-L-fucosyltransferase A
- Putative fucosyltransferase-like protein
- Alpha-
- Beta-hexosaminidase 2
- Alpha-galactosidase 3
- Alpha-galactosidase 1
- Alpha-galactosidase 2
- Beta-galactosidase 17
- Beta-galactosidase 2
- Beta-hexosaminidase 3
Sequence:
MSTNLLRLILLFITLSITSSLSTPSPADSPPYLWPLPAEFSFGNETLSVDPTVTLIVAGNGGGSLIIRAAFDRYMGIIFKHASGRGSLLSRIRFLKMVEYDITSLKIVVHSDSEELQLGVDESYTLMVSKKNEQSIVGAATIEANTVYGALRGLETFSQLCAFDYITKSVQIYKAPWYIQDKPRFGYRGLLIDTSRHYLPIDVIKQIIESMSFAKLNVLHWHIVDEQSFPLETPTYPNLWKGAYSRWERYTVEDASEIVRFAKMRGINVMAEVDVPGHAESWGTGYPDLWPSLSCREPLDVTKNFTFDVISGILADMRKIFPFELFHLGGDEVNTDCWKNTTHVKEWLQGRNFTTKDAYKYFVLRAQQIAISKNWTPVNWEETFSSFGKDLDPRTVIQNWLVSDICQKAVAKGFRCIFSNQGYWYLDHLDVPWEEVYNTEPLNGIEDPSLQKLVIGGEVCMWGETADTSVVLQTIWPRAAAAAERMWSTREAVSKGNITLTALPRLHYFRCLLNNRGVPAAPVDNFYARRPPLGPGSCYAQ
Protein: Choline transporter-like protein 1 (CDw92) (Solute carrier family 44 member 1) (CD antigen CD92) (Q8WWI5)
Organism: Homo sapiens (Human)
Function: Choline transporter. Involved in membrane synthesis and myelin production.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19357133, ECO:0000269|PubMed:31855247}; Multi-pass membrane protein {ECO:0000269|PubMed:19357133}. Mitochondrion outer membrane {ECO:0000269|PubMed:19357133}; Multi-pass membrane protein {ECO:0000269|PubMed:19357133}.
Interaction partners:
Sequence:
MGCCSSASSAAQSSKREWKPLEDRSCTDIPWLLLFILFCIGMGFICGFSIATGAAARLVSGYDSYGNICGQKNTKLEAIPNSGMDHTQRKYVFFLDPCNLDLINRKIKSVALCVAACPRQELKTLSDVQKFAEINGSALCSYNLKPSEYTTSPKSSVLCPKLPVPASAPIPFFHRCAPVNISCYAKFAEALITFVSDNSVLHRLISGVMTSKEIILGLCLLSLVLSMILMVIIRYISRVLVWILTILVILGSLGGTGVLWWLYAKQRRSPKETVTPEQLQIAEDNLRALLIYAISATVFTVILFLIMLVMRKRVALTIALFHVAGKVFIHLPLLVFQPFWTFFALVLFWVYWIMTLLFLGTTGSPVQNEQGFVEFKISGPLQYMWWYHVVGLIWISEFILACQQMTVAGAVVTYYFTRDKRNLPFTPILASVNRLIRYHLGTVAKGSFIITLVKIPRMILMYIHSQLKGKENACARCVLKSCICCLWCLEKCLNYLNQNAYTATAINSTNFCTSAKDAFVILVENALRVATINTVGDFMLFLGKVLIVCSTGLAGIMLLNYQQDYTVWVLPLIIVCLFAFLVAHCFLSIYEMVVDVLFLCFAIDTKYNDGSPGREFYMDKVLMEFVENSRKAMKEAGKGGVADSRELKPMASGASSA
Protein: Putative serine/threonine-protein phosphatase 4 regulatory subunit 1-like (Q9P1A2)
Organism: Homo sapiens (Human)
Function: May be a regulatory subunit of serine/threonine-protein phosphatase 4.
Interaction partners:
Sequence:
MAEIPLYFVDLQDDLDDYGFEDYGTDCDNMRVTAFLDIPGQDNLPPLTRLEKYAFSENTFNRQIIARGLLDIFRDFGNNEEDFLTVMEIVVRLSEDAEPTVRTELMEQIPPIAIFLQENRSNFPVVLSEYLIPIVVRYLTDPNNQIICKMASMLSKSTVERLLLPRFCELCGDRKLFQVRKVCAANFGDICHAVGQEATEKFLIPKFFELCSDAVWGMRKACAECFTAVSHSSSPGVRRTQLFPLFIRLVSDPCRWVHQAAFQSLGPFTSTFANPSRAGLYLREDGALSIWPLTQDLDSGFASGSPAPSSGGNTSPASLTRSAKPVRSEPELPVEGTSAKTSDCPHSSSSSDGPAESPVESCVSAGAEWTRVSPETSACSKLSDMNDLPISSYPGSDSWACPGNTEDVFSHFLYW
Protein: adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Q583D0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phosphodiesterase
- Phosphodiesterase
- 3', 5'-cyclic nucleotide phosphodiesterase, putative
Sequence:
MVTFMRELYVRDGAVTYLVFSLLLQVLTASSLANDKIQVKVYNMLYSNKISAKIYDPIIAGFNASITNGNPPSGANVEVVYVPTMDDSKYADYLGKHMTTHDGKELPVILGPVGDKNTLGLLKYFKEKNVTSFSPFTGSSKVRSWNPNLYFLTASPAAEMLALLRYAITQLRLHRLGFMYLKDVSYGDDEYKLAVELTTRMDRKLCGVFALKSQIGKESDDSSFSAEWDKFANARPQGVIVFGSPIPDTKKFLIKSLEDERTKGGYLLIPSTLQYVIENKWAKELGRDRFVPDKIIITGTNPLAKDDGYDAIKRSKDDMAKYLKLNRNNFSKDNWNVNLNVDESNFTEQDTEGELMVSGWIAGEVLKQALSCREWLTSRDAFITSLYNQRRYVIDDIVVGDFGGECRGMAGERGASCLCNQGGNVVYMKKMEEDHRLYPMKEGVLALTSSRCYRDLSQLYAPLSGIMFKLTDDPKALRTAEAIYDGAFYVVGKGQLGHSDRFFLHWLSSKSHDTSTALYDEVEKRVVTAVFGVVDDSLLSTKGMAFIDPITLTPQLSNPRRNVIHLSPTLEQQLFVIVEHIIQNGAGKMHAIVRSGDTRGVRKVLQKTLDIFNASLSSFVASGEGSTLRDKLPTAGEVLVAGLISDDIPIILSHLGKHHNVRIFVPFFDVALLYDELVSAFRDKPFADRLLFATNLPHWGDKNTESDLVREFHRVVRDESKWKPLSLLGYVTARAMINVLQRMGHVTPEELVDAIFSQSVITVDDMRYGPFDDKCTNGASFEEKHCAVNYGATHISVWSMSRVLNPFVSPVVTHVTPSMKYGDTEGFRLKRGHIAAIAVSCAVVLALFVTVLVLVIRSSRRNARDNNNAPKEPTDPVTLIFTDIESSTAQWAAHPEQMPDLVATHHRLIRSLITRYECYEVKTVGDSFMIACKSPFAAAQLACDLQRDFLNHDWKTTELDESYREFERKRAEDDSDYTPPTASLDPEVYRQLWNGLRVRVGIHTGLCDIRHDEVTKGYDYYGRTSNMAARTESVGNGGQVLMTRSTYLSLSGEEREQLNVTPLGDVPLRGVPKPVEMYQLNAVPGRTFAALRLDREAEEEEDNVTGSITSGSGSFAHGLTATAQQVAGCIDALLGTFPATQRQKMLATFCERWRVKKPPGMDAWNEASCRCVTRRIAAKVGCVMDFGTRNTSGSGGSFERGGSLFSPGGAAAIMLASSSSSFCGEGDCSGVQLIDLENVSAAS
Protein: Metal transporter Nramp1 (OsNramp1) (Q0D7E4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable metal transporter that may participate in the control of iron homeostasis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGVTKAEAVAGDGGKVVDDIEALADLRKEPAWKRFLSHIGPGFMVCLAYLDPGNMETDLQAGANHKYELLWVILIGLIFALIIQSLSANLGVVTGRHLAELCKTEYPVWVKTCLWLLAELAVIASDIPEVIGTGFAFNLLFHIPVWTGVLIAGSSTLLLLGLQRYGVRKLEVVVALLVFVMAGCFFVEMSIVKPPVNEVLQGLFIPRLSGPGATGDSIALLGALVMPHNLFLHSALVLSRNTPASAKGMKDVCRFFLFESGIALFVALLVNIAIISVSGTVCNATNLSPEDAVKCSDLTLDSSSFLLRNVLGKSSATVYGVALLASGQSSTITGTYAGQYVMQGFLDIKMKQWLRNLMTRSIAIVPSLIVSIIGGSSGAGRLIVIASMILSFELPFALIPLLKFSSSSNKMGENKNSIYIVGFSWVLGFVIIGINIYFLSTKLVGWILHNALPTFANVLIGIVLFPLMLLYVVAVIYLTFRKDTVKFVSRRELQAGDDTEKAQVATCVADEHSKEPPV
Protein: TNF receptor-associated factor 5 (P70191)
Organism: Mus musculus (Mouse)
Function: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol.
Interaction partners:
- Baculoviral IAP repeat-containing protein 2
- TNF receptor-associated factor 6
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- TNF receptor-associated factor 2
- Receptor-interacting serine/threonine-protein kinase 1
- Baculoviral IAP repeat-containing protein 3
- TNF receptor-associated factor 3
- Tumor necrosis factor receptor superfamily member 5
- Tumor necrosis factor receptor superfamily member 1A
- Serine/threonine-protein kinase TBK1
Sequence:
MAHSEEQAAVPCAFIRQNSGNSISLDFEPDTEYQFVEQLEERYKCAFCHSVLHNPHQTGCGHRFCQQCIRSLRELNSVPICPVDKEVIKPQEVFKDNCCKREVLNLHVYCKNAPGCNARIILGRFQDHLQHCSFQAVPCPNESCREAMLRKDVKEHLSAYCRFREEKCLYCKRDIVVTNLQDHEENSCPAYPVSCPNRCVQTIPRARVNEHLTVCPEAEQDCPFKHYGCTVKGKRGNLLEHERAALQDHMLLVLEKNYQLEQRISDLYQSLEQKESKIQQLAETVKKFEKELKQFTQMFGRNGTFLSNVQALTSHTDKSAWLEAQVRQLLQIVNQQPSRLDLRSLVDAVDSVKQRITQLEASDQRLVLLEGETSKHDAHINIHKAQLNKNEERFKQLEGACYSGKLIWKVTDYRVKKREAVEGHTVSVFSQPFYTSRCGYRLCARAYLNGDGSGKGTHLSLYFVVMRGEFDSLLQWPFRQRVTLMLLDQSGKKNHIVETFKADPNSSSFKRPDGEMNIASGCPRFVSHSTLENSKNTYIKDDTLFLKVAVDLTDLEDL
Protein: Dedicator of cytokinesis 4 (H0Y599)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
XIASFRGTVPYGLSLEIGDTVQILEKCDGWYRGFALKNPNIKGIFPSSYVHLKNACVKNKGQFEMVIPTEDSVITEMTSTLRDWGTMWKQLYVRNEGDLFHRLWHIMNEILDLRRQVLVGHLTHDRMKDVKRHITARLDWGNEQLGLDLVPRKEYAMVDPEDISITELYRLMEHRHRKKDTPVQASSHHLFVQMKSLMCSNLGEELEVIFSLFDSKENRPISERFFLRLNRNGLPKAPDKPERHCSLFVDLGSSELRKDIYITVHIIRIGRMGAGEKKNACSVQYRRPFGCAVLSIADLLTGETKDDLILKVYMCNTESEWYQIHENIIKKLNARYNLTGSNAGLAVSLQLLHGDIEQIRREYSSVFSHGVSITRKLGFSNIIMPGEMRNDLYITIERGEFEKGGKSVARNVEVTMFIVDSSGQTLKDFISFGSGEPPASEYHSFVLYHNNSPRWSELLKLPIPVDKFRGAHIRFEFRHCSTKEKGEKKLFGFSFVPLMQEDGRTLPDGTHELIVHKCEENTNLQDTTRYLKLPFSKGIFLGNNNQAMKATKESFCITSFLCSTKLTQNGDMLDLLKWRTHPDKITGCLSKLKEIDGSEIVKFLQDTLDTLFGILDENSQKYGSKVFDSLVHIINLLQDSKFHHFKPVMDTYIESHFAGALAYRDLIKVLKWYVDRITEAERQEHIQEVLKAQEYIFKYIVQSRRLFSLATGGQNEEEFRCCIQELLMSVRFFLSQESKGSGALSQSQAVFLSSFPAVYSELLKLFDVREVANLVQDTLGSLPTILHVDDSLQAIKLQCIGKTVESQLYTNPDSRYILLPVVLHHLHIHLQEQKDLIMCARILSNVFCLIKKNSSEKSVLEEIDVIVASLLDILLRTILEITSRPQPSSSAMRFQFQDVTRTGFLNRESSHGSTTLSTFSVCADTYGKVPMTSRHTGEFVACLLSLLRQMTDRHYQQLLDSFNTKEELRDFLLQIFTVFRILIRPEMFPKDWTVMRLVANNVIITTVLYLSDALRKNFLNENFDYKIWDSYFYLAVIFINQLCLQLEMFTPSKKKKVLEKYGDMRVTMGCEIFSMWQNLGEHKLHFIPALIGPFLEVTLIPQPDLRNVMIPIFHDMMDWEQRRSGNFKQVEAKLIDKLDSLMSEGKGDETYRELFNSIIPLFGPYPSLLKKIERETWRESGVSLIATVTRLMERLLDYRDCMKMGEVDGKKIGCTVSLLNFYKTELNKEEMYIRYIHKLYDLHLKAQNFTEAAYTLLLYDELLEWSDRPLREFLTYPMQTEWQRKEHLHLTIIQNFDRGKCWENGIILCRKIAEQYESYYDYRNLSKMRMMEASLYDKIMDQQRLEPEFFRVGFYGKKFPFFLRNKEFVCRGHDYERLEAFQQRMLNEFPHAIAMQHANQPDETIFQAEAQYLQIYAVTPIPESQEVLQREGVPDNIKSFYKVNHIWKFRYDRPFHKGTKDKENEFKSLWVERTSLYLVQSLPGISRWFEVEKREVVEMSPLENAIEVLENKNQQLKTLISQCQTRQMQNINPLTMCLNGVIDAAVNGGVSRYQEAFFVKEYILSHPEDGEKIARLRELMLEQAQILEFGLAVHEKFVPQDMRPLHKKLVDQFFVMKSSLGIQEFSACMQASPVHFPNGSPRVCRNSAPASVSPDGTRVIPRRSPLSYPAVNRYSSSSLSSQASAEVSNITGQSESSDEVFNMQPSPSTSSLSSTHSASPNVTSSAPSSARASPLLSDKHKHSRENSCLSPRERPCSAIYPTPVEPSQRMLFNHIGDGALPRSDPNLSAPEKAVNPTPSSWSLDSGKEAKNMSDSGKLISPPVPPRPTQTASPARHTTSVSPSPAGRSPLKGSVQSFTPSPVEYHSPGLISNSPVLSGSYSSGISSLSRCSTSETSGFENQVNEQSAPLPVPVPVPVPSYGGEEPVRKESKTPPPYSVYERTLRRPVPLPHSLSIPVTSEPPALPPKPLAARSSHLENGARRTDPGPRPRPLPRKVSQL
Protein: Probable Resistance-Nodulation-Cell Division (RND) efflux membrane fusion protein (Q9HXW3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable Resistance-Nodulation-Cell Division
- Probable Resistance-Nodulation-Cell Division
- Pyoverdine export ATP-binding/permease protein PvdT
- Bcr/CflA family efflux transporter
- Probable beta-lactamase
- Efflux pump membrane transporter
- Probable outer membrane protein
- Probable transcriptional regulator
Sequence:
MYRHIPLVALSLFSSLFLAACGNGTPPPAAARPAIVVQPQPAGEVSQAFPGEIRARHEPELAFRIGGKVIRRLVEVGERVKKDQPLAELDPQDVRLQLEAARAQVSAAEANLQTVRAEYRRYRTLLDRNLVSHSQFENIQNSYRAGEARLKQIRAEFNVADNQAGYAVLRSPQDGVIASRRVEVGQVVAAGQTVFSLAADGEREVLIGLPEHSFERFRIGQPVSVELWSQRDRRFAGHIRELSPAADPQSRTFAARVAFDDRATPAELGQSARVYVAAAEAVPLSVPLSALTAEAGQAFVWVVEPGSSTLRRQAVRTGPYAEDRVPVLEGLKAGDWVVATGVQVLREGQQVRPIDRANRTVKLAAKE
Protein: Galectin-2 (Gal-2) (Q9CQW5)
Organism: Mus musculus (Mouse)
Function: This protein binds beta-galactoside. Its physiological function is not yet known.
Interaction partners:
- Galanin peptides
- Galectin-1
- Spexin
Sequence:
MSEKFEVKDLNMKPGMSLKIKGKIHNDVDRFLINLGQGKETLNLHFNPRFDESTIVCNTSEGGRWGQEQRENHMCFSPGSEVKITITFQDKDFKVTLPDGHQLTFPNRLGHNQLHYLSMGGLQISSFKLE
Protein: Procyclin associated gene 3 (D6XHD4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFRKSSELEGKCSSSPFVRRDSHTEASTKQAATLLLTFWFILFPYFSVGVFLLPPLGIGHSHMKALASAAKGGSVWYFLWRHLSSFPFRPPLFPWRKASGTVLPDDLCPVRSIMNNSYKSVCRYGGGYFPNRFGCFYYFVGRFKVGNSVHFQKNCDSYIWFYMEGGRAENVYVLAWMSRKINSSFRVFSVHYVIYGLAFRFV
Protein: Leiomodin-2 (Cardiac leiomodin) (C-LMOD) (Leiomodin) (Q6P5Q4)
Organism: Homo sapiens (Human)
Function: Mediates nucleation of actin filaments and thereby promotes actin polymerization. Plays a role in the regulation of actin filament length (By similarity). Required for normal sarcomere organization in the heart, and for normal heart function.
Subcellular location: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966, ECO:0000269|PubMed:26370058}. Cytoplasm, myofibril {ECO:0000269|PubMed:20685966}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26370058}. Note=Colocalizes with actin filaments in sarcomeres. Detected close to the M line. {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966, ECO:0000269|PubMed:26370058}.
Interaction partners:
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Myozenin-2
- Cysteine and glycine-rich protein 3
- Xin actin-binding repeat-containing protein 2
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin light chain 1/3, skeletal muscle isoform
- Nebulin-related-anchoring protein
- Nebulin
- Troponin I, slow skeletal muscle
Sequence:
MSTFGYRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRNLPVGLRQKSLTEKTPTGTFSREALMAYWEKESQKLLEKERLGECGKVAEDKEESEEELIFTESNSEVSEEVYTEEEEEESQEEEEEEDSDEEERTIETAKGINGTVNYDSVNSDNSKPKIFKSQIENINLTNGSNGRNTESPAAIHPCGNPTVIEDALDKIKSNDPDTTEVNLNNIENITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNVNVESNFITGKGILAIMRALQHNTVLTELRFHNQRHIMGSQVEMEIVKLLKENTTLLRLGYHFELPGPRMSMTSILTRNMDKQRQKRLQEQKQQEGYDGGPNLRTKVWQRGTPSSSPYVSPRHSPWSSPKLPKKVQTVRSRPLSPVATPPPPPPPPPPPPPSSQRLPPPPPPPPPPLPEKKLITRNIAEVIKQQESAQRALQNGQKKKKGKKVKKQPNSILKEIKNSLRSVQEKKMEDSSRPSTPQRSAHENLMEAIRGSSIKQLKRVEVPEALR
Protein: Prolyl hydroxylase EGLN2 (EC 1.14.11.-) (Egl nine homolog 2) (EC 1.14.11.29) (HPH-3) (Hypoxia-inducible factor prolyl hydroxylase 1) (HIF-PH1) (HIF-prolyl hydroxylase 1) (HPH-1) (Prolyl hydroxylase domain-containing protein 1) (PHD1) (Q6AYU4)
Organism: Rattus norvegicus (Rat)
Function: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as ATF4, IKBKB, CEP192 and HIF1A. Target proteins are preferentially recognized via a LXXLAP motif (By similarity). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A (By similarity). Also hydroxylates HIF2A (By similarity). Has a preference for the CODD site for both HIF1A and HIF2A (By similarity). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (By similarity). Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes (By similarity). EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle (By similarity). Also regulates susceptibility to normoxic oxidative neuronal death (By similarity). Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation (By similarity). Hydroxylates IKBKB, mediating NF-kappa-B activation in hypoxic conditions (By similarity). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16765982}.
Interaction partners:
- Endothelial PAS domain-containing protein 1
- Hypoxia-inducible factor 1-alpha
- Hypoxia-inducible factor 3-alpha
- Protein kinase C gamma type
- Protein kinase C beta type
- Prolyl hydroxylase EGLN3
- von Hippel-Lindau disease tumor suppressor
- Aryl hydrocarbon receptor nuclear translocator
Sequence:
MDSPCQPQALNQALPQLPGSVSESLEPSRARMGVESYLPCPLLPSYHRSGASGEASAGNGTPRTTATATTTTASPLREGFGGQDGGELWPLQSEGAAALVTKECQRLAAQGARPEAPKRKWAKDGGDAPSPSKRPWARQENQEAKGESGVGCDSGGGSSNSTTHSSGEASSRLREEAQPSAPERLALDYIVPCMRYYGICVKDNFLGAVLGGRVLAEVEALKWGGRLRDGQLVSQRAIPPRSIRGDQIAWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGNYVINGRTKAMVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAARDKYQLASGQKGVQVPVSQPATPT
Protein: Cell adhesion molecule 1 (Immunoglobulin superfamily member 4) (IgSF4) (Nectin-like protein 2) (NECL-2) (Spermatogenic immunoglobulin superfamily) (SgIgSF) (Synaptic cell adhesion molecule) (SynCAM) (Tumor suppressor in lung cancer 1) (TSLC-1) (Q8R5M8)
Organism: Mus musculus (Mouse)
Function: Mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in a Ca(2+)-independent manner. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ T-cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM1 in vivo. In mast cells, may mediate attachment to and promote communication with nerves (By similarity). CADM1, together with MITF, is essential for development and survival of mast cells in vivo. By interacting with CRTAM and thus promoting the adhesion between CD8+ T-cells and CD8+ dendritic cells, regulates the retention of activated CD8+ T-cell within the draining lymph node. Required for the intestinal retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent, intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells. Interaction with CRTAM promotes the adhesion to gut-associated CD103+ dendritic cells, which may facilitate the expression of gut-homing and adhesion molecules on T-cells and the conversion of CD4+ T-cells into CD4+ CD8+ T-cells. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:20739279, ECO:0000269|PubMed:24687959}; Single-pass type I membrane protein {ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:20739279}. Synaptic cell membrane {ECO:0000269|PubMed:20739279, ECO:0000269|PubMed:23209303}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized to the basolateral plasma membrane of epithelial cells in gall bladder. {ECO:0000269|PubMed:12826663}.
Interaction partners:
- Cytotoxic and regulatory T-cell molecule
- Hepatitis A virus cellular receptor 2 homolog
- Band 4.1-like protein 3
- Nectin-3
- Cell adhesion molecule 3
- Protein 4.1
- Syntenin-1
- Vascular cell adhesion protein 1
- Band 4.1-like protein 2
- Interleukin-6
Sequence:
MASAVLPSGSQCAAAAAVAAAAAPPGLRLRLLLLLLSAAALIPTGDGQNLFTKDVTVIEGEVATISCQVNKSDDSVIQLLNPNRQTIYFRDFRPLKDSRFQLLNFSSSELKVSLTNVSISDEGRYFCQLYTDPPQESYTTITVLVPPRNLMIDIQKDTAVEGEEIEVNCTAMASKPATTIRWFKGNKELKGKSEVEEWSDMYTVTSQLMLKVHKEDDGVPVICQVEHPAVTGNLQTQRYLEVQYKPQVHIQMTYPLQGLTREGDAFELTCEAIGKPQPVMVTWVRVDDEMPQHAVLSGPNLFINNLNKTDNGTYRCEASNIVGKAHSDYMLYVYDPPTTIPPPTTTTTTTTTTTTTILTIITDTTATTEPAVHDSRAGEEGTIGAVDHAVIGGVVAVVVFAMLCLLIILGRYFARHKGTYFTHEAKGADDAADADTAIINAEGGQNNSEEKKEYFI
Protein: Xyloglucan endotransglucosylase/hydrolase protein 15 (At-XTH15) (XTH-15) (EC 2.4.1.207) (EC 3.2.1.151) (Q38911)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues. Has a high XET activity, but little or no XEH activity in vitro. Acceptor preferences are XXXGol > XLLGol = XLFGol > XXLGol > XXFGol.
Subcellular location: Secreted, cell wall {ECO:0000305}. Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Transcription factor PIL1
- Transcription factor HFR1
- Transcription factor PIF5
- Transcription factor PIF4
- Homeobox-leucine zipper protein HAT4
- Argininosuccinate lyase
- NAD
- Expansin-A8
- Auxin-responsive protein IAA29
- Vacuolar protein sorting-associated protein 29
Sequence:
MGPSSSLTTIVATVLLVTLFGSAYASNFFDEFDLTWGDHRGKIFNGGNMLSLSLDQVSGSGFKSKKEYLFGRIDMQLKLVAGNSAGTVTAYYLSSQGATHDEIDFEFLGNETGKPYVLHTNVFAQGKGDREQQFYLWFDPTKNFHTYSIVWRPQHIIFLVDNLPIRVFNNAEKLGVPFPKSQPMRIYSSLWNADDWATRGGLVKTDWSKAPFTAYYRGFNAAACTASSGCDPKFKSSFGDGKLQVATELNAYGRRRLRWVQKYFMIYNYCSDLKRFPRGFPPECKKSRV
Protein: Citrate synthase (A0A060WKC7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
- malate synthase
- Malate dehydrogenase
- Malate dehydrogenase
- Cytoplasmic aconitate hydratase
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
Sequence:
MSFLATSISRLAPRLLQSKNASCVIVASRHASSSTNLKDVLSDLIPKEQSRIKSFKQQYGKTNIGSITVDMVYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQQLLPKAPGGQEPLPEGLFWLLVTGQVPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAITALNSESSFARAYSEGVNKAKYWEFIYEDSMDLIAKLPCVAAKIYRNLYREGSSIGAIDSNQDWSANFANMLGYSNSAEFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLVWLTALQKEMGGEVSDEKMRDYIWNTLKSGRVVPGYGHAVLRKTDPRYQCQQEFAFKHLPNDPMFKLVHQLYKIVPPVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMTLVGANKSG