wanglab/gogpt-training-data huggingface dataset:
Protein: Calpain-3 (EC 3.4.22.54) (Calcium-activated neutral proteinase 3) (CANP 3) (Calpain L3) (Calpain p94) (Muscle-specific calcium-activated neutral protease 3) (Q64691)
Organism: Mus musculus (Mouse)
Function: Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-410'. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P20807}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P20807}.
Interaction partners:
- Titin
- Dysferlin
- Calpastatin
- Beta-parvin
- Ankyrin repeat domain-containing protein 1
- Caveolin-3
- Telethonin
- Myopalladin
- Ankyrin repeat domain-containing protein 23
- Ribitol 5-phosphate transferase FKRP
Sequence:
MPTVISPTVAPRTGAEPRSPGPVPHPAQGKTTEAGGGHPSGIYSAIISRNFPIIGVKEKTFEQLRRKCLEKKVLYLDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIGGANRTDICQGDLGDCWFLAAIACLTLNERLLFRVIPHDQSFTENYAGIFHFQFWRYGDWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFFEIKDAPSDMYKIMRKAIERGSLMGCSIDDGTNMTYGTSPSGLNMGELIARMVRNMDNSLLRDSDLDPRGSDDRPSRTIVPVQYETRMACGLVKGHAYSVTGLEEALFKGEKVKLVRLRNPWGQVEWNGSWSDGWKDWSFVDKDEKARLQHQVTEDGEFWMSYDDFVYHFTKLEICNLTADALESDKLQTWTVSVNEGRWVRGCSAGGCRNFPDTFWTNPQYRLKLLEEDDDPEDSEVICSFLVALMQKNRRKDRKLGANLFTIGFAIYEVPKEMHGNKQHLQKDFFLYNASKARSKTYINMREVSQRFRLPPSEYVIVPSTYEPHQEGEFILRVFSEKRNLSEEAENTISVDRPVKKKKNKPIIFVSDRANSNKELGVDQEAEEGKDKAGPEKRGETPQPRPGHTDQESEEQQQFRNIFRQIAGDDMEICADELKNVLNTVVNKHKDLKTQGFTLESCRSMIALMDTDGSGRLNLQEFHHLWKKIKAWQKIFKHYDTDHSGTINSYEMRNAVNDAGFHLNSQLYDIITMRYADKHMNIDFDSFICCFVRLEGMFRAFNAFDKDGDGIIKLNVLEWLQLTMYA
Protein: Transmembrane inner ear (D4AE26)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- LHFPL tetraspan subfamily member 5 protein
- Transmembrane channel-like protein
- Calcium and integrin-binding family member 2
Sequence:
MAGRQRGSGRLWALGGAALGACLAGVASQLVEPSTAPPKPKPPPLTKETVVFWDMRLWHVVGIFSLFVLSIIITLCCVFNCRVPRTRKEIEARYLQRKAAKMYTDKLETVPPLNELTEIPGEDKKKKKKDSVDTVAIKVEEDEKNEAKKKGEK
Protein: Matrix metalloproteinase-19 (MMP-19) (EC 3.4.24.-) (Matrix metalloproteinase RASI) (Q9JHI0)
Organism: Mus musculus (Mouse)
Function: Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis (By similarity). Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Nidogen-1
Sequence:
MDWQQLWLAFLLPMTVSGRALGPTEKEAVLDYLLQYGYLQKPLEGADDFRLEDITEALRTFQEASGLPISGQMDDATRARMKQPRCGLEDPFNQKSLKYLLLGHWRKKNLTFRIFNVPSTLSLPRVRAALHQAFKYWSSVAPLTFREVKAGWADIRLSFHGRQSLYCSNTFDGPGKVLAHADIPELGSIHFDKDELWTEGTYQGVNLRIIAAHEVGHALGLGHSRYTQALMAPVYAGYQPFFKLHPDDVAGIQALYGKRSPETRDEEEETEMLTVSPVTAKPGPMPNPCSGEVDAMVLGPRGKTYAFKGDYVWTVTDSGPGPLFQISALWEGLPGNLDAAVYSPRTRRTHFFKGNKVWRYVDFKMSPGFPMKFNRVEPNLDAALYWPVNQKVFLFKGSGYWQWDELARTDLSRYPKPIKELFTGVPDRPSAAMSWQDGQVYFFKGKEYWRLNQQLRVAKGYPRNTTHWMHCGSQTPDTNSSTGDVTPSTTDTVLGTTPSTMGSTLDIPSATDSASLSFSANVTLLGA
Protein: T-box transcription factor tbx-35 (Q09376)
Organism: Caenorhabditis elegans
Function: Transcription factor which plays a role in mesoderm development, probably by regulating expression of target genes, such as homeobox protein ceh-51. Binds to DNA consensus motif 5'-[AG]T[GC][GT]CACC[TC][AGCT][AGCT][CT][CT]-3' in promoter elements.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
Interaction partners:
- Homeobox protein ceh-51
- GATA-type domain-containing protein
- GATA-type domain-containing protein
- GATA-type domain-containing protein
- Defective pharyngeal development protein 4
- Homeobox protein pal-1
- GATA transcription factor END-1
- Transcription factor elt-7
Sequence:
MSFNYSMNTPSPSMLSFDMDIPITAFLHNSDVFQLFHPDIMEQVVVNKERVFFPTPSFNVLNLESDCLYKMSLRFDKTNNKRFQFNRQTKQWTEYDKVSNHKESEVFVHPSEIRTGDDWMKSPVEFFIKVTNLRSSESDEVICLESQCKYQPTLLIQKVFRDCFGCFQAHGPPVEIKFALLTFIATTRYCSRRIADIKSSLNPFSSQDTKKKNKRNTLKAVSQEENQPIENSSFHQSFSNQYLSKPDLDLKSTTLLQIAPDHSFEPTNFVSSSHFPCWDSIFCQQSFPTPSSSPYSDSLPHFTNEWNTPTFYNENFMSYPNFPNY
Protein: Probable arabinosyltransferase ARAD1 (EC 2.4.2.-) (Arabinan alpha-1,5-arabinosyltransferase) (L-Arabinosyltransferase) (Protein ARABINAN DEFICIENT 1) (Q6DBG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan. May function as inverting enzyme using UDP-beta-L-arabinopyranoside. May be important for arabinan side chains of rhamnogalacturonan I (RG-I), a major component of pectins. Cell wall pectic arabinans are involved in thigmomorphogenesis response of inflorescence stems to mechanical stress.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:22270560}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Glycosylinositol phosphorylceramide mannosyl transferase 1
- Probable galacturonosyltransferase 7
- Polygalacturonate 4-alpha-galacturonosyltransferase
- Xyloglucan 6-xylosyltransferase 2
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase
- Xyloglucan galactosyltransferase MUR3
- Beta-1,2-xylosyltransferase
- Xyloglucan 6-xylosyltransferase 1
- Galactan beta-1,4-galactosyltransferase GALS1
- Xyloglucan glycosyltransferase 4
Sequence:
MARKSSLLKRAAIAVVSVIAIYVILNASVSRSLPSSSDLPRQLIREDDDDEGRAPIQPRVRVYMYNLPKRFTYGLIEQHSIARGGIKKPVGDVTTLKYPGHQHMHEWYLFSDLNQPEVDRSGSPIVRVSDPADADLFYVPVFSSLSLIVNAGRPVEAGSGYSDEKMQEGLVEWLEGQEWWRRNAGRDHVIPAGDPNALYRILDRVKNAVLLVSDFGRLRPDQGSFVKDVVIPYSHRVNLFNGEIGVEDRNTLLFFMGNRYRKDGGKVRDLLFQVLEKEDDVTIKHGTQSRENRRAATKGMHTSKFCLNPAGDTPSACRLFDSIVSLCVPLIVSDSIELPFEDVIDYRKFSIFVEANAALQPGFLVQMLRKIKTKKILEYQREMKSVRRYFDYDNPNGAVKEIWRQVSHKLPLIKLMSNRDRRLVLRNLTEPNCSCLCTNQTGLITSI
Protein: GH10260p (Q8T0S7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHVGQLQVRLPVQLQFFRLYVKYADLNRYTLALCSPSYLRSNGQPITRFYNKDLILYVIYNLIIRGVWPAVPGKSAVSKCVPSAIYKNMI
Protein: Probable translation initiation factor, mitochondrial (Q76PC7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in mitochondrial translation initiation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Translation initiation factor IF-2, mitochondrial
- Uncharacterized protein C106.19
- Small ribosomal subunit protein mS35
- Uncharacterized protein PB1E7.11c
- Heat shock protein 60, mitochondrial
Sequence:
MNSYLQFPHRKLFIQFSYSLTSVFRKCQSRTFMNSQFASAKLSNSIKKYFDGRIDESIKYQEIFIRGLENKGKLSKTSLVEALARVRAKPETVLYKVADPNENNKYPICSIISYTELSKLRENQSSRLREAEKSKHKNKTRTRYVLFSWRTDVNDIERKLKSVKDFLQDGNIVEIHVQNKKRSQPVSQEVRDSILSKIQLEIEGLGKDMKPPIVNSHSATFLLQPLVSKSSEL
Protein: Insulin-like growth factor 1 (Insulin-like growth factor I) (IGF-I) (Somatomedin) (P05017)
Organism: Mus musculus (Mouse)
Function: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation (By similarity). Ca(2+)-dependent exocytosis of IGF1 is required for sensory perception of smell in the olfactory bulb. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:21496647}.
Interaction partners:
- Insulin receptor
- Insulin-like growth factor-binding protein 1
- Insulin-like growth factor 1 receptor
- Insulin-like growth factor-binding protein 2
- Insulin-like growth factor-binding protein 5
- Insulin-1
- Insulin-2
- Insulin-like growth factor-binding protein 3
- Insulin-like growth factor-binding protein 6
- Insulin-like growth factor 2
Sequence:
MGKISSLPTQLFKICLCDFLKIKIHIMSSSHLFYLALCLLTFTSSTTAGPETLCGAELVDALQFVCGPRGFYFNKPTGYGSSIRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPTKAARSIRAQRHTDMPKTQKEVHLKNTSRGSAGNKTYRM
Protein: Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1) (P18588)
Organism: Rattus norvegicus (Rat)
Function: Interferon-induced dynamin-like GTPase which has antiviral activity against influenza A virus, (IAV) and Thogoto virus (THOV). Inhibits IAV by interefering with the process of primary transcription, probably by affecting the viral polymerase function (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:2173790}. Cytoplasm {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
Interaction partners:
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Ubiquitin-like protein ISG15
- Interferon-induced GTP-binding protein Mx3
- Ubl carboxyl-terminal hydrolase 18
- 2'-5'-oligoadenylate synthase 1A
- Interferon-induced, double-stranded RNA-activated protein kinase
- Interferon regulatory factor 7.
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon regulatory factor 9
- Interferon-induced protein with tetratricopeptide repeats 1
Sequence:
MKERTSACRHGTPQKHPDTSEESQAMESVDNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKQLKQGEKWSGKVIYKDTEIEISHPSLVEREINKAQNLIAGEGLKISSDLISLEVSSPHVPDLTLIDLPGITRVAVGDQPADIEHKIKRLITEYIQKQETINLVVVPSNVDIATTEALKMAQEVDPQGDRTIGILTKPDLVDRGTEDKVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRVLLEDGKATVPCLAKRLTMELTSHICKSLPILENQINVNHQIASEELQKYGADIPEDDSKRLSFLMNKINVFNKDILSLVQAQENISWEESRLFTKLRNEFLAWNDYIEEHFKKTLGSSEKHSQMEKFESHYRGRELPGFVDYKAFENIIKKEVKALEEPALNMLHRVTTMVKNAFTKVSSNNFGDFLNLHSTAKSKIEDIRFNQEKEAEKLIRLHFQMEHIVYCQDQAYKKALQEIREKEAEKEKSTFGAFQHNSPRKELTTTEMTQHLNAYYQECGRNIGRQIPLIIQYSILQTFGQEMEKAMLQLLQDTSKCNWFLTEQSDSREKKKFLKRRLLRLDEAQRKLAKFSN
Protein: Longitudinals lacking protein, isoforms F/I/K/T (Q867Z4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Putative transcription factor required for axon growth and guidance in the central and peripheral nervous systems. Repels CNS axons away from the midline by promoting the expression of the midline repellent sli and its receptor robo.
Subcellular location: Nucleus {ECO:0000269|PubMed:8050351}.
Interaction partners:
- Chromosomal serine/threonine-protein kinase JIL-1
Sequence:
MDDDQQFCLRWNNHQSTLISVFDTLLENETLVDCTLAAEGKFLKAHKVVLSACSPYFATLLQEQYDKHPIFILKDVKYQELRAMMDYMYRGEVNISQDQLAALLKAAESLQIKGLSDNRTGGGVAPKPESSGHHRGGKLSGAYTLEQTKRARLATGGAMDTSGDVSGSREGSSSPSRRRRKVRRRSMENDAHDNSNSSVLQAAASNQSILQQTGAGLAVSALVTTQLSSGPAAGTSSQASSTQQQQPLTSTNVTKKTESAKLTSSTAAPASGASASAAVQQAHLHQQQAQTTSDAINTENVQAQSQGGAQGVQGDDEDIDEGSAVGGPNSATGPNPASASASAVHAGVVVKQLASVVDKSSSNHKHKIKDNSVSSVGSEMVIEPKAEYDDDAHDENVEDLTLDEEDMTMEELDQTAGTSQGGEGSSQTYATWQHDRSQDELGLMAQDAQQRDPQASKQDKGEQTEGAQDEFELDDCLLESNDIVITQNKDGFVLHVKKLGNITAAKLEENQAVAQQQGQAAVTVTGPAGQPTPTITELLNAAAASHSEPKPTLTTLTSTPIKLPSSECELINIKKIIPATTTIATHHPHTSSTIIHPHHIIQHVSQEPHHQEHHQQHQTIHIEEVPQTSQQHHQQQHHHQLQTVQPTHTQVQSIITAHPGQTINLVGLRNVQLADSKPIASRIRYSRGKIIGPTVQNLQIVETHEPIQHQHHELSDGTKYEISEIDLNNPNASAAIISDLVKYAEIDDIELPDGTKIGIGFAPSEITEHMQTSGGETHITTIEHEPQELQTVHQHEQTQQTHHIHAGQLQTHHIQTVVQSSSGQQQHDQQQHHQHHSIELQDDDGVETITPEELGMHDSSKSYTILTTRPMKEESEHDPSGMTYELSLSDSSLGPCDDPESRYVCRHCGKKYRWKSTLRRHENVECGGKEPCHPCPYCSYKAKQRGNLGVHVRKHHPEKPQLESKRGRKV
Protein: Alpha-2C adrenergic receptor (Alpha-2 adrenergic receptor subtype C4) (Alpha-2C adrenoreceptor) (Alpha-2C adrenoceptor) (Alpha-2CAR) (P18825)
Organism: Homo sapiens (Human)
Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-13
- Sodium-dependent dopamine transporter
- Alpha-2A adrenergic receptor
- Angiotensinogen
- Sodium-dependent noradrenaline transporter
- Guanine nucleotide-binding protein G
Sequence:
MASPALAAALAVAAAAGPNASGAGERGSGGVANASGASWGPPRGQYSAGAVAGLAAVVGFLIVFTVVGNVLVVIAVLTSRALRAPQNLFLVSLASADILVATLVMPFSLANELMAYWYFGQVWCGVYLALDVLFCTSSIVHLCAISLDRYWSVTQAVEYNLKRTPRRVKATIVAVWLISAVISFPPLVSLYRQPDGAAYPQCGLNDETWYILSSCIGSFFAPCLIMGLVYARIYRVAKLRTRTLSEKRAPVGPDGASPTTENGLGAAAGAGENGHCAPPPADVEPDESSAAAERRRRRGALRRGGRRRAGAEGGAGGADGQGAGPGAAESGALTASRSPGPGGRLSRASSRSVEFFLSRRRRARSSVCRRKVAQAREKRFTFVLAVVMGVFVLCWFPFFFSYSLYGICREACQVPGPLFKFFFWIGYCNSSLNPVIYTVFNQDFRRSFKHILFRRRRRGFRQ
Protein: Proteasome subunit beta (Q38DP7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome regulatory non-ATP-ase subunit 7
- Proteasome regulatory non-ATP-ase subunit 9
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome regulatory ATPase subunit 1
- Proteasome alpha 7 subunit
- Proteasome subunit beta
- Proteasome regulatory non-ATP-ase subunit 10
Sequence:
MTGFSFENVQRNLNLEQQGLHPPRTLKTGTTIVGVVFEGGVVLGADTRATEGSIVADKRCKKIHYMAPNIMCCGAGTAADTEAVTNMTAANLTLHRLGTGKQSRVSEALTLLKRHLYRYQGHVSAALVLGGVDVGGAFLATVAPHGSTDRLPFVAMGSGSIAAMAALETGYKENLTLEEAKQLVVSAIHKGIFNDPYSGTQVDLCVITKAKTEMLIGYDKPNDRKYPKHDIKLPPGTTPILREEIRQLVTITELE
Protein: Growth hormone secretagogue receptor type 1 (GHS-R) (GH-releasing peptide receptor) (GHRP) (Ghrelin receptor) (Q95254)
Organism: Sus scrofa (Pig)
Function: Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Appetite-regulating hormone
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- Somatostatin
- Pro-neuropeptide Y
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- G protein subunit alpha i3
- Endothelin-1
- Somatoliberin
Sequence:
MWNATPSEEPGPNLTLPDLGWDAPPENDSLVEELLPLFPTPLLAGVTATCVALFVVGIAGNLLTMLVVSRFREMRTTTNLYLSSMAFSDLLIFLCMPLDLFRLWQYRPWNLGNLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVILVIWAVAFCSAGPIFVLVGVEHDNGTDPRDTNECRATEFAVRSGLLTVMVWVSSVFFFLPVFCLTVLYSLIGRKLWRRKRGEAAVGSSLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSLEPGSVEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFKLLGFEPFSQRKLSTLKDESSRAWTESSINT
Protein: Host-nuclease inhibitor protein gam (P03702)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Both GamL and GamS bind to host RecBCD nuclease and inhibit its activities, protecting the viral DNA against RecBCD mediated degradation. Isoform GamS mimics DNA, preventing RecBCD from binding DNA. Expression of this protein in E.coli renders cells more sensitive to fluoroquinolone antibiotics (which inhibit topoisomerases and induce dsDNA breaks). Frameshift mutations that delete most of this protein (starting from position 78 or 97 of GamL) allow the bacteriophage to overcome the retron Ec48 bacteriophage defense system. Overexpression of the wild-type gam protein in E.coli with an intact Ec48 retron leads to a dramatic decrease in cell growth, the frameshift mutants do not have this effect.
Interaction partners:
Sequence:
MDINTETEIKQKHSLTPFPVFLISPAFRGRYFHSYFRSSAMNAYYIQDRLEAQSWARHYQQLAREEKEAELADDMEKGLPQHLFESLCIDHLQRHGASKKSITRAFDDDVEFQERMAEHIRYMVETIAHHQVDIDSEV
Protein: Pyruvate kinase (EC 2.7.1.40) (Q9FNN1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- L-lactate dehydrogenase
- Cytosolic enolase 3
- Bifunctional enolase 2/transcriptional activator
- Enolase 1, chloroplastic
- Pyruvate decarboxylase 4
- Malate dehydrogenase 2, mitochondrial
- Malate dehydrogenase 1, cytoplasmic
- Malate dehydrogenase 1, mitochondrial
- Glucose-6-phosphate isomerase, cytosolic
- Malate dehydrogenase 3, cytoplasmic
Sequence:
MSNIDIEGILKELPNDGRIPKTKIVCTLGPASRTVSMIEKLLKAGMNVARFNFSHGSHEYHQETLDNLRSAMHNTGILAAVMLDTKGPEIRTGFLKDGNPIQLKEGQEITITTDYDIQGDESTISMSYKKLPLDVKPGNTILCADGSISLAVLSCDPESGTVRCRCENSAMLGERKNVNLPGVVVDLPTLTDKDIEDILGWGVPNSIDMIALSFVRKGSDLVNVRKVLGSHAKSIMLMSKVENQEGVINFDEILRETDAFMVARGDLGMEIPIEKIFLAQKLMIYKCNLAGKPVVTATQMLESMIKSPRPTRAEATDVANAVLDGTDCVMLSGESAAGAYPEIAVKVMAKICIEAESSLDYNTIFKEMIRATPLPMSPLESLASSAVRTANKARAKLIIVLTRGGSTANLVAKYRPAVPILSVVVPVMTTDSFDWSCSDESPARHSLIYRGLIPMLAEGSAKATDSEATEVIIEAALKSATQRGLCNRGDAIVALHRIGAASVIKICVVK
Protein: Cbp/p300-interacting transactivator 1 (Melanocyte-specific protein 1) (P97769)
Organism: Mus musculus (Mouse)
Function: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Enhances SMAD-mediated transcription by strengthening the functional link between the DNA-binding SMAD transcription factors and the p300/CBP transcription coactivator complex. Stimulates estrogen-dependent transactivation activity mediated by estrogen receptors signaling; stabilizes the interaction of estrogen receptor ESR1 and histone acetyltransferase EP300. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Induces transcription from estrogen-responsive promoters and protection against cell death. Potentiates EGR2-mediated transcriptional activation activity from the ERBB2 promoter. Acts as an inhibitor of osteoblastic mineralization through a cAMP-dependent parathyroid hormone receptor signaling. May play a role in pigmentation of melanocytes. Associates with chromatin to the estrogen-responsive TGF-alpha promoter region in a estrogen-dependent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:14673158, ECO:0000269|PubMed:17938205}. Cytoplasm {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm by a nuclear export signal (NES) and in a CRM1-dependent manner. {ECO:0000250}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Histone acetyltransferase p300
- Homeobox protein SIX2
Sequence:
MPTMSRPALDVKGGTTSGKEDANQEMNSLAYSNLGVKDRKAVTVLHYPGVTANGAKANGVPTSSSGSTSPIGSPTATPSSKPPSFNLHPTPHLMASMQLQKLNSQYQGAAATAAAALTGAGLPGEEEPMQNWVTAPLVVGGSPGSVSPPAGAQSPALIDSDPVDEEVLMSLVVELGLDRANELPELWLGQNEFDFTADFPSGC
Protein: FYVE-type domain-containing protein (Q38AR4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTGNSHCVLCKRSFGIFLWKHKCAKCNRNVCDDCAPKVSGVRKCEECSAVKPADSSAKTPANQPRVQGSEENPVLEAAMRRRQQHMLGVGPNTVNSEEKIRLLTEITTILKQRGEDEPFGLRSMDETKLRVYLRHIREKYGITAVKQS
Protein: Hemoglobin subunit gamma-1 (Gamma-1-globin) (Hb F Agamma) (Hemoglobin gamma-1 chain) (Hemoglobin gamma-A chain) (P69891)
Organism: Homo sapiens (Human)
Function: Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.
Interaction partners:
Sequence:
MGHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDATKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTAVASALSSRYH
Protein: Serine/threonine-protein kinase ICK (EC 2.7.11.1) (Ciliogenesis associated kinase 1) (Intestinal cell kinase) (hICK) (Laryngeal cancer kinase 2) (LCK2) (MAK-related kinase) (MRK) (Q9UPZ9)
Organism: Homo sapiens (Human)
Function: Required for ciliogenesis. Phosphorylates KIF3A (By similarity). Involved in the control of ciliary length. Regulates the ciliary localization of SHH pathway components as well as the localization of IFT components at ciliary tips (By similarity). May play a key role in the development of multiple organ systems and particularly in cardiac development (By similarity). Regulates intraflagellar transport (IFT) speed and negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner and this regulation requires its kinase activity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12103360, ECO:0000269|PubMed:19185282}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q62726}. Cell projection, cilium {ECO:0000269|PubMed:24797473}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9JKV2}. Note=Also found at the ciliary tip (PubMed:24797473). Nuclear localization has been observed with a GFP-tagged construct in transfected HeLa cells (PubMed:12103360, PubMed:19185282). {ECO:0000269|PubMed:12103360, ECO:0000269|PubMed:19185282, ECO:0000269|PubMed:24797473}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:15988018}. Note=Predominant cytoplasmic localization has been observed with a N-terminally GFP-tagged construct. {ECO:0000269|PubMed:15988018}.
Interaction partners:
- Cyclin-L2
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM7
- Origin recognition complex subunit 3
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM2
- DNA replication factor Cdt1
- DNA replication licensing factor MCM6
Sequence:
MNRYTTIRQLGDGTYGSVLLGRSIESGELIAIKKMKRKFYSWEECMNLREVKSLKKLNHANVVKLKEVIRENDHLYFIFEYMKENLYQLIKERNKLFPESAIRNIMYQILQGLAFIHKHGFFHRDLKPENLLCMGPELVKIADFGLAREIRSKPPYTDYVSTRWYRAPEVLLRSTNYSSPIDVWAVGCIMAEVYTLRPLFPGASEIDTIFKICQVLGTPKKTDWPEGYQLSSAMNFRWPQCVPNNLKTLIPNASSEAVQLLRDMLQWDPKKRPTASQALRYPYFQVGHPLGSTTQNLQDSEKPQKGILEKAGPPPYIKPVPPAQPPAKPHTRISSRQHQASQPPLHLTYPYKAEVSRTDHPSHLQEDKPSPLLFPSLHNKHPQSKITAGLEHKNGEIKPKSRRRWGLISRSTKDSDDWADLDDLDFSPSLSRIDLKNKKRQSDDTLCRFESVLDLKPSEPVGTGNSAPTQTSYQRRDTPTLRSAAKQHYLKHSRYLPGISIRNGILSNPGKEFIPPNPWSSSGLSGKSSGTMSVISKVNSVGSSSTSSSGLTGNYVPSFLKKEIGSAMQRVHLAPIPDPSPGYSSLKAMRPHPGRPFFHTQPRSTPGLIPRPPAAQPVHGRTDWASKYASRR
Protein: Vacuolar protein sorting-associated protein 35 (Q9W277)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- FI18122p1
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 26
- Sorting nexin-3
- WASH complex subunit 2
- Sorting nexin 6, isoform B
- LD13361p
- GH10459p
- Sorting nexin
- von Willebrand factor A domain-containing protein 8
Sequence:
MYPWSSSSYGGQIPSAANVRTMPNGLDDQEKLLAEAIGLARKQAFQMNHFLDKERMLDSLKCASTMLGELRTSVLSPKSYYELYMAVTNELCHLELYLSEKIDKKTDLYELVQYSHTIVPRLYLLITVGIVYIKNDPTLKRSILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDVMVEENEHEGNVYDAIDFVLTNFAEMNKLWVRMQHQGHSSEKTRREKEREELKILVGTNLVRLSQLESATLEIYQRLILPGILEQVVSCRDAIAQEYLMECIIQVFPDEFHLKTLDPFLKSCAQLETGVNVKNIIISLIERLAAYNQRSGKTSGNAIDAIIPAEVELFEVFSVQVANIVQTRMDMPLEDTISLQVALLSLAQKVYPDRVDYVDKVLGTTAQILQRMNMNNISHLLSVNQELSRLLRICIDFYNNALTIIQLQNFCPLLEKFDYTSRKSLALYLVMNILDNETLVPTADQADSLLTIITPLIKDDDTNKENGAAAGNTTPDAEEFAEEQGVVARFIHLMRSDEPDMQYKMLQTARKHLGNGGGQRLKHVLPPLVFAAYQLAFKYKAIAEQDENWDKKCQKIVQYCHSTISALAKADLADLALRLYLQGALVIGEIGYTNHETVAYEFMTQAFSLYEDEISDSKAQLAAITLIMSTFEQMSCFGEENAEPLRTNCALAASKLLKKPDQCRGVVACAALFWSGKQNGEEMRDEKRTLDCLKKGARIASQCLDTGVQVQLYVELLNHYLFYFERGNSLITVAMLNQLIAKVNEELPNLEPSEETKQIESHYKNTLAHIRSRMESNDSSLEVSFAGITLN