wanglab/gogpt-training-data huggingface dataset:
Protein: Methylsterol monooxygenase 1-3 (EC 1.14.18.11) (EC 1.14.18.9) (Sterol 4-alpha-methyl-oxidase 1-3) (AtSMO1-3) (F4JLZ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Non-heme iron oxygenase involved in sterols biosynthesis by catalyzing the removal of the first methyl group at the C-4 position (By similarity). 4,4-dimethyl-9-beta,19-cyclopropylsterols such as 24-methylenecycloartanol are the preferred substrates (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31341004}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1
- Sterol 14-demethylase
- Cycloartenol-C-24-methyltransferase
- Delta
- Putative Delta
- Putative sterol 14-demethylase-like protein
- Delta
- Ergosterol biosynthetic protein 28
Sequence:
MIPYPTVEDASVALGRNLTWFETVWFDYSATKSNFHVYCHTILVLFLVFSLAPFPLVIVEWTGWFDQFKIQKKVKYSLSDMFQCYKEVMKLFLLVVGTLQIVSYPSIQMVGIRSGLPLPSLMEIVAQLVVYFLIEDYTNYWIHRWMHCKWGYEKIHRIHHEYTSPIGYASPYAHWAEILILGIPTFLGPAIAPGHIMTFWLWISLRQFEAIETHSGYDFPWSVTKLIPFYGGPEYHDYHHYVGGQSQSNFASVFTYCDYIYGTDKGYRIHKKLLHHQIKEEAEEKRVRKHD
Protein: P/Homo B domain-containing protein (G5EB75)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Neutral protease 2
- Alkaline protease 1
- Neutral protease 2
- Neutral protease 2 homolog AN3393
- Metalloprotease MEP1
- Calnexin, putative
Sequence:
MRLQGAAAALGLFCAATASLHPRRSYETRDYFALHLDASTSPSDIAARLGARHEGQVGELDGHHTFSLPRENGADLDALLEDLQIKRKLRRRDGDLGALDKRDKDLAGILWSQKLTPKQRLVKRTPPPEKLARDPSSDGEEKEDVEAAQARSKLVSTLGIEDPIFTKQWHLFNTVQVGHDLNVTGVWLEGITGKGATAAIVDDGLDMYSNDLSPNYFPEGSWDFNDHTAEPRPRLRDDRHGTRCAGEVAAARNDVCGVGVAYDSRIAGIRILSGPIDDTDEASAINYAYQENDIYSCSWGPPDDGATMDAPGILVSRAIVNGVQKGRDGKGSIFVFAAGNGAASGDNCNFDGYTNSIYSITVGAIDREGQHPQYSESCSAQLVVAYSSGISDAISTTDVGTDRCYSVHGGTSAAGPLVVGAISLALSVRPELTWRDAQYIVLETAVPVHEDDGSWQVTKSGRKFSHDWGYGKIDVYSLVQKAKTWELVKPQAWYHSPWLRVQHEVPQGDKGVAASWEVTEQMMKDANLEKLEHVTVTMNVNHTRRGDLSVELRSPEGIVSHLSTPRKNDNAEVGYIDWTFMTVAHWGESGVGTWTVIVKDSTVNDNVGEFIDWRLNLWGMAVDGAKQKLHPLPDEHDDDHSIEDAIVVTTSVQPAPTATEAPVEPSHTVDRPVKVKPTSTGSASETETPTPTPTPASDSFLPSFFPTFGASKHTQVWIYAAISSIIVFCIGLGIYFHVQRRRRLRNDRDDYDFEMIEDEDEAKAMNGSSRRRGGELYNAFAGESEEEPLFSDEDDDEPYRDQTTGAELRTSADDTRRND
Protein: Heterogeneous nuclear ribonucleoprotein A1 (Q0VAC0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSKSASPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPQNQGGYGVSSSSSSYGSGRRF
Protein: Urease accessory protein UreH (Q09067)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01384}.
Interaction partners:
- Urease accessory protein UreE
- Urease accessory protein UreG
- Urease accessory protein UreF
- Urease subunit alpha
- Urease subunit beta
- Acid-activated urea channel
- Phosphoglucosamine mutase
- Hydrogenase/urease maturation factor HypB
Sequence:
MNTYAQESKLRLKTKIGADGRCVIEDNFFTPPFKLMAPFYPKDDLAEIMLLAVSPGMMRGDAQDVQLNIGPNCKLRITSQSFEKIHNTEDGFASRDMHIVVGENAFLDFAPFPLIPFENAHFKGNTTISLRSSSQLLYSEIIVAGRVARNELFKFNRLHTKISILQDEKPIYYDNTILDPKTTDLNNMCMFDGYTHYLNLVLVNCPIELSGVRECIEESEGVDGAVSETASSHLCVKALAKGSEPLLHLREKIARLVTQTTTQKV
Protein: C-C chemokine receptor type 6 (C-C CKR-6) (CC-CKR-6) (CCR-6) (KY411) (CD antigen CD196) (O54689)
Organism: Mus musculus (Mouse)
Function: Receptor for the C-C type chemokine CCL20. Binds to CCL20 and subsequently transduces a signal by increasing the intracellular calcium ion levels. Although CCL20 is its major ligand it can also act as a receptor for non-chemokine ligands such as beta-defensins. Binds to defensin DEFB1 leading to increase in intracellular calcium ions and cAMP levels. Its binding to DEFB1 is essential for the function of DEFB1 in regulating sperm motility and bactericidal activity (By similarity). Binds to defensins DEFB4 and DEFB4A/B and mediates their chemotactic effects. The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases. CCR6-mediated signals are essential for immune responses to microbes in the intestinal mucosa and in the modulation of inflammatory responses initiated by tissue insult and trauma. CCR6 is essential for the recruitment of both the pro-inflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation. Required for the normal migration of Th17 cells in Peyers patches and other related tissue sites of the intestine and plays a role in regulating effector T-cell balance and distribution in inflamed intestine. Plays an important role in the coordination of early thymocyte precursor migration events important for normal subsequent thymocyte precursor development, but is not required for the formation of normal thymic natural regulatory T-cells (nTregs). Required for optimal differentiation of DN2 and DN3 thymocyte precursors. Essential for B-cell localization in the subepithelial dome of Peyers-patches and for efficient B-cell isotype switching to IgA in the Peyers-patches. Essential for appropriate anatomical distribution of memory B-cells in the spleen and for the secondary recall response of memory B-cells. Positively regulates sperm motility and chemotaxis via its binding to CCL20.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23765988}; Multi-pass membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P51684}.
Interaction partners:
- C-C motif chemokine 20
- C-C motif chemokine 2
- C-X-C motif chemokine 16
- C-X-C motif chemokine 9
- C-C motif chemokine 19
- C-C motif chemokine 1
- Stromal cell-derived factor 1
- C-X-C motif chemokine 13
- C-C motif chemokine
- C-C chemokine receptor type 2
Sequence:
MNSTESYFGTDDYDNTEYYSIPPDHGPCSLEEVRNFTKVFVPIAYSLICVFGLLGNIMVVMTFAFYKKARSMTDVYLLNMAITDILFVLTLPFWAVTHATNTWVFSDALCKLMKGTYAVNFNCGMLLLACISMDRYIAIVQATKSFRVRSRTLTHSKVICVAVWFISIIISSPTFIFNKKYELQDRDVCEPRYRSVSEPITWKLLGMGLELFFGFFTPLLFMVFCYLFIIKTLVQAQNSKRHRAIRVVIAVVLVFLACQIPHNMVLLVTAVNTGKVGRSCSTEKVLAYTRNVAEVLAFLHCCLNPVLYAFIGQKFRNYFMKIMKDVWCMRRKNKMPGFLCARVYSESYISRQTSETVENDNASSFTM
Protein: Hemolysin expression-modulating protein Hha (P0ACE3)
Organism: Escherichia coli (strain K12)
Function: Down-regulates hemolysin (hly) expression in complex with H-NS. Stimulates transposition events in vivo. Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. Binds DNA and influences DNA topology in response to environmental stimuli; does not however interact with DNA in the absence of H-NS. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repressing the transcription of fimbrial genes fimA and ihfA, and by repressing the transcription of tRNAs corresponding to rare codons, which are abundant in type 1 fimbrial genes.
Interaction partners:
- Hha toxicity modulator TomB
- DNA-binding protein H-NS
- DNA-binding protein StpA
- mRNA interferase toxin MqsR
- HTH-type transcriptional activator AaeR
Sequence:
MSEKPLTKTDYLMRLRRCQTIDTLERVIEKNKYELSDNELAVFYSAADHRLAELTMNKLYDKIPSSVWKFIR
Protein: Enolase 2 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 2) (2-phosphoglycerate dehydratase 2) (Q88VW2)
Organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
Interaction partners:
- Pyruvate kinase
- Phosphoglycerate kinase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- Phosphoenolpyruvate synthase
- phosphoenolpyruvate carboxykinase
Sequence:
MEKQVIETVKAREIFDSRGNPTVEADVILSDGTLGRAEVPSGASTGEKEAVELRDGGDRLAGKGVLKAVNNVNTVINHALHGADPFNQAHIDQIMIDLDGTPNKARLGANAILGVSMATARAAANALQQPLYRYLGGTDLELPQTFHNVINGGEHADNGIDIQEFMITPVERTSFRDGFEKIVNTYHTLKKVIEDAGYTSGLGDEGGFAPDLKNSEEALQMLHDAIIKAGYTPGKEIAIAFDAAASYFYNRTTHNYDFEGKTYTPAALGDYYLQLLAKFPEIVSIEDPYGEEDWDNFASFTAAHGDQLQIVADDPVCTNPQLIRQAIQRGMANNILIKLNQIGTVTETLAAIRLARKNGYATMMSHRSGETGDTFVADFTVATNAAQLKAGAPARSERVEKYNQLLRIEEELGADGARLAHFPNNVMFD
Protein: Ferrochelatase, mitochondrial (EC 4.98.1.1) (Heme synthase) (Protoheme ferro-lyase) (O59786)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Bound to the mitochondrial inner membrane in eukaryotic cells with its active site on the matrix side of the membrane. {ECO:0000250}.
Interaction partners:
- Protoporphyrinogen oxidase
- Protoheme IX farnesyltransferase, mitochondrial
- Uroporphyrinogen decarboxylase
- Frataxin homolog, mitochondrial
- Probable oxygen-dependent coproporphyrinogen-III oxidase
- Putative holocytochrome-c1 synthase
- Uroporphyrinogen-III synthase
- Putative holocytochrome-c synthase
- Delta-aminolevulinic acid dehydratase
- Porphobilinogen deaminase
Sequence:
MIRFCPSCFALKRTAPVLNHTSRLGNYFNNTFSKFSVNRMSVSSYSSDASSTVMDESPPNGVTKSVSGKGPTAVVMMNMGGPSNLDEVGPFLERLFTDGDIIPLGYFQNSLGKFIAKRRTPKVQNHYSDIGGGSPILHWTRIQGSEMCKILDKKCPESAPHLPFVAFRYAPPLTEDMLDELKKANVSRAVAFSQYPQWSCATSGASLNELRRKLIEKGMEKDFEWSIVDRWPLQQGLINAFAENIEETLKTYPEDVRDDVVIVFSAHSLPMSQVAKGDPYVYEIAATSQAVMKRLNYKNKFVNAWQSKVGPLPWMSPATDFVIEQLGNRGQKNMILVPIAFTSDHIETLKELEDYIEDAKQKGITGVKRVSSINGSMTAIQGMADLVAEHLKAKVPYSRQFTQRCPGCTSESCAERINFFQDF
Protein: Nocturnin (EC 3.1.3.108) (Carbon catabolite repression 4-like protein) (O35710)
Organism: Mus musculus (Mouse)
Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Represses translation and promotes degradation of target mRNA molecules (By similarity). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control. Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis. Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance. Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity. Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone. Critical for proper development of early embryos.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23449310}. Nucleus {ECO:0000269|PubMed:23449310}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20498072}. Mitochondrion {ECO:0000250|UniProtKB:Q9UK39}.
Interaction partners:
- CCR4-NOT transcription complex subunit 1
- Solute carrier family 38 member 6
- Rab3 GTPase-activating protein catalytic subunit
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 3
- Basic helix-loop-helix ARNT-like protein 1
- CCR4-NOT transcription complex subunit 8
- Probable ATP-dependent RNA helicase DDX6
- CCR4-NOT transcription complex subunit 9
Sequence:
MYQSPRRLCSALLLRDAPGLRRTLVPGPRRTLAPPVLGSRPKSPQLQAAAASGAARSRPRTVSSMGNGTSRLYSALAKTVNSSAAAQHPEYLVSTDPEHLEPIDPKELLEECRAVLHTRPPRYQRDFVDLRTDCSSSHSPIRVMQWNILAQALGEGKDNFVQCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFFLQNRFKLISSTNIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITQGAKIPLIVCGDFNAEPTEEVYKHFASSSLNLNSAYKLLSPDGQSEPPYTTWKIRTSGECRHTLDYIWYSRHALSVTSALDLLTEEQIGPNRLPSFHYPSDHLSLVCDFSFNEEPHELF
Protein: Thiosulfate sulfurtransferase (EC 2.8.1.1) (Rhodanese-like protein) (P52197)
Organism: Azotobacter vinelandii
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MDDFASLPLVIEPADLQARLSAPELILVDLTSAARYAEGHIPGARFVDPKRTQLGQPPAPGLQPPREQLESLFGELGHRPEAVYVVYDDEGGGWAGRFIWLLDVIGQQRYHYLNGGLTAWLAEDRPLSRELPAPAGGPVALSLHDEPTASRDYLLGRLGAADLAIWDARSPQEYRGEKVLAAKGGHIPGAVNFEWTAAMDPSRALRIRTDIAGRLEELGITPDKEIVTHCQTHHRSGLTYLIAKALGYPRVKGYAGSWGEWGNHPDTPVEL
Protein: NPC intracellular cholesterol transporter 2 homolog a (Niemann Pick type C2 protein homolog) (Q9VQ62)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions redundantly with Npc2b in regulating sterol homeostasis and ecdysteroid biosynthesis, probably by controlling the availability of sterol substrate.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Niemann-Pick type C-1a, isoform A
- Niemann-Pick type C-2c
- Niemann-Pick type C-2e
- GEO08227p1
- Niemann-Pick type C-2g, isoform A
- NPC intracellular cholesterol transporter 1 homolog 1b
- GEO07678p1
Sequence:
MLRYAVIACAALVVFAGALEFSDCGSKTGKFTRVAIEGCDTTKAECILKRNTTVSFSIDFALAEEATAVKTVVHGKVLGIEMPFPLANPDACVDSGLKCPLEKDESYRYTATLPVLRSYPKVSVLVKWELQDQDGADIICVEIPAKIQ
Protein: Probable dipeptidase (Q9I187)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PvdN
- PvdO
- Probable thioesterase
- Acyl-homoserine lactone acylase PvdQ
- L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, PvdH
- Pyoverdine biosynthesis protein PvdE
- PvdP
- L-ornithine N
- MbtH-like domain-containing protein
- Pyoverdine export membrane fusion protein PvdR
Sequence:
MTRTRTRKALYLGLPIFLILVGGGLLAWKTFGPSEAGYPRKVMKHAEELHERILSFDSRITIPPDFGTEGNEFDKDGPNQLDLVKAGRGRLSGAALAIFGWPEMWNGPNAPHKPTPGFVDEARHQQEIRYKILTGMVRDFPNQVGIAYSPEDFRRLAMEGKFAIVMSMLNAYPLGDDLSQLDKWAARGVRMFGFNYVGNNDWSDSSRPLPFFNDTADALGGLSPLGKQAVERLNDLGVIIDVSQMSTKALEQVAALSRAPIVASHSAPRALVDIKRNLSDHEMQLIKDSGGVIQVVGFPAYLRPLSKPTLDKLNALRARFDLPPLEGLDYALMPGDPIITIWPEQRFGEYASALYGILEEEPKAGLKELVDAIDYTVKKVGIDHVGISSDFNDGGGVDGWKDVSEIRNVTAELITRGYSDADIAKLWGGNFLRAWGEVQKRAKPTATP
Protein: RE36793p (Q9W2F6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSPRRSLLCCLLVSSILVLHQAQANIETNDVNDPSYYMLQGVRVYPNDRQCVMVGGLCVAESDCIEPTSNKGLCPTSAGEGVECCYELPVRPAPCAEHLGQCMDRCHQRLLRPGSDCKNGQVCCVLI
Protein: Melanopsin (Opsin-4) (Q8R456)
Organism: Rattus norvegicus (Rat)
Function: Photoreceptor that binds cis-retinaldehydes (By similarity). Contributes to pupillar reflex, photoentrainment and other non-image forming responses to light (By similarity). May be involved in the optokinetic visual tracking response (By similarity). May be involved in the regulation of retinal hyaloid vessel growth and regression (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11834834}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:Q9QXZ9}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QXZ9}. Perikaryon {ECO:0000250|UniProtKB:Q9QXZ9}.
Interaction partners:
- Hypocretin neuropeptide precursor
- Cyclic nucleotide-gated channel alpha-3
- Cryptochrome-1
- Cryptochrome-2
- Ig lambda-2 chain C region
- Period circadian protein homolog 2
- POU domain, class 4, transcription factor 1
- POU domain, class 4, transcription factor 2
- Basic helix-loop-helix ARNT-like protein 1
- Serotonin N-acetyltransferase
Sequence:
MNSPSESRVPSSLTQDPSFTASPALLQGIWNSTQNISVRVQLLSVSPTTPGLQAAAWVPFPTVDVPDHAHYTLGTVILLVGLTGMLGNLTVIYTFCRNRGLRTPANMLIINLAVSDFLMSFTQAPVFFASSLYKKWLFGETGCKFYAFCGAVFGIVSMITLTAIAMDRYLVITRPLATIGMRSKRRTALVLLGVWLYALAWSLPPFFGWSAYVPEGLLTSCSWDYVTFTPLVRAYTMLLFCFVFFLPLLIIIFCYIFIFRAIRETGRACEGCGESPLRRRQWQRLQSEWKMAKVALIVILLFVLSWAPYSTVALVGFAGYSHILTPYMSSVPAVIAKASAIHNPIIYAITHPKYRAAIAQHLPCLGVLLGVSGQRSHPSLSYRSTHRSTLSSQSSDLSWISGQKRQESLGSESEVGWTDTETTAAWGAAQQASGQSFCSHDLEDGEVKAPSSPQEQKSKTPKTKRHLPSLDRRM
Protein: 5'-3' exoribonuclease 2 (EC 3.1.13.-) (Ribonucleic acid-trafficking protein 1) (p116) (Q02792)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Possesses 5'->3' exoribonuclease activity. Required for the processing of nuclear mRNA, rRNA and small nucleolar RNA (snoRNA) precursors. May promote termination of transcription by RNA polymerase II via the recruitment of 3'-end processing factors to the poly(A) site and by the degradation of nascent RNA downstream of the poly(A) site.
Subcellular location: Nucleus {ECO:0000269|PubMed:12612077, ECO:0000269|PubMed:8417335, ECO:0000269|PubMed:9315672}.
Interaction partners:
- Regulator of Ty1 transposition protein 103
- Decapping nuclease RAI1
- Decapping and exoribonuclease protein 1
- 5'-3' exoribonuclease 1
- Antiviral helicase SKI2
- Helicase SEN1
- Exosome complex exonuclease RRP6
- Polynucleotide 5'-hydroxyl-kinase GRC3
- Protein PCF11
- Ribonuclease 3
Sequence:
MGVPSFFRWLSRKYPKIISPVLEEQPQIVDGVILPLDYSASNPNGELDNLYLDMNGIVHPCSHPENKPPPETEDEMLLAVFEYTNRVLNMARPRKVLVMAVDGVAPRAKMNQQRARRFRSARDAQIENEAREEIMRQREEVGEIIDDAVRNKKTWDSNAITPGTPFMDKLAAALRYWTAFKLATDPGWKNLQVIISDATVPGEGEHKIMNFIRSQRADPEYNPNTTHCIYGLDADLIFLGLATHEPHFKILREDVFAQDNRKRNNLKDTINMTEEEKQFLQKQNSEQPFLWLHINVLREYLSAELWVPGLPFTFDLERAIDDWVFMCFFCGNDFLPHLPCLDVRENSIDILLDIWKVVLPKLKTYMTCDGVLNLPSVETLLQHLGSREGDIFKTRHIQEARKKEAFERRKAQKNMSKGQDRHPTVATEQLQMYDTQGNLAKGSWNLTTSDMVRLKKELMLANEGNEEAIAKVKQQSDKNNELMKDISKEEIDDAVSKANKTNFNLAEVMKQKIINKKHRLEKDNEEEEIAKDSKKVKTEKAESECDLDAEIKDEIVADVNDRENSETTEVSRDSPVHSTVNVSEGPKNGVFDTDEFVKLFEPGYHERYYTAKFHVTPQDIEQLRKDMVKCYIEGVAWVLMYYYQGCASWNWFYPYHYAPLATDFHGFSHLEIKFEEGTPFLPYEQLMSVLPAASGHALPKIFRSLMSEPDSEIIDFYPEEFPIDMNGKKMSWQGIALLPFIDQDRLLTAVRAQYPLLSDAERARNIRGEPVLLISNKNANYERFSKKLYSKENNNNNVVVKFQHFKSGLSGIVSKDVEGFELNGKIVCPIQGGSLPNLSTTLILKMSYRLIPLPSRNKSIILNGFIPSEPVLTAYDLDSIMYKYNNQNYSRRWNFGNDLKQNIVPVGPKGITQYKPRTGGYRAFFYFAELSRNNVQPAHNYGRNSYNSQPGFNNSRYDGGNNNYRQNSNYRNNNYSGNRNSGQYSGNSYSRNNKQSRYDNSRANRR
Protein: Growth hormone receptor (GH receptor) (Somatotropin receptor) [Cleaved into: Growth hormone-binding protein (GH-binding protein) (GHBP) (Serum-binding protein)] (P10912)
Organism: Homo sapiens (Human)
Function: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:2825030}; Single-pass type I membrane protein {ECO:0000255}. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. {ECO:0000250|UniProtKB:P19941}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:9360546}; Single-pass type I membrane protein {ECO:0000255}. Note=Remains fixed to the cell membrane and is not internalized. {ECO:0000269|PubMed:9360546}.; SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted {ECO:0000269|PubMed:2825030}. Note=Complexed to a substantial fraction of circulating GH. {ECO:0000269|PubMed:2825030}.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Somatotropin
- Suppressor of cytokine signaling 2
- Chorionic somatomammotropin hormone 1
- Chorionic somatomammotropin hormone 2
- Chorionic somatomammotropin hormone 1
- Signal transducer and activator of transcription 5B
- Prolactin
- Insulin-like growth factor 1
- Signal transducer and activator of transcription 5A
Sequence:
MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKTEESDTDRLLSSDHEKSHSNLGVKDGDSGRTSCCEPDILETDFNANDIHEGTSEVAQPQRLKGEADLLCLDQKNQNNSPYHDACPATQQPSVIQAEKNKPQPLPTEGAESTHQAAHIQLSNPSSLSNIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHPEMVSLCQENFLMDNAYFCEADAKKCIPVAPHIKVESHIQPSLNQEDIYITTESLTTAAGRPGTGEHVPGSEMPVPDYTSIHIVQSPQGLILNATALPLPDKEFLSSCGYVSTDQLNKIMP
Protein: Beta-casein (T1T0C1)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKVLILACLVALALARELEELNVPGEIVESLSSSEESITRINKKIEKFQSEEQQQTEDELQDKIHPFAQTQSLVYPFPGPIPNSLPQNIPPLTQTPVVVPPFLQPEVMGVSKVKGAMAPKHKEMPFPKYPVEPLTESQSLTLTDVENLHLPLPLLQSWMHQPHQPLPPTVMFPPQSVLSLSQSKVLPVPQKAVPYPQRDMPIQAFLLYQEPVLGPVRGPFPIIV
Protein: Tubulin beta-1 chain (Beta-1-tubulin) (P12456)
Organism: Caenorhabditis elegans
Function: TTubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. Plays a role in mechanosensory transduction (touch sensitivity).
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin alpha-3 chain
- Degenerin mec-4
- Tubulin alpha chain
- Tubulin alpha-2 chain
- Tubulin alpha chain
- Serine/threonine-protein kinase zyg-8
- Degenerin mec-10
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
Sequence:
MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPSGQYVGDSDLQLERINVYYNEAGSNKYVPRAVLVDLEPGTMDSVRSGPFGQLFRPDNYVFGQSGAGNNWAKGHYTEGAELVDNVLDVVRKEAESTDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDSTFCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRSNQQYRAITVPELTQQCFDAKNMMAACDPRHGRYLTAAAIFRGRMSMKEVDEQMLNIQNKNSSYFVDWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEAAADEDAAEAFDGE
Protein: Merozoite surface protein 3 (Q8IJ55)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Merozoite surface protein 1
- Merozoite surface protein 6
- Merozoite surface protein 2
- Merozoite surface protein 5
- Merozoite surface protein 4
- Merozoite surface protein 8
- Apical membrane antigen 1
Sequence:
MKSFINITLSLFLLHLYIYINNVASKEIVKKYNLNLRNAILNNNSQIENEENVNTTITGNDFSGGEFLWPGYTEELKAKKASEDAEKAANDAENASKEAEEAAKEAVNLKESDKSYTKAKEACTAASKAKKAVETALKAKDDAEKSSKADSISTKTKEYAEKAKNAYEKAKNAYQKANQAVLKAKEASSYDYILGWEFGGGVPEHKKEENMLSHLYVSSKDKENISKENDDVLDEKEEEAEETEEEELEEKNEEETESEISEDEEEEEEEEEKEEENDKKKEQEKEQSNENNDQKKDMEAQNLISKNQNNNEKNVKEAAESIMKTLAGLIKGNNQIDSTLKDLVEELSKYFKNH