wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-binding protein rnp24 (Q09100)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Uncharacterized RNA-binding protein C4F6.14
- Ribosome production factor 2 homolog
- Protein sda1
- Ribosome assembly factor mrt4
- Nucleolar protein 58
- Ribosome biogenesis protein enp2 homolog
- Nucleolar protein 56
- Uncharacterized protein C57A7.06
- rRNA 2'-O-methyltransferase fibrillarin
- 25S rRNA
Sequence:
MEPIQKMDSLNNKEGQPDKKRKKHESEKEGENEVLEIDVTKPVPPSKKLMRKLRKAGKIDKDGNWTPEALEEAKKKEEKRLKRLDAKYGRKEEGESQEESKRSPWGIWVGNLSFHTTKEILTDFFVRETSEMIKEVSEENIKPITTEQITRIHMPMSKEKRFQNKGFAYVDFATEDALKLALQCSEKALNGRNILIKSNTDFSGRPSKPANTLSKTASIQSSKKEPSSILFVGNLDFETTDADLKEHFGQVGQIRRVRLMTFEDTGKCKGFGFVDFPDIDTCMKAMELGHNSWRLEYGEDRSKRMRNKSPMARSGRFNDAESLGQEDKPNFKRARKIDPRSVRPGAALAKAQRSSAAIVEPAGQKIKFD
Protein: Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2'] (P11223)
Organism: Avian infectious bronchitis virus (strain Beaudette) (IBV)
Function: Attaches the virion to the host cell membrane by interacting with sialic acids, initiating the infection.
Subcellular location: [Spike protein S2]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers may be transported to the plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04098}.; SUBCELLULAR LOCATION: [Spike protein S1]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers may be transported to the plasma membrane, where they may mediate cell-cell fusion. S1 is not anchored to the viral envelope, but associates with the extravirion surface through its binding to S2. {ECO:0000255|HAMAP-Rule:MF_04098}.
Interaction partners:
Sequence:
MLVTPLLLVTLLCALCSAVLYDSSSYVYYYQSAFRPPSGWHLQGGAYAVVNISSEFNNAGSSSGCTVGIIHGGRVVNASSIAMTAPSSGMAWSSSQFCTAHCNFSDTTVFVTHCYKHGGCPLTGMLQQNLIRVSAMKNGQLFYNLTVSVAKYPTFRSFQCVNNLTSVYLNGDLVYTSNETIDVTSAGVYFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPRGLLACQYNTGNFSDGFYPFTNSSLVKQKFIVYRENSVNTTCTLHNFIFHNETGANPNPSGVQNIQTYQTKTAQSGYYNFNFSFLSSFVYKESNFMYGSYHPSCKFRLETINNGLWFNSLSVSIAYGPLQGGCKQSVFKGRATCCYAYSYGGPSLCKGVYSGELDHNFECGLLVYVTKSGGSRIQTATEPPVITQNNYNNITLNTCVDYNIYGRTGQGFITNVTDSAVSYNYLADAGLAILDTSGSIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQLLENQFYIKITNGTRRFRRSITENVANCPYVSYGKFCIKPDGSIATIVPKQLEQFVAPLFNVTENVLIPNSFNLTVTDEYIQTRMDKVQINCLQYVCGSSLDCRKLFQQYGPVCDNILSVVNSVGQKEDMELLNFYSSTKPAGFNTPVLSNVSTGEFNISLLLTNPSSRRKRSLIEDLLFTSVESVGLPTNDAYKNCTAGPLGFFKDLACAREYNGLLVLPPIITAEMQALYTSSLVASMAFGGITAAGAIPFATQLQARINHLGITQSLLLKNQEKIAASFNKAIGHMQEGFRSTSLALQQIQDVVSKQSAILTETMASLNKNFGAISSVIQEIYQQFDAIQANAQVDRLITGRLSSLSVLASAKQAEYIRVSQQRELATQKINECVKSQSIRYSFCGNGRHVLTIPQNAPNGIVFIHFSYTPDSFVNVTAIVGFCVKPANASQYAIVPANGRGIFIQVNGSYYITARDMYMPRAITAGDVVTLTSCQANYVSVNKTVITTFVDNDDFDFNDELSKWWNDTKHELPDFDKFNYTVPILDIDSEIDRIQGVIQGLNDSLIDLEKLSILKTYIKWPWYVWLAIAFATIIFILILGWVFFMTGCCGCCCGCFGIMPLMSKCGKKSSYYTTFDNDVVTEQYRPKKSV
Protein: Dimethylsulfoniopropionate lyase 2 (DMSP lyase 2) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 2) (P0DN23)
Organism: Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi)
Function: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
Interaction partners:
Sequence:
MGSASSKTRKDKAKSSTIAACPTDTAAAKACPTRLDDGLAQVAMFAGLRQVTMGVLRIDYDYQTNLGDILDPRSFDFRLVSATVEGLTFKRAQEGEPLPCYVMSNLDGAVKKLIDAGADFIVGDCGFLVYWQVYVRDFAQQYAGGRACPVMLSSLVLSLPLLATIPVGGKIGILTASKGSLMKMQKKLASVIELQKEEARTRAVPAAVQPSGIEINFSDPRFKVVGLDTVNSFKTALADDSGVDDRRSIAIEIAKYCKQVACEDPAICAWLIECTEAGGFSWAIKLGTGLPVWDPVTIGRFLSLGFTSSLPSVALTLGETGQVALDPNETDVSKGRPTKAEHRFGPEFEEMLQ
Protein: tRNA (cytosine(72)-C(5))-methyltransferase NSUN6 (EC 2.1.1.-) (NOL1/NOP2/Sun and PUA domain-containing protein 1) (NOL1/NOP2/Sun domain family member 6) (Q8TEA1)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C5 position of cytosine 72 in tRNA(Thr)(TGT) and tRNA(Cys)(GCA). In vitro also methylates tRNA(Thr)(AGT). Methylation requires, in the acceptor stem region, the presence of the 3'-CCA terminus, the target site C72, the discriminator base U73, and the second and third base pairs (2:71 and 3:70) in the tRNA substrates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26160102}.
Interaction partners:
- ATP-dependent RNA helicase DDX18
- GTP-binding protein 4
- Ribosome biogenesis protein BOP1
- Nucleolar complex protein 2 homolog
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- mRNA turnover protein 4 homolog
- Probable rRNA-processing protein EBP2
- Ribosomal L1 domain-containing protein 1
- Ribosome biogenesis protein BRX1 homolog
Sequence:
MSIFPKISLRPEVENYLKEGFMNKEIVTALGKQEAERKFETLLKHLSHPPSFTTVRVNTHLASVQHVKNLLLDELQKQFNGLSVPILQHPDLQDVLLIPVIGPRKNIKKQQCEAIVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKCKKGAKEFDGTKVFLGNGISELSRKEIFSGLPELKGMGIRMTEPVYLSPSFDSVLPRYLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKLDMVEDTEGEPPFLPESFDRILLDAPCSGMGQRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLKQLQRFDPSAVPLPDTDMDSLREARREDMLRLANKDSIGFFIAKFVKCKST
Protein: Pyridoxal reductase, chloroplastic (EC 1.1.1.65) (Q56Y42)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+). Involved in the PLP salvage pathway.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Cysteine/Histidine-rich C1 domain family protein
- Pyridoxal kinase
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 2
- Inorganic pyrophosphatase 1
- Inorganic pyrophosphatase 2
- Thiamine phosphate phosphatase-like protein
- Putative OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 8
- Nuclear pore complex protein NUP107
Sequence:
MALTLSTTKTFTNINCSNNTSNITTFKPLKLPLFWPWQKVKMGPLSVSPMGFGTWAWGNQLLWGYQTSMDDQLQQAFELALENGINLFDTADSYGTGRLNGQSERLLGKFIKESQGLKGKQNEVVVATKFAAYPWRLTSGQFVNACRASLDRLQIDQLGIGQLHWSTASYAPLQELVLWDGLVQMYEKGLVRAVGVSNYGPQQLVKIHDYLKTRGVPLCSAQVQFSLLSMGKEQLEIKSICDELGIRLISYSPLGLGMLTGKYSSSKLPTGPRSLLFRQILPGLEPLLLALSEIAKKRGKTMPQVAINWCICKGTVPIPGIKSVRHVEDNLGALGWKLTNDEQLQLEYAAKESPKSMIQNIFQTR
Protein: Glutathione S-transferase Mu 2 (EC 2.5.1.18) (GST 5-5) (GST class-mu 2) (Glutathione S-transferase pmGT2) (P15626)
Organism: Mus musculus (Mouse)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase theta-2
- Cytochrome P450 2C55
- Glutathione S-transferase theta-1
- Cytochrome P450 2C38
- Glutathione S-transferase theta-3
- Epoxide hydrolase 1
- Glutathione S-transferase Mu 5
- Cytochrome P450 2C39
- Glutathione S-transferase omega-1
- Alcohol dehydrogenase 1
Sequence:
MPMTLGYWDIRGLAHAIRLLLEYTDTSYEDKKYTMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLARKHNLCGETEEERIRVDILENQAMDTRIQLAMVCYSPDFEKKKPEYLEGLPEKMKLYSEFLGKQPWFAGNKVTYVDFLVYDVLDQHRIFEPKCLDAFPNLKDFMGRFEGLKKISDYMKSSRFLSKPIFAKMAFWNPK
Protein: 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (26S proteasome-associated PAD1 homolog 1) (O00487)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 3
- Ubiquitin carboxyl-terminal hydrolase 14
- Proteasome subunit alpha type-2
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit 6B
- 26S proteasome regulatory subunit 8
- Proteasomal ubiquitin receptor ADRM1
Sequence:
MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK
Protein: Inner nuclear membrane protein Man1 (LEM domain-containing protein Man1) (Q7JRE4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Inner nuclear membrane protein. Acts as a negative regulator of the BMP (Dpp) signaling cascade during crossvein development in pupal wings and possibly during synaptic transmission at the neuromuscular junction (NMJ). Appears to be required for pupal development and consequently transition to the adult stage. During pupal development, plays essential and redundant functions with the other LEM domain proteins; bocks and Ote.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:16439308}; Multi-pass membrane protein {ECO:0000269|PubMed:16439308}. Cytoplasm {ECO:0000269|PubMed:16439308}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308}. Note=During anaphase and metaphase, detected in the nuclear envelope and spindle poles. {ECO:0000269|PubMed:16439308}.
Interaction partners:
- Barrier-to-autointegration factor
- Lamin-B receptor
- Lamin-C
- Otefin
- LEM domain-containing protein Bocksbeutel
- Lamin Dm0
- Mothers against decapentaplegic homolog
- Cell division cycle 5, isoform A
- Protein mothers against dpp
- Heterochromatin protein 1
Sequence:
MSTESLNSLSDKELHRKLIQSGFPSTPVTETTRAVLIEKLRKHTRADKLKKRSNKYVLYSKEQQESPPFPQYHQYHAPQPPQNYANGLDNNNDLDQTGGSSAYNRSLDESDSSPLQLSASKMYAPPPVVASNYDGDCSPHSLGLNGKYLQPCSMPYAIDTSNNYGKPSGKAKLSDGGVVNRLLSFRDTTIQRKFNYPTGQASRIPLRKERLTRFALSDLKSFIRNPDIRPYVIPRVLISLFLIFLTIITVLYVGKRFEQSPIDKAALKYTLCNPNDMQMISEKVNCIEKDSLRGALDMSEELFRHLNERARLHHCKDANLSPALEIGEFVREMVSNPKTHRGNLHSNLMAAKYLITENPQWSIQVVDSTKHLGQTSHFELSEPNLPLKCIVLKKVTRFFTVIGALLLIVAGFLIVYVAVVIYRVKQKEALLAVDQFQKDIINELIYLSSQSESPEVVINQLQEKFLPAKKRSKLLSSWNKALKQLEKNDSRVLFGMVNRDGKAMRTIAWNRNVDKKDVGLVKKWQSPAFDNSNKIANPPTPCLKIRHMFDSSEVDQANLKQSIVESIIEKVGTRCKICDVQLDVQSCCVYIRCASEEDAGTIHKEINGWWFDKRLISIKFLRLERYLSRFPKPSAEPLYFHTNEAANTHS
Protein: TPX2 domain-containing protein (TPX2-related alternative variant a) (G5EDE7)
Organism: Caenorhabditis elegans
Interaction partners:
- Spindle-defective protein 5
- Aurora kinase
- Zygote defective protein 9
- Regulator of spindle assembly protein 2
- Spindle-defective protein 2
- Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1
- Transforming acid coiled-coil-containing protein 1
- Serine/threonine-protein kinase plk-1
- Mitotic spindle organiZing protein
- Serine/threonine-protein phosphatase 6 regulatory subunit
Sequence:
MSKSQTIQEFDENFFSSFAVPKVKDYSRLSSSPSRDQPCETSYFENHFPSLECDTPVKMQLPKTKRESDDDLPSPTIDNLLSSSSESTVINASQNDNTEEKQQQPIREPLKIVPNEDASASGSGGENQLIEGLEKLSMFAPKAPEERLSQRRRSEQRKKEEEDKRTSVIAPASGTRSRSISTKRSMSREPAAAAPRAPSVPRPPHNSVTRTISAPIANTGPGVITRAMAARVAENVTKTSVRRSVMPLKVAQKTPVAAVKSDAATAGGDRSRDRTRRTNTTASRRSVFPNKPAAAAANTTPIAPPRRSASANKATAPTSVSKLTPKIRPIATANRSSILRMNVVKPTVPAPAPADAQQNKAASRPAVPAGGAARNRQPLRVNPGTPSTTIKKPPVASSVQRQPPTRARSVDRSGQPPISASTPGKASRADLFNRLATPKVTATPTRTSHEGPASSIRKSAVRPVPSYVYSSYKGMPSAGGLHGIRAPSKDRSTQKPPAAASTPQSKQ
Protein: Phosphoglycerate mutase (EC 5.4.2.11) (Q6FUX8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase
- Enolase 1
- Triosephosphate isomerase
- Glucose-6-phosphate isomerase
- Enolase 2
- Phosphoglycerate mutase
- 2-oxoglutarate reductase
- Candida glabrata strain CBS138 chromosome K complete sequence
- Transaldolase
Sequence:
MPKLVLVRHGQSEWNEKNLFTGWVDVRLSAKGEQEAARAGELLKEKNVHPDILYTSKLSRAIQTANIALSKADRLWIPVKRSWRLNERHYGALQGKDKAETLETYGEEKFNTWRRSFDVPPPVIEADSPYSQKNDERYRDVDPNVLPQTESLALVIDRLLPYWEDVIAKDLLAGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVAAQGKK
Protein: La-related protein 7 homolog (La ribonucleoprotein domain family member 7 homolog) (Telomerase subunit p43) (Q9GSF8)
Organism: Euplotes aediculatus (Ciliate)
Function: RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex. Specifically binds telomerase RNA and promotes its assembly with catalytic subunit p123, thereby stimulating enzymatic activity and processivity of p123. Telomerase is a ribonucleoprotein enzyme essential that copies new telomeric repeats onto chromosome ends and functions to maintain cell division.
Subcellular location: Nucleus {ECO:0000269|PubMed:12665556, ECO:0000269|PubMed:12741831}. Chromosome, telomere {ECO:0000305}. Note=Localizes to the macronucleus. {ECO:0000269|PubMed:12665556, ECO:0000269|PubMed:12741831}.
Interaction partners:
Sequence:
MEMDIDLDDIENLLPNTFNKYSSSCSDKKGCKTLKSGSKSPSLTIPKLQKQLEFYFSDANLYNDSFLRKLVLKSGEQRVEIETLLMFKKIRSLLKEHYGENYLILKANNDEYIKFICECVKGSRYIRLTKDKLAIKRKKKFDNRTAEELIAFTIRIDGELPSLETIEKAVYNCRNRSSESSDVNKPNKPCKFNGIYVKSFGTNAHCIYIGFLKHRYTECFRDCFSLQQITCFDYSCSSLISLKEAGEMKRRLKKEISKFVDSSVTGINNKNISNEKEEELSQSCFLKISKIPAGSKKYQIREALDCDRPSYIQYDDKETAVIRFKNSAMRTKFLESRNGAEILIKKNCVDIAKESNSKSFVNKYYQSCLIEEIDEATAQKIIKEIKDQRSSIDEIKAELKLDNKKYKPWSKYCGRKRRPVSKRKNKAINKMSTEVKK
Protein: Insulin-like growth factor 1 (Insulin-like growth factor I) (Q13429)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
LKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKYQPPSTNKNTKSQRRKGSTFEERK
Protein: Amine oxidase domain-containing protein (Q54HR9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- PWWP domain-containing protein
Sequence:
MSNVYDIVVIGSGVSGLMCGYKLEKDGYKVLVVEANNIIGGRTRQDFNFTSYPVELGGEMIHGGDTLYYRLAMENKWELFEVFSMDLFNSPINSTYLYLGRERKLIRADQRDEDIQKLADALVSLSDEIDNPNREMNLLEHLIKKQVPFRVLGLADAIYSKTWATDLDRIGVKEAAREDSKPNTIPNNYKVQQSSKIMLDHFSKSLDINLNWRVKHIDTTKDEKLVKVTSYNGQVVQAQRVVVTVPLQILKDGDITFTPELPERKKIAIKTIGMDGGMKIIAKFNKKFWLNNCQLVLCGDSPVPQIWMDGPPYRPLVPGQPSEYVSVGFITGDQAKAISALSPQKQIRTFLDQLDAMFGTSENGWTPASDSFISHMVYDWQKNPFVRGAYSYPSIIPSTYPYKNYPNEILAEPIDNKLFFAGEATATTYDLSTINGALETGVRVYEELKTSLPISNKLQSKPKM
Protein: Ycf3-interacting protein 1, chloroplastic (E5KCJ8)
Organism: Nicotiana tabacum (Common tobacco)
Function: Nuclear genome-encoded factor that participates in photosystem I (PSI) biogenesis. Cooperates with the plastid genome-encoded protein PSI assembly Ycf3 in the assembly of stable PSI units in the thylakoid membrane.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:20807881}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MASNMLQLSLPPLSSSSSSLPFLSSSVYVLPFTHQRRHFSFFNVQNYRFRLSRSTSLGPLFVNKEEDSATYAVTEEEEDNDDDDPDPQSLEYVSQIKRVLELLKRNRDMLFGEVKLTIMIEDPRDVERRRLLGIDDENAPTRDDLAAALEEINEGKVPKDFAALQMLAEEMNSWPNLEVEATKQNKPGRSLYAKATDTGIDPKEAAKRLKIDWDSAAEIDESAESDEPDVPPALGYGALYLVSAFPIIIGISVVLILFYNSLQ
Protein: Activin receptor type-1C (EC 2.7.11.30) (Activin receptor type IC) (ACTR-IC) (Activin receptor-like kinase 7) (ALK-7) (Q8NER5)
Organism: Homo sapiens (Human)
Function: Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis.
Subcellular location: Membrane {ECO:0000269|PubMed:12606401}; Single-pass type I membrane protein {ECO:0000269|PubMed:12606401}.
Interaction partners:
- Growth/differentiation factor 3
- Activin receptor type-2B
- Activin receptor type-2A
- Inhibin beta B chain
- Embryonic growth/differentiation factor 1
- Inhibin beta A chain
- Mothers against decapentaplegic homolog 2
- Protein Cripto
- Nodal homolog
- Activin receptor type-1B
Sequence:
MTRALCSALRQALLLLAAAAELSPGLKCVCLLCDSSNFTCQTEGACWASVMLTNGKEQVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHLPTASPNAPKLGPMELAIIITVPVCLLSIAAMLTVWACQGRQCSYRKKKRPNVEEPLSECNLVNAGKTLKDLIYDVTASGSGSGLPLLVQRTIARTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQLCVKEDCKA
Protein: Protein SCARECROW (AtSCR) (GRAS family protein 20) (AtGRAS-20) (Protein SHOOT GRAVITROPISM 1) (Q9M384)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor required for quiescent center cells specification and maintenance of surrounding stem cells, and for the asymmetric cell division involved in radial pattern formation in roots. Essential for cell division but not differentiation of the ground tissue. Also required for normal shoot gravitropism. Regulates the radial organization of the shoot axial organs. Binds to the promoter of MGP, NUC, RLK and SCL3. Restricts SHR movment and sequesters it into the nucleus of the endodermis.
Subcellular location: Nucleus.
Interaction partners:
- Protein SHORT-ROOT
- Zinc finger protein JACKDAW
- Protein PAT1 homolog
- Zinc finger protein MAGPIE
- WUSCHEL-related homeobox 5
- Putative cyclin-D6-1
- Defensin-like protein 232
- Holliday junction resolvase MOC1, chloroplastic
- Defensin-like protein A
- Putative pentatricopeptide repeat-containing protein At5g43820
Sequence:
MAESGDFNGGQPPPHSPLRTTSSGSSSSNNRGPPPPPPPPLVMVRKRLASEMSSNPDYNNSSRPPRRVSHLLDSNYNTVTPQQPPSLTAAATVSSQPNPPLSVCGFSGLPVFPSDRGGRNVMMSVQPMDQDSSSSSASPTVWVDAIIRDLIHSSTSVSIPQLIQNVRDIIFPCNPNLGALLEYRLRSLMLLDPSSSSDPSPQTFEPLYQISNNPSPPQQQQQHQQQQQQHKPPPPPIQQQERENSSTDAPPQPETVTATVPAVQTNTAEALRERKEEIKRQKQDEEGLHLLTLLLQCAEAVSADNLEEANKLLLEISQLSTPYGTSAQRVAAYFSEAMSARLLNSCLGIYAALPSRWMPQTHSLKMVSAFQVFNGISPLVKFSHFTANQAIQEAFEKEDSVHIIDLDIMQGLQWPGLFHILASRPGGPPHVRLTGLGTSMEALQATGKRLSDFADKLGLPFEFCPLAEKVGNLDTERLNVRKREAVAVHWLQHSLYDVTGSDAHTLWLLQRLAPKVVTVVEQDLSHAGSFLGRFVEAIHYYSALFDSLGASYGEESEERHVVEQQLLSKEIRNVLAVGGPSRSGEVKFESWREKMQQCGFKGISLAGNAATQATLLLGMFPSDGYTLVDDNGTLKLGWKDLSLLTASAWTPRS
Protein: Keratin, type II cytoskeletal 8 (Cytokeratin-8) (CK-8) (Keratin-8) (K8) (Type-II keratin Kb8) (P05787)
Organism: Homo sapiens (Human)
Function: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:19188445}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix {ECO:0000250|UniProtKB:Q10758}.
Interaction partners:
- Keratin, type I cytoskeletal 18
- Desmoplakin
- Epithelial cell adhesion molecule
- Cadherin-1
- Sequestosome-1
- Keratin, type I cytoskeletal 19
- Periplakin
- Plectin
- Cellular tumor antigen p53
- Epidermal growth factor receptor
Sequence:
MSIRVTQKSYKVSTSGPRAFSSRSYTSGPGSRISSSSFSRVGSSNFRGGLGGGYGGASGMGGITAVTVNQSLLSPLVLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLESGMQNMSIHTKTTSGYAGGLSSAYGGLTSPGLSYSLGSSFGSGAGSSSFSRTSSSRAVVVKKIETRDGKLVSESSDVLPK
Protein: YopO (Q93KQ6)
Organism: Yersinia enterocolitica
Interaction partners:
Sequence:
MKIMGTMSPSISLAKAHERISKHWQNPVGELNIEGKRYRIIDNQVLRLNPHSGFSLFREGVGKIFSGKMFSFSIARNLTDTLHAAQKTTSQELRSDIPNALSNLFGAKPQTELPLGWKGKPLSGAPDLEGMRVAETDKFAEGESHISIIETKDKQRLVAKIERSIAEGHLFAELEAYKHIYKTAGKHPNLANVHGMAVVPYGNRKEEALLMDEVDGWRCSDTLRSLADSWKQGKINSEAYWGTIKFIAHRLLDVTNHLAKAGIVHNDIKPGNVVFDRASGEPVVIDLGLHSRSGEQPKGFTESFKAPELGVGNLGASEKSDVFLVVSTLLHGIEGFEKDPEIKPNQGLRFITSEPAHVMDENGYPIHRPGIAGVETAYTRFITDILGVSADSRPDSNEARLHEFLSDGTIDEESAKQILKDTLTGEMSPLPTDVRRITPKKLRELSDLLRTHLSSAATKQLDMGVVLSDLDTMLVALDKAEREGGVDKDQLKSFNSLILKTYSVIGAYIKGREGDTKSSSTEVSPYHRSNFMLSIVEPSLQRIQKHLDQTHSFSDIGSLMRAHKHLETLLEVLVTLSQQGQPVSSETYSFLNRLAEAKVTLSQQLNTLQQQQESAKAQLSILINRSGSWADVARQSLQRFDSTRPVVKFGTEQYTAIHRQMMAAHAAITLQEVSEFTDDMRNFTADSIPLLIQLGRSSLMDEHLVEQREKLRELTTIAERLNRLEREWM
Protein: C1GALT1-specific chaperone 1 (C38H2-like protein 1) (C38H2-L1) (Core 1 beta1,3-galactosyltransferase 2) (C1Gal-T2) (C1GalT2) (Core 1 beta3-Gal-T2) (Core 1 beta3-galactosyltransferase-specific molecular chaperone) (Q96EU7)
Organism: Homo sapiens (Human)
Function: Probable chaperone required for the generation of 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Probably acts as a specific molecular chaperone assisting the folding/stability of core 1 beta-3-galactosyltransferase (C1GALT1).
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- C1GALT1-specific chaperone 1-like protein
- Polypeptide N-acetylgalactosaminyltransferase 2
Sequence:
MLSESSSFLKGVMLGSIFCALITMLGHIRIGHGNRMHHHEHHHLQAPNKEDILKISEDERMELSKSFRVYCIILVKPKDVSLWAAVKETWTKHCDKAEFFSSENVKVFESINMDTNDMWLMMRKAYKYAFDKYRDQYNWFFLARPTTFAIIENLKYFLLKKDPSQPFYLGHTIKSGDLEYVGMEGGIVLSVESMKRLNSLLNIPEKCPEQGGMIWKISEDKQLAVCLKYAGVFAENAEDADGKDVFNTKSVGLSIKEAMTYHPNQVVEGCCSDMAVTFNGLTPNQMHVMMYGVYRLRAFGHIFNDALVFLPPNGSDND