wanglab/gogpt-training-data huggingface dataset:
Protein: DNA helicase (EC 3.6.4.12) (O81047)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Double-stranded DNA-binding family protein
- Nucleic acid-binding, OB-fold-like protein
Sequence:
MARKMSLEAFVSTMAPLIDMEKEAEISMSLTSGASRNIETAQKKGTTILNLKCVDVQTGLMGKSLIEFQSNKGDVLPAHKFGNHDVVVLKLNKSDLGSSPLAQGVVYRLKDSSITVVFDEVPEEGLNTSLRLEKLANEVTYRRMKDTLIQLSKGVLRGPASDLVPVLFGERQPSVSKKDVKSFTPFNKNLDQSQKDAITKALSSKDVFLLHGPPGTGKTTTVVEIVLQEVKRGSKILACAASNIAVDNIVERLVPHKVKLVRVGHPARLLPQVLDSALDAQVLKGDNSGLANDIRKEMKALNGKLLKAKDKNTRRLIQKELRTLGKEERKRQQLAVSDVIKNADVILTTLTGALTRKLDNRTFDLVIIDEGAQALEVACWIALLKGSRCILAGDHLQLPPTIQSAEAERKGLGRTLFERLADLYGDEIKSMLTVQYRMHELIMNWSSKELYDNKITAHSSVASHMLFDLENVTKSSSTEATLLLVDTAGCDMEEKKDEEESTYNEGEAEVAMAHAKRLMESGVQPSDIGIITPYAAQVMLLRILRGKEEKLKDMEISTVDGFQGREKEAIIISMVRSNSKKEVGFLKDQRRMNVAVTRSRRQCCIVCDTETVSSDAFLKRMIEYFEEHGEYLSASEYTN
Protein: COP9 signalosome complex subunit 6 (Q1EC57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367006}. Nucleus {ECO:0000256|RuleBase:RU367006}.
Interaction partners:
Sequence:
MAPSSSSGLTFKLHPLVIVNISDHYTRVKTQLNPPASICASGHGSNNGEAMFQQNPRVYGCVIGVQRGRTVEIFNSFELLYDPSTQTLDRSFLEKKQELYKKVFPDFYILGWYSTGSDAEESDMHIHKALMDINESPVYVLLNPAINHTQKDLPVTIYESELHVIDGIPQLIFAHTSYTIETVEAERISVDHVAHLKPSDGGSAATQLAAHLTGIHSAIKMLNSRIRVLYQNLAAMQKGDKSCDNSVLRQVSSLLRRLPAMESERFQDNFLMEYNDKLLITYLAMITNCSSNMNEMVDKFNTAYDRNTRRGGRTAFM
Protein: Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit) (Telomerase subunit P133) (O77448)
Organism: Tetrahymena thermophila (strain SB210)
Function: Catalytic component of telomerase, an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular location: Nucleus {ECO:0000255|RuleBase:RU365061}. Chromosome, telomere {ECO:0000255|RuleBase:RU365061, ECO:0000269|PubMed:16462747}.
Interaction partners:
Sequence:
MQKINNINNNKQMLTRKEDLLTVLKQISALKYVSNLYEFLLATEKIVQTSELDTQFQEFLTTTIIASEQNLVENYKQKYNQPNFSQLTIKQVIDDSIILLGNKQNYVQQIGTTTIGFYVEYENINLSRQTLYSSNFRNLLNIFGEEDFKYFLIDFLVFTKVEQNGYLQVAGVCLNQYFSVQVKQKKWYKNNFNMNGKATSNNNQNNANLSNEKKQENQYIYPEIQRSQIFYCNHMGREPGVFKSSFFNYSEIKKGFQFKVIQEKLQGRQFINSDKIKPDHPQTIIKKTLLKEYQSKNFSCQEERDLFLEFTEKIVQNFHNINFNYLLKKFCKLPENYQSLKSQVKQIVQSENKANQQSCENLFNSLYDTEISYKQITNFLRQIIQNCVPNQLLGKKNFKVFLEKLYEFVQMKRFENQKVLDYICFMDVFDVEWFVDLKNQKFTQKRKYISDKRKILGDLIVFIINKIVIPVLRYNFYITEKHKEGSQIFYYRKPIWKLVSKLTIVKLEEENLEKVEEKLIPEDSFQKYPQGKLRIIPKKGSFRPIMTFLRKDKQKNIKLNLNQILMDSQLVFRNLKDMLGQKIGYSVFDNKQISEKFAQFIEKWKNKGRPQLYYVTLDIKKCYDSIDQMKLLNFFNQSDLIQDTYFINKYLLFQRNKRPLLQIQQTNNLNSAMEIEEEKINKKPFKMDNINFPYYFNLKERQIAYSLYDDDDQILQKGFKEIQSDDRPFIVINQDKPRCITKDIIHNHLKHISQYNVISFNKVKFRQKRGIPQGLNISGVLCSFYFGKLEEEYTQFLKNAEQVNGSINLLMRLTDDYLFISDSQQNALNLIVQLQNCANNNGFMFNDQKITTNFQFPQEDYNLEHFKISVQNECQWIGKSIDMNTLEIKSIQKQTQQEINQTINVAISIKNLKSQLKNKLRSLFLNQLIDYFNPNINSFEGLCRQLYHHSKATVMKFYPFMTKLFQIDLKKSKQYSVQYGKENTNENFLKDILYYTVEDVCKILCYLQFEDEINSNIKEIFKNLYSWIMWDIIVSYLKKKKQFKGYLNKLLQKIRKSRFFYLKEGCKSLQLILSQQKYQLNKKELEAIEFIDLNNLIQDIKTLIPKISAKSNQQNTN
Protein: Leucine-rich repeat and WD repeat-containing protein 1 (Origin recognition complex-associated protein) (A0A140VJD0)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGPLSARLLMQRGRPKSDRLGKIRSLDLSGLELLSEHLDPKLLCRLTQLQELDLSNNHLETLPDNLGLSHLRVLRCANNQLGDVTALCQFPKLEELSLEGNPFLTVNDNLKVSFLLPTLRKVNGKDASSTYSQVENLNRELTSRVTAHWEKFMATLGPEEEAEKAQADFVKSAVRDVRYGPESLSEFTQWRVRMISEELVAASRTQVQKANSPEKPPEAGAAHKPRARLAALKRPDDVPLSLSPSKRACASPSAQVEGSPVAGSDGSQPAVKLEPLHFLQCHSKNNSPQDLETQLWACAFEPAWEEGATSQTVATCGGEAVCVIDCQTGIVLHKYKAPGEEFFSVAWTALMVVTQAGHKKRWSVLAAAGLRGLVRLLHVRAGFCCGVIRAHKKAIATLCFSPAHETHLFTASYDKRIILWDIGVPNQDYEFQASQLLTLDTTSIPLRLCPVASCPDARLLAGCEGGCCCWDVRLDQPQKRRVCEVEFVFSEGSEASGRRVDGLAFVNEDIVASKGSGLGTICLWSWRQTWGGRGSQSTVAVVVLARLQWSSTELAYFSLSACPDKGIVLCGDEEGNVWLYDVSNILKQPPLLPAALQAPTQILKWPQPWALGQVVTKTMVNTVVANASFTYLTALTDSNIVAIWGRM
Protein: Protein S100-A6 (Calcyclin) (Growth factor-inducible protein 2A9) (MLN 4) (Prolactin receptor-associated protein) (PRA) (S100 calcium-binding protein A6) (P06703)
Organism: Homo sapiens (Human)
Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative.
Subcellular location: Nucleus envelope. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Calcyclin-binding protein
- Annexin A11
- Advanced glycosylation end product-specific receptor
- Protein S100-A10
- Annexin A2
- Retinoblastoma-associated protein
- Annexin A1
- Thymosin beta-10
- Glyceraldehyde-3-phosphate dehydrogenase
- Cellular tumor antigen p53
Sequence:
MACPLDQAIGLLVAIFHKYSGREGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMEDLDRNKDQEVNFQEYVTFLGALALIYNEALKG
Protein: Tankyrase (E7EWY6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKVRHTPEQSARLSTEQPAALNTASLSPIFLKKLIL
Protein: Eukaryotic initiation factor 4F subunit p150 (eIF-4F p150) (eIF4F p150) (Translation initiation factor 4(4)-F(6) subunit gamma(3) protein 1) (eIF4G1) (mRNA cap-binding protein complex subunit p150) (P39935)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the eIF4F complex, which interacts with the mRNA cap structure and serves as an initial point of assembly for the translation apparatus. Stimulates translation by interaction with polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. TIF4631 is probably essential when TIF4632 is missing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23222640}. Cytoplasm, P-body {ECO:0000269|PubMed:23222640}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23222640}.
Interaction partners:
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Eukaryotic translation initiation factor 4E
- ATP-dependent RNA helicase eIF4A
- Protein NAM8
- U1 small nuclear ribonucleoprotein A
- Eukaryotic translation initiation factor 4B
- Eukaryotic initiation factor 4F subunit p130
- ATP-dependent RNA helicase DED1
- Nuclear cap-binding protein complex subunit 1
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
Sequence:
MTDETAHPTQSASKQESAALKQTGDDQQESQQQRGYTNYNNGSNYTQKKPYNSNRPHQQRGGKFGPNRYNNRGNYNGGGSFRGGHMGANSSNVPWTGYYNNYPVYYQPQQMAAAGSAPANPIPVEEKSPVPTKIEITTKSGEHLDLKEQHKAKLQSQERSTVSPQPESKLKETSDSTSTSTPTPTPSTNDSKASSEENISEAEKTRRNFIEQVKLRKAALEKKRKEQLEGSSGNNNIPMKTTPENVEEKGSDKPEVTEKTKPAEEKSAEPEVKQETPAEEGEQGEKGQIKEESTPKVLTFAERLKLKKQQKEREEKTEGKENKEVPVQEETKSAIESAPVPPSEQVKEETEVAETEQSNIDESATTPAIPTKSDEAEAEVEAEAGDAGTKIGLEAEIETTTDETDDGTNTVSHILNVLKDATPIEDVFSFNYPEGIEGPDIKYKKEHVKYTYGPTFLLQFKDKLNVKADAEWVQSTASKIVIPPGMGRGNRSRDSGRFGNNSSRGHDFRNTSVRNMDDRANSRTSSKRRSKRMNDDRRSNRSYTSRRDRERGSYRNEEKREDDKPKEEVAPLVPSANRWVPKFKSKKTEKKLAPDGKTELLDKDEVERKMKSLLNKLTLEMFDAISSEILAIANISVWETNGETLKAVIEQIFLKACDEPHWSSMYAQLCGKVVKELNPDITDETNEGKTGPKLVLHYLVARCHAEFDKGWTDKLPTNEDGTPLEPEMMSEEYYAAASAKRRGLGLVRFIGFLYRLNLLTGKMMFECFRRLMKDLTDSPSEETLESVVELLNTVGEQFETDSFRTGQATLEGSQLLDSLFGILDNIIQTAKISSRIKFKLIDIKELRHDKNWNSDKKDNGPKTIQQIHEEEERQRQLKNNSRSNSRRTNNSSNRHSFRRDAPPASKDSFITTRTYSQRNSQRAPPPKEEPAAPTSTATNMFSALMGESDDEE
Protein: Ras-related protein Rap-2b (EC 3.6.5.2) (P61226)
Organism: Mus musculus (Mouse)
Function: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells.
Subcellular location: Recycling endosome membrane {ECO:0000269|PubMed:19061864}; Lipid-anchor {ECO:0000269|PubMed:19061864}; Cytoplasmic side {ECO:0000269|PubMed:19061864}. Note=Associated with red blood cells-released vesicles. {ECO:0000250}.
Interaction partners:
Sequence:
MREYKVVVLGSGGVGKSALTVQFVTGSFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYERVPMILVGNKVDLEGEREVSYGEGKALAEEWSCPFMETSAKNKASVDELFAEIVRQMNYAAQPNGDEGCCSACVIL
Protein: 4'-phosphopantetheinyl transferase A (PPTase A) (EC 2.7.8.7) (Acyl-carrier-protein synthase pptA) (Phosphopantetheine:protein transferase pptA) (Q4X1W0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Acyl-carrier-protein synthase that transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi-domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). PptA is able to transfer the cofactor to a broad range of enzymes with acyl- or peptidyl-carrier protein domains and activates target enzymes involved in the synthesis of lysine, but also secondary metabolites including gliotoxin, fumigaclavine C, fumiquinazole A, fumiquinazoline C, pyripyroprene A, fumagillin, the siderophores triacetylfusarinine C (TAFC) and ferricrocin (FC), and dihydroxy naphthalene (DHN)-melanin. Plays an essential role in virulence.
Interaction partners:
- Dephospho-CoA kinase, putative
- 4'-phosphopantetheinyl transferase B, mitochondrial
- Non-reducing polyketide synthase spyA
- [acyl-carrier-protein] S-malonyltransferase
- Nonribosomal peptide synthetase sidC
- Nonribosomal peptide synthetase sidD
- 3-oxoacyl-[acyl-carrier-protein] synthase
Sequence:
MGSAQNERIPSLTRWYIDTRQLTVTNPSLPLLEALQPSDQEAVKRFYHLRDRHMSLASNLLKYLFIHRSCCIPWNKISISRTPDPHRRPCFIPSPALTEATDEPIPGIEFNVSHQASLVALAGTIIPQSHGASPNPTTVFANPSPSSVPAPSVPQVGIDITCVDERHARTSSAPSTRDQLAGYVDIFAEVFSSRELDTIKNLGGRFPADAQDGEAVEYGLRLFYTYWALKEAYIKMTGEALLAPWLRELEFTDVIAPEPAPAPGQGSAENWGEPYTGVKIWLYGKRVEDVRIEVVAFETGYIFATAARGAGLGAESRPLSRDAGVAVSVDRWMHMEKIDIDRDIAPCATGVCQCTKKQP
Protein: Acetate kinase (EC 2.7.2.1) (Acetokinase) (P75245)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
Interaction partners:
- Phosphate acetyltransferase
- Acyl carrier protein homolog
- Uncharacterized protein MG356 homolog
- PTS system glucose-specific EIICBA component
- Phosphoglycerate kinase
- FMN-dependent NADH:quinone oxidoreductase
- L-lactate dehydrogenase
- NADH oxidase
Sequence:
MNDNKILVVNAGSSSIKFQLFDYHKKVLAKALCERIFVDGFFKLEFNEQKVEEKVAFPDHHAAVTHFLNTLKKHKIIQELSDIILVGHRVVQGANYFKDSVIVDAEALAKIKEFIKLAPLHNKPEADVIEIFFKEVPSAKNVAVFDTTFHTTIPQENYLYAVPRSWEQKHLVRRYGFHGTSYKFINNYLEKHLNKQNLNLIVCHLGNGASVCAIKNGKSFNTSMGFTPLEGLIMGTRSGDLDPAIIGYVAEQENMSASDVVNALNKKSGMLALTGASDMRDVFAKPQENAVAIKMYVNRVADYIAKYLNQLEGNIDGLVFTGGIGENASDCVELFINAVKSLGFATDLKLFVKYGDSCVVSTPQSKYKIYRVRTNEELMIVEDSIRLTQK
Protein: Flagellar associated protein (Q385B6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFGGSKSDLIMSPPPHPKANMLDLYMTRYDYDYNRDIDPSGQGEKKSNFTVSGEVRNRPIFRAGAQTGGEGTTYRSHYVKHDVEGKDFRDILQSCCRAGEPETAFVHGRSTHVMGCSTGDGVPPNTTYKTDYVYNGRSIGGEPQLYAGAKATAFSPNLLAIPPTEEELRKMAEVAPKITSIESLAPKPKPSLEGLPANKEDLLASRRPQLTTGGHPTDYYCTSWVYGDKSLVYPSQLPCGLTNSQNGHLIGTIQNKAELLALLAGRKKAAAKATNPMPDTTNPIAIDKAAQPYCGVTRRLENEGHVKMSMYKSNYIDQAVLPELPDAAVQAGNHDPNDESDTTNRRAATTNAGTLTKRMHRLGTLRNSHGYVHKQRALDSDIDLQTWRRMRIIEKRIDVDKADPHRHKLNHRAHQ
Protein: Lamin B receptor (C9JXK0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIKPLTSFRQRKGGSTSSSPSRRRGSRSRSRSRSPGRPPKSARRSASASHQADIKEARREVEVKLTPLILKPFGNSISRYNGEPEHIERNDAPHKNTQEKFSLSQESSYIATQYSLRPRREEVKLKEIDSKEEKYVAKELAVRTFEVTPIRAKDLEFGGVP
Protein: Melanoma-associated antigen B18 (MAGE-B18 antigen) (Q8BQR7)
Organism: Mus musculus (Mouse)
Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22332604}.
Interaction partners:
- E3 ubiquitin-protein ligase LNX
Sequence:
MPRGQKSKLRAREKRRQARAKNAQEKEASPGPFYGCPHQASPVASMPTSPNMPMGEQSTFSHSYTSTSDQNLDEKSSDDSEDTEDWCKDPINHKVVLLVQFLMEKYQKKEVITKADMLKYVIKTSKNHFNEILKRASEHMELAFGIDLKEVDPNRHCYALFNKLEHTFDGVMGEEKMPSSGLLMIVLGVIFMNDNCVSETEIWNVLSMMGVYANRKHFIYGDPKKVITEDMVQLKYLEYQQVPNSNPPSFEFTWGPRACAEISKMKILEFWAKIHDTTPDSFPTLYEAALKDEEERAQARAVARAHTAAMASPYSRATVCSSSHTNI
Protein: Zinc finger C4H2 domain-containing protein (Hepatocellular carcinoma-associated antigen 127) (Q9NQZ6)
Organism: Homo sapiens (Human)
Function: Plays a role in interneurons differentiation. Involved in neuronal development and in neuromuscular junction formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23623388}. Nucleus {ECO:0000269|PubMed:23623388, ECO:0000269|PubMed:26056227}. Postsynaptic cell membrane {ECO:0000269|PubMed:23623388}. Note=Upon transfection into mouse primary hippocampal neurons, localizes at excitatory, but not inhibitory, postsynaptic sites.
Interaction partners:
- E3 ubiquitin-protein ligase RNF220
Sequence:
MADEQEIMCKLESIKEIRNKTLQMEKIKARLKAEFEALESEERHLKEYKQEMDLLLQEKMAHVEELRLIHADINVMENTIKQSENDLNKLLESTRRLHDEYKPLKEHVDALRMTLGLQRLPDLCEEEEKLSLDYFEKQKAEWQTEPQEPPIPESLAAAAAAAQQLQVARKQDTRQTATFRQQPPPMKACLSCHQQIHRNAPICPLCKAKSRSRNPKKPKRKQDE
Protein: Translation initiation factor IF3-2, chloroplastic (AtIF3-2) (AtINFC-2) (Protein SUPPRESSOR OF VARIEGATION 9) (O82234)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chloroplast translation initiation factor that is essential for the coordination of leaf and chloroplast development. IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:25630975, ECO:0000269|PubMed:27535792}.
Interaction partners:
- Translation initiation factor IF-2
- Large ribosomal subunit protein uL24c
- Peptide chain release factor 1
- AT3g09210/F3L24_8
- Large ribosomal subunit protein uL3c
- Class I peptide chain release factor
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- RNA-binding protein CP31B
- Large ribosomal subunit protein mL45
- 50S ribosomal protein L33
Sequence:
MAGITSSTVGFNAVFTGITKTVSSHSLFSVDSKLCSLRLSKTELSFTNLTPSPRRAFAVTCRFGGGGGGYRFSGDNRRGRPKEAEIDEALDISSIRSATVRLIDGQQNMLGLVSKDEAVRMADDAELDLVILSPDADPPVVKMMDYSKYRYEQQKRKKDQQKKTTRMDLKELKMGYNIDQHDYSVRLRAAQKFLQDGDKVKVIVSMKGRENEFRNIAIELLRRFQTEIGELATEESKNFRDRNMFIILVPNKEMIRKPQEPPTRKKKKTAENEASASAAEITAEPEPEPEPEPEPEPEPEPEPEPEPLQIDS
Protein: Sarcolipin (Q9CQD6)
Organism: Mus musculus (Mouse)
Function: Reversibly inhibits the activity of ATP2A1 and ATP2A2 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesis.
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:26816378}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27923914}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Phospholamban
- Sarcoplasmic/endoplasmic reticulum calcium ATPase regulator DWORF
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
- Myoregulin
- Myozenin-1
- Myosin regulatory light chain 2, atrial isoform
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Cysteine and glycine-rich protein 3
Sequence:
MERSTQELFINFTVVLITVLLMWLLVRSYQY
Protein: EPIDERMAL PATTERNING FACTOR-like protein 4 (EPF-like protein 4) [Cleaved into: CHALLAH-LIKE2] (Q2V3I3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts primarily as positive regulator of inflorescence growth. Endodermal expression is sufficient for proper inflorescence architecture. Redundantly involved with EPFL6 in procambial development regulation. Controls stomatal patterning. Mediates stomatal development inhibition. TMM (AC Q9SSD1) functions to dampen or block CLL2 signaling. Acts as growth-regulatory ligand for ERECTA family receptors.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- LRR receptor-like serine/threonine-protein kinase ERL2
- Protein EPIDERMAL PATTERNING FACTOR 2
- EPIDERMAL PATTERNING FACTOR-like protein 1
- Protein EPIDERMAL PATTERNING FACTOR 1
- EPIDERMAL PATTERNING FACTOR-like protein 9
- LRR receptor-like serine/threonine-protein kinase ERL1
- EPIDERMAL PATTERNING FACTOR-like protein 2
- Transcription factor SPEECHLESS
- EPIDERMAL PATTERNING FACTOR-like protein 8
- EPIDERMAL PATTERNING FACTOR-like protein 7
Sequence:
MGTFRRRRRFLLAALVTFALLHLFSASSIVSADGRWIGQRTGSDLPGGFIRSNKRFGGPGSSPPTCRSKCGKCQPCKPVHVPIQPGLSMPLEYYPEAWRCKCGNKLFMP
Protein: Defective proboscis extension response 4 (FI04761p) (Q59DX6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dpr-interacting protein eta, isoform B
Sequence:
MWTTDCPRALKAICLVPLWLLLFLDCGMVGGEVPPHYWETPYSQPYFDNSSRREVTATVGQAALLHCRVRNLGDRAVSWIRKRDLHILTVGILTYTNDQRFQSLHSEGSDEWTLRISSPQPRDSGTYECQVSTEPKISQGFRLNVVVSRAKILGNAELFIKSGSDINLTCLAMQSPVPPSFIYWYKGKRVMNYSQRGGINVITERSTRTSKLLIAKATPADSGNYTCSPSSSDSASVVVHVINGEHPAAMQHGNSSATCLRPLSSTSVPFVLATWMSMTVASVAWNSNLNINWNWSPDWRWHWNPKWNWSNLAAGLVGIWSWS
Protein: Uncharacterized protein (Q72AL2)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
Sequence:
MSDNDREARAGRQAVRHWLEDMCTAVRDIEREAADALHDKEDETAYREAMRRKALLLASLPDRGRDAVSLLPPQDRTPVEERLHRFAASAANALSIGSVFYMSALLYPEDHAPGEPNDLERFAASFTEPA
Protein: Isocitrate/homoisocitrate dehydrogenase (HICDH) (EC 1.1.1.286) (Beta-decarboxylating dehydrogenase) (O59394)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Catalyzes the NAD(+)-dependent oxidative decarboxylation of homoisocitrate to 2-oxoadipate (alpha-ketoadipate), and of isocitrate to 2-oxoglutarate, at near equal efficiency. May thus play a dual role in glutamate and lysine biosynthesis in vivo. Preferentially uses NAD over NADP.
Interaction partners:
- 3-isopropylmalate dehydratase large subunit
- 3-isopropylmalate dehydratase small subunit
- Homocitrate synthase
- ACT domain-containing protein
- Putative [LysW]-aminoadipate semialdehyde/glutamate semialdehyde transaminase
- Aminotransferase class I/classII large domain-containing protein
- 307aa long hypothetical phosphoglycerate dehydrogenase
- Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase
- 281aa long hypothetical ferredoxin oxidoreductase beta subunit
- 284aa long hypothetical ferredoxin oxidoreductase beta subunit
Sequence:
MYKVAVIKGDGIGPEVIDAAIRVVKSVTDKIKFYEFEGGLSVFKKYGVPIREEDLEEIRKMDAILFGATTTPFDVPRYKSLIITLRKELDLYANLRIIPNFKLRKEIIIVRENSEGLYSGEGAYDSNKVVDFRIITRKGAERIAKFAVKLAKDRSTFLTFVHKANILESDRFFRKIVLDIARKEDVKVREEIVDSFTIKLVKDPWNLGIILSENMFGDILSDLATIHAGSIGIVPSGNYGEDIALFEPIHGSAPDIAGKGIANPIGAILSAAMMLDYLGLDGSIIWKAVGRYVRRGNLTPDMEGRATTLEVTNGIISEIYRLDEYEIDEVWRDEVRLGRILLEIS
Protein: DNA-binding transcriptional regulator BolA (P0ABE2)
Organism: Escherichia coli (strain K12)
Function: Transcriptional regulator that plays an important role in general stress response. Has many effects on cell morphology, cell growth and cell division. Acts by regulating the transcription of many genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably involved in the coordination of genes that adapt the cell physiology in order to enhance cell adaptation and survival under stress conditions. Essential for normal cell morphology in stationary phase and under conditions of starvation. Also regulates a complex network of genes encoding proteins related to biofilm development, and negatively modulates flagellar biosynthesis and swimming capacity. Could be a motile/adhesive transcriptional switch, specifically involved in the transition between the planktonic and the attachment stage of biofilm formation. Overexpression produces round cell shape, impairs cell growth rate and induces biofilm development.
Interaction partners:
- Glutaredoxin 4
- Glutaredoxin 1
- Acid stress protein IbaG
- RNA polymerase sigma factor RpoS
- DNA protection during starvation protein
- Universal stress protein B
- Iron-sulfur cluster assembly protein SufB
- Fe/S biogenesis protein NfuA
Sequence:
MMIRERIEEKLRAAFQPVFLEVVDESYRHNVPAGSESHFKVVLVSDRFTGERFLNRHRMIYSTLAEELSTTVHALALHTYTIKEWEGLQDTVFASPPCRGAGSIA
Protein: Proteasome subunit alpha type-4-A (20S proteasome alpha subunit C-1) (Proteasome 27 kDa subunit) (Proteasome component 9) (Proteasome subunit alpha type-3) (O81148)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-1
- Proteasome subunit beta type-2-A
- Proteasome subunit beta type-2-B
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3-A
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-2-B
- Proteasome subunit alpha type-1-A
- Proteasome subunit alpha type-2-A
Sequence:
MSRRYDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTSLTSEKLELAEVYLTPSKTVKYHVHSPESLTKLLVKHGVTQPAAETS