wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phosphatase EYA1 (EC 3.1.3.16) (EC 3.1.3.48) (Eyes absent homolog 1) (Q99502)
Organism: Homo sapiens (Human)
Function: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (By similarity). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis (By similarity). Has also phosphatase activity with proteins phosphorylated on Ser and Thr residues (in vitro) (By similarity). Required for normal embryonic development of the craniofacial and trunk skeleton, kidneys and ears (By similarity). Together with SIX1, it plays an important role in hypaxial muscle development; in this it is functionally redundant with EYA2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12500905}. Nucleus {ECO:0000269|PubMed:12500905, ECO:0000269|PubMed:19234442}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000269|PubMed:19234442}.
Interaction partners:
- Homeobox protein SIX1
- Homeobox protein SIX2
- T-cell leukemia homeobox protein 1
- Homeobox protein SIX5
- Dachshund homolog 1
- Homeobox protein SIX4
- Paired box protein Pax-2
- Paired box protein Pax-3
- Sal-like protein 1
- Histone H2AX
Sequence:
MEMQDLTSPHSRLSGSSESPSGPKLGNSHINSNSMTPNGTEVKTEPMSSSETASTTADGSLNNFSGSAIGSSSFSPRPTHQFSPPQIYPSNRPYPHILPTPSSQTMAAYGQTQFTTGMQQATAYATYPQPGQPYGISSYGALWAGIKTEGGLSQSQSPGQTGFLSYGTSFSTPQPGQAPYSYQMQGSSFTTSSGIYTGNNSLTNSSGFNSSQQDYPSYPSFGQGQYAQYYNSSPYPAHYMTSSNTSPTTPSTNATYQLQEPPSGITSQAVTDPTAEYSTIHSPSTPIKDSDSDRLRRGSDGKSRGRGRRNNNPSPPPDSDLERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYNFGTDGFPAAATSANLCLATGVRGGVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEEEQGAKKHAMPFWRISSHSDLMALHHALELEYL
Protein: Bone morphogenetic protein receptor type-2 (BMP type-2 receptor) (BMPR-2) (EC 2.7.11.30) (Bone morphogenetic protein receptor type II) (BMP type II receptor) (BMPR-II) (Q13873)
Organism: Homo sapiens (Human)
Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25187962}; Single-pass type I membrane protein.
Interaction partners:
- Bone morphogenetic protein 10
- Bone morphogenetic protein 4
- Bone morphogenetic protein 2
- Bone morphogenetic protein receptor type-1B
- Activin receptor type-1
- Bone morphogenetic protein receptor type-1A
- Bone morphogenetic protein 7
- Bone morphogenetic protein 6
- Growth/differentiation factor 2
- Growth/differentiation factor 9
Sequence:
MTSSLQRPWRVPWLPWTILLVSTAAASQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDETIIIALASVSVLAVLIVALCFGYRMLTGDRKQGLHSMNMMEAAASEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGTCVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEIFMRCTDLFPGESVPEYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGMTTISEMPYPDETNLHTTNVAQSIGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEATGQQDFTQTANGQACLIPDVLPTQIYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGSKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRNHSVNSHAATTQYANGTVLSGQTTNIVTHRAQEMLQNQFIGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDVLAQGVPSTAADPGPSKPRRAQRPNSLDLSATNVLDGSSIQIGESTQDGKSGSGEKIKKRVKTPYSLKRWRPSTWVISTESLDCEVNNNGSNRAVHSKSSTAVYLAEGGTATTMVSKDIGMNCL
Protein: Homeobox protein goosecoid (P54366)
Organism: Drosophila melanogaster (Fruit fly)
Function: Appears to regulate regional development of specific tissues. Can rescue axis polarity in UV-radiated Xenopus embryos.
Subcellular location: Nucleus.
Interaction partners:
- EG:115C2.6 protein
- Male-specific sperm protein Mst84Dd
- LD24318p
- TAR DNA-binding protein 43
- CKII-alpha subunit interactor-3, isoform B
- LD27370p
- Uncharacterized protein, isoform B
- IP01243p
- WD repeat-containing protein 26 homolog
- Thioredoxin-T
Sequence:
MVETNSPPAGYTLKRSPSDLGEQQQPPRQISRSPGNTAAYHLTTAMLLNSQQCGYLGQRLQSVLQQQHAQHQQSQSQTPSSDDGSQSGVTILEEERRGGAAAASLFTIDSILGSRQQGGGTAPSQGSHISSNGNQNGLTSNGISLGLKRSGAESPASPNSNSSSSAAASPIRPQRVPAMLQHPGLHLGHLAAAAASGFAASPSDFLVAYPNFYPNYMHAAAVAHVAAAQMQAHVSGAAAGLSGHGHHPHHPHGHPHHPHLGAHHHGQHHLSHLGHGPPPKRKRRHRTIFTEEQLEQLEATFDKTHYPDVVLREQLALKVDLKEERVEVWFKNRRAKWRKQKREEQERLRKLQEEQCGSTTNGTTNSSSGTTSSTGNGSLTVKCPGSDHYSAQLVHIKSDANGYSDADESSDLEVA
Protein: Cytoplasmic export protein 1 (Q12453)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the nuclear tRNA export machinery that my collect tRNA from the nuclear tRNA export receptors of the aminoacylation-dependent export and may deliver aminoacylated tRNAs to the translation machinery pathway at the nuclear pore complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Exportin-T
- Nucleoporin NUP116/NSP116
- GTP-binding nuclear protein GSP1/CNR1
- Coatomer subunit delta
- Uncharacterized membrane protein YLR326W
- U3 small nucleolar RNA-associated protein 8
Sequence:
MNFSSIFKSISNFQFPYTIEETAITETALWQCFDGTRKADSLPVTVFKAKRSPENESLILNAVHKSKILKIPGLCTVLETFDSDPQSTFIVTERVVPFPWDNLGSLSQNKFGVELGISQLLATLGFLKNFVLGTLSKDSVFINIKGEWVLFGLELCSSKEGLSAFEFASRARSYYNIIGSQLPCEDPNTIDSMGLGLLIKSLMAPSCLPKDWIVNVNMISDGKITIENFRKRLENTETWRSNPLINFYQELRELHIKDPQGKLVVMSNLENLYLESREIFRNLTPGMIENFIIPELCEIIKLLMTQSISSAASPIGMNFNASHKLVPFLAIVLDLTSETNTFPVGFNDLITQSFKLPDRQVRFLLLIYLPKLIGPLSKSEISSRIYPHFIQGLTDSDATLRLQTLKTIPCIVSCLTERQLNNELLRFLAKTQVDSDVEIRTWTVIIISKISTILSTSVGNRSNILATAFTKSLKDPQVKPRLAALYGLEKSIELFDVNTIANKILTVIAPGLLDKSPIVRGRAKILFEEYLEKLEKEAQLIQTNDSTADSEDVKDIDFENYGCDEEDMNKEDNLLAAQFLNNLRLNSPSATTPSNITESEIDSAQDGSGWDDLSDTDGFITNGTTESFDETTNPVTTASTPKLFGKPIKINKSWNDELNDDGWIQDESGPSKVPQKHTRPQNSTLAKSIAPSSRLSIKKKKTTILAPRNIASNSTVTTKSSLSNKTARSKPISSIRGSVTKKGNVDGWDDDGDSDSWDTNW
Protein: UDP-Gal or UDP-GlcNAc-dependent glycosyltransferase, putative (Q38CR0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MISRKTYLWFKFEVETLKPTNPYKMKADDDIFMRAPLYLKYLEVLPREKLNMGRAMGHVDDSIWRMRWHAVGYANTLSRDVVEEIVGYSGLCKLLFERISFRNFEKYIDYGALNEDIMVGEVIRNKLKIEGLLTVDMQDCHYAMNVQRPLDPFVEDNPNLIVLHHIANDEYRWLMLHCQALAPHNQQPPSIFQITAFWHEFTC
Protein: Multifunctional fusion protein [Includes: Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (L-glutamate gamma-semialdehyde dehydrogenase); L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88)] (A0A024RAC7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGRMEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWSYAYMQ
Protein: cAMP-dependent protein kinase catalytic subunit beta (PKA C-beta) (EC 2.7.11.11) (P68182)
Organism: Rattus norvegicus (Rat)
Function: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P22694}. Cell membrane {ECO:0000250|UniProtKB:P22694}. Membrane {ECO:0000250|UniProtKB:P22694}; Lipid-anchor {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000250|UniProtKB:P05131}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. {ECO:0000250|UniProtKB:P05131}.
Interaction partners:
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- Calmodulin-like protein 3
- Calmodulin-1
- Calmodulin-like protein 4
- Protein kinase cAMP-dependent type I regulatory subunit beta
- Cyclic AMP-responsive element-binding protein 1
- Ezrin
- Ryanodine receptor 2
- cAMP-dependent protein kinase inhibitor alpha
- cAMP-dependent protein kinase type II-alpha regulatory subunit
Sequence:
MGNTAIAKKGSEVESVKEFLAKAKEDFLRKWENPPPSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEEIRVSITEKCGKEFCEF
Protein: Response regulator UvrY (P0AED5)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system. UvrY activates the transcription of the untranslated csrB RNA and of barA, in an autoregulatory loop. Mediates the effects of CsrA on csrB RNA by BarA-dependent and BarA-independent mechanisms.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Signal transduction histidine-protein kinase BarA
- UvrABC system protein C
- Regulatory protein SdiA
- Carbon storage regulator
- RNase E specificity factor CsrD
- Ribosomal RNA small subunit methyltransferase B
- RNA polymerase sigma-54 factor
- RNA polymerase sigma factor RpoS
- Transcriptional regulatory protein PhoP
- Beta-galactosidase
Sequence:
MINVLLVDDHELVRAGIRRILEDIKGIKVVGEASCGEDAVKWCRTNAVDVVLMDMSMPGIGGLEATRKIARSTADVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRSVYSGQRYIASDIAQQMALSQIEPEKTESPFASLSERELQIMLMITKGQKVNEISEQLNLSPKTVNSYRYRMFSKLNIHGDVELTHLAIRHGLCNAETLSSQ
Protein: Importin subunit beta-4 (Importin-123) (Karyopherin subunit beta-4) (Karyopherin-123) (Ran-binding protein YRB4) (P40069)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Its predominant cargo substrate seems to be ribosomal proteins. Required for import of the ribosomal assembly factor NMD3. May be involved in nuclear transport of YAP1. Mediates the nuclear import of histones H3 and H4. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9238021, ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9238021, ECO:0000269|PubMed:9321403}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:9321403}.
Interaction partners:
- GTP-binding nuclear protein GSP1/CNR1
- Importin subunit beta-2
- Histone H4
- Importin beta SMX1
- Importin subunit beta-1
- Importin subunit beta-5
- Nucleoporin NUP60
- Nonsense-mediated mRNA decay protein 5
- Importin subunit alpha
- Importin beta-like protein KAP122
Sequence:
MDQQFLSQLEQTLHAITSGVGLKEATKTLQTQFYTQPTTLPALIHILQNGSDDSLKQLAGVEARKLVSKHWNAIDESTRASIKTSLLQTAFSEPKENVRHSNARVIASIGTEELDGNKWPDLVPNLIQTASGEDVQTRQTAIFILFSLLEDFTSSLSGHIDDFLALFSQTINDPSSLEIRSLSAQALNHVSALIEEQETINPVQAQKFAASIPSVVNVLDAVIKADDTMNAKLIFNCLNDFLLLDSQLTGNFIVDLIKLSLQIAVNSEIDEDVRVFALQFIISSLSYRKSKVSQSKLGPEITVAALKVACEEIDVDDELNNEDETGENEENTPSSSAIRLLAFASSELPPSQVASVIVEHIPAMLQSANVFERRAILLAISVAVTGSPDYILSQFDKIIPATINGLKDTEPIVKLAALKCIHQLTTDLQDEVAKFHEEYLPLIIDIIDSAKNIVIYNYATVALDGLLEFIAYDAIAKYLDPLMNKLFYMLESNESSKLRCAVVSAIGSAAFAAGSAFIPYFKTSVHYLEKFIQNCSQIEGMSEDDIELRANTFENISTMARAVRSDAFAEFAEPLVNSAYEAIKTDSARLRESGYAFIANLAKVYGENFAPFLKTILPEIFKTLELDEYQFNFDGDAEDLAAFADSANEEELQNKFTVNTGISYEKEVASAALSELALGTKEHFLPYVEQSLKVLNEQVDESYGLRETALNTIWNVVKSVLLASKVEPESYPKGIPASSYVNADVLAVIQAARETSMGNLSDEFETSMVITVMEDFANMIKQFGAIIIMDNGDSSMLEALCMQVLSVLKGTHTCQTIDIEEDVPRDEELDASETEATLQDVALEVLVSLSQALAGDFAKVFDNFRPVVFGLFQSKSKNKRSSAVGAASELALGMKEQNPFVHEMLEALVIRLTSDKSLEVRGNAAYGVGLLCEYASMDISAVYEPVLKALYELLSAADQKALAAEDDEATREIIDRAYANASGCVARMALKNSALVPLEQTVPALLAHLPLNTGFEEYNPIFELIMKLYQENSPVITNETPRIIEIFSAVFTKENDRIKLEKESTLGREENMERLKQFQTEEMKHKVIELLKYLNTTYNGIVAQNPVLAAVIA
Protein: UDP-N-acetylglucosamine transporter yea4 (O74750)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Sugar transporter that specifically mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc) and is required for cell wall chitin synthesis.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- AMP deaminase
- Uncharacterized transporter C22F8.04
- Uncharacterized protein C12G12.12
- GDP-mannose transporter
- UDP-galactose transporter homolog 1
- Putative transporter C83.11
- Protein phosphatase PP2A regulatory subunit B
- UDP-galactose transporter
- UDP-glucose 4-epimerase uge1
- Protein bem46
Sequence:
MIASALSFIFGGCCSNAYALEALVREFPSSGILITFSQFILITIEGLIYFLLNDVQSLKHPKVPRKRWFVVVVMFFAINVLNNVALGFDISVPVHIILRSSGPLTTMAVGRILAGKRYSSLQIGSVFILTIGVIIATLGNAKDLHLHVESMTRFGIGFTILVITQILGAIMGLVLENTYRIYGSDWRESLFYTHALSLPFFLFLLRPIRSQWNDLFAIHTKGFLNLPSGVWYLCFNTLAQYFCVRGVNALGAETSALTVSVVLNVRKFVSLCLSLILFENEMGPAVKFGALLVFGSSAVYASARSKPKTNGLKKND
Protein: 4-hydroxy-2-oxoglutarate aldolase, mitochondrial (EC 4.1.3.16) (Dihydrodipicolinate synthase-like) (DHDPS-like protein) (Probable 2-keto-4-hydroxyglutarate aldolase) (Probable KHG-aldolase) (Protein 569272) (Q86XE5)
Organism: Homo sapiens (Human)
Function: Catalyzes the final step in the metabolic pathway of hydroxyproline.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q0P5I5}.
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- Alanine--glyoxylate aminotransferase
- 2-Hydroxyacid oxidase 1
- 2-Hydroxyacid oxidase 2
- Aspartate aminotransferase, mitochondrial
- Putative aspartate aminotransferase, cytoplasmic 2
- Aspartate aminotransferase, cytoplasmic
- D-amino-acid oxidase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Mitochondrial translation release factor in rescue
Sequence:
MLGPQVWSSVRQGLSRSLSRNVGVWASGEGKKVDIAGIYPPVTTPFTATAEVDYGKLEENLHKLGTFPFRGFVVQGSNGEFPFLTSSERLEVVSRVRQAMPKNRLLLAGSGCESTQATVEMTVSMAQVGADAAMVVTPCYYRGRMSSAALIHHYTKVADLSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGMKDSGGDVTRIGLIVHKTRKQDFQVLAGSAGFLMASYALGAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELSPAEEEALRMDFTSNGWL
Protein: Transcription initiation factor IIF subunit alpha (TFIIF-alpha) (General transcription factor IIF subunit 1) (Transcription initiation factor RAP74 homolog) (AtRAP74) (Q9SU25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16905668}.
Interaction partners:
- General transcription and DNA repair factor IIH subunit TFB2
- DNA-directed RNA polymerase II subunit 4
- General transcription and DNA repair factor IIH subunit TFB4
- At1g75700
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription factor IIH subunit 2
- DNA-directed RNA polymerases II, IV and V subunit 11
- Transcription initiation factor IIA subunit 2
- Pentatricopeptide repeat-containing protein At4g30825
- TATA-box-binding protein 1
Sequence:
MSNCLQLNTSCVGCGSQSDLYGSSCRHMTLCLKCGRTMAQNKSKCHECGTVVTRLIREYNVRAAAPTDKNYFIGRFVTGLPNFKKGSENKWSLRKDIPQGRQFTDAQREKLKNKPWILEDETGQFQYQGHLEGSQSATYYLLVMQNKEFVAIPAGSWYNFNKVAQYKQLTLEEAEEKMKNRRKTADGYQRWMMKAANNGPALFGEVDNEKESGGTSGGGGRGRKKSSGGDEEEGNVSDRGDEDEEEEASRKSRLGLNRKSNDDDDEEGPRGGDLDMDDDDIEKGDDWEHEEIFTDDDEAVGNDPEEREDLLAPEIPAPPEIKQDEDDEENEEEEGGLSKSGKELKKLLGKANGLDESDEDDDDDSDDEEETNYGTVTNSKQKEAAKEEPVDNAPAKPAPSGPPRGTPPAKPSKGKRKLNDGDSKKPSSSVQKKVKTENDPKSSLKEERANTVSKSNTPTKAVKAEPASAPASSSSAATGPVTEDEIRAVLMEKKQVTTQDLVSRFKARLKTKEDKNAFANILRKISKIQKNAGSQNFVVLREKCQPKPGKRESRVNKLNIRSNLQPRKMELVTEDEIRKVLMEKKQLTTLELVMRFKERLTTTEDKDSFSHILKKIAKLQKNPGSEKFVVVLRDNVTPLASDLTRLSIS
Protein: Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) (P78012)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Interaction partners:
- Co-chaperonin GroES
- Chaperone protein DnaK
- Protein GrpE
- Heat-inducible transcription repressor HrcA
- Chaperone protein DnaJ
- Trigger factor
- DNA-directed RNA polymerase subunit beta
- Probable cytosol aminopeptidase
- Thioredoxin
- Chaperone protein ClpB
Sequence:
MAKELVFGKNARNKLLAGINKLADAVKVTVGPKGQNVILGRKFSNPLITNDGVTIAKEIELTDPLENIGAKVISVAAVSTNDIAGDGTTTATILAQEMTNRGVEAVNNGANPVNVRRGIEDASQLIITELDKRSKKINTNEEIEQVAAISSGSKEIGKLIAQAMALVGKNGVITTDDAKTINTTLETTEGIEFKGTYASPYMVSDQEKMEVVLDQPKILVSAMKINTIKEILPLLEGSMENGNPLLIVAPDFAEEVVTTLAVNKLRGTINVVAVKCNEYGERQKAALEDLAISTGTLAYNNELGGGFKDVTVNHLGEARRVQVAKEKTTVIGGKGSKETIQKHLDLLNGRLKQTTEKYDTDLLKERIAHLSQGVAVVRVGGATELAQKELKLRIEDALNSTKAAVEEGIISGGGIALLNVSTILNDSKLADKYKAETSAENLKEILVGYEIVRKSLEAPVRQIIENSGVNPVKVFAELRSEADGVGFDAETKKKVDMIRSGIIDPTKVTKTALEKAASVASSLITTSVAVYDIKENKEGSFQE
Protein: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ (EC 4.2.1.59) ((3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase) ((3R)-hydroxymyristoyl-ACP dehydrase) (17 kDa actomyosin component) (Beta-hydroxyacyl-ACP dehydratase) (P0A6Q6)
Organism: Escherichia coli (strain K12)
Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Subcellular location: Cytoplasm.
Interaction partners:
- UDP-3-O-
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- Enoyl-[acyl-carrier-protein] reductase FabI
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Acyl carrier protein
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Sequence:
MTTNTHTLQIEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCARSREA
Protein: cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 7 (EC 3.1.4.35) (EC 3.1.4.53) (Phosphodiesterase 7) (ddPDE7) (Q54HY0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Phosphodiesterase with dual cAMP/cGMP specificity. However, displays a preference for cAMP over cGMP. Seems to regulate cAMP/cGMP concentration especially during cell aggregation.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:17040207}. Cell surface {ECO:0000269|PubMed:17040207}.
Interaction partners:
- 3',5'-cyclic-AMP phosphodiesterase 4
- cGMP-specific 3',5'-cGMP phosphodiesterase 3
- cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B
Sequence:
MKYLILILIFFIEINNGSRLINSGNLFSELKDYYIPENLNYYSGGYSEQHCKDSSYITIPLGVTGGLDEGSLSSFLLTKKGSSLFIGLDAGTVWQGVRRLTMLQDFNSVFNITYPPWATLPEQRATWFIKNHIQGYLIGHSHLDHVGGLIVESAEDQLSPKKNELEVSQPEIYRGCIEMIHKMGYVSDFPNITSIPDQKKPIIGINETLYSMATDLFNGFVWPSLPNYGRYSYYYLGNGNQYSFKDLTPYANKYVTKVQNDFPFNHLVKSFEICHDSLTSTAFILTDSQSGEQIVFFSDTGISTTKCDWEFKILQVWRNIKIDKLKAVYIESSFTNEVADNVLFGHLRPKDIMKLMDSLLENSIQTSPPKTNLKHVKLIIEHIKPQVGMNQYYLTSQRMVYQQLQEINNHGVKVIIPNQGVPICL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9FYC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cell division cycle 5-like protein
Sequence:
MAEDKNNGRVNDESEYSSEDEGTEDYKKGGYHTVRVGDTFKNGAYVIQSKLGWGHFSTVWLAWDTQESRYVALKVQKSAQHYTEAAMDEIKILKQIAEGDSGDKKCVVKLLDHFKHTGPNGKHVCMVFEYLGDNLLSVIKYSDYRGVPLHMVKELCFHILVGLDYLHRELSIIHTDLKPENVLLLSTIDPSRDVRRSGVPLVLPITKDKIVSESAVKPETKSYTYNGDLTKNQKKKIRKKAKKVVAQDFGGEEALEESERDSNSEARINGNSTVERSEGSSTRLMEGEEAREKANKKNGRGSRRGSRSTRQKLLSDIECKCKLVDFGNACWTYKQFTSDIQTRQYRCPEVVLGSKYSTSADMWSFACICFELATGDVLFDPHSGENYDRDEDHLALMMELLGMMPRKIALGGRYSRDFFNRQGELRHIRRLRFWPISKVLKEKYDFSEQDAKDMSDFLVTILEFVPEKRPTAAQCLKHPWFNPGPRLLEPSLKPQQPKGEEEGAANENIEKEKDEREAMEAGVGNIAIDVSEPK
Protein: DNA-directed RNA polymerase II subunit RPB11 (RNA polymerase II subunit B11) (DNA-directed RNA polymerase II subunit J) (RNA polymerase II 13.3 kDa subunit) (RPB14) (O08740)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P52435}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MNAPPAFESFLLFEGEKKITINKDTKVPNACLFTINKEDHTLGNIIKSQLLKDPQVLFAGYKVPHPLEHKIIIRVQTTPDYSPQEAFTNAITDLISELSLLEERFRGAIKDKQEGIE