wanglab/gogpt-training-data huggingface dataset:
Protein: Sporulation-specific protein (SPR6) (Q01684)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Not essential for sporulation.
Interaction partners:
- Nuclear envelope morphology protein 1
- Prospore membrane adapter protein SPO71
Sequence:
MAVSNIWQSYSSSNLHWIYPLYTNNCSQNVKSSFTAEILLKRRCNDIQDILNDRMIELLLQGACDPNKQQNYLQGMSPSRKKKTHVKKFLKKQKKSRKPITLEHGCLSGPVTLRFGNFAGIRDLRGTRCPLHGIKHGVHPKPGERCACQQATLFPSPLARFSCDQSAVLGCAASSTRVYDSIADEFSSLYF
Protein: WUSCHEL-related homeobox 5 (Q8H1D2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor, which may be involved in the specification and maintenance of the stem cells (QC cells) in the root apical meristem (RAM).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- CLAVATA3/ESR
- Protein CLAVATA 3
- Serine/threonine-protein kinase-like protein ACR4
- Receptor protein kinase CLAVATA1
- Probable polyol transporter 3
- Histone deacetylase 19
- Protein TOPLESS
- Zinc finger protein MAGPIE
- Cyclic dof factor 4
- LOB domain-containing protein 16
Sequence:
MSFSVKGRSLRGNNNGGTGTKCGRWNPTVEQLKILTDLFRAGLRTPTTDQIQKISTELSFYGKIESKNVFYWFQNHKARERQKRRKISIDFDHHHHQPSTRDVFEISEEDCQEEEKVIETLQLFPVNSFEDSNSKVDKMRARGNNQYREYIRETTTTSFSPYSSCGAEMEHPPPLDLRLSFL
Protein: Polypyrimidine tract-binding protein 1 (Q503D3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein A1b.
- Transformer 2 beta homolog.
- Serine/arginine repetitive matrix protein 4
- Heterogeneous nuclear ribonucleoprotein U
- Pcbp2 protein
- RNA-binding protein FUS
- RE1-silencing transcription factor
- Heterogeneous nuclear ribonucleoprotein C
- Serine/arginine-rich splicing factor 2
Sequence:
MDGRLETDLYPLGSSYVTEIDSVHDITVGTKRGSDELFSSCISNGPYIMSSGAANGNDSKKFKGDIRSPGIPSRVIHVRKLPNDINEAEVISLGLPFGKVTNLLMLKGKNQAFLEMNTEESAQTMVSYYSSVTPVIRNHPIFMQYSNHKELKTDNSPNQVRAQAALQAVNAVQTGGMSLAAIDGAGMGSQSPVLRVIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALVQYSDGMTAQHAKLSLDGQNIYNACCTLRISFSKLTSLNVKYNNDKSRDYTRPDLPTGDSQPSFDAQTMAAAALTAPGIISASPYAGAHGFPQAFAIQQAAGLSLQGMPAGALASLSVPGAAAAAAAAAAAGRLGLSGLTAAGNSVLLVSNLNPESVTPQCLFILFGVYGDVMRVKILFNKKENALVQMSDGTQAQLAMSHLNGQKLYGKALRATLSKHTTVQLPREGHEDQGLTKDYSNSPLHRFKKPGSKNYSNIFPPSSTLHLSNIPPSVTEDDLRGLFLSSGAVVKAFKFFQKDRKMALIQLASVEEAIESLIKFHNHDLGENHHLRVSFSKSTI
Protein: Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) (Q9AEP7)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
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
- Chaperone protein DnaJ
- Heat-inducible transcription repressor HrcA
- Chaperone protein ClpB
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease ATP-binding subunit ClpE
- ATP-dependent Clp protease ATP-binding subunit
- ATP-dependent Clp protease ATP-binding subunit ClpX
Sequence:
MSKEIKFSSDARTAMMRGIDILADTVKTTLGPKGRNVVLEKSYGSPLITNDGVTIAKEIELEDHFENMGAKLVSEVASKTNDIAGDGTTTATVLTQAIVREGLKNVTAGANPVGIRRGIELAAETAVASIKEMAIPVHDKSAIAQVATVSSRSEKVGEYISDAMERVGSDGVITIEESKGMQTELDVVEGMQFDRGYLSQYMVSNTEKMVAELDNPYILITDKKISNIQEILPLLEQILKTNRPLLIVADDVDGEALPTLVLNKIKGVFNVVAVKAPGFGDRRKAQLEDLAILTGGTVITEELGLDLKDATLEALGQAAKATVDKDHTTIVEGAGSVGAISDRVAIIKAQIEKITSDFDREKLQERLAKLAGGVAVVKVGAATETELKAMKLLIEDALNATRAAVEEGIVSGGGTALVNAIAALDKLSEEGDIQTGINIVRRALEEPVRQIAANAGYEGSVIIDKLRSEKVGTGFNAATGQWVNMIEEGIVDPAKVTRSALQNAASVAGLILTTEAVVANKPEPAAPAMPPMDPSMGMGGMM
Protein: Amyloid beta precursor like protein 2 (APPH) (Amyloid beta (A4) precursor-like protein 2) (Amyloid protein homolog) (Amyloid-like protein 2) (APLP-2) (CDEI box-binding protein) (CDEBP) (Sperm membrane protein YWK-II) (Q06481)
Organism: Homo sapiens (Human)
Function: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Amyloid beta precursor protein binding family B member 1
- Amyloid beta precursor protein binding family B member 2
- Tumor necrosis factor receptor superfamily member 21
- Amyloid-beta precursor protein
- Amyloid-beta A4 precursor protein-binding family B member 3
- Beta-secretase 1
- Amyloid-beta A4 precursor protein-binding family A member 1
- C-Jun-amino-terminal kinase-interacting protein 1
- Spondin-1
- Presenilin-1
Sequence:
MAATGTAAAAATGRLLLLLLVGLTAPALALAGYIEALAANAGTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKKQCKSRFVTPFKCLVGEFVSDVLLVPEKCQFFHKERMEVCENHQHWHTVVKEACLTQGMTLYSYGMLLPCGVDQFHGTEYVCCPQTKIIGSVSKEEEEEDEEEEEEEDEEEDYDVYKSEFPTEADLEDFTEAAVDEDDEDEEEGEEVVEDRDYYYDTFKGDDYNEENPTEPGSDGTMSDKEITHDVKAVCSQEAMTGPCRAVMPRWYFDLSKGKCVRFIYGGCGGNRNNFESEDYCMAVCKAMIPPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAERQTLIQHFQAMVKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAVDPEKAAQMKSQVMTHLHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRADMDQFTASISETPVDVRVSSEESEEIPPFHPFHPFPALPENEDTQPELYHPMKKGSGVGEQDGGLIGAEEKVINSKNKVDENMVIDETLDVKEMIFNAERVGGLEEERESVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQMQI
Protein: Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (E7EM57)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIRGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEAT
Protein: At3g25640 (Q84WS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKSILANTSLDSSFSLSKRYFNWKKKKVQEDDDEEEEEEEDDYNHNEKKVLTRFNFSSDPTRPDQFNAQQIMKKKKKKTLEKIRYALGFSNSGLGFRVVGTLFGNRRGHVYFAVQDDPTRLPAVLIQLPTPTSVLVREMASGLVRIALETAAYKTDSKKKLLEESTWRTYCNGKKCGYAARKECGEAEWKVLKAVGPITMGAGVLPATTTTVDEEGNGAVGSEKGELMYMRARFERVVGSRDSEAFYMMNPDVSSGGPELSVYFLRV
Protein: Guanine nucleotide-binding protein alpha-14 subunit (Q9BIG2)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. In association with the G-protein coupled dopamine receptor dop-2, modulates two types of learning: touch habituation and chemosensory associative conditioning.
Interaction partners:
- Guanine nucleotide-binding protein alpha-9 subunit
- Dopamine receptor 2
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit gamma
- G protein gamma domain-containing protein
- G Protein, Alpha subunit
- Guanine nucleotide-binding protein alpha-13 subunit
- Guanine nucleotide-binding protein G
Sequence:
MAFSCFDKFSYTYCYQCMHGPDGCMVPSRNGEGTELYAHSEELEAKLRELARRGHMEIEKELALEKKTYGSHIKILILGGPLSGKSTIFKQMQIIHVDGFKTDQELIQYRGLIDNNIRDIYLQLIAGSRVVGIPLDPIEHITYEIDEIYAPMSDAFSVRTISELLEPLTEFWNSKQIQEIYKRRCEFELLDSTKYYLENLTRIADPTYLPNQEDIVHSRKATMSINSIVFEYTGVSLLMIDVGGQRSERKKWLHLFDDAKVVLFVIDLTGYAKRSEESRMELSRFPKFFRDVGSNAYDMKVALKIFNEVAAASALANAVFLLFFNKVDLFKEILSQVNLQPCFSKFDGENTYEETSKYICEKFIRAASSKKSVFPHFTTATNTENVKLVFRACMESVFKANAKATGLS
Protein: Protein Njmu-R1 (Q9HAS0)
Organism: Homo sapiens (Human)
Function: As component of the WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1. May have a role in spermatogenesis.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:29426865}. Cytoplasmic vesicle {ECO:0000269|PubMed:29426865}.
Interaction partners:
- Protein FAM91A1
- WD repeat-containing protein 11
- Vacuolar protein-sorting-associated protein 25
- TBC1 domain family member 23
- Vacuolar protein sorting-associated protein 4A
- Vacuolar protein sorting-associated protein 4B
- Vacuolar-sorting protein SNF8
- Vacuolar protein-sorting-associated protein 36
Sequence:
MLPSLQESMDGDEKELESSEEGGSAEERRLEPPSSSHYCLYSYRGSRLAQQRGDSEDGSPSGTNAETPSGDDFSLSLADTNLPSEVEPELRSFIAKRLSRGAVFEGLGNVASVELKIPGYRVGCYYCLFQNEKLLPETVTIDSERNPSEYVVCFLGGSEKGLELFRLELDKYIQGLKNNMNCEARGLESHIKSYLSSWFEDVVCPIQRVVLLFQEKLTFLLHAALSYTPVEVKESDEKTKRDINRFLSVASLQGLIHEGTMTSLCMAMTEEQHKSVVIDCSSSQPQFCNAGSNRFCEDWMQAFLNGAKGGNPFLFRQVLENFKLKAIQDTNNLKRFIRQAEMNHYALFKCYMFLKNCGSGDILLKIVKVEHEEMPEAKNVIAVLEEFMKEALDQSF
Protein: Protein Wnt (M0R9D3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
- LDL receptor related protein 5
- Frizzled-5
- Frizzled-4
- Frizzled-2
- Low-density lipoprotein receptor-related protein
- Protein-serine O-palmitoleoyltransferase porcupine
- Frizzled-9
- Frizzled class receptor 7
- Receptor-like tyrosine kinase.
- NOTUM, palmitoleoyl-protein carboxylesterase
Sequence:
MTRKARRCLGHLFLSLGIVYLRIGDFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK
Protein: Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Peroxidase TXNRD1) (EC 1.11.1.2) (Thioredoxin reductase TR1) (O62768)
Organism: Bos taurus (Bovine)
Function: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis. Also has reductase activity on hydrogen peroxide (H2O2).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q16881}.
Interaction partners:
- Thioredoxin
- Selenide, water dikinase 1
- Thioredoxin
- Selenocysteine lyase
- Cystathionine gamma-lyase
- Aminotran_1_2 domain-containing protein.
- Kynurenine--oxoglutarate transaminase 3
- Thioredoxin reductase 2, mitochondrial
- thioredoxin-disulfide reductase
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
Sequence:
MNGSKDLPEPYDYDLIIIGGGSGGLAAAKEAAKYDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALRDSRNYGWNVEETVKHDWERMTEAVQNHIGSLNWGYRVALREKKVTYENAYGEFVGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMQEHGIKFIRQFVPIKVEQIEAGTPGRLRVIAKSTDSDQTIEGEYNTVLLAIGRDACTRKIGLENVGVKINEKTGKIPVTEEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSTVKCDYENVPTTVFTPLEYGSCGLSEEKAVEKFGEENVEVYHSYFWPLEWTIPSRDNNKCYAKVVCNIKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKDQLDSTIGIHPVCAEVFTTLSVTKRSGGNILQTGCUG
Protein: Translocated intimin receptor Tir (Secreted effector protein Tir) (Q7DB77)
Organism: Escherichia coli O157:H7
Function: Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion. In strain EDL933, acts via the effector protein EspF(U), in a phosphotyrosine- and NCK-independent manner. Tir binds to host BAIAP2, which mediates association with EspF(U) and leads to stimulation of actin polymerization.
Subcellular location: Secreted. Host cell membrane; Multi-pass membrane protein. Note=Secreted via the type III secretion system (T3SS). Released into the host cytoplasm via T3SS and then independently inserts into the plasma membrane from a cytoplasmic location. In host cells, localizes to the tip of the actin pedestal.
Interaction partners:
- Intimin
- Intimin
- T3SS secretion switching protein SepL
- Secreted effector protein EspF
- Tir chaperone
- EspD
- EspF
- T3SS secreted effector NleA/EspI
- Transcription regulator Ler
- EspB
Sequence:
MPIGNLGHNPNVNNSIPPAPPLPSQTDGAGGRGQLINSTGPLGSRALFTPVRNSMADSGDNRASDVPGLPVNPMRLAASEITLNDGFEVLHDHGPLDTLNRQIGSSVFRVETQEDGKHIAVGQRNGVETSVVLSDQEYARLQSIDPEGKDKFVFTGGRGGAGHAMVTVASDITEARQRILELLEPKGTGESKGAGESKGVGELRESNSGAENTTETQTSTSTSSLRSDPKLWLALGTVATGLIGLAATGIVQALALTPEPDSPTTTDPDAAASATETATRDQLTKEAFQNPDNQKVNIDELGNAIPSGVLKDDVVANIEEQAKAAGEEAKQQAIENNAQAQKKYDEQQAKRQEELKVSSGAGYGLSGALILGGGIGVAVTAALHRKNQPVEQTTTTTTTTTTTSARTVENKPANNTPAQGNVDTPGSEDTMESRRSSMASTSSTFFDTSSIGTVQNPYADVKTSLHDSQVPTSNSNTSVQNMGNTDSVVYSTIQHPPRDTTDNGARLLGNPSAGIQSTYARLALSGGLRHDMGGLTGGSNSAVNTSNNPPAPGSHRFV
Protein: LIM domain only 4 (LIM domain transcription factor LMO4a) (LIM only 4 protein) (Lmo4 protein) (Q8QG63)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Endothelial transcription factor GATA-2a
Sequence:
MVNSRVESSAVAVTGGSGGAVRSCAGCGGRISDRFLLFSMDRYWHTRCLKCSCCQAQLGEIGSTCFSKGGMILCRNDYIRLFGHSGACSACGQSIPASEMVMRAQGNVYHLKCFTCATCRNRLVPGDRFHYVNGTIFCEHDRPGGALLSSHLTPLQSNTLLPDQKVC
Protein: Leukocyte cell derived chemotaxin 2 (E5RHW6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFSTKALLLAGLISTALAGPWANICAGKSSNEIRTCDRHGCGQYSAQRSQRPHQGVDILCSAGSTVYAPFTGMIVGQEKPYQNKNAINNGVRISGREITTDTPIFNNYYPDQSAAVNIKTRSSTSKKMMTH
Protein: Putative inorganic phosphate transporter C1683.01 (Q9P6J9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: High-affinity transporter for external inorganic phosphate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized transporter C3B8.04c
- Putative uncharacterized oxidoreductase C513.07
- Uncharacterized protein PB2B2.06c
Sequence:
MKLNIFKSHGDSNTAEERPVPLEQVEAEDQQHENRFWLGLTAKEFRLMMLAGVGFFLDSYDLFIINLVTPIFEYLYWGGIEKGPNGKGHYPSGIRGLVNAASNIGNIFGQLMFGFMGDFFGRKFVYGKEMIIVIIATILLIAMPKSIHSPLSKMMWVFCWRWLLGVGIGGDYPMSAAITSERSKLNRRGTLISLIFAFQGFGTLAGAIVTIILLGCFEHPLNREGHYRKLEGVWRLQFGLALVPAIGVLIPRLMMEETQKFKNSQQLNSGDNRDPKTSLNFEDDELVKNPSVTKGHPEIHESSENYLSRSNTVENEPENIEKQFESVSAPANRSGFIQYFRQWHHFKHLLGTSVCWFLLDIAFYGVNLNQSVILKNIGFSSGTNEYRTLMKNAIGNLIIAVAGYVPGYWFNVFLVEILGRKWIQLQGFVITGLMFAILAGRWNEISTGGRFACFVIAQLFSNFGPNSTTFIYPAEVFPARVRGTAHGISAALGKCGAILASLLFNFLTSIIGYGNVMWIFCGCMWGGILFTLLLPETKGRDADEIDRVELFYGGDGKVECNSKWKSWYVNGIF
Protein: rRNA 2'-O-methyltransferase fibrillarin (Histone-glutamine methyltransferase) (Q38AL4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar protein 56
- Nucleolar RNA binding protein, putative
- H/ACA ribonucleoprotein complex subunit 2
- Uncharacterized protein
- Nrap protein domain-containing protein
- HEAT repeat-containing protein 1
- Centromere/microtubule binding protein cbf5, putative
- 50S ribosomal protein L7Ae, putative
- U3 small nucleolar ribonucleoprotein protein IMP3, putative
- Periodic tryptophan protein 2, putative
Sequence:
MRGGFGRGGGSGFRGGRGGGAPSRGRGGAGRGGGRGGNAGPHGRGGRGGGGRGGGAGAKVVVEPHLLHPGVFISKGKADSLCTLNMVPGVSVYGEKRVEVGATQSGDEKKEYRLWNPYRSKLAAAIYAGVGSIHMKPGSKVLYLGAASGTTVSHVSDLVGPEGMVYAVEFSNRSGRDLVDMSKRRPNIVPIIEDARYPMKYRMLMPMVDCIFMDVAQPDQARILALNAQAFLKNGGHYVISIKANCIDSTLDAPVVIAAELDKLRKDRLKPLEQASLEPFERDHAVVVGVYRSMKKAVQQ
Protein: Innexin inx1 (Innexin-1) (G-Inx1) (Q9XYN0)
Organism: Schistocerca americana (American grasshopper)
Function: Structural components of the gap junctions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction.
Interaction partners:
Sequence:
MYKLLGGLKEYLKWQDIVTDNAIFRLHNLFTTVLLLTCSLIITATQYVGNPIHCIVNGLPVRPINTYCWITSTFTMPDAFLRQVGSEVAHPGVANDFGDEDAKKYYTYYQWVCFVLFFQAMLCYTPKWIWDSIEGGLLRTLIMGLNRGLCQDDEKCMKKKALIEYLLRHIKRHNMYALKYWFCETLCLVNIIGQLYLMNHFFDGEFFSYGLRVVAFSEQSQEERVDPMVYVFPRVTKCTFHKYGASGSIQKHDSLCVLPLNIVNEKTYIFLWFWYIILAALLSVLVVYRAVILAVPSVRPILLHARNRMVPKEVTNAICRKTDVGDWWILYMLGRNMDPMIYGEVIADLAKKIETPSSNNP
Protein: Ribonuclease P protein component (RNase P protein) (RNaseP protein) (EC 3.1.26.5) (Protein C5) (P25814)
Organism: Bacillus subtilis (strain 168)
Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Interaction partners:
- Large ribosomal subunit protein bL34
- Membrane protein insertase MisCA
- Beta sliding clamp
- Chromosomal replication initiator protein DnaA
- Putative membrane protein insertion efficiency factor
- RNA-binding protein KhpB
- Large ribosomal subunit protein uL4
- DNA replication and repair protein RecF
- Large ribosomal subunit protein uL3
- Transcription termination factor Rho
Sequence:
MKKRNRLKKNEDFQKVFKHGTSVANRQFVLYTLDQPENDELRVGLSVSKKIGNAVMRNRIKRLIRQAFLEEKERLKEKDYIIIARKPASQLTYEETKKSLQHLFRKSSLYKKSSSK
Protein: Transcription factor mef2A (Myocyte enhancer factor 2A) (Serum factor response C) (Q55F37)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Transcription factor that regulates cell differentiation during development. Seems to negatively regulate prestalk gene expression and positively regulate prespore gene expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Probable ATP-dependent RNA helicase ddx20
- Mitochondrial import inner membrane translocase subunit tim50
Sequence:
MGRNKITIEKISNERNRQATFTKRKNGLIKKAMELSILCDCEIAMIVFSSNNKLFQYSSRDMDKLLIRYTDNTDNTRKNLTNQDYNRVFGNKKSKNDDEDGDDDGDEDLGETPTTPHGNLNAHPIGSMENNNNNNNNNNNNNNNNNNNINNNNNNNNNSHHNNNNGNNNNNNNNNNNNNSNNNSNNNNSNNGNSNNNNNGNNANHNMHHHNGNSANISPMQMSQQANNNNSNNNNNNGNNNSNSNSNNNNNSNGYQQQQQAAQQAVQQAQMAQQMHLQQQQQYQQLQHIQQQQQQQHQQQQQNMGPNGYNHQQQQLQHQSPPPPPQQQQQQMQHSQQQQNMNGIIGHHSPVIVGNGVSLLQPSKWSASPYGEDLAPLTPRSASYKGIYGNQYPPQMQPVVNSNNNSNGNSNSMNNGISSPPINQQNQQNQKPPIMNKPGGGGQPMYYDYNGYPQQQQPPQNYNSNGGYWGQNVSSPPPPQQQQSANPYIQQQQQPQHQSPYYHGNYSPQQQSPVLNSQNGHHSSPMHPHQMHHQQHQHQQHPQMQQQQQQQQQHQQHPQMQQIQQQQHPQMQQHQQHQQQHPQMQQQHMNNHQINHHHLNSSPEINSQKNVHSSPLIMNSNNNNNNNNNNHHGNDNNNNNNNNSNNNNNNNNSNNNNNINNNINSNSNNNSNVNNGNNNNSGKVYNNNNNSNNGNNNNNKPEQTIPVKIEKEHSSSPTIPEQPSINVSTSSNSAHVFNNITSNSNNNNNNNNNNNNNNNNTNNNNNNNNNNNNNNNTNNINSNNNSSNTNVNVINNSSSSSTPPISPANINTQSPAISPALVPVVTSLNPQGEETSKPKFKKSLNLSIVIPEVGNSKYPPPQCKLTPINVEATKQPDIPTLPSPRDFYPEINLHHDNVSLTPNYWGGWHQTPRGSLLLTGNGGSNNSNSSNNNNNNNNNNNNTNNNNISGNGSSSSSSSSTQNPNGFLGCLSPRSFNFLNENNNNNNNNSSSGNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNPDESDQSFNRKRKSMEPKN
Protein: Proteasome subunit beta type-2 (Macropain subunit C7-I) (Multicatalytic endopeptidase complex subunit C7-I) (Proteasome component C7-I) (Proteasome subunit beta-4) (beta-4) (P49721)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000269|PubMed:34711951}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 6B
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit 8
- Proteasome subunit alpha type-2
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 7
- Proteasome subunit alpha type-7
- Proteasome subunit beta type-10
- Proteasome subunit beta type-7
Sequence:
MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS
Protein: Alkyl hydroperoxide reducatase (Alkylhydroperoxide reductase) (Peroxiredoxin (EC 1.11.1.-)) (Q5UC28)
Organism: Helicobacter pylori (Campylobacter pylori)
Interaction partners:
Sequence:
MLVTKLAPDFKAPAVLGNNEVDEHFELSKNLGKNGAILFFWPKDFTFVCPTEIIAFDKRVKDFHEKGFNVIGVSIDSEQVHFAWKNTPVEKGGIGQVSFPMVADITKSISRDYDVLFEEAIALRGAFLIDKNMKVRHAVINDLPLGRNADEMLRMVDALLHFEEHGEVCPAGWRKGDKGMKATHQGVAEYLKENSIKL