wanglab/gogpt-training-data huggingface dataset:
Protein: Single-stranded DNA-binding protein (SSB) (Q3IJB1)
Organism: Pseudoalteromonas translucida (strain TAC 125)
Interaction partners:
- DNA polymerase III subunit alpha
- DNA polymerase III, chi subunit
- DNA topoisomerase 1
- DNA-directed DNA polymerase
- Replicative DNA helicase
- ATP-dependent DNA helicase PriA
- Small ribosomal subunit protein bS6
- Transporter
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS7
Sequence:
MARGVNKVILVGNLGQDPEVRYMPNGNGVANITLATSDSYKDKNTGQMVDKTEWHRVVFFGKLAEIVGEYCRKGSQIYVEGKLQTRKWTDPQGQEKYTTEIVVDGFTGQMQMLGSRGGDQQGGQQSGGYQGNQSQGGQQSGGYQNNQSQGGQQSGGYQSNQGQNNQQQGGYTPQQQSAPAAQPQSAPAPQQNNQYQQPQGGFAPQQSSAPQQQGGFAPKPQNAPQGGASNPMEPTIDFDDDIPF
Protein: Larval serum protein 1 beta chain (Hexamerin-1-beta) (P11996)
Organism: Drosophila melanogaster (Fruit fly)
Function: Larval storage protein (LSP) which may serve as a store of amino acids for synthesis of adult proteins.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Larval serum protein 1 alpha chain
- Larval serum protein 2
- Larval serum protein 1 gamma chain
- General odorant-binding protein 99b
- Fat body protein 2
Sequence:
MKIAIALLACLGLAAAASFHQTHEVKIADKAFLMKQKFLFEIVYRVEDPLMFEDHIKQGEKFYFEESYYTHYDMYMKKFFEAYKAHALLPKGEFFGALVMSHAKQARGLFNFFYYAKDWETFAANVAWARMHVNEGMFVYALTMAVIHRNDFHGLMLPSIYEIFPQFFFNSKFVFEAEKFDYEMWMKMTMYEKEYMDVYYKTNGYDYSTMYRSSDYTYMKDFKTWQWWKLMGLGEHWYTEDKFILRENIYEFNQETKWLSMMKDVKKFYMPVDYTRDLNLYNKESKLSYFTEDLGWNAYWYYLNMDYSFFLDGNTFDLKNDRRGEWWLYNVHQLLSRYYMERLSHGFGEIPEFSWYQQIEMGYDPQLIYYNGIGYSFRKNYYEMETYANYDMLDKITGFLKRIHNIVEMGYYKTADGHTIDLRKPEAIEFIGNMLQGNVDAMDKMFYQFWYMLAHMYFADADYYQMDVYPNVMLNFETMMRDPMYYMFYKSIAQVYFQFMHYLPKYTKEQLLMPGVTMKNVEVSDLTTYFDLVDFDVTNMLNDKMIFQDGKFVWDMSLFARQMRLNHKPFTYTYTIESEKVEKVVIRAFLGPKFDEFGKVISLAENRMNFMEIDEFYYELKAGTNKITRKSSEFYWTVKDRTTYTELYYYTMMAFDGKYDFPLDISEPHCGFPDRLVLPMGWQKGMPMQMFFMVVPYVAPAHEQFSTFDYTYSCGIGSGARYVDSLPFGYPFDRAIDEYEFFVPNMYFKDVSIYHADTMEPYYKYKSYSNYGHFDYTFFNDYYTKYFKF
Protein: Collagen alpha-1(XXVI) chain (Alpha-1 type XXVI collagen) (EMI domain-containing protein 2) (Emilin and multimerin domain-containing protein 2) (Emu2) (Q91VF6)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Collagen alpha-1
- Furin
Sequence:
MKLVLLLPWACCCLCGSALATGFLYPFPAAALQQHGYPEQGAGSPGNGYSSRRHWCHHTVTRTVSCQVQNGSETVVQRVYQSCRWPGPCANLVSYRTLIRPTYRVSYRTVTALEWRCCPGFTGSNCEEECMNCTRLSDMSERLTTLEAKVLLLEAAEQPSGPDNDLPPPQSTPPTWNEDFLPDAIPIAHPGPRRRRPTGPAGPPGQMGPPGPAGPPGSKGEQGQTGEKGPVGPPGLLGPPGPRGLPGEMGRPGPPGPPGPAGSPGLLPNTPQGVLYSLQTPTDKENGDSQLNPAVVDTVLTGIPGPRGPPGPPGPPGPHGPPGPPGAPGSQGLVDERVVARPSGEPSVKEEEDKASAAEGEGVQQLREALKILAERVLILEHMIGVHDPLASPEGGSGQDAALRANLKMKRGGPRPDGILAALLGPDPAQKSADQAGDRK
Protein: C-C motif chemokine 19 (Beta-chemokine exodus-3) (CK beta-11) (Epstein-Barr virus-induced molecule 1 ligand chemokine) (EBI1 ligand chemokine) (ELC) (Macrophage inflammatory protein 3 beta) (MIP-3-beta) (Small-inducible cytokine A19) (Q99731)
Organism: Homo sapiens (Human)
Function: May play a role not only in inflammatory and immunological responses but also in normal lymphocyte recirculation and homing. May play an important role in trafficking of T-cells in thymus, and T-cell and B-cell migration to secondary lymphoid organs. Binds to chemokine receptor CCR7. Recombinant CCL19 shows potent chemotactic activity for T-cells and B-cells but not for granulocytes and monocytes. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.
Subcellular location: Secreted.
Interaction partners:
- C-C chemokine receptor type 7
- Atypical chemokine receptor 4
- C-X-C chemokine receptor type 5
- C-X-C motif chemokine 13
- C-X-C chemokine receptor type 4
- C-C chemokine receptor-like 2
- C-C motif chemokine 21
- C-C chemokine receptor type 5
- Platelet factor 4 variant
- C-C chemokine receptor type 6
Sequence:
MALLLALSLLVLWTSPAPTLSGTNDAEDCCLSVTQKPIPGYIVRNFHYLLIKDGCRVPAVVFTTLRGRQLCAPPDQPWVERIIQRLQRTSAKMKRRSS
Protein: Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) (Q7KWQ2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Tryptophan--tRNA ligase, cytoplasmic
- serine--tRNA ligase
- Tryptophan--tRNA ligase, mitochondrial
- GTP-binding protein Rheb homolog
- Acyl carrier protein, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Probable isoleucine--tRNA ligase, mitochondrial
- Probable isoleucine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Probable asparagine--tRNA ligase, mitochondrial
Sequence:
MGLDIVLFRADKGGNPDLIRQSQKVRYANVDAVQEVIDLDKVVKETKYRLDNTNAEYAKLNKSVAMKKKAGESADEIIAQAEELNQSIIKLKAEVSEVELLLRKKLRPIGNIVHESVPIDNNEDNNQIIKTWGECKTSEGLLHHHELLEMIDGYDPERGTLVSGHRCYFLKGIGVLLNQAIINFALMHMTKRGSVPLQTPFFMNKDVMAKTAQLEQFDDELYKVTGDNEEKYLIATSEQPISAFHQDEWIEEKDLPKKYVGYSTCFRKEAGSHGRDTWGIFRVHQFEKIEQFCITEPEKSWDMMEEMINNSEQFYQELGIPYRVVNIVSGALNNAASKKYDLEGWFPGYNQYRELVSCSNCTDYQSRDLEIRCGMKKQGQQQKKYVHMLNSTLAATTRVICCILENYQTEGGITVPVPLRPYLGKDFIPFVKAAPKQKAIPKQKTTTPEQK
Protein: Gephyrin a (Gephyrin1) (D3KYK7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASDGMILTNHDHQIRVGILTVSDSCFRNLAEDRSGINLKDLVHDPSLLGGIISAYKIVPDEIDEIKEILVDWCDEKELNLILTTGGTGFAPRDVTPEATREVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDALEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEDEEKKDSGVASTEDSGSSHITAAAIAAKIPESIISRGVQVLPRDTASLSTTPSESPCAQQSRLSTASCPTPKVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTLTVMPGQVMRVTTGAPIPCGADAVVQVEDTELLRESEDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGARKLIFALPGNPVSAVVTCNLFVIPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
Protein: Pro-resilin (Q9V7U0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a central role in insect flight by providing low stiffness, high strain and efficient energy storage.
Interaction partners:
- Protein slit
- Roundabout 1, isoform A
- RE49895p
- IP03705p
- Bent, isoform F
Sequence:
MFKLLGLTLLMAMVVLGRPEPPVNSYLPPSDSYGAPGQSGPGGRPSDSYGAPGGGNGGRPSDSYGAPGQGQGQGQGQGGYAGKPSDTYGAPGGGNGNGGRPSSSYGAPGGGNGGRPSDTYGAPGGGNGGRPSDTYGAPGGGGNGNGGRPSSSYGAPGQGQGNGNGGRSSSSYGAPGGGNGGRPSDTYGAPGGGNGGRPSDTYGAPGGGNNGGRPSSSYGAPGGGNGGRPSDTYGAPGGGNGNGSGGRPSSSYGAPGQGQGGFGGRPSDSYGAPGQNQKPSDSYGAPGSGNGNGGRPSSSYGAPGSGPGGRPSDSYGPPASGSGAGGAGGSGPGGADYDNDEPAKYEFNYQVEDAPSGLSFGHSEMRDGDFTTGQYNVLLPDGRKQIVEYEADQQGYRPQIRYEGDANDGSGPSGPGGPGGQNLGADGYSSGRPGNGNGNGNGGYSGGRPGGQDLGPSGYSGGRPGGQDLGAGGYSNGKPGGQDLGPGGYSGGRPGGQDLGRDGYSGGRPGGQDLGASGYSNGRPGGNGNGGSDGGRVIIGGRVIGGQDGGDQGYSGGRPGGQDLGRDGYSSGRPGGRPGGNGQDSQDGQGYSSGRPGQGGRNGFGPGGQNGDNDGSGYRY
Protein: Structural maintenance of chromosomes protein 5 (Q18237)
Organism: Caenorhabditis elegans
Function: Core component of the smc-5/smc-6 complex. Functions in DNA double strand break repair by promoting sister-chromatid homologous recombination during meiosis. Acts in a DNA repair pathway for removal of ionizing radiation- and ultraviolet (UV) radiation-induced DNA lesions that is distinct from classical nucleotide excision repair and the translesion synthesis pathway. Also involved in the recovery of stalled replication forks.
Subcellular location: Nucleus {ECO:0000269|PubMed:20661436}. Chromosome {ECO:0000269|PubMed:20661436}. Note=Localizes on chromosomes during diplotene and diakinesis in oocytes. {ECO:0000269|PubMed:20661436}.
Interaction partners:
- Structural maintenance of chromosomes protein 6 homolog smc-6
- Phorbol-ester/DAG-type domain-containing protein
- E3 SUMO-protein ligase NSE2
- Non-structural maintenance of chromosomes element 4
- Structural maintenance of chromosomes protein 3
- RecF/RecN/SMC N-terminal domain-containing protein
- Small ubiquitin-related modifier
- MAGE domain-containing protein
- DNA topoisomerase 3
- Prion-like-
Sequence:
MASQDSDEALPANYKDYPDGSLLRVVFHNFLTYEHTSFLPTASLNMILGHNGSGKSSIICGICLACGGSPKSLGRSERIVEYIRHGCTEGYVEIAIADKQKGPQVVRLTIRVGEQPKYRLNDSATTQSEIADLRKHYNIQIDNPCAFLAQDKVKSFSEQSSIELLRNTEKAASADLDQQHIDLMKQREDSTSIEDKCTTSENAIKRLEDEIGKIMPLVENYRKKLALQSKLRLLEKKMKIMEFEKFDREYKAELQNMDGAMIEYREVEKSIAECEKHRKNLEDRIKKDRSQISQMQRSCNEILAKVQEKGDKKLMEDMMQRAKAKLESAKKAADQHEKDVEKARKMIDQARARLQEAVDTLNGYEEFQSEMKSLEQKYSTAERDSRQEEDAIQKKSYEMRQLENKKRDEEQNSQLNRQDRYRVLQNFSSDASKAYRWYQQNRSQFKGDVYMPIMDMVLKTPEAAKALENSVGVRDRTMFVCCYKEDELLINGKQHSWRINTSVVPAEKIYSEDIDAQLPSELSRLGFKYLVSNCFDAPAPLKQFLCNVSGLNRIPFGGSDVEKKIAEVSQAIEQTRYSVFLTANIRCQNSKSRYANNTLQSQSATREANTWRDQFFKVSPVAKRTDNSILEEIQKLKAEIDIRSEQLREKRGAIQKERDVLRQEQMQWKSKKQVHTKWKTELASEMAKLEALENEVVDISAIEEEYANVEKKAILETKKMLENSIRWHKEIIDKHRLIGIFELSESICKSRVNKSNSEAETHRSKLEDLKSVKDAAEDLLKTALNHKKAAASALMKECSLKTLDESKMSPAENKIYSSLVKMFEEADVPTDMNTLDQAITSEKTRLKLAEDSGEDGSIVHEQRLKVLDDDLVLEKTRQEKLIENRARIHDKLGDEINNWRKEVETMIEQINVNYVQFFDSLGCRGEVSLEVPENPLDIEKYGIMIMVCFRKGESMKRLDNKVQSGGERSVATMLYLLALQQLCPVPFRCIDEINQGMDPTNERKVFDIMVGMWNGTTGTLSKTQYFLLSPKLLHGLDMRENVNIVMVNSTLTNSHGKHYDTSAKIDATFAKMGISA
Protein: glutathione transferase (EC 2.5.1.18) (H3BRM6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLK
Protein: Putative extracellular sulfatase Sulf-1 homolog (CeSulf-1) (EC 3.1.6.-) (Q21376)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Cell surface {ECO:0000250}. Note=Also localized on the cell surface. {ECO:0000250}.
Interaction partners:
- Sulfatase N-terminal domain-containing protein
- Sulfatase N-terminal domain-containing protein
- GDP-fucose protein O-fucosyltransferase 1
- Tumor susceptibility gene 101 protein
- Mediator of RNA polymerase II transcription subunit 14
- D-glucuronyl C5-epimerase
- Protein CLASP-3
- Mediator of RNA polymerase II transcription subunit 17
- Sulfotransferase domain-containing protein
- Mediator of RNA polymerase II transcription subunit 31
Sequence:
MISNLRISNYFIIFYVLFLIIPIKVTSIHFVDSQHNVILILTDDQDIELGSMDFMPKTSQIMKERGTEFTSGYVTTPICCPSRSTILTGLYVHNHHVHTNNQNCTGVEWRKVHEKKSIGVYLQEAGYRTAYLGKYLNEYDGSYIPPGWDEWHAIVKNSKFYNYTMNSNGEREKFGSEYEKDYFTDLVTNRSLKFIDKHIKIRAWQPFALIISYPAPHGPEDPAPQFAHMFENEISHRTGSWNFAPNPDKQWLLQRTGKMNDVHISFTDLLHRRRLQTLQSVDEGIERLFNLLRELNQLWNTYAIYTSDHGYHLGQFGLLKGKNMPYEFDIRVPFFMRGPGIPRNVTFNEIVTNVDIAPTMLHIAGVPKPARMNGRSLLELVALKKKKKKHMTALKPWRDTILIERGKMPKLKKIRDRYIKQKKKFNKENRLSKECKRRKWQRDCVHGQLWKCYYTVEDRWRIYKCRDNWSDQCSCRKKREISNYDDDDIDEFLTYADRENFSEGHEWYQGEFEDSGEVGEELDGHRSKRGILSKCSCSRNVSHPIKLLEQKMSKKHYLKYKKKPQNGSLKPKDCSLPQMNCFTHTASHWKTPPLWPEELGEFCFCQNCNNNTYWCLRTKNETHNFLYCEFVTEFISFYDFNTDPDQLINAVYSLDIGVLEQLSEQLRNLRKCKNRQCEIWSTSQMLRSPKLVDLRVNEKSFLTYQPEKT
Protein: Ribonuclease VapC46 (RNase VapC46) (EC 3.1.-.-) (Toxin VapC46) (O50411)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB46.
Interaction partners:
- Antitoxin VapB46
- Ribonuclease VapC1
- Antitoxin MazE3
- Ribonuclease VapC12
- Probable endoribonuclease MazF7
Sequence:
MAAIYLDSSAIVKLAVREPESDALRRYLRTRHPRVSSALARAEVMRALLDKGESARKAGRRALAHLDLLRVDKRVLDLAGGLLPFELRTLDAIHLATAQRLGVDLGRLCTYDDRMRDAAKTLGMAVIAPS
Protein: CXXC-type zinc finger protein 1 (Q9XUE7)
Organism: Caenorhabditis elegans
Function: Transcriptional activator that exhibits a unique DNA binding specificity for CpG motifs; enriched at promoters containing the trimethylation mark on histone H3 'Lys-4' (H3K4me3). Forms part of the SET2 complex and interacts with the SIN3S HDAC complex at promoters. Required for H3K4 trimethylation and plays a repressive role in the expression of heat shock and salt-inducible genes. Required for fertility, in cooperation with class I histone deacetylases (HDACs).
Subcellular location: Nucleus {ECO:0000305|PubMed:24653213}.
Interaction partners:
- Retinoblastoma-binding protein homolog 5
- Set1/Ash2 histone methyltransferase complex subunit ash-2
- Anaphase-promoting complex subunit 4-like WD40 domain-containing protein
- Dosage compensation protein dpy-30
- Histone-lysine N-methyltransferase set-2
- WD_REPEATS_REGION domain-containing protein
- WD repeat-containing protein wdr-5.1
- WD repeat-containing protein wdr-5.3
- WD repeat-containing protein wdr-5.2
- RING-type E3 ubiquitin transferase
Sequence:
MSNKEIEDNEDVWKERCMNCIRCNDEKNCGTCWPCRNGKTCDMRKCFSAKRLYNEKVKRQTDENLKAIMAKTAQREAAHQAATTTAPSAPVVIEQQVEKKKRGRKKGSGNGGAAAAAQQRKANIINERDYVPNRPTRQQSADLRRKRTQLNAEPDKHPRQCLNPNCIYESRIDSKYCSDECGKELARMRLTEILPNRCKQYFFEGPSGGPRSLEDEIKPKRAKINREVQKLTESEKNMMAFLNKLVEFIKTQLKLQPLGTEERYDDNLYEGCIVCGLPDIPLLKYTKHIELCWARSEKAISFGAPEKNNDMFYCEKYDSRTNSFCKRLKSLCPEHRKLGDEQHLKVCGYPKKWEDGMIETAKTVSELIEMEDPFGEEGCRTKKDACHKHHKWIPSLRGTIELEQACLFQKMYELCHEMHKLNAHAEWTTNALSIMMHKQPNIIDSEQMSLFNKSQSTSSSASAHGATTPISSTSSSSSSSSKNDDEMEDTAEFLANLAVQKEEETQNN
Protein: GEO08928p1 (GH10915p) (Inverted repeat binding protein 18 kDa, isoform A) (Inverted repeat binding protein 18 kDa, isoform B) (Q9VTE8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Xrp1, isoform A
- Cryptocephal, isoform A
- RE59279p
Sequence:
MPAKKRTAASTSKNSDSPLSPHTDDPAYKEKRKKNNEAVQRTREKTKKSAEERKKRIDDLRKQNDALKVQIETSEKHISTLRDLIIQGEKTEDGHRIIQEILAEPDPDPKDND
Protein: Nascent polypeptide-associated complex subunit alpha (NAC-alpha) (Alpha-NAC) (Q94518)
Organism: Drosophila melanogaster (Fruit fly)
Function: May promote appropriate targeting of ribosome-nascent polypeptide complexes (By similarity). Required for correct localization of the osk/oskar protein to the posterior pole during embryonic development. The osk protein directs the recruitment of molecules responsible for posterior body patterning and germline formation in the embryo.
Interaction partners:
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein uL22
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL8
- FI01658p
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL24
Sequence:
MPELTEIKSEAAPSTSAEAKPEDVRVEDDGSDSDSDGGMPGLEEAVAATTQLGGGATGLPIDLVSKAKQSRGEKKARKIMLKLGLKQIQGVNRVTIRKSKNILFVINNPDVYKNPHSDTYIVFGEAKIEDLSQQAQVAAAEKFKAPEAAGAADSVGATTSVAPIAEEDEEDVDDTGVDEKDIELVITQANTTRAKAIKALKNNNNDIVNAIMELTML
Protein: Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.4) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) (Q9R0Y5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (By similarity). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By similarity). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (By similarity). May provide a mechanism to buffer the adenylate energy charge for sperm motility.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00568, ECO:0000255|HAMAP-Rule:MF_03171}.
Interaction partners:
- Adenylate kinase 7
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Adenylate kinase 2, mitochondrial
- Adenylate kinase 9
- Pyruvate kinase PKM
- Adenylate kinase 4, mitochondrial
- Adenylate kinase 8
- Ectonucleoside triphosphate diphosphohydrolase 2
Sequence:
MEEKLKKAKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSERGKKLSAIMEKGELVPLDTVLDMLRDAMLAKVDSSNGFLIDGYPREVKQGEEFEQKIGQPTLLLYVDAGAETMTQRLLKRGETSGRVDDNEETIKKRLETYYNATEPVISFYDKRGIVRKVNAEGTVDTVFSEVCTYLDSLK
Protein: Purple acid phosphatase 25 (EC 3.1.3.2) (O23244)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- At3g43110
Sequence:
MRMNKILLVFVFLSIATVINSGTTSNFVRTAQPSTEMSLETFPSPAGHNAPEQVHIVQGDYNGRGIIISWVTPLNLAGSNVVTYWKAVDGDVKPKKKRGHASTSSYRFYDYTSGFLHHATIKGLEYDTKYIYEVGTDGSVRQFSFTSPPKVGPDVPYTFGIIGDLGQTLASNETLYHYMSNPKGQAVLFPGDLSYADDHPNHDQRKWDSWGRFVEPCAAYQTFIYAAGNHEIDFVPNIGEPHAFKPYIHRYHNAYKASKSISPLWYSIRRASAHIIVLSSYSAYGKYTPQYVWLEQELKKVNREETPWLIVMVHSPWYNSNNYHYMEGESMRAMFESWFVNSKVDLVLSGHVHSYERSERVSNIKYNITNGLSYPVKDPSAPIYITIGDGGNIEGIANSFTDPQPSYSAYREASFGHAVLEIYNRTHAYYTWHRNQDNEPVAADSIMLHNRYFFPVEELESGNTRA
Protein: Propanal dehydrogenase (CoA-propanoylating) (EC 1.2.1.87) (Coenzyme-A-acylating propionaldehyde dehydrogenase) (Propanediol utilization protein PduP) (Q9XDN1)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: A CoA-acylating aldehyde dehydrogenase required for optimal 1,2-propanediol (1,2-PD) degradation. Optimizes growth in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by minimizing propionaldehyde toxicity (Probable). Directly targeted to the BMC. NAD(+) and NADH are regenerated internally within the Pdu BMC by the PduP and PduQ enzymes, which reduce NAD(+) and oxidize NADH respectively, although there must also be cofactor transport across the BMC.
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:14504694, ECO:0000269|PubMed:20308536, ECO:0000269|PubMed:26283792, ECO:0000269|PubMed:27063436, ECO:0000305|PubMed:12923081, ECO:0000305|PubMed:23077559}. Note=Probably located inside the BMC shell. {ECO:0000305|PubMed:20308536}.
Interaction partners:
- Propanediol dehydratase large subunit
- Propanediol dehydratase medium subunit
- Phosphate propanoyltransferase
- 1-propanol dehydrogenase PduQ
- Propanediol dehydratase small subunit
- Bacterial microcompartment shell protein PduJ
- Bacterial microcompartment shell protein PduA
- Bacterial microcompartment shell vertex protein PduN
- Bacterial microcompartment shell protein PduK
- Corrinoid adenosyltransferase PduO
Sequence:
MNTSELETLIRTILSEQLTTPAQTPVQPQGKGIFQSVSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLAPLAEESANETGMGNKEDKFLKNKAALDNTPGVEDLTTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSIYFSPHPGAKKVSLKLISLIEEIAFRCCGIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLLSPADTDKLRAVCLPEGQANKKLVGKSPSAMLEAAGIAVPAKAPRLLIALVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHHTAIMHSQNVSRLNLAARTLQTSIFVKNGPSYAGIGVGGEGFTTFTIATPTGEGTTSARTFARSRRCVLTNGFSIR
Protein: 3-methylcrotonyl-CoA carboxylase biotin-containig subunit (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase biotin-containing subunit) (Q6T5L7)
Organism: Emericella nidulans (Aspergillus nidulans)
Interaction partners:
Sequence:
MPLSSLLRTSARLGQTVVARRSRRTASTVTSNSSSNFRALDSILIANRGEIALRVGRTAAQHGIRVTTLYTDPDSQAQHALSTPYAFNLGSVSAYLDGDRIIEIAKAQGCQGIHPGYGFLSENSEFARKCTEAGLVFIGPPWKAIEDMGDKRCSKHIMTAAGVPCVPSYHGENQDPNFLEAEADKIKYPVLIKAIKGGGGKGMRIARSKEEFQAQLQSAKSEAMNSFGDDHVLVEKYITTPRHIEVQVFADKHGNCVALGERDCSIQRRHQKILEESPAPHLPDATRKDIWAKARSAALAVRYEGAGTVEFIFDNDTGEFFFMEMNTRLQVEHPVTEMVTGQDLVHWQLKVAEGAELPLTQEEVEANIATHGHAIEARIYAENPAQGFIPDSGALLHVRTPATTEDVRIDAGFVQGDEVSAHYDPMIAKLIVRGADRQEAIRKLACSIGRVEVAGPATNIEFLKSVCKSADFISGKVETGYIEKHHDELFAQSPIEPEVLAQVALACLHDDARLAAQKATNFQGSAVGFGPGFQQHHMTFTNSASANNEAFDVKVQQTGENVFNVKIGEHTFEQVTSHPNADFRIITSFFPHTRLDTTVIRDGDSIVVFQRGRQYRLTTPRAKWMEKALGMKDVTNSVLAPMPCKVLRVEVQAGDTVEKDQPLVVIESMKMETVIRSPQRGKLPKSSIKKETNAKAGHRLWSLLVKTKRRRNRYGRIEAMLHQ
Protein: Membrane-bound carbonic anhydrase 14 (RCG52058, isoform CRA_b) (A2IBE0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLFFVLLLKVTWILAADGGHHWTYEGPHGQDHWPASYPECGGNAQSPIDIQTDGVIFDPDLPTVQPHGYDQLGTEPLDLHNNGHTVQLSLPPTLHLGGLPRKYTAAQLHLHWGQKGTLKGSEHQINSEATAAELHVVHYDSESYGSLSEAAQKPQGLAVLGILIEVGETENPAYDHILSHLHEVRYKDQKTSVPPFNVRELLPQQLEQFFRYNGSLTTPPCYQSVLWTVFNRRAQISMGQLEKLQETLSSTEEDPSEPLVQNYRVPQPLNQRTIFASFIQVGPLYTTGEMLGLGMGISAGCLCLLLTIYFIAQKIRRKRLGNRKSVVFTSARATTEA
Protein: Heat shock factor protein 2 (HSF 2) (Heat shock transcription factor 2) (HSTF 2) (Q03933)
Organism: Homo sapiens (Human)
Function: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8339932}. Nucleus {ECO:0000269|PubMed:8339932}. Note=Cytoplasmic during normal growth and moves to the nucleus upon activation.
Interaction partners:
- Heat shock factor protein 1
- Heat shock factor protein 4
- Lutropin-choriogonadotropic hormone receptor
Sequence:
MKQSSNVPAFLSKLWTLVEETHTNEFITWSQNGQSFLVLDEQRFAKEILPKYFKHNNMASFVRQLNMYGFRKVVHIDSGIVKQERDGPVEFQHPYFKQGQDDLLENIKRKVSSSKPEENKIRQEDLTKIISSAQKVQIKQETIESRLSELKSENESLWKEVSELRAKHAQQQQVIRKIVQFIVTLVQNNQLVSLKRKRPLLLNTNGAQKKNLFQHIVKEPTDNHHHKVPHSRTEGLKPRERISDDIIIYDVTDDNADEENIPVIPETNEDVISDPSNCSQYPDIVIVEDDNEDEYAPVIQSGEQNEPARESLSSGSDGSSPLMSSAVQLNGSSSLTSEDPVTMMDSILNDNINLLGKVELLDYLDSIDCSLEDFQAMLSGRQFSIDPDLLVDLFTSSVQMNPTDYINNTKSENKGLETTKNNVVQPVSEEGRKSKSKPDKQLIQYTAFPLLAFLDGNPASSVEQASTTASSEVLSSVDKPIEVDELLDSSLDPEPTQSKLVRLEPLTEAEASEATLFYLCELAPAPLDSDMPLLDS
Protein: Xylose isomerase (EC 5.3.1.5) (Q9P8C9)
Organism: Piromyces sp. (strain E2)
Interaction partners:
Sequence:
MAKEYFPQIQKIKFEGKDSKNPLAFHYYDAEKEVMGKKMKDWLRFAMAWWHTLCAEGADQFGGGTKSFPWNEGTDAIEIAKQKVDAGFEIMQKLGIPYYCFHDVDLVSEGNSIEEYESNLKAVVAYLKEKQKETGIKLLWSTANVFGHKRYMNGASTNPDFDVVARAIVQIKNAIDAGIELGAENYVFWGGREGYMSLLNTDQKREKEHMATMLTMARDYARSKGFKGTFLIEPKPMEPTKHQYDVDTETAIGFLKAHNLDKDFKVNIEVNHATLAGHTFEHELACAVDAGMLGSIDANRGDYQNGWDTDQFPIDQYELVQAWMEIIRGGGFVTGGTNFDAKTRRNSTDLEDIIIAHVSGMDAMARALENAAKLLQESPYTKMKKERYASFDSGIGKDFEDGKLTLEQVYEYGKKNGEPKQTSGKQELYEAIVAMYQ