wanglab/gogpt-training-data huggingface dataset:
Protein: Cysteine synthase A (CSase A) (EC 2.5.1.47) (O-acetylserine (thiol)-lyase A) (OAS-TL A) (O-acetylserine sulfhydrylase A) (S-carboxymethylcysteine synthase) (EC 4.5.1.5) (Sulfate starvation-induced protein 5) (SSI5) (P0ABK5)
Organism: Escherichia coli (strain K12)
Function: (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 and X90, both K12 derivatives). This protein is not required for CDI of strain EC93, whose toxin may function by forming inner cell membrane pores. CysK stabilizes CdiA-CT, allowing it to bind tRNA substrate; neither CdiA-CT nor CysK bind tRNA alone in vitro.
Interaction partners:
- Serine acetyltransferase
- Sulfite reductase flavoprotein alpha-component
- Sulfite reductase hemoprotein beta-component
- Cystathionine beta-lyase MetC
- Cystathionine gamma-synthase
- Sulfate adenylyltransferase subunit 2
- Phosphoadenosine 5'-phosphosulfate reductase
- Protein MalY
- Thiosulfate-binding protein
- Sulfate adenylyltransferase subunit 1
Sequence:
MSKIFEDNSLTIGHTPLVRLNRIGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASNPEKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKGTKGKTDLISVAVEPTDSPVIAQALAGEEIKPGPHKIQGIGAGFIPANLDLKLVDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDESFTNKNIVVILPSSGERYLSTALFADLFTEKELQQ
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q22KT7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MSISHVLWSTALIALTSVKTADANIDTGANRREFGAMCNVLRWTSTTFTNKADDWDDDKIYNSIADINMTLAEKEWRAMFLQEGQAEKWQLKLPTKHAENAAFQKMWALWACAAQRVGSERGLTDKLKKLKANELTATDLSLRRQRVQQIADKAHGIYFELKKLNRKKLKATPATIKAKIYTAVLGKADAVLGTDPTDDDSITSGGTSAATRSNGCGNSNIANQPGKNLGTVALCVCAKGASGTAVDDACWSETAAEVAYPTAASQAKTKIHELIKMCGTAAHTKLTADAVEASIKGLTSIMHTSSSGTYIGEYLATGCNGEDNGVVCFKYGTLTTTTNSNLMTIPWLAELHQLKQDLTGDDNLERAGQPLVQQLTILEAEVKEITAGELLMRQDSLFVNQPTHPASPEKVATVGEVCSKHNGSNTTCPRDKRTYDEKENKCNPIKQVEGVTAEGTGEKTTTEKCRGKLEKDCKSPDCKWEETVCKDSSFLVNKKLALISTNFVDLMF
Protein: Uncharacterized protein Rv2077c (P9WLL1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable integrase
- Large ribosomal subunit protein bL9
- PE family protein
- Uncharacterized protein Rv2076c
- Probable biotin-dependent acyl-coenzyme A carboxylase beta2 subunit
Sequence:
MLATLSQIRAWSTEHLIDAAGYWTETADRWEDVFLQMRNQAHAIAWNGAGGDGLRQRTRADFSTVSGIADQLRRAATIARNGAGTIDAAQRRVMYAVEDAQDAGFNVGEDLSVTDTKTTQPAAVQAARLAQAQALAGDIRLRVGQLVAAENEVSGQLAATTGDVGNVRFAGAPVVAHSAVQLVDFFKQDGPTPPPPGAPHPSGGADGPYSDPITSMMLPPAGTEAPVSDATKRWVDNMVNELAARPPDDPIAVEARRLAFQALHRPCNSAEWTAAVAGFAGSSAGVVGTALAIPAGPADWALLGAALLGVGGSGAAVVNCATK
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (Q5ZLJ0)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MSQERPKFYRQELNKTVWEVPERYQNLSPVGSGAYGSVCSAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPAKSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLTVNEDCELE
Protein: Vacuolar iron transporter homolog 3 (Protein NODULIN-LIKE 3) (Q9M2C3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable vacuolar iron transporter that may be involved in the regulation of iron distribution throughout the plant.
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:Q9LPU9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vacuolar iron transporter 1
- Nodulin/glutamine synthase-like protein
- Cation-chloride cotransporter 1
Sequence:
MESHNTLNLDMEKDQEKAFDYSKRAQWLRAAVLGANDGLVSTASLMMGVGAVKQNVKIMILTGFAGLVAGACSMAIGEFVSVYSQYDIEVAQMKRETGGEIEKEKLPSPTQAAAASALAFSLGAMVPLLAAAFVKEYKVRIGAIVAAVTLALVMFGWLGAVLGKAPVVKSSLRVLVGGWLAMAITYGFTKLIGSHSHMYV
Protein: Aprataxin and PNK-like factor (EC 3.1.1.-) (Apurinic-apyrimidinic endonuclease APLF) (A8JR14)
Organism: Drosophila melanogaster (Fruit fly)
Function: Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro.
Interaction partners:
- ATP-dependent DNA helicase II subunit 2
- ATP-dependent DNA helicase 2 subunit 1
- FI04011p
- DNA ligase 4
- RE31086p
- LP02352p
- Tyrosyl-DNA phosphodiesterase 1
- DNA repair protein complementing XP-C cells homolog
- Poly [ADP-ribose] polymerase
- DNA ligase
Sequence:
MSATDASTADSGAKRKSSEDITHNCNANFGAENGLRKRVKSEEPVASIKDETNPEVPMKIKAEPVENADEPTSTTPAIKIKAEPADNGNSPAAAMVKTEPTNSNAQDAADESTVSSSSIRTSCRFGIRCYRRNPAHRSAEAHPGDQDYRRPNFPAPPLGTPACPFGNACYRRNPVHFQDYSHPADFNSAQNIRNRLRQRRAQRQNDDDSGTDEEDEPFGGDNDRDADYRPGADINEDEDDELEFDSQPISGDDYD
Protein: Transient receptor potential cation channel subfamily M member 5 (A7L640)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
VFTLRLIHIFAIHKQLGPKIIIVERMMKDVFFFLFFLSVWLVAYGVTTQALLHPHDGRLEWIFRRVLYRPYLQIFGQIPLDEIDEARVNCSLHPLLLDSSASCPNLYANW
Protein: Prostatic acid phosphatase (PAP) (EC 3.1.3.2) (5'-nucleotidase) (5'-NT) (EC 3.1.3.5) (Acid phosphatase 3) (Ecto-5'-nucleotidase) (Protein tyrosine phosphatase ACP3) (EC 3.1.3.48) (Thiamine monophosphatase) (TMPase) [Cleaved into: PAPf39] (P15309)
Organism: Homo sapiens (Human)
Function: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.
Subcellular location: [Isoform 1]: Secreted {ECO:0000305|PubMed:17638863}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:20498373}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:20498373}. Cytoplasm, cytosol {ECO:0000269|PubMed:20498373}. Note=Appears to shuttle between the cell membrane and intracellular vesicles. Colocalizes with FLOT1 at cell membrane and in intracellular vesicles (PubMed:17638863). Colocalizes with LAMP2 on the lysosome membrane (PubMed:17897319). {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319}.
Interaction partners:
- Prostate-specific antigen
- Kallikrein-2
- Plasma kallikrein
- Beta-microseminoprotein
- Solute carrier family 45 member 3
- Protein-glutamine gamma-glutamyltransferase 4
- Lysosomal acid glucosylceramidase
- Anoctamin-7
- Zinc-alpha-2-glycoprotein
- Metalloreductase STEAP2
Sequence:
MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQGTEDSTD
Protein: DAZ associated protein 1 (K7EK33)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNNSGADEIGKLFVGGLDWSTTQETLRSYFSQYGEVVDCVIMKDKTTNQSRGFGFVKFKDPNCVGTVLASRPHTLDGRNIDPKPCTPRGMQPERTRPKEGWKGPRSDNSKSNKIFVGGIPHNCGETELREYFKKFGVVTEVVMIYDAEKQRPRGFGFITFEDEQSVDQAVNMHFHDIMGKKVEVKRAEPRDSKSQAPGQPGASQWGSRVVPNAANGWAGQPPPTWQQGYGPQGMWVPAGQAIGGYGPPPAGRGAPPPPPPFTSYIVSTPPGGFPPPQGFPQGYGAPPQFSFGYGPPPPPPDQFAPPGVPPPPATPGAAPLAFPPPPSQAAPDMSKPPTAQPDFPYGQYAGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSGFGRGQNHNVQGFHPYRR
Protein: Glutaminase 1 (EC 3.5.1.2) (P77454)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Inner membrane transport protein YbaT
- Glutamate decarboxylase alpha
- Glutamate decarboxylase beta
- Glutamate/gamma-aminobutyrate antiporter
- Glutamine synthetase
- Glutamate synthase large chain
- Glutaminase 2
- Bifunctional protein PutA
- 5-oxoprolinase subunit B
- Glutamate racemase
Sequence:
MLDANKLQQAVDQAYTQFHSLNGGQNADYIPFLANVPGQLAAVAIVTCDGNVYSAGDSDYRFALESISKVCTLALALEDVGPQAVQDKIGADPTGLPFNSVIALELHGGKPLSPLVNAGAIATTSLINAENVEQRWQRILHIQQQLAGEQVALSDEVNQSEQTTNFHNRAIAWLLYSAGYLYCDAMEACDVYTRQCSTLLNTIELATLGATLAAGGVNPLTHKRVLQADNVPYILAEMMMEGLYGRSGDWAYRVGLPGKSGVGGGILAVVPGVMGIAAFSPPLDEDGNSVRGQKMVASVAKQLGYNVFKG
Protein: N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) (EC 3.5.1.114) (Acylase III) (Aminoacylase III) (AAIII) (Aminoacylase-3) (ACY-3) (Aspartoacylase-2) (Hepatitis C virus core-binding protein 1) (HCBP1) (Q91XE4)
Organism: Mus musculus (Mouse)
Function: Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:14656720}; Peripheral membrane protein {ECO:0000269|PubMed:14656720}. Cytoplasm {ECO:0000269|PubMed:14656720}. Note=Predominantly localized in the apical membrane of cells in the S1 segment. In the proximal straight tubules (S2 and S3 segments) is expressed diffusely throughout the cytoplasm.
Interaction partners:
- Aminoacylase-1
Sequence:
MSSLPGSREPLLRVAVTGGTHGNEMCGVYLARYWLQNPGELQRPSFSAMPVLANPAATAACCRYLDRDLNRSCTLTFLGSTATPDDPYEVKRARELNQLLGPKGTGQAFDFTLDLHNTTANTGVCLISESNISFNLHLCHYLQRQNPGMPCRLFLYEPAGTETFSVESISKNGICLEMGPQPQGVLRADLFSRMRALVASILDFIELFNQGMDLPAFEMDIYRNLGSVDFPRTADGDLAGTVHPQLQDHDFEPLRPGEPIFKLFSGEDVLYEGDSIVYPVFINEAAYYEKHVAFLKSEKIRVTVPALLRLTPRSTQTP
Protein: Heat shock protein, putative (Q388X2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Heat shock 70 kDa protein, putative
- Lipophosphoglycan biosynthetic protein, putative
- Heat shock 70 kDa protein, mitochondrial, putative
- GrpE protein homolog
- Ankyrin repeat protein
- Heat shock protein, mitochondrial, putative
- Heat shock protein 83
- Glucose-regulated protein 78, putative
- 10 kDa heat shock protein, putative
- Hsc70-interacting protein
Sequence:
MSVFGVDFGNLNTTVAITRHGGVDIVTNEVSKRETTTIASFVDNERFIGEPGLDRYVRNSSNTIFLLKRFIGMYMDDPSLESERRFLTCAIKGDDKGRLMFGVNYCGELTYFYPEQVLAMMLQRLRGYVNLASLSDSKVTVDSRECVLTVPCYYTAEQRKLLMQACEIAGLNCLSLVNDTTAAGIDYGIFRGSSLGETEDKGQVVGILDMGYGTTVFAVACFWRGHLKLLSRTFDRHLGTRDIDYKLFEYMAEEVKKKYHVDVKENKRASLRLLQACERLRYLLSGNQVAQLNVENLMDVDVNIPSFPRSTLEELSVCLVERFKAVIKKGFEESGLSPDQFHSIEMIGGGSRIPMFKSAAEELLGRAPNFTLNASETAARGAAITAAVYSPKFKVREFVVSDIPTYPIKLGYYMENASAVSHVPFLPDINKVVSVQGTDDHYPKVLEITIKRPGGFKLYAFYDSEHPKVKAYLPRKDFVIGEWEIGTQRKDSNATEVRVRVRLLPNGLVSVESAVSVEVYEVEEPADAEEGGKGETANEEGEQPAEKKPMVKKQKQRRVELSVTPRLDVIGLTGQEIVEFQKKETEMNDRDALITKTRDSKNELESYILDNRPRIADGGILCEYVTKEQQAKFIQLANEYENWLYEDGADAELNVYQERVKTLRAIADAASDRRRNFEDVEFELPTFKQEVNKAKNTALAAIGKEAHITEEELRGAAAKCDEALAWAENEMEKYRKQHKSESPVLTCSTLREKQKEVAEAVRAVVKRPPPPKPKEATPEAKDGETAADGNVPPEVSQAGDGEKPPSDDQLD
Protein: Major prion protein (PrP) (CD antigen CD230) (P23907)
Organism: Ovis aries (Sheep)
Function: Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000250|UniProtKB:P04156}.
Interaction partners:
- Neural cell adhesion molecule 1
- Neural cell adhesion molecule 2
- Tyrosine-protein kinase.
- Caveolin
- Caveolin-1
- Amyloid-beta precursor protein
- Stress-induced-phosphoprotein 1
- Endoplasmic reticulum chaperone BIP
- Glycogen synthase kinase-3 beta
- Caveolin-2
Sequence:
MVKSHIGSWILVLFVAMWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGSHSQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDRYSNQNNFVHDCVNITVKQHTVTTTTKGENFTETDIKIMERVVEQMCITQYQRESQAYYQRGASVILFSSPPVILLISFLIFLIVG
Protein: Ras-related protein Rab-7a (B5X127)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- RILP-like protein 2
- RILP-like protein 2
- TBC1 domain family member 15
- TBC1 domain family member 15
- TBC1 domain family member 15-like
- Rab proteins geranylgeranyltransferase component A 2-like isoform X1
- FYVE and coiled-coil domain-containing protein 1
- FYVE and coiled-coil domain-containing protein 1
- Cytoplasmic dynein 1 heavy chain 1
- Dynein light intermediate chain
Sequence:
MASRKKILLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVYDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVTTKRAQAWCTSKGSIPYFETSAKEAINVDQAFQTICRNALKQESEVETYDFPDQIKLRDDRPASSSDGCSC
Protein: Histone deacetylase (EC 3.5.1.98) (A0A0G2K082)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDTKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAGNVTENEASVLPPTPHPEQLVPQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSPLSASNSLKDKQKCETQMLRQGVPLPGQYGSGIAASSSHAHVAMEGKPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMEERATSKDSGTGKDSSACVEDTLGQVGAVKVKEEPVDSDEDAQMQEMECGEQAAFMQQTPLLESSHTRALSVHQARLAAAGIDGLEKHGLLSRTHSSPAPSMSPHPAADCPRQPASATGIAYDCLMLKHQCICGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKLDPRTLLALPLVNAGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVALALEGGHDLTAICDASEACINALLGNEPGSLEEDVLHQSVNTNAAASLQKTIEIQSKYWKSIKMVAVARGCALPASQLQEETETVSALASLTVDVEQPFAQEDGRYGSNMGGQCGQ
Protein: UDP-glycosyltransferase 71A16 (EC 2.4.1.-) (UDP-glucose:chalcone 2'-O-glucosyltransferase) (UDP-glucose:flavonol 2'-O-glucosyltransferase) (D3UAG1)
Organism: Pyrus communis (Pear) (Pyrus domestica)
Function: Glycosyltransferase that possesses chalcone and flavonol 2'-O-glycosyltransferase activity. Converts phloretin to phlorizin (phloretin 2'-O-glucoside), a potent antioxidant. Possesses glycosyltransferase activity toward eriodictyol, apigenin, luteolin, kaempferol, quercetin, isoliquiritigenin, butein and caffeic acid.
Interaction partners:
Sequence:
MKRSAQLVFVPAPGIGHIVSTVEMAKQLVARDDQLFITVLVMKLPYDQPFTNTDSSISHRINFVNLPEAQLDKQDTVPNPGSFFRMFVENHKTHVRDAVINLLPESDQSESTSKPRLAGFVLDMFSASLIDVANEFEVPSYVFFTSNSSTLALLSHFQSLRDEGGIDITELTSSTAELAVPSFINPYPVAVLPGSFLDKESTKSTLNNVGRYKQTKGILVNTFLELESHALHYLDSGVKIPPVYPVGPLLNLKSSHEDKGSDILRWLDDQPPLSVVFLCFGSMGSFGDAQVKEIACTLEHSGHRFLWSLRQPPSKGKRALPSDYADLKTVLPEGFLDRTATVGRVIGWAPQAAILGHPAIGGFVSHCGWNSTLESIWNGVPIAAWPMYAEQNMNAFQLVVELGLAVEIKMDYRKDSDVVVSAEDIERGIRQVMELDSDVRKRVKEMSEKSKKALVDGGSSYSSLGRFIDQI
Protein: Thioredoxin 2 (Trx-2) (EC 1.8.1.8) (Protein-disulfide reductase) (P0AGG4)
Organism: Escherichia coli (strain K12)
Function: Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin.
Subcellular location: Cytoplasm.
Interaction partners:
- Thioredoxin reductase
- Glutaredoxin 1
- Glutathione reductase
- Catalase-peroxidase
- DNA-binding transcriptional dual regulator OxyR
- Glutaredoxin 3
- Alkyl hydroperoxide reductase C
- Alkyl hydroperoxide reductase subunit F
Sequence:
MNTVCTHCQAINRIPDDRIEDAAKCGRCGHDLFDGEVINATGETLDKLLKDDLPVVIDFWAPWCGPCRNFAPIFEDVAQERSGKVRFVKVNTEAERELSSRFGIRSIPTIMIFKNGQVVDMLNGAVPKAPFDSWLNESL
Protein: Uncharacterized protein C630.04c (Q9UUH8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MGEEISAIDLVMANDQLVSTSDASDIPYDPYSQFWGKVLVLTFGIICVVFVIFMLHHERIKACRTIISAREQQRTQHSIHRRERSSSGASQQFEHHVRQTDCLPLYEPITALNQQYLKTLPTTSTPPPPAIFDENGEFVGDVPSVAGAIERPPSYESLPAPQNDEV
Protein: Indole-3-acetaldehyde oxidase (IAA oxidase) (EC 1.2.3.7) (Aldehyde oxidase 1) (AO-1) (AtAO-1) (AtAO1) (Q7G193)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. AO-alpha may be involved in the biosynthesis of auxin, and in biosynthesis of abscisic acid (ABA) in seeds. In vitro, AO-alpha uses heptaldehyde, protocatechualdehyde, benzaldehyde, indole-3-aldehyde (IAld), indole-3-acetaldehyde (IAAld), cinnamaldehyde and citral as substrates; AO-beta uses IAAld, IAld and naphtaldehyde as substrates.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Nitrilase 1
- Amidase 1
- Nitrilase 3
- Nitrilase 2
- Aldehyde dehydrogenase family 7 member B4
- Aldehyde dehydrogenase family 3 member H1
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
- Aldehyde dehydrogenase family 3 member F1
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
Sequence:
MGEKAIDEDKVEAMKSSKTSLVFAINGQRFELELSSIDPSTTLVDFLRNKTPFKSVKLGCGEGGCGACVVLLSKYDPLLEKVDEFTISSCLTLLCSIDGCSITTSDGLGNSRVGFHAVHERIAGFHATQCGFCTPGMSVSMFSALLNADKSHPPPRSGFSNLTAVEAEKAVSGNLCRCTGYRPLVDACKSFAADVDIEDLGFNAFCKKGENRDEVLRRLPCYDHTSSHVCTFPEFLKKEIKNDMSLHSRKYRWSSPVSVSELQGLLEVENGLSVKLVAGNTSTGYYKEEKERKYERFIDIRKIPEFTMVRSDEKGVELGACVTISKAIEVLREEKNVSVLAKIATHMEKIANRFVRNTGTIGGNIMMAQRKQFPSDLATILVAAQATVKIMTSSSSQEQFTLEEFLQQPPLDAKSLLLSLEIPSWHSAKKNGSSEDSILLFETYRAAPRPLGNALAFLNAAFSAEVTEALDGIVVNDCQLVFGAYGTKHAHRAKKVEEFLTGKVISDEVLMEAISLLKDEIVPDKGTSNPGYRSSLAVTFLFEFFGSLTKKNAKTTNGWLNGGCKEIGFDQNVESLKPEAMLSSAQQIVENQEHSPVGKGITKAGACLQASGEAVYVDDIPAPENCLYGAFIYSTMPLARIKGIRFKQNRVPEGVLGIITYKDIPKGGQNIGTNGFFTSDLLFAEEVTHCAGQIIAFLVADSQKHADIAANLVVIDYDTKDLKPPILSLEEAVENFSLFEVPPPLRGYPVGDITKGMDEAEHKILGSKISFGSQYFFYMETQTALAVPDEDNCMVVYSSTQTPEFVHQTIAGCLGVPENNVRVITRRVGGGFGGKAVKSMPVAAACALAASKMQRPVRTYVNRKTDMITTGGRHPMKVTYSVGFKSNGKITALDVEVLLDAGLTEDISPLMPKGIQGALMKYDWGALSFNVKVCKTNTVSRTALRAPGDVQGSYIGEAIIEKVASYLSVDVDEIRKVNLHTYESLRLFHSAKAGEFSEYTLPLLWDRIDEFSGFNKRRKVVEEFNASNKWRKRGISRVPAVYAVNMRSTPGRVSVLGDGSIVVEVQGIEIGQGLWTKVKQMAAYSLGLIQCGTTSDELLKKIRVIQSDTLSMVQGSMTAGSTTSEASSEAVRICCDGLVERLLPVKTALVEQTGGPVTWDSLISQAYQQSINMSVSSKYMPDSTGEYLNYGIAASEVEVNVLTGETTILRTDIIYDCGKSLNPAVDLGQIEGAFVQGLGFFMLEEFLMNSDGLVVTDSTWTYKIPTVDTIPRQFNVEILNSGQHKNRVLSSKASGEPPLLLAASVHCAVRAAVKEARKQILSWNSNKQGTDMYFELPVPATMPIVKEFCGLDVVEKYLEWKIQQRKNV
Protein: CST complex subunit STN1 (Suppressor of cdc thirteen homolog) (Q8II42)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Replication factor A protein 3, putative
Sequence:
MDMNFGFCDDNFFEQGHKSTDKEEIEELTKRGSPEGLAKIKENEEEKALPKELCVPVTIKLLINKMMNTEELKIHDFQISGIIVFGKVVSIKELASAIIFEICDYTGNIEAKYNKDAKNEKVKNHIESIKVNDYIKIVGVVYSPESKSESIQISILYINKVTDWVSYFTYFTSDVVYCYLKLLKLKNICTPNGINNEEKPWSHINLDTYYNHLDDIDSDIIKYLHTTEEKYASQQDIFNNLQKYHSEFNIKKSLTKLIEQYDLAQYEDIISIP
Protein: Cold shock domain-containing protein C2 (RNA-binding protein PIPPin) (Q63430)
Organism: Rattus norvegicus (Rat)
Function: RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain.
Subcellular location: Nucleus. Cytoplasm. Note=PIPPin-RNA complexes are located to the nucleus.
Interaction partners:
Sequence:
MTSESTSPPVVPPLHSPKSPVWPTFPFHRESSRIWERGGGVSPRDLPSPLPTKRTRTYSATARASAGPVFKGVCKQFSRSQGHGFITPENGSEDIFVHVSDIEGEYVPVEGDEVTYKMCPIPPKNQKFQAVEVVLTQLAPHTPHETWSGQVVGS
Protein: glycerol kinase (EC 2.7.1.30) (Q8C635)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
- Glycerol kinase 2
- Monoglyceride lipase
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol-3-phosphate acyltransferase 3
- Aldo-keto reductase family 1 member B1
- Aldose reductase-related protein 2
- Aldo-keto reductase family 1 member B7
- Aldo-keto reductase family 1 member A1
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- aldose reductase
Sequence:
MAEAPKAVLGPLVGAVDQGTSSTRFLVFNPQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGQQSIDISNIKAIGVTNQRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIEDGRAIFGTVDSWLIWCMTGGINGGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSGVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGRQEPVYYALEGSVAIAGAVVSWIKNNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGVSVWSLDPKDLSSVQMEKFEPQINVEESEGRYATWKKAVLKSMGWVLTQSPDGRDPSIFSSLTLGFYVVSSMVILIGARYM
Protein: Transmembrane 9 superfamily protein C1105.08 (Q9Y819)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- L-type lectin-like domain-containing protein C4F6.05c
Sequence:
MLLPSIPSCSFSFVVFVSVLLQTCFSFQLTPLSPKNYPPGASIDTTVNTISPFIGDGRGSDIFNYEYYDERFHFCRPENIAKQSESLGSVLFGDRLYNSPIEIKMLENQDCVPLCASIIPSSDVSFIRDLISKNYVVNWNIDNLPVATYLEGTNSKNYSLSPGFPLGKNTEKGVILFNHYDIVIEYHTTSSDQHRVVGAYVKPVSKESTLVDGNPVCSSSSNPQYLPEGADLTLVTSYSVSWKYSDTPWATRWDKYMHIESRQIRWIFIIHSAIIDTFLIFVVSIILYRTLNRDINKYNSAFVDQEDVQEDFGWKLVHGDVFRPPRRPMLFSILLGTGAQLLFMSSGIVLFAIFGIVAPSRRGSLATATVALFIISGFVSGYVSALSYKLMQGMLRKRNLLLTPFVVPGFMLAAALFFNMVFWSKSSSSTVPFSSWLLLIFLYLLFTVPLSFVGSLIGFRSREFVPPVRTNQIPRQIPSHSIWLSSFPSAIIGGSIPFLVILIELFSILDSLWFHPLYFMFGFSFFCFGILVTTCIMVSIITVYFQLCSENYNWWWRSFITPGFCGIYVFIFSVFYWFFKISSSSLATAVLYFGYSLLISVLVFFLCGSVGFFGAFLFVNKIYASIKID
Protein: Ubiquitin carboxyl-terminal hydrolase 13 (EC 3.4.19.12) (Deubiquitinating enzyme 13) (Ubiquitin thioesterase 13) (Ubiquitin-specific-processing protease 13) (P38187)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- DUB-associated factor 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin
Sequence:
MIRRWLTISKSGKKKKAVNDTITEEVEKVDFKPVNHDINDELCYSESSDNPSSSLFVSNLDTKETFLNEDNNLQISSGLDYSSETCNQGSNYSQDGIFYISNAKAINAYGGIITQGPEAPILAMKVSDSMPYGDGSNKVFGYENFGNTCYCNSVLQCLYNLSSLRENILQFPKKSRESDQPRKKEMRGKKPRIFTEASFEKSIAGTNGHLPNPKPQSVDDGKPTPVNSVNSNTAGPSEKKSKFFKSFSAKHVQDNNKKEGSPAILTTGKPSSRPQDAPPLIVETPNEPGAPSRLSFENVTDRPPDVPRKIIVGRVLNYENPSRGSSNSNNLDLKGESNSSLSTPLDKKDTRRSSSSSQISPEHRKKSALIRGPVLNIDHSLNGSDKATLYSSLRDIFECITENTYLTGVVSPSSFVDVLKRENVLFNTTMHQDAHEFFNFLLNELSEYIERENKKIAASDINSDSEPSKSKNFISDLFQGTLTNQIKCLTCDNITSRDEPFLDFPIEVQGDEETDIQEILKSYHQREMLNGSNKFYCDECCGLQEAERLVGLKQLPDTLTLHLKRFKYSEKQNCNIKLFNNIHYPLTLNVCSSINSKVCQKYELAGIVVHMGGGPQHGHYVSLCKHEKFGWLLFDDETVEAVKEETVLEFTGESPNMATAYVLFYKAMYSNAVEKNDRENMAKEQDDNIDNLIKYDDWLRTCNSGQKKKEELPIADDLDTAIDDSFVSNTPIKSSKKKSRMFSFRKS