wanglab/gogpt-training-data huggingface dataset:
Protein: Topoisomerase I damage affected protein 2 (P40045)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Cell projection {ECO:0000269|PubMed:19053807}. Note=Concentrates at cytoplasmic punctate structures and localizes at the mating projection tip. {ECO:0000269|PubMed:19053807}.
Interaction partners:
- Altered inheritance of mitochondria protein 21
- F-actin-capping protein subunit alpha
- F-actin-capping protein subunit beta
Sequence:
MSMQIEIKDGRSDNSPLPERKLVTLIQESYDSLKDDNEINLSTESTSNLLIKLVLEKLEKHSSLYKYIASVTTLNIEGLNEENANFSLKNDIGASWESKKDGIFNYKLEDKNNNECYLITILWLHK
Protein: Mediator of RNA polymerase II transcription subunit 27 (Mediator complex subunit 27) (dCRSP34) (dMED27) (dTRAP37) (Q9VNG0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for activated transcription of the MtnA gene.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 31
Sequence:
MDKLNSTLTAVKNLRSNVRLCFEHLADGTDGESGEESRNKFVNDFQERFAAINSQIREVEQLINGLPVPPTPYSLGNTAYLAQETSQDRQALYPQLVNSYKWMDKVHDHSFLAFNNLNQNTLRRSYNYCSQKRQRLPFSSFNNDPDHIDKLLSEINTPPHTSYRIFRPFGTNAVTIVTISNVMKAAIVFKGVLIEWVTVKGFDEPLEHDDLWAESRYEVFRKVQDHAHSAMLHFFSPTLPDLAVKSYITWLNSHVKLFLEPCKRCGKFVVNGLPPTWRDLRTLEPFHEDCRNC
Protein: Peroxygenase (EC 1.11.2.3) (Caleosin) (A0A1I9R3Y5)
Organism: Pinus elliottii (Slash pine)
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:27889638}. Microsome membrane {ECO:0000250|UniProtKB:Q9SQ57}.
Interaction partners:
Sequence:
MASNESLQTTAAMAPVTIERRVNPNLDDELPKPFLPRALVAVDTEHPSGTPGHQHGDMSVLQQHVAFFDRNNDGIVYPWETFLGLRAVGFNIIISFFGCLIINISLSYATLPGWIPSPFFPIYIDRIHRAKHGSDSEVYDTEGRFVPSKFEEIFTKNARTHPDKLSFSELWNLTEHNRNALDPLGWVAAKLEWFLLYLLAKDPHGFVPKEAARGVFDGSLFEFCEKSRRSNKQQ
Protein: Nuclear autoantigenic sperm protein (E9PI86)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAMESTATAAVAAELVSADKIEDVPAPSTSADKVESLDVDSEAKKLLGLGQKHLVMGDIPAAVNAFQEAASLLGKKYGETANECGEAFFFYGKSLLELARMENGVLGNALEGVHVEEEEGEKTEDESLVENNDNIDETEGSEEDDKENDKTEEMPNDSVLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYG
Protein: AcetylCholine Receptor (G5EDF1)
Organism: Caenorhabditis elegans
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- Acetylcholine receptor subunit beta-type acr-3
- Acetylcholine receptor subunit alpha-type unc-38
- CUB domain-containing protein
- Acetylcholine receptor subunit alpha-type unc-63
- Acetylcholine receptor subunit beta-type acr-2
- Protein unc-50
- Resistance to inhibitors of cholinesterase protein 3
Sequence:
MLYKKRLQMFSFNWALILLVAVGGTNAFKIKRTAKDLESQLYEDLLFDYNKVPRPVKNSSDILTVDVGASLIRIIDVDEKNQVLTTNLWLEMKWNDAKLTWTPEKYGGLKTLHIPSDFIWTPDLVLYNNAAGDPDITILTDALVTFEGNVYWQPPAIYKSFCPIDVTWFPYDSQKCEMKFGTWTYTGRYVDLKQLPQEEVVTITKDDNDVEFMQQGMDLSFFYRSAEWDLLSLTSERHSVLYASCCGPEKYVDITYYFGLRRKTLFFTCNLILPCFLISILTTFVFYLSDHKITFSISILVTLTVFFLVLIDLMPPTSLVIPMFGRYLITTMILVALSTVVSVITVNFRFRSGSAHKMSPWIRAVFLKFLPKILLMSRPEKGEVTKQPPLVNAASLVGSNYATAAKAANEYRNKAKGKNNDLMSLRGKPSSQAVLNNTFDMRMRNNDSTVENRLKPYLCAQNNNAPTVAFRKTKRQKSKSVDDVVFMNLLNQVRFIAEHFRHNELEGEISDDWTFVAMVLDRLFLIIFSVLNVGTVFIILESPSLYDYSKPMNITVPNKPLGQANFYSSWNLK
Protein: COP9 signalosome complex subunit 4 (AtS4) (Signalosome subunit 4) (Constitutive photomorphogenesis protein 8) (Protein FUSCA 4) (Q8L5U0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of IAA6 by regulating the activity of the Ubl ligase SCF-TIR complex.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 6a
- COP9 signalosome complex subunit 6b
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 5a
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 5b
- COP9 signalosome complex-related / CSN complex-like protein
Sequence:
MDEALTNASAIGDQRQKIEQYKLILSSVLSSNDLLQAQRFIDHILSDDVPLVVSRQLLQSFAQELGRLEPETQKEIAQFTLTQIQPRVVSFEEQALVIREKLAGLYESEQEWSKAAQMLSGIDLDSGMRAVDDNFKLSKCIQIARLYLEDDDAVNAEAFINKASFLVSNSQNEVLNLQYKVCYARILDMKRKFLEAALRYYGISQIEQRQIGDEEIDENALEQALSAAVTCTILAGAGPQRSRVLATLYKDERCSKLKIYPILQKVYLERILRRPEIDAFSEELRPHQKASLPDKSTVLDRAMIEHNLLSASKLYTNIRFDELGTLLAIDPRKAEKIAANMIGQDRMRGSIDQEEAVIHFEDDVEELQQWDQQISGLCQALNDILDGMAKKGMSVPV
Protein: mRNA-decapping enzyme subunit 1 (Q9P805)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- mRNA decapping complex subunit 2
- Uncharacterized protein C18G6.09c
- Putative ATP-dependent RNA helicase ste13
- Enhancer of mRNA-decapping protein 3
- LSM1-LSM7 complex subunit lsm1
- 5'-3' exoribonuclease 1
- Deadenylation-dependent mRNA-decapping factor pdc2
- Probable tubulin--tyrosine ligase C12B10.04
- NAD
- ATP-dependent helicase upf1
Sequence:
MEDENILRNAVNLQVLKFHYPEIESIIDIASHVAVYQFDVGSQKWLKTSIEGTFFLVKDQRARVGYVILNRNSPENLYLFINHPSNVHLVDRYLIHRTENQHVVGLWMFDPNDMSRIFNIVKESLLR
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (P07632)
Organism: Rattus norvegicus (Rat)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
- Superoxide dismutase, mitochondrial
- Apoptosis regulator Bcl-2
- Non-selective voltage-gated ion channel VDAC1
- Copper chaperone for superoxide dismutase
- Parkinson disease protein 7 homolog
- RCG31562, isoform CRA_c.
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Endoplasmic reticulum chaperone BiP
- Neurofilament light polypeptide
- Derlin
Sequence:
MAMKAVCVLKGDGPVQGVIHFEQKASGEPVVVSGQITGLTEGEHGFHVHQYGDNTQGCTTAGPHFNPHSKKHGGPADEERHVGDLGNVAAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Protein: Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64) (P01108)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release. Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}. Note=Localization to the nucleolus is dependent on HEATR1. {ECO:0000250|UniProtKB:P01106}.
Interaction partners:
- Protein max
- Myc box-dependent-interacting protein 1
- Breast cancer type 1 susceptibility protein homolog
- Transformation/transcription domain-associated protein
- Zinc finger and BTB domain-containing protein 17
- Glycogen synthase kinase-3 beta
- Transcription factor E2F1
- F-box/WD repeat-containing protein 7
- Histone acetyltransferase KAT2A
- Cellular tumor antigen p53
Sequence:
MDFLWALETPQTATTMPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQADEHKLTSEKDLLRKRREQLKHKLEQLRNSGA
Protein: Evasin P983 (A0A023FFB5)
Organism: Amblyomma cajennense (Cayenne tick) (Acarus cajennensis)
Function: Salivary chemokine-binding protein which binds to host chemokines CCL2, CCL3 and CCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKASFCVIASCLVVFALKGTAEDTGTEDDFDYGNTGCPFPVLGNYKSNMTKPVGCKNKCGSGYEVLNDTTPCYVIDQKVFNNMVPLRQYSKCPLGFCENGECKPNDQAEDCYKGREEQK
Protein: Nucleoprotein (Nucleocapsid protein) (NP) (Protein N) (P14155)
Organism: Sendai virus (strain Harris) (SeV)
Function: Encapsidates the genome in a ratio of one N per six ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure with 13.07 N per turn. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Replication is dependent on intracellular concentration of newly synthesized N, termed N(0), which corresponds to the protein not associated with RNA. In contrast, when associated with RNA, it is termed N. During replication, encapsidation by N(0) is coupled to RNA synthesis and all replicative products are resistant to nucleases.
Subcellular location: Virion {ECO:0000305}. Host cytoplasm.
Interaction partners:
Sequence:
MAGLLSTFDTFSSRRSESINKSGGGAVIPGQKSTVSVFVLGPSVTDDADKLFIATTFLAHSLNTDKQHSQRGGFLVSLLAMAYSSPELYLTTNGVNADVKYVIYNIEKDPKRTKTDRFIVKTRDMEYERTTEWLFGPMVNKSPLFQGQRDAADPDTLLQTYGYPACLGA
Protein: Xylose reductase (W5RZ21)
Organism: Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Interaction partners:
Sequence:
MTADYVVLNRTGDKMPLRGFGCWKIEKDVCADVIYKAIKVGYRHFDGACDYGNEVEVGRGIKKAIDEGIVKREDLFIVTKLWNTFHNKKNVRPACERQLKDWGLDYFDLYLVHFPIPLAYVDPSQNYPPEWFKGNSTAIEIESSPMHECWAEMERLVNDGLSRNIGVCNFNTQALIDMLTYAKIKPAVLQIELHPYLPQAELTKWVKSQGIHITAYSSFGPASYVTLGEHGKRAAPLLEHDAVKSLADKHKVSAGQILLRWALDREYVVIPKSVNENRMKANFDVLDIKLDESDNKALDALKSNQRFNDPLVWFDLPLFA
Protein: Syntaxin binding protein 1 (A0A2R8Y5D4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIAPVIKLSAPCLHMYCMNVVLLTFLLPPNFSWT
Protein: Translation initiation factor, putative (Q57Z81)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Translation initiation factor, putative
- protein-synthesizing GTPase
- Glucose-1-phosphate adenylyltransferase/Bifunctional protein GlmU-like C-terminal hexapeptide domain-containing protein
- Translation initiation factor eIF-2B alpha subunit, putative
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor 5, putative
- Eukaryotic translation initiation factor 1A, putative
- Eukaryotic translation initiation factor 3 subunit I
- Translation initiation factor eIF2B subunit gamma
- Elongation initiation factor 2 alpha subunit, putative
Sequence:
MAEQPEVSKELRLGGRSRGANAAGDNRRSKAPRASEAVPYEEATTLKDPFVTSSVSGPTTTTTNPPPPVAPSPVVAEDIFAIAYDTYSAADLHALLQQVTRSEVERRMAEFDQQRRKTNHAPRVERFLDVTGSSSSNNNNSNGTGSEVCTGYTYNDMLQRIFIALNRNKESSGMSERNQLPVPQVEKISKKKVVIVNFRRICEVFSRPIEDVKDYIEKELSVGGNLDSNDSLILKYEIQKVTDFDKILIKYLDEYVKCNSCHKIDTTLTKEGRRMELRCNWCTATRSVQAVGSATYSAQVGKRSRARRQAMTL
Protein: Protein lin-8 (Abnormal cell lineage protein 8) (G5EDW7)
Organism: Caenorhabditis elegans
Function: Acts as a synthetic multivulva class A (synMuvA) protein and redundantly inhibits lin-3/EGF expression to prevent inappropriate vulva induction.
Subcellular location: Nucleus {ECO:0000269|PubMed:16020796}.
Interaction partners:
- Protein lin-56
- Protein lin-15A
- Protein lin-9
- C2H2-type domain-containing protein
- Retinoblastoma-like protein homolog lin-35
Sequence:
MSKIKTHSTGSKRTVPFYKLPPPVPLPPLPPPDPTRYFSTEKYIALSKDEKFKFDDYDVNDETLKKVVLNEIGKCPDIWSSRSQAAIMEHYPIVATETYRRTGLLLSIKSLKQIYKCGKDNLRNRLRVAIVSKRLTPAQVEAYMWRWEFYGFIRYYRDYTQRWEADLLKDLDVVLGLEARRASKNMEKVDSGELMEPMEPMDSTMDEMCVEEEPYEETGSNWSDPAPEPSQSKSQSPEAKYPQAYLLPEADEVYNPDDFYQEEHESASNAMYRIAFSQQYGGGGSPAVQKPVTFSAQPAPAPVREAPSPVVENVSSSSFTPKPPAMINNFGEEMNQITYQAIRIAREQPERLKLLRKALFDVVLAFDQKEYADVGDLYRDLAQKNS
Protein: Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20) (Tyrosylprotein sulfotransferase 2) (TPST-2) (O60704)
Organism: Homo sapiens (Human)
Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:25660941}; Single-pass type II membrane protein {ECO:0000269|PubMed:25660941}.
Interaction partners:
- Coagulation factor VIII
- Podocalyxin-like protein 2
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
Sequence:
MRLSVRRVLLAAGCALVLVLAVQLGQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQLVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPGDVVRDMAQIAPMLAQLGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLKGYFQVNQNSTSSHLGSS
Protein: ribonucleoside-diphosphate reductase (EC 1.17.4.1) (P88997)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Interaction partners:
Sequence:
MDFVKEFLYVSDHAGFLELTTETWKNMWFPSQIPLSSDVAGIAQLNETDREFYKFLFVFLGLAERLVNFNIEDLVKEFNCHDATHYYAEQMAMENIHGKVYANILQLFFNGDMMKLKEYAVKVVADPTLKAKLDWLHTRVKNTKTRAEKVLIFLLIEGIFFISSFYSISLFRVRGMLNGICLANDYISKDELLHTRAAAVLYNSLIPAKERPDAAWIKRLFQEAVEVEYSFIAAKSKNVTLVVPGEIKKFLQATCDRILQSIGVEPIYGSHAPVTCPLSYNGCIKSVNFFEREGTDYSTKVTNDL
Protein: Cruzioseptin-7 (CZS-7) (A0A193H365)
Organism: Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer)
Function: Has antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:27321580}.
Interaction partners:
Sequence:
MAKLKKSLFLVLFLGLVSLSICEEEKREEENEEVQEDDDQSEEKRGFLDVVKHVGKAVGKAALNAVTEMVNQAEQ
Protein: RNA polymerase I-specific transcription initiation factor RRN3 (B2RS91)
Organism: Mus musculus (Mouse)
Function: Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12015311}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA polymerase iota
Sequence:
MAAPLLHTRLSGDVTAAASATLSASRTGLSDMLALESDFFNSPPKKTVRFGGTVTEVLLKYKKGETNDLELLKNQLSDPDIKDDQIINWLLEFRSSVMYLTKDFEQLINIILRLPWLNRSQRVVEEYLAFLGNLVSAQTVFLRPCLSMIASHFVPPRVIVKEGGIDVSDSDDEDDNLPAIFDTCHRALQIITRYVPSTPWFLMPILVEKFPFVRKSERTLECYVHNLLRISLYFPTLRREILELVIEKLLKLDVSVSRQDIEDAEEKAAQTCGGTDTTEGLFNMDEDEDTDPEKKADQEQPNQMAHPTAERLDVLLCLLLSYIEDVCRVHGKIDNNKTKDLYRDLISIFDKLLLPTHASCHVQFFMFFLCSFKLGFAEAFLEHLWKKLQDPNNPAIIRQAAANYIGSFLARAKFIPLITVKTCLDLLVNWLHMYLTNQDSGTKAFCDVALHGPFYSACQAVFYTVVFRHKQLLSGNLKQGLQYLQSLNFERIVLSQLNPLKICLPQVVNFFAAITNKYQLVFCYTIMERNSRQMLPVIRSTAGGDSVQTCTNPLDTFFPFDPCVLKRSKKFIDPIYQIWEDGSAEELQEFKKSTKKEVVEDEDDDFLKGEVPQSDTVTGLTPSSFDTHFQSPSSSVGSPPVLYIPGQSPLLTRIYD
Protein: Ribose-phosphate pyrophosphokinase 3 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase 3) (P38689)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (PRS2, PRS3, PRS4 and PRS5).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 5
- Ribose-phosphate pyrophosphokinase 4
- Orotate phosphoribosyltransferase 2
- Amidophosphoribosyltransferase
- ADP-ribose pyrophosphatase
- Transketolase 1
- Orotate phosphoribosyltransferase 1
- Ribose-5-phosphate isomerase
- Transketolase 2
Sequence:
MPTNSIKLLAPDVHRGLAELVAKRLGLQLTSSKLKRDPTGEVSFSIGESVRDQDIFIITQIGSGVVNDRVLELLIMINASKTASARRITAIIPNFPYARQDRKDKSRAPITAKLMADMLTTAGCDHVITMDLHASQIQGFFDVPVDNLYAEPSVVRYIKENVNYMDSIIISPDAGGAKRAATLADRLDLNFALIHKERARANEVSRMVLVGDVTDKICIIVDDMADTCGTLAKAAEILLENRAKSVIAIVTHGVLSGRAIENINNSKLDRVVCTNTVPFEEKIKKCPKLAVIDISSVLAESIRRLHNGESISYLFKNYPL
Protein: Peptide YY-A (Peptide YY) (Peptide YYa) (Q9I8P2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted.
Interaction partners:
- Neuropeptide Y receptor type 2
- Neuropeptide Y receptor Y2
- Neuropeptide Y /peptide YY receptor Yb
- Neuropeptide Y receptor type 2
- Neuropeptide Y receptor Y4
- Neuropeptide Y receptor type 1
- Neuropeptide Y receptor Y8a
- Pro-neuropeptide Y
- Appetite-regulating hormone isoform X1
- Si:dkey-27p18.2
Sequence:
MAVMLKPWTVVATVLICVLLCLGTFVDAYPPKPENPGDDAAPEELAKYYTALRHYINLITRQRYGKRSTSEDVMAELLFGDDTEHKQRSRYDDSFMW
Protein: Cocaine- and amphetamine-regulated transcript protein [Cleaved into: CART(1-39); CART(42-89)] (Q16568)
Organism: Homo sapiens (Human)
Function: Satiety factor closely associated with the actions of leptin and neuropeptide Y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. It promotes neuronal development and survival in vitro.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Enoyl-CoA delta isomerase 2
- Hydroxysteroid dehydrogenase-like protein 2
- Pro-neuropeptide Y
- Agouti-related protein
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Pro-opiomelanocortin
- Lambda-crystallin homolog
- Metastasis-suppressor KiSS-1
Sequence:
MESSRVRLLPLLGAALLLMLPLLGTRAQEDAELQPRALDIYSAVDDASHEKELIEALQEVLKKLKSKRVPIYEKKYGQVPMCDAGEQCAVRKGARIGKLCDCPRGTSCNSFLLKCL
Protein: Cell wall protein ECM33 (Extracellular mutant protein 33) (P38248)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall. Important for apical bud growth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10383953, ECO:0000269|PubMed:12583915, ECO:0000269|PubMed:18434410}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10383953}. Secreted, cell wall {ECO:0000269|PubMed:12583915, ECO:0000269|PubMed:15781460}. Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. {ECO:0000269|PubMed:12583915, ECO:0000269|PubMed:15781460}.
Interaction partners:
- 1,3-beta-glucanosyltransferase GAS1
- GPI ethanolamine phosphate transferase 2
- 1,3-beta-glucanosyltransferase GAS5
- Probable circularly permuted 1,3-beta-glucanase TOS1
Sequence:
MQFKNALTATAILSASALAANSTTSIPSSCSIGTSATATAQADLDKISGCSTIVGNLTITGDLGSAALASIQEIDGSLTIFNSSSLSSFSADSIKKITGDLNMQELIILTSASFGSLQEVDSINMVTLPAISTFSTDLQNANNIIVSDTTLESVEGFSTLKKVNVFNINNNRYLNSFQSSLESVSDSLQFSSNGDNTTLAFDNLVWANNITLRDVNSISFGSLQTVNASLGFINNTLPSLNLTQLSKVGQSLSIVSNDELSKAAFSNLTTVGGGFIIANNTQLKVIDGFNKVQTVGGAIEVTGNFSTLDLSSLKSVRGGANFDSSSSNFSCNALKKLQSNGAIQGDSFVCKNGATSTSVKLSSTSTESSKSSATSSASSSGDASNAQANVSASASSSSSSSKKSKGAAPELVPATSFMGVVAAVGVALL
Protein: Tricarboxylate transport protein (Citrate transport protein) (CTP) (P38152)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transport of citrate across inner mitochondrial membrane.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- Sec sixty-one protein homolog
Sequence:
MSSKATKSDVDPLHSFLAGSLAGAAEACITYPFEFAKTRLQLIDKASKASRNPLVLIYKTAKTQGIGSIYVGCPAFIIGNTAKAGIRFLGFDTIKDMLRDSETGELSGTRGVIAGLGAGLLESVAAVTPFEAIKTALIDDKQSATPKYHNNGRGVVRNYSSLVRDKGFSGLYRGVLPVSMRQAANQAVRLGCYNKIKTLIQDYTDSPKDKPLSSGLTFLVGAFSGIVTVYSTMPLDTVKTRMQSLDSTKYSSTMNCFATIFKEEGLKTFWKGATPRLGRLVLSGGIVFTIYEKVLVMLA
Protein: AT-rich interactive domain-containing protein 3C (ARID domain-containing protein 3C) (A6PWV5)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:A6NKF2}. Note=Interaction with NPM1 mediates ARID3C nuclear shuttling. {ECO:0000250|UniProtKB:A6NKF2}.
Interaction partners:
Sequence:
MEALQRQQAARLAQGVGPLAPPRLPLPQPPLLGARTLQAPEGAIGVVGAEEEEGAEDEEGETPLAEEETAEQSHPGARCPNSPSSQSPGIQPHEWTYEEQFKQLYELDADPKRKEFLDDLFSFMQKRGTPVNRVPIMAKQVLDLYALFRLVTAKGGLVEVINRKVWREVTRGLSLPTTITSAAFTLRTQYMKYLYPYECETRALSSPGELQAAIDSNRREGRRQAYTAVPLFNLAGPTPRGAPGPASSHGPAPTATPNCPGPTQGSASGLPAHACAQLSPSPVKKEESGIPPPRLALPMGLASEATREKLAPEEPPEKRAVLMGPVDSPRLGAPPSFLPRGKAPLREERLDGPLNLAGSGISSINVALEINGVVYTGILFARRQPVPASLGPTNPPPLPSTGPPSSTLP