wanglab/gogpt-training-data huggingface dataset:
Protein: Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Cyclophilin-related protein) (Rotamase D) (Q08752)
Organism: Homo sapiens (Human)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}. Nucleus, nucleolus {ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Non-selective voltage-gated ion channel VDAC1
- Heat shock 70 kDa protein 4
- Prostaglandin E synthase 3
- Stress-induced-phosphoprotein 1
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Activator of 90 kDa heat shock protein ATPase homolog 1
Sequence:
MSHPSPQAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGHTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKLCVIAECGELKEGDDGGIFPKDGSGDSHPDFPEDADIDLKDVDKILLITEDLKNIGNTFFKSQNWEMAIKKYAEVLRYVDSSKAVIETADRAKLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKAQKDKEKAVYAKMFA
Protein: Protein LATE ELONGATED HYPOCOTYL (PhLHY) (A0A0G3VTN5)
Organism: Petunia hybrida (Petunia)
Function: Transcription repressor involved in the circadian clock. Binds to the promoter region of target genes to repress their transcription (e.g. PRR5 and GI). Regulates the timing of floral scent, by restricting the expression of ODO1 and other floral volatile benzenoids and phenylpropanoids (FVBP) pathway genes (e.g. EPSPS and IGS1) to the evening. This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta). Binds to and repress ODO1 and FVBP genes (e.g. EPSPS and IGS1) promoters via cis-regulatory evening elements.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
Sequence:
MDPYSSGEELVVKTRKPYTITKQRERWTEEEHNRFLEALKLYGRAWQRIEEHIGTKTAVQIRSHAQKFFTKLEKEALIKGVPISEALDIEIPPPRPKRKPSNPYPRKTSIAVPTSQVGTKDGKLSTPFPSICENRNLLDLEKEPIIESVGGNEKLSNVQENQNKKNFSQGFTLFKEGASAASVSLGKSSQTLAEPTDSCTLNESVSVSKGVINHDVANKSFPAVESKGHQQLDILDAKQSFQFDSSCNTSSVGKSCQSNEKWAQGEQKDQPSQPDHFEEFSRNDMQVPHNYPRHVPVHILDGTLGANGAQTTPDMFYHKSVSHQVGGLQGLSDMYTNPASSATSEQHSNAARSSIHQSFPCFHPIFTPIRDPDDYRSFLQLSSTFSSLVVSALLQNPAAHAAASFAASFWPYANMEAPVDSTGNNTASQINSAPSMAAIAAATVAAATAWWAAHGLLPLCSPFHSSLTCVPTSATSMQVDVCQPKEGKSEGREGTHNSPPHVQQPGPECSEALQEQHSASKLPTSPSSDSGESEGRNLKNGLTATDTEQGAAVTETHEPNAEKVRKQVDRSSCGSNTPSSSEVETDALEKDEKGKEEPEEPNVNLLAGDAANRRGRNCISNSNDSWKEVSEEGRMAFQALFSREVLPQSFSRSNYLKTKGNIDFEKFQQKPDEQGPSGSQLDLNDQASNICSSHQAVEENVQFLLGNKEGAEKCQPTMELGEIRLKARRTGFKPYKRCSLEAKDSRVANSSCQDEEKSCKRLRLEGEAST
Protein: LDL receptor repeat-containing protein egg-1 (E3LYX0)
Organism: Caenorhabditis remanei (Caenorhabditis vulgaris)
Function: Probable receptor which is required for the oocyte-to-zygote transition although its exact function is controversial (By similarity). Seems to be required for fertilization probably by promoting the interaction or fusion between sperm and oocyte. Conversely, shown to be dispensable for fertilization but required for the formation of a continuous and cohesive eggshell chitin layer by maintaining a homogenous distribution of chitin synthase chs-1 at the unfertilized oocyte cell membrane (By similarity). Appears to recruit or maintain together to the unfertilized oocyte cortex several proteins including chs-1, kinase mbk-2 and pseudophosphatases egg-3, and possibly egg-4 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q09967}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q09967}. Note=Localizes to the cell membrane of developing oocytes. Plasma membrane localization requires extracellular matrix protein cbd-1. After fertilization, localizes to endosomes in zygotes. {ECO:0000250|UniProtKB:Q09967}.
Interaction partners:
- Phosphatidylinositol-3-phosphatase SAC1
- CRE-UNC-52 protein
- Immunoglobulin I-set domain-containing protein
- Uncharacterized protein
- CRE-AGR-1 protein
- CRE-DAB-1 protein
- Alpha-2-macroglobulin RAP C-terminal domain-containing protein
- CRE-CED-6 protein
- Uncharacterized protein
- CRE-LIN-17 protein
Sequence:
MSQQPGSDRRVNFAQEEPMTLGEKISHRMDQFKEMVSSGCCSCASRCPSVAIVLILALVILGILAAIPLTLMLTSSAQRMSTDSTDLSPYSIRHPKFWPKTDKIHFNDLDGIPMSSLFPPNVSTCSGFGFACTGAVHMIIPSSKRCDGIKDCQDGSDEENCKECQSVFSCRSHVEEDSKTKRKTKVLPTLICLTAEKLCNDVQDCPDGSDESVCKSTCSKDQFKCTGNNACLPTSAKCDGVNDCTDGSDEKNCNECQKGAHKCGKQCIKASHVCDGVAQCADRSDEKECDCKSCSGSDKALCEDGTCIKRTQVCDGKKDCTDGMDEENCPGSCSIEAFSTKTKQLTCSDEKRYTESEACSGVVEACEQSCPKCHPKLTFTCPAVGGSQKRCIRRSKVCDGINDCDDGADEKNCTPIKECGIENASQFTCDRKCLDASRRCDGVWDCEDKSDEQNCQQCSSGSIRCAADKKCLPAYTRCNGVAECSDGSDEQKCSCEECLGAHSNTYMCNESNRCLKRDEVCSPYSMCPNATYTDKAYCAALVLKNSGRFPY
Protein: FI01658p (Ribosomal protein L23A, isoform A) (Ribosomal protein L23A, isoform B) (Rpl23A) (Q9W0A8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein bS16m
- IP17351p
- Small ribosomal subunit protein eS19A
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL15
- Eukaryotic translation initiation factor 4C
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL34
Sequence:
MPPKKPTEKSAKPGDKKPEQKKTAAAPAAGKKEAAPSAAKPAAAAPKKAAAPAAKKAAPAAKKPATAGAAAKKPAAVKTTAAAKAKSKDAKKKVLAGKKPQSVLAKLSAKARAAAKAKKGVKPVTKPAKGTAKAKAVALLNAKKVQKKIIKGAFGTRARKIRTNVHFRRPTTLKLPRSPKYPRKSVPTRNRMDAYNIIKYPLTTEAAMKKIEDNNTLVFLTHLRANKNHVRAAVRKLYDIKVAKVNVLIRPDGQKKAYVRLARDYDALDIANKIGII
Protein: HRF1 protein (Integral membrane HRF1 family protein) (F4J8C0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004653}.
Interaction partners:
- Protein YIP
- Protein YIP
Sequence:
MYNNMGPRPGMAMPQANPQPSPFGNPFSGPGSGLIRSGLGAYGEKIFGSSSEYVQSNISRYFSDPQYYFQVNDQYVRNKLKIVLLPFLHRGHWTRISEPVGGRLSYKPPIYDINAPDLYIPLMAFGTYVVLAGLSLGLYGKFTPEALNWLFVKGMVGWFLQVMLLKITLLSLGSGEAPLLDIVAYAGYTFTGLCLAVLGKIIWGYSYYVLIPWTCLCTGVFLVKTMKRVLFAESRSYDSSRHHYLLIFVALAQFPLLIWLGNISVNWLF
Protein: Draxin (Dorsal inhibitory axon guidance protein) (Dorsal repulsive axon guidance protein) (Neural-specific antagonist of canonical Wnt/beta-catenin signaling) (Q4V9H3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Chemorepulsive axon guidance protein required for the development of spinal cord and forebrain commissures. Acts as a chemorepulsive guidance protein for commissural axons during development. Able to inhibit or repel neurite outgrowth from dorsal spinal cord.
Subcellular location: Secreted {ECO:0000255|HAMAP-Rule:MF_03060}.
Interaction partners:
- Netrin-1
- Netrin 2.
- Netrin-1
- Neogenin
- Neogenin 1b
- Down syndrome cell adhesion molecule a.
Sequence:
MVAPGLCQLFILLLITLSHTSHSSEISSDHFKQSLTTSTTTSKEHPETGLTGGRQQKRHWSGKERDSAGLFSQRHMDRLEDDGTSMEGLSPVRLEMGPGDTMKAEVHGEVRASAQMRQGSHPAEGELNRKGRRHSHRLLAEHRKHGGKKDKGRGKGDLSDPEPELDSLLKDLNAFEDGLNTSPPNYNSVPLNEVPSPLSPILVTTAIKGHPPTLPPASTKPQKSSQGRTQGEVMPTLDMTLFDWTDYEDMKPADSWPSNKRKDKRRSKNKSNGNTTTEAGIVEPCDHHLDCLSGSCCDLREFECKPHNRGLNNKCFDDCMCEEGLRCYAKFHRKRRVTRRRGRCVDPESVNSNQGAFITV
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (G3I8R9)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}. Melanosome {ECO:0000250|UniProtKB:P11021}. Cytoplasm {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epithelial cells; high levels of free iron promotes cell surface localization (By similarity). {ECO:0000250|UniProtKB:P11021}.
Interaction partners:
- Endoplasmin
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Hypoxia up-regulated protein 1
- Calnexin
- Mesencephalic astrocyte-derived neurotrophic factor
- DnaJ homolog subfamily B member 11
- Protein disulfide-isomerase A3
- DnaJ homolog subfamily C member 10
- Calreticulin
- Nucleotide exchange factor SIL1
Sequence:
MKFPMVAAALLLLCAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTSEKDEL
Protein: Protein AF-10 (O54826)
Organism: Mus musculus (Mouse)
Function: Probably involved in transcriptional regulation. Binds to cruciform DNA (By similarity). In cells, binding to unmodified histone H3 regulates DOT1L functions including histone H3 'Lys-79' dimethylation (H3K79me2) and gene activation (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Protein AF-9
- AF4/FMR2 family member 1
- Btk-PH-domain binding protein translocated to, 1)
- Myeloid/lymphoid or mixed-lineage leukemia; translocated to, 6
- RNA polymerase II elongation factor ELL
- Afadin
- Histone-lysine N-methyltransferase 2A
- Phosphatidylinositol-binding clathrin assembly protein
- AF4/FMR2 family member 4
Sequence:
MVSSDRPVSLEDEVSHSMKEMIGGCCVCSDERGWAENPLVYCDGHGCSVAVHQACYGIVQVPTGPWFCRKCESQERAARVRCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQSVPHDRYNKTCYICDEQGRESKAATGACMTCNKHGCRQAFHVTCAQFAGLLCEEEGNGADNVQYCGYCKYHFSKLKKSKRGSNRSYEQSLSDSSSHSQDKHHEKEKKKYKEKDKHKQKHKKQPEPSPALVPSLTVTTEKTYTSTSNNSISGSLKRLEDTAARFTNANFQEVSAHTSSGKDVSEARGSEGKGKKSSAHSSGQRGRKPGAGRNPGTAVSASSPFPQGSFSGTPGSVKSSSGSSVQSPQDFLSFTDSDLRSDSYTHTQQPSSTKDVHKGESGSQEAAVNSFSSLVGHPVTSTVISQPKSFDNSPGELGSSSLPTAGYKRAQTSGIEEEAVKEKKRKGNKQSKHGPGRPKGNKNQENVSHLSVSSASPTSSVASAAGSVTSSSLQKSPTLLRNGSLQSLSVGSSPVGSEISMQYRHDGACPTTTFSELLNAIHNGIYNSNDVAVSFPNVVSGSGSSTPVSSSHIPQQSSGHLQQVGALSPSAASSVTPAAATTQANTVSGSSLSQAPAHMYGSRLNQNPSMAVLIAQSESSQTDQDLGDNARSLGGRGSSPRGSLSPRSPVSNLQLRYDQPSNSSLETVPPVAASIEQLLERQWSEGQQFLLEQGTPGDILGMLKSLHQLQVENRRLEEQIKNLTAKKERLQLLNAQLSVPFPAITTNPSPSHQMHTYTAQTAPPPDSLNSSKSPHIGNSFLPDNSLPVLNQDLTSSGQSTSSSSALSTPPPAGQSPAQQSSGVSGVQQVNGVTVGALASGMQTVTSTIPAVSAVGGIIGALPGNQLAINGIVGALNGVIQTPVTISQNPAPLTHTSVPPNAAHPMPAAALTNSASGLGLLSDQQRQMFIQQQQFQQLLNSQQLTPEQHQAFLYQLMQQQHHPPELQQLQLPGPTQIPINNLLAGAQAPPLHTATTNPFLTIHGDSTSQKVTRLSDKTGPVAQEKS
Protein: NEDD8 ultimate buster 1 (Negative regulator of ubiquitin-like proteins 1) (Renal carcinoma antigen NY-REN-18) (Q9Y5A7)
Organism: Homo sapiens (Human)
Function: Specific down-regulator of the NEDD8 conjugation system. Recruits NEDD8, UBD, and their conjugates to the proteasome for degradation. Isoform 1 promotes the degradation of NEDD8 more efficiently than isoform 2.
Subcellular location: Nucleus {ECO:0000269|PubMed:11259415}. Note=Predominantly nuclear.
Interaction partners:
- Ubiquitin-like protein NEDD8
- 26S proteasome non-ATPase regulatory subunit 4
- Aryl-hydrocarbon-interacting protein-like 1
- Ubiquitin D
- Synphilin-1
Sequence:
MAQKKYLQAKLTQFLREDRIQLWKPPYTDENKKVGLALKDLAKQYSDRLECCENEVEKVIEEIRCKAIERGTGNDNYRTTGIATIEVFLPPRLKKDRKNLLETRLHITGRELRSKIAETFGLQENYIKIVINKKQLQLGKTLEEQGVAHNVKAMVLELKQSEEDARKNFQLEEEEQNEAKLKEKQIQRTKRGLEILAKRAAETVVDPEMTPYLDIANQTGRSIRIPPSERKALMLAMGYHEKGRAFLKRKEYGIALPCLLDADKYFCECCRELLDTVDNYAVLQLDIVWCYFRLEQLECLDDAEKKLNLAQKCFKNCYGENHQRLVHIKGNCGKEKVLFLRLYLLQGIRNYHSGNDVEAYEYLNKARQLFKELYIDPSKVDNLLQLGFTAQEARLGLRACDGNVDHAATHITNRREELAQIRKEEKEKKRRRLENIRFLKGMGYSTHAAQQVLHAASGNLDEALKILLSNPQMWWLNDSNPETDNRQESPSQENIDRLVYMGFDALVAEAALRVFRGNVQLAAQTLAHNGGSLPPELPLSPEDSLSPPATSPSDSAGTSSASTDEDMETEAVNEILEDIPEHEEDYLDSTLEDEEIIIAEYLSYVENRKSATKKN
Protein: DNA helicase B (hDHB) (EC 3.6.4.12) (Q8NG08)
Organism: Homo sapiens (Human)
Function: 5'-3' DNA helicase involved in DNA damage response by acting as an inhibitor of DNA end resection. Recruitment to single-stranded DNA (ssDNA) following DNA damage leads to inhibit the nucleases catalyzing resection, such as EXO1, BLM and DNA2, possibly via the 5'-3' ssDNA translocase activity of HELB. As cells approach S phase, DNA end resection is promoted by the nuclear export of HELB following phosphorylation. Acts independently of TP53BP1. Unwinds duplex DNA with 5'-3' polarity. Has single-strand DNA-dependent ATPase and DNA helicase activities. Prefers ATP and dATP as substrates. During S phase, may facilitate cellular recovery from replication stress.
Subcellular location: Nucleus {ECO:0000269|PubMed:15146062}. Cytoplasm {ECO:0000269|PubMed:15146062}. Chromosome {ECO:0000269|PubMed:26774285}. Note=Predominantly nuclear (PubMed:15146062). Phosphorylation at Ser-967 by CDK2 during the G1/S transition results in its nuclear export into the cytoplasm as cells approach and progress through S phase (PubMed:15146062). Following DNA damage, recruited to sites of double-strand breaks by the RPA complex (PubMed:26774285). Recruited to chromatin following DNA damage induced by UV irradiation, or camptothecin or hydroxyurea treatment (PubMed:22194613). {ECO:0000269|PubMed:15146062, ECO:0000269|PubMed:22194613, ECO:0000269|PubMed:26774285}.
Interaction partners:
- Replication protein A 70 kDa DNA-binding subunit
- Replication protein A 14 kDa subunit
- Replication protein A 32 kDa subunit
- DNA replication ATP-dependent helicase/nuclease DNA2
- Proliferating cell nuclear antigen
Sequence:
MARSSPYLRQLQGPLLPPRDLVEEDDDYLNDDVEEDEESVFIDAEELCSGGVKAGSLPGCLRVSICDENTQETCKVFGRFPITGAWWRVKVQVKPVVGSRSYQYQVQGFPSYFLQSDMSPPNQKHICALFLKECEVSSDDVNKFLTWVKEVSNYKNLNFENLRETLRTFHKETGRKDQKQPTQNGQEELFLDNEMSLPLENTIPFRNVMTALQFPKIMEFLPVLLPRHFKWIIGSGSKEMLKEIEEILGTHPWKLGFSKITYREWKLLRCEASWIAFCQCESLLQLMTDLEKNALIMYSRLKQICREDGHTYVEVNDLTLTLSNHMSFHAASESLKFLKDIGVVTYEKSCVFPYDLYHAERAIAFSICDLMKKPPWHLCVDVEKVLASIHTTKPENSSDDALNESKPDEVRLENPVDVVDTQDNGDHIWTNGENEINAEISEVQLDQDQVEVPLDRDQVAALEMICSNPVTVISGKGGCGKTTIVSRLFKHIEQLEEREVKKACEDFEQDQNASEEWITFTEQSQLEADKAIEVLLTAPTGKAAGLLRQKTGLHAYTLCQVNYSFYSWTQTMMTTNKPWKFSSVRVLVVDEGSLVSVGIFKSVLNLLCEHSKLSKLIILGDIRQLPSIEPGNLLKDLFETLKSRNCAIELKTNHRAESQLIVDNATRISRRQFPKFDAELNISDNPTLPISIQDKTFIFVRLPEEDASSQSSKTNHHSCLYSAVKTLLQENNLQNAKTSQFIAFRRQDCDLINDCCCKHYTGHLTKDHQSRLVFGIGDKICCTRNAYLSDLLPENISGSQQNNDLDASSEDFSGTLPDFAKNKRDFESNVRLCNGEIFFITNDVTDVTFGKRRSLTINNMAGLEVTVDFKKLMKYCRIKHAWARTIHTFQGSEEQTVVYVVGKAGRQHWQHVYTAVTRGRCRVYVIAEESQLRNAIMKNSFPRKTRLKHFLQSKLSSSGAPPADFPSPRKSSGDSGGPSTPSASPLPVVTDHAMTNDVTWSEASSPDERTLTFAERWQLSSPDGVDTDDDLPKSRASKRTCGVNDDESPSKIFMVGESPQVSSRLQNLRLNNLIPRQLFKPTDNQET
Protein: heparosan-N-sulfate-glucuronate 5-epimerase (EC 5.1.3.17) (Q29RD8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- [heparan sulfate]-glucosamine N-sulfotransferase
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- [heparan sulfate]-glucosamine N-sulfotransferase
- D-glucuronyl C5-epimerase B
- Sulfotransferase
Sequence:
MRCLVARINHKTLIVICAVFALITILLWNKCSSDKDLPSPVRPLEFAAPTPEKEEENEGQAPEAPPGSREVAYEQIDCLINEDVLIKGRREGGEVYLPFSWVEKYFDVYGRLVQYDGMERFEFSHSYSRVYAQREPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPISTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPDIKIYGMLEEKEGGSSQWDVPKGCTLSKIQDQGRSGFVHHFVTAENSEGVSLVLDNAKDFVLTFDVKFISNGSVSVVLETTEKGPYFIIHYITSPLLLSFKDREVIYGIGPRATWSTVSRDLVTDLRKGVGLSNTKVVKATKIMPRRVVQLVLKGSGFISNITVSSTAHMAAFFAASDWLLHNQDEHGGWPIKVTRKLGEGFKSLEPGWYSAMAQGQAMSTLVRAYLVTHNPSYLGAAIRATSPFKRTPEQHGVKATFMNKFDWYEEYPTTPSSFVLNGFIYSLIGLYDVAETAGNKLGREAGILFSQGLESLKAMLPLFDTGSGTVYDLRHFTLGVAPNLARWDYHTTHINQLQLLASIDGAPIFRDYVKRWKTYLKGGRAKHN
Protein: Inhibitor-t (Q9VGJ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- AT25465p
- MORN repeat-containing protein 5
- GEO12017p1
- Serine/threonine-protein phosphatase alpha-2 isoform
- FI08029p
Sequence:
MHKNFKSLQNTNPSNMKKAKTAAKGFPIHLGFYRNPSEYDDRTTTNRDYGLKSSKGSGTPFPQKQKKLDTAALTAKLETDSLLRSELSDLSIVISERKASSEPQVASNTTTEPTFEMRRKLFDEAEFTICKGHKLNQDFHHIVEDEKHFNKRQSAKDNIPYSNFMDLKNFCDQNNIKFSKGFDG
Protein: Signal recognition particle 9 kDa protein (SRP9) (P21262)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.
Subcellular location: Cytoplasm.
Interaction partners:
- Signal recognition particle subunit SRP68
- Signal recognition particle 14 kDa protein
- Signal recognition particle 19 kDa protein
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP54
- 40S ribosomal protein S7
- Protein transport protein Sec61 subunit beta
- Large ribosomal subunit protein eL15
- Ribosomal protein S5
- 40S ribosomal protein S30
Sequence:
MAQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGSLCIKVTDDLVCLVYRTDQAQDVKKIEKFHSQLMRLMVAKESRSVAMETD
Protein: Glutathione synthetase, chloroplastic (GSH synthetase) (GSH-S) (Glutathione synthase) (EC 6.3.2.3) (P46416)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Glutamate--cysteine ligase, chloroplastic
- Glutathione hydrolase 1
- Glutathione reductase, chloroplastic
- Glutathione hydrolase 3
- Putative inactive glutathione hydrolase 4
- Glutathione reductase, cytosolic
- Glutathione hydrolase 2
- Glutathione S-transferase DHAR2
- Probable glutathione peroxidase 2
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
Sequence:
MGSGCSSLSYSSSSTCNATVFSISSSPSSSSSLKLNPSSFLFQNPKTLRNQSPLRCGRSFKMESQKPIFDLEKLDDEFVQKLVYDALVWSSLHGLVVGDKSYQKSGNVPGVGLMHAPIALLPTAFPEAYWKQACNVTPLFNELIDRVSLDGKFLQDSLSRTKKVDVFTSRLLDIHSKMLERNKKEDIRLGLHRFDYMLDEETNSLLQIEMNTISCSFPGLSRLVSQLHQSLLRSYGDQIGIDSERVPINTSTIQFADALAKAWLEYSNPRAVVMVIVQPEERNMYDQHLLSSILREKHNIVVIRKTLAEVEKEGSVQEDETLIVGGQAVAVVYFRSGYTPNDHPSESEWNARLLIEESSAVKCPSIAYHLTGSKKIQQELAKPGVLERFLDNKEDIAKLRKCFAGLWSLDDSEIVKQAIEKPGLFVMKPQREGGGNNIYGDDVRENLLRLQKEGEEGNAAYILMQRIFPKVSNMFLVREGVYHKHQAISELGVYGAYLRSKDEVIVNEQSGYLMRTKIASSDEGGVAAGFGVLDSIYLI
Protein: Neuronal PAS domain-containing protein 1 (Neuronal PAS1) (P97459)
Organism: Mus musculus (Mouse)
Function: May control regulatory pathways relevant to schizophrenia and to psychotic illness. May play a role in late central nervous system development by modulating EPO expression in response to cellular oxygen level. Forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) leading to transcriptional repression on its target gene TH.
Subcellular location: Nucleus.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator
- LIM/homeobox protein Lhx6
Sequence:
MATPYPRSGGRGEVKCGGGRGAGVPWDFLPGLMVKAPPGPCLQAQRKEKSRNAARWRRGKENLEFFELAKLLPLPGAISSQLDKASIVRLSVTYLRLRRFAALGAPPWGLRAVGPPAGLAPGRRGPVALVSEVFEQHLGGHILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQLGLRAASIGPPTPPSVSSSSSSSSSSLVDTPEIEASPTEASPAFRAQERSFFVRMKSTLTKRGLNVKASGYKVIHVTGRLRARALGLVALGHTLPPAPLAELPLHGHMIVFRLSLGLTILACESRVSDHMDMGPSELVGRSCYQFVHGQDATRIRQSHLDLLDKGQVVTGYYRWLQRAGGFVWLQSVATVAGNGKSTGEHHVLWVSHVLSNAEGSQTPLDAFQLPAIVSQEEPSRPGPEPTEEEPPVDGKQAVPADQDKDKDPQARGKRIKVEASPKEARGSEDSGEEELSDPPAPPRPEFTSVIRAGALKHDPVLPWGLTTPGDPSPALLHAGFLPPVVRGLCTPGTIRYGPAELSLMYPHLHRLGAGPSLPEAFYPTLGLPYPGPTGTRVQRKGD
Protein: CABIT domain-containing protein (O61770)
Organism: Caenorhabditis elegans
Interaction partners:
- Ig-like domain-containing protein
- CTLH domain-containing protein
- SKN-1 Dependent Zygotic transcript
- SET domain-containing protein
- Laminin-like protein lam-2
- A-to-I RNA editing regulator adr-1
- Double-stranded RNA-specific adenosine deaminase adr-2
- Cilia- and flagella-associated protein 157
- Protein CASP
- FTH domain-containing protein
Sequence:
MDVVFETVNCLESNRKIIIVKLPDGSSEKFFFNVTKRAFEKIVCVDGKPVQMDSDLTPHHSVWCPHIHKNIIFAYNHLLRMNLQYLFDSETLSFHETKCDQCHLDPKKSTNVKQILLVAASPKIRRPIVLTMSQEGRVLKMCYDEIEKNYVDMSPTEIKALTQLKDVTAAMEDLTLDSKVMESDLIPLVKEKSVFLPHDSILIAKNKKTNKIGQYVFDRYHHQFLEVVMSDIEIKQEMPNIAKLINVTMSTKTEQAISIRCTPGIGELKKFHYNRETASFDPMEEKAIVESDEEIQSFIEEIEKTQDIVCKKIKAILWFYHNVKPFLAKKLENPVKKNNDYKRYVFKPVEPEEKVDDEMDSVSEPESDSLSMSSSSRSSSRSSLSSDDSFEMVVDIDFVE