wanglab/gogpt-training-data huggingface dataset:
Protein: Lysine-specific demethylase 6A (EC 1.14.11.68) (Histone demethylase UTX) (Ubiquitously transcribed TPR protein on the X chromosome) (Ubiquitously transcribed X chromosome tetratricopeptide repeat protein) ([histone H3]-trimethyl-L-lysine(27) demethylase 6A) (O70546)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A (By similarity). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- PAX-interacting protein 1
- Nuclear receptor coactivator 6
- Histone-lysine N-methyltransferase 2C
- Histone-lysine N-methyltransferase 2D
- WD repeat-containing protein 5
- Retinoblastoma-binding protein 5
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- PAXIP1-associated glutamate-rich protein 1A
- Protein dpy-30 homolog
- Histone H3.3
Sequence:
MKSCGVSLATAAAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATILQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGNAPPPVEQQTHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRQTGVAQVRPTGILNGPTVDSSLPTNSVSGQQPQLPLTRMPSVSQPGVHTACPRQTLANGPFSAGHVPCSTSRTLGSTDTVLIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGPSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTVPETSRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDKVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSMSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRKGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQNVKSIVPMVHLSWNMARNIKVSDPKLFEMIKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCARKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
Protein: Guanine nucleotide-binding protein alpha-6 subunit (Q93743)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Interaction partners:
- Guanine nucleotide-binding protein alpha-9 subunit
- Serpentine receptor class gamma-13
- C2H2-type domain-containing protein
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit gamma
- G protein gamma domain-containing protein
- G Protein, Alpha subunit
Sequence:
MGAGATGLRGARLSPEERANSSKSRAIDRALSKDHTDDLNRFKILLLGTAESGKSTIFKQMRVLHLDGYAKEDALEYLSIIHSNCMEALTQLVDACTAFGINHDITVQEDVNRFEDFKRKLRDPEGLVIPVVIGRCMDRVWHSPSLQLCYDTRRFRFALLDSAKYFMDNIVRLTEDNYVPSIQDIVHCRISTTGINELAFNYKKMDFKMVDVGGQRSERRKWIHCFDNVDMILFIVSMSDYDQLDPEDNKYNRMKQSYEIFKTIVHSDLFRHASIVLFLNKYDVFVEKLKTSPLRRSFKNYEGDNSEESAREFIKKLFRRCITDRHKFFVFETTATDTGNIDLVFGSAVAHIVNENLRSAGLHE
Protein: BPI fold-containing family A member 2 (Neonatal submandibular gland protein) (Parotid secretory protein) (PSP) (Q63471)
Organism: Rattus norvegicus (Rat)
Function: Has strong antibacterial activity against P. aeruginosa.
Subcellular location: Secreted.
Interaction partners:
- BPI fold-containing family B member 4
- Prolactin-inducible protein homolog
- BPI fold containing family A, member 6
- BPI fold containing family A, member 5
- Opiorphin prepropeptide
- Carbonic anhydrase
Sequence:
MFQLGSLVVLCGLLIGTSESLLGDVANAVNNLDILNSPSEAVAQNLNLDVGSLQQATTWPSAKDSILETLNKVELGNSNGFTPLNGLLLRVNKFRVLDLQAGLSSNGKDIDLKLPLVFEISFSLPVIGPTLDVAVSLDLLNSVSVQTNAQTGLPGVTLGKCSGNTDKISISLLGRRLPFVNRILDGVSGLLTGAVSILLQNILCPVLQYLLSTMSGSAIQGLLSNVLTGQLAVPL
Protein: Keratin-associated protein 10-5 (High sulfur keratin-associated protein 10.5) (Keratin-associated protein 10.5) (Keratin-associated protein 18-5) (Keratin-associated protein 18.5) (P60370)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 10-9
- Keratin-associated protein 10-1
- Keratin-associated protein 10-8
- Keratin-associated protein 10-7
- Keratin-associated protein 10-4
- Keratin-associated protein 10-3
Sequence:
MAACTMSVCSSACSDSWRVDDCPESCCEPPCGTAPCLTLVCTPVSCVSSPCCQAACEPSPCQSGCTSSCTPSCCQPACCASSPCQQACCVPVCCKPVCCLPTCSKDSSSCCQQSSCQPTCCASSSCQQSCCVPVCCKPVCCVPTCSEDSSSCCQHSSCQPTCCTSSPCQQSCYVPVCCKPVCCKPICCVPVCSGASTSCCQQSSCQPACCTTSCCRPSSSVSLLCRPICRPACCLPISSCCAPASSYQASCCRPASCVSLLCRPACSPLAC
Protein: Altered inheritance of mitochondria protein 9, mitochondrial (Found in mitochondrial proteome protein 29) (P40053)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized protein YER078W-A
- Uncharacterized trans-sulfuration enzyme YHR112C
- Uncharacterized protein YER079W
- 5-formyltetrahydrofolate cyclo-ligase
- Uncharacterized vacuolar membrane protein YML018C
- Altered inheritance of mitochondria protein 6
- Protein AIM2
Sequence:
MIRYTVAGHSRRCVVGASKRVGAIKCITVAATKRFISNKPNEVFTKLTNDNDPKRDAFFKYTWGSWLKNDKQEKEKRFTKFSIEGLNRILNDIYIQSNEMAKAPDGKILPPVFNKNLTVSLVNNVVPKNIGKINPNEKVQVTTLSSIHEGKHHRIYKVDTNLNKAFILRIPYPLENENTLSYRIRSEVATMDFADLKLGIKVPKIFCYGVNSLNPVRQPFVLQEFIEGELLMKDWDPLIEDGSSNQKKYDNVIKQVSDFQSKLVSLKLNAFGSIYFNNDLKDGNEKEFVKEDIYDGETNPDLQNRWKIGPSVERCLWRHKSHLDFHKQMKPFLGPWPKKSPMDIIKNTGLLEAENAKTRIAMKEAGSSAELMYPRTLKEQITTYENLAKIAPDLFNVKTKAIPNMQELLSPRLFHPDLDPMNIIVNKEAQEAYLLDFEGACTKPFILQNSPQFIAYDGPKIYDLKEDITDFDKLSEAEKVQYQFMYKRTRNQHQWEKKLNDNNPKLITAVAPPVKLLRSPYIAAVERKTEEEYLLIDESLLQLKEVWDIFAQNELVNQKKFPLNYSKEDIERHVEDLQKLHEKLISTPFAATQGWIPQDMFDQLLNSGSIVKQENGDYTVKQPEATK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8IIL5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Pre-mRNA-processing factor 6, putative
- U5 small nuclear ribonucleoprotein component, putative
- Pre-mRNA-processing-splicing factor 8, putative
- U4/U6 small nuclear ribonucleoprotein PRP31, putative
- U4/U6.U5 tri-snRNP-associated protein 2, putative
- Splicing factor 3B subunit 1, putative
- U5 small nuclear ribonucleoprotein 40 kDa protein, putative
- RNA helicase
- Sm protein F
- U6 snRNA-associated Sm-like protein LSm4
Sequence:
MSKDKRNSFASNSFDSSNDEKKSKNGNKIYKSKHEENSPDGDSYKINNNEKEKSKEKLKKDQKKKSKEIYNSFNSPNSTSSDSDGNGLHLNFSNASSSSSENGFKILRTQENEDKLLEERRRKREALKEKLKNMVKENEQNNDANEILQNDQINKDYNNETFLLSENKNDNDIITNEIPSNPSYIDQNDAACIFAPNNDVIEDTCSSLSSDHEIIEEKQNKEKPEAVKECSDLYNDLKKKIDEEKAKIRSFIIKQKELHERLKMNVDDSLYVNKSKGNADTHNNLTNKKSPLENEEDEMQEEYDEDNDDFDMFSCVQANKKRKVEKVHITDYYTTGNNANLSDNWNDSEGYYKAMVGEVIDKRYSVVCELVGKGVFSNVLKCYDMVNKIPVAVKVIRDNDMMKKAAEKEISILKKLNQYDKDNKRHIIRLLSSIKYKNHLCLVFEWMWGNLRIALKKYGNGHGLNATAVHCYTKQLFIALRHMRKCRIMHADLKPDNILINEKFNALKVCDLGSASDISENEITSYLVSRFYRAPEIILGFRYDAQIDVWSAAATVFELATGKILFPGKSNNHMIKLMMEYKGKFSHKMIKGGQFYSQHFNENLDFLYVDRDHYSKKEVVRVISDLRPTKNITCDLLEHQYWLKGNSPKMQFLKKKIKQLGDLLEKCLILDPSKRYTPDQALQHPYLRESIHFSKSQNE
Protein: Glucuronoxylan 4-O-methyltransferase 3 (EC 2.1.1.112) (Q9LQ32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methyltransferase catalyzing 4-O-methylation of glucuronic acid side chains on xylan.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23045523}; Single-pass membrane protein {ECO:0000269|PubMed:23045523}.
Interaction partners:
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- Probable beta-1,4-xylosyltransferase IRX10L
- Probable beta-1,4-xylosyltransferase IRX10
- Beta-1,4-xylosyltransferase IRX9
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 2
- Probable galacturonosyltransferase 12
- Probable beta-1,4-xylosyltransferase IRX14H
- Xylan O-acetyltransferase 1
- Probable galacturonosyltransferase-like 1
- Probable glucuronoxylan glucuronosyltransferase IRX7
Sequence:
MRTKSPSSLNLKVIFIGSSILILIIIYLARSNISSSSSKPISKTNLSQEEEETQHKQEGCPTTQQCTKMPLSLSDALVHYVTSNVTPQQTFDEVSVSKRVLDKKSPCNFLVFGLGHDSLMWASLNHGGRTLFIEEDQAWIAIVTKKFPNLESYHVVYDTKVKDSDKLMELGRSEECRSVSDPRNSKCDLALKDFPADFYETKWDLIMVDAPTGYHEEAPGRMSAIYTAGLLARNREDGETDVFVHDVNRPVEDEFSATFLCKGYMREQNGRLRHFTIPSHRARAGRPFCPVEVDRRR
Protein: DEP domain-containing protein 1A (Q5TB30)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation as a transcriptional corepressor. The DEPDC1A-ZNF224 complex may play a critical role in bladder carcinogenesis by repressing the transcription of the A20 gene, leading to transport of NF-KB protein into the nucleus, resulting in suppression of apoptosis of bladder cancer cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:17452976, ECO:0000269|PubMed:20587513}. Note=Colocalizes with ZNF224 at the nucleus.
Interaction partners:
- Dual specificity protein kinase TTK
- Hyaluronan mediated motility receptor
- Targeting protein for Xklp2
- Kinesin-like protein KIF20A
- Kinetochore protein Nuf2
- Cyclin-A2
- Disks large-associated protein 5
- Centrosomal protein of 55 kDa
- Kinesin-like protein KIF14
- G2/mitotic-specific cyclin-B1
Sequence:
MESQGVPPGPYRATKLWNEVTTSFRAGMPLRKHRQHFKKYGNCFTAGEAVDWLYDLLRNNSNFGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGSENVDDNNQLFRFPATSPLKTLPRRYPELRKNNIENFSKDKDSIFKLRNLSRRTPKRHGLHLSQENGEKIKHEIINEDQENAIDNRELSQEDVEEVWRYVILIYLQTILGVPSLEEVINPKQVIPQYIMYNMANTSKRGVVILQNKSDDLPHWVLSAMKCLANWPRSNDMNNPTYVGFERDVFRTIADYFLDLPEPLLTFEYYELFVNILVVCGYITVSDRSSGIHKIQDDPQSSKFLHLNNLNSFKSTECLLLSLLHREKNKEESDSTERLQISNPGFQERCAKKMQLVNLRNRRVSANDIMGGSCHNLIGLSNMHDLSSNSKPRCCSLEGIVDVPGNSSKEASSVFHQSFPNIEGQNNKLFLESKPKQEFLLNLHSEENIQKPFSAGFKRTSTLTVQDQEELCNGKCKSKQLCRSQSLLLRSSTRRNSYINTPVAEIIMKPNVGQGSTSVQTAMESELGESSATINKRLCKSTIELSENSLLPASSMLTGTQSLLQPHLERVAIDALQLCCLLLPPPNRRKLQLLMRMISRMSQNVDMPKLHDAMGTRSLMIHTFSRCVLCCAEEVDLDELLAGRLVSFLMDHHQEILQVPSYLQTAVEKHLDYLKKGHIENPGDGLFAPLPTYSYCKQISAQEFDEQKVSTSQAAIAELLENIIKNRSLPLKEKRKKLKQFQKEYPLIYQKRFPTTESEAALFGDKPTIKQPMLILRKPKFRSLR
Protein: Ecotin-like protein 2 (Q4QFD4)
Organism: Leishmania major
Interaction partners:
- Serine peptidase
Sequence:
MPAGMSDAAGKTLADFKAPYPEPTSQQRRYVIFLDPKGDSKELNDYKVELIPGRVEKVDGTNVYRMGGNIEERTIDGWGYPYYIVTLTTMSGTLMMPLGDAALKRPRFVAMNTKNLYRYNSRLPIVVYMPKDGELRYRIWTVKSTGSGTAKSTKAREM
Protein: U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (m7GpppN-mRNA hydrolase) (Q6P3D0)
Organism: Mus musculus (Mouse)
Function: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation (By similarity). Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96DE0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm {ECO:0000250|UniProtKB:Q96DE0}. Note=Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm. {ECO:0000250|UniProtKB:Q6TEC1, ECO:0000250|UniProtKB:Q96DE0}.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Nucleoside diphosphate kinase homolog 7
- Adenylosuccinate synthetase isozyme 1
- AMP deaminase 2
- AMP deaminase 3
- AMP deaminase 1
- Adenylosuccinate synthetase isozyme 2
- Inosine-5'-monophosphate dehydrogenase 1
- Inosine-5'-monophosphate dehydrogenase 2
- U8 snoRNA-decapping enzyme
Sequence:
MEGHRKVELSEALALGPDWRHACHALLYAPDPRKLFGRIPMRFAVLMQMRFDGRLGFPGGFVDAQDSCLEDGLNRELREELGEAMSAFRVERSDYRSSHIAARPRVVAHFYAKRLTLEQLQAVEARAPQAKDHGLEVLGLVRVPLYVLRDGEGGLPAFLENSFIGAAREQLLEALQDLKLLDPGIIAKLKIPDSK
Protein: Phosphatidate cytidylyltransferase (EC 2.7.7.41) (Q57U32)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Lipin, putative
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidic acid phosphatase, putative
- Phosphatidic acid phosphatase protein, putative
- Phosphatidic acid phosphatase alpha, putative
- 3'
- Phosphatidylinositol 4-phosphate 5-kinase alpha, putative
Sequence:
MKSKSSKQVLLPLQGNISPSAESPRPGSLMTTEGRTRNYKDLINRTVFSLIMAYFFLGLVSIGAEAIIFLLIIILCLMFHEVSRINQRERKNKQLPSVFIMKVWFLCTTMFSMTAYSIRDPLVATYPGAMRYYRNAWMIAFGFPLVGMVGFVLSLRKGMYRYQFMQLAAIVMTLLYVTAQGYAQISNVMRGMLWFVLPISCVINNDTWAYIFGKLFGRTKLLALSPKKTVEGFVGAFVFTIIWSFWFAGFLSYFPHMYCAKTDFHSAFHCEKDPLFVKRDVPMPAFVQALTFNRLTTIRCARVQQHALVFAAFASLIAPFGGFFASGLKRAFKMKDFGDLIPGHGGITDRMDCQGIMGFFTWVYLQSYVYRDENCPSWHTISSCALQLPEEQRRSLLSTLNRSLTE
Protein: Large ribosomal subunit protein eL13B (60S ribosomal protein L13-B) (P40212)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL8B
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein uL22A
Sequence:
MAISKNLPILKNHFRKHWQERVKVHFDQAGKKVSRRNARAARAAKIAPRPLDLLRPVVRAPTVKYNRKVRAGRGFTLAEVKAAGLTAAYARTIGIAVDHRRQNRNQEIFDANVQRLKEYQSKIIVFPRDGKAPEAEQVLSAAATFPIAQPATDVEARAVQDNGESAFRTLRLARSEKKFRGIREKRAREKAEAEAEKKK
Protein: Uncharacterized protein C19D5.02c (Q1K9B6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to the nuclear rim. {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MLGQGLIFISLAFVAHALEIPISCAVSHNEQTEIFPHGTIDIPEMTFRPSDSQIDWSNLSHSDFVQCGVYEDSTNTWLAGASKYKIDEIKTLPKVPRDHYIILCDSSESNEIAKFTQVVHSFDFSSDSESAVVEQLHPSSPIPILTTAVRKKGSRPSKPQKEKQGNKQGSKTEESPNVDEDELESEPEEKTFFQKYGLYLIPILFLIIMSGNNANQQAANTAK
Protein: Autophagy receptor Nbr1 (Q9P792)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}. Endosome, multivesicular body {ECO:0000269|PubMed:26365378}. Vacuole lumen {ECO:0000269|PubMed:26365378}.
Interaction partners:
- Autophagy-related protein 8
- Aspartyl aminopeptidase 1
- Alpha-mannosidase
- Autophagy protein 5
- Ubiquitin-like modifier-activating enzyme atg7
- Autophagy-related protein 3
- Ubiquitin-like protein ATG12
- Aminopeptidase 1
- Leucine aminopeptidase 2
- Autophagy-related protein 101
Sequence:
MLCNRTCPSSDCGILCNHSVPSFPPFHSSVANIHFTKENNLKSNIFEHNNNSPTLRSSSVACNTCLKIIRNDSFHCTKCFDFDVCRDCYAKQAFLHPCPKPHFVLVRSSIPSVASLTCSVNSMSVSPQSNFMYAICDHCEQPIHNVRYKCSVCDDYDICESCLTDNSHSNTHAFVRITKAYPHGLPSFHLFPQFLSAELFESASTVHRSVQCDNCLAHPIVGPRFHCLVCEDYDLCSSCVSHVHHDHHSMLRLTREISASPLHLSKPEKPKVLNFDFKLVEDSILPLELSPGCPFYKIWHIRNTSCQSWPSPLYVKFNGGDKLFPGDNPYSFPITSSVHPGEDVNFTVALKVPEKSNKEIFTAFFNICSDDGSVFHKSLCAFLRVPKSFSRISKSSF
Protein: Mitogen-activated protein kinase kinase kinase 12 (EC 2.7.11.25) (Dual leucine zipper bearing kinase) (DLK) (Leucine-zipper protein kinase) (ZPK) (MAPK-upstream kinase) (MUK) (Mixed lineage kinase) (Q12852)
Organism: Homo sapiens (Human)
Function: Part of a non-canonical MAPK signaling pathway. Activated by APOE, enhances the AP-1-mediated transcription of APP, via a MAP kinase signal transduction pathway composed of MAP2K7 and MAPK1/ERK2 and MAPK3/ERK1. May be an activator of the JNK/SAPK pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q60700}. Cell membrane {ECO:0000250|UniProtKB:Q60700}. Note=Behaves essentially as an integral membrane protein. {ECO:0000250|UniProtKB:Q60700}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
- MAP3K12-binding inhibitory protein 1
- Threonine--tRNA ligase 1, cytoplasmic
- C-Jun-amino-terminal kinase-interacting protein 1
- Threonine--tRNA ligase, mitochondrial
- Threonine--tRNA ligase 2, cytoplasmic
Sequence:
MACLHETRTPSPSFGGFVSTLSEASMRKLDPDTSDCTPEKDLTPTHVLQLHEQDAGGPGGAAGSPESRASRVRADEVRLQCQSGSGFLEGLFGCLRPVWTMIGKAYSTEHKQQQEDLWEVPFEEILDLQWVGSGAQGAVFLGRFHGEEVAVKKVRDLKETDIKHLRKLKHPNIITFKGVCTQAPCYCILMEFCAQGQLYEVLRAGRPVTPSLLVDWSMGIAGGMNYLHLHKIIHRDLKSPNMLITYDDVVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSSCPDGFKILLRQCWNSKPRNRPSFRQILLHLDIASADVLSTPQETYFKSQAEWREEVKLHFEKIKSEGTCLHRLEEELVMRRREELRHALDIREHYERKLERANNLYMELNALMLQLELKERELLRREQALERRCPGLLKPHPSRGLLHGNTMEKLIKKRNVPQKLSPHSKRPDILKTESLLPKLDAALSGVGLPGCPKGPPSPGRSRRGKTRHRKASAKGSCGDLPGLRTAVPPHEPGGPGSPGGLGGGPSAWEACPPALRGLHHDLLLRKMSSSSPDLLSAALGSRGRGATGGAGDPGSPPPARGDTPPSEGSAPGSTSPDSPGGAKGEPPPPVGPGEGVGLLGTGREGTSGRGGSRAGSQHLTPAALLYRAAVTRSQKRGISSEEEEGEVDSEVELTSSQRWPQSLNMRQSLSTFSSENPSDGEEGTASEPSPSGTPEVGSTNTDERPDERSDDMCSQGSEIPLDPPPSEVIPGPEPSSLPIPHQELLRERGPPNSEDSDCDSTELDNSNSVDALRPPASLPP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A2R8Q421)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKCLESPVGKRKRSLAVSSSQDPSFSGLNQLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSGGQGQQAQTPTGKQTDKPKSNMKG
Protein: Kinesin, putative (Q57UV7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Serine/threonine-protein phosphatase
- Uncharacterized protein
Sequence:
MEYKRCNSSRTTASISRSPQLRTSATSTPVRSATPMRTPTSARSGASSARRTLTGTGTGSGALRSVGLDGASPRAKGPGLPRPIAYKRSGTATSGGQVDSGNDMSMVSSRSAIGDSPKGKRGAHKPAVAKTGGNGRVNVYARVRAFSPAETADNQHSAVHLSDNKVEVVVSPKSVYTFMLDGCFSSTGSPSDEGFASQSSVFDAIGRPLAENALAGYNAAIMVYGQTGSGKTYTMFGPPKSLGTEEQGLVPRVCNMIFERADACLQKGITCRVCVSMLEVYLEDVFDLFSNRKQVTVRKDYLDNSFHVVGAKSIPVRQYKDVEELLQRAEALRTFAATAIHARSSRAHALFQLELYTTFESTDIAPRTAKILLADLAGCERIKLAQTETGIPFEEARNINLSLLSLGSCIEAVTMRKGSSQNIPEFRNSTLTKLLKEYLGGNSVSSIVVTVGPSVRDARLSVQSLRFADRAMKVVTHAKINTVKPITELDDADGSEDKVREAYNKKKEALQVEFQVQSELQKLQNKITILECQLMNSVDDEVVARLQEEISTYQKSLADADLELQQQRRVLYDSEVMLEEQLKELNTRMQEMIEENEEATENLLAECRKKHTERLEVEQKRHEEEVDVLLKSHEFELERINQLLQDSDTKCAELTTTLFKTKEDLRKTDGLVDEMQMALEELGDASKATETELYGYVEQLRSENSRLSTAIDTLRQQLKESEASVEDRDNRLKEHEESLDTLRQQLKESEASVEDRDNRLKEHEESLNTLRQQLKESEASVEDRDNRLKEHETSLDTLRQQLKESEASVEDRDNRLKEHEESLNTLRQQLKESEASVEDRDNRLKEHETSLDTLRQQLKESEASVEDRDNRLKEHETSLNTLRQQLKESEASVEDRDNRLKEHEESLNTLRQQLKESEASVENRDNRLKEHEESLNTLRQQLKESEASVEDRDNRLKEHEESLNTLRQQLKESEASVEDRDNRLKEHEESLNTLRQQLKESEASVEDRDNRLKEHEESLNTLRQQLKESEASVEDRDNRLKEHETSLNTLRQQLKESEASVEDRDNRLKEHETSLDTLRQQLKESEASVEDRDNRLKEHEESLDTLRQQLKESEASVEDRDNRLKEHEESLNTLRQQLKESEASVEDRDNRLKEHEESLDTLRQQLKESEASVEDRDNRLKEHETSLDTLRQQLKESEASVEDRDNRLKEHEESLNTLRQQLKESEASVEDRDNRLKEHETSLDTLRQQLKESETTVVVLTADLKQLEEEMFIDQADLKERIAFLEVELKRCEEKGAYYSALVDEMQAELHCANERVAAMSDQVQNMEVRVFDVCGYMFEAFSVKCQDTVSAFASFTKGVTEDLTKGTTERLRLLAEVVELRSSTVARKAATQRRASAVSSLVQSAQEILSKIADEVEDADNFSDRSAVVASFVNSPKESWGADLSPRFTEESLTC
Protein: Amino acid transporter AVT3B (AtAvt3B) (Aromatic and neutral amino acid transporter-like protein 1) (F4ILY9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Translocates preferentially neutral amino acids from the vacuole to the cytoplasm.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:27925655}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phospholipase D beta 1
- Carboxylesterase SOBER1
Sequence:
MGLEEQGRAREDTPLLGKGRPLSSKFKTFANVFIAIVGAGVLGLPYAFKRTGWLMGLLTLFSVAALINHCMMLLVHIRRKLGVSNIGSFGDLGFAACGNLGRFVVDILIILSQAGFCVGYLIFIGNTLANLSKPTKSTTLMSLRHLMGVSPKSLYIWGCFPFQLGLNSIKTLTHLAPLSIFADVVDLGAMAVVIVEDIKITVVQRPQVVAFGGMSVFFYGMGVAVYAFEGVGMVLPLESETKDKDKFGKVLALSMLFIAVMYGSFGVLGYMAFGDDTMDIITANLGAGVVSSLVQLGLCINLFFTFPLMMNPVFEIVERRFWSGMYCVWLRWLLVLAVTLVALLVPNFADFLSLVGSSVCCALGFVLPSLFHLMVFKDEMEWKQRALDVGILLLGVILGVSGTWSSLTEIFQE