wanglab/gogpt-training-data huggingface dataset:
Protein: Agamous-like MADS-box protein AGL81 (Q9FIX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may function in the maintenance of the proper function of the central cell in pollen tube attraction.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Gb|AAF18257.1 hydroxyproline-rich glycoprotein family)
- Late embryogenesis abundant
- Late embryogenesis abundant
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Late embryogenesis abundant
- At5g54370 protein-like protein)
- Late embryogenesis abundant
- Late embryogenesis abundant protein-related / LEA protein-like protein
- Late embryogenesis abundant protein At1g64065
- F6D8.10
Sequence:
MAIRSLPSSSRCSSSSSSSSYSLASTSLSNRLETIFKKASELCTLCDIEACVIYYGPDGELKTWPPEREKVEDIALRYSQLNEALRRKKSVTLYDFLNKKKDKTNLEKKAKITDNDDLKTCLKNVNILKYPLADHYSPDQVSQLIQSLEPHVSKVRERIRFVESQKHKETKPDHQSLASSSLNHQTQSLNPSQFSLFMYNHGDNTLSQIPVSASNFNQDYFSALLEQSELKSQIMKQDLCGYEQNMCMSNHGDATLSQIPLSASNLNQDFSALLQDESGLMQQELCGYDQNMFMNNNNFQHSFVSNTQDHSAPVVQESVNNNYGLMPHVPCGYDQNLFTSDITNNNLLINNSMFL
Protein: WRKY transcription factor 71 (WRKY DNA-binding protein 71) (Q93WV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
Sequence:
MDDHVEHNYNTSLEEVHFKSLSDCLQSSLVMDYNSLEKVFKFSPYSSPFQSVSPSVNNPYLNLTSNSPVVSSSSNEGEPKENTNDKSDQMEDNEGDLHGVGESSKQLTKQGKKKGEKKEREVRVAFMTKSEIDHLEDGYRWRKYGQKAVKNSPYPRSYYRCTTQKCNVKKRVERSFQDPSIVITTYEGKHNHPIPSTLRGTVAAEHLLVHRGGGGSLLHSFPRHHQDFLMMKHSPANYQSVGSLSYEHGHGTSSYNFNNNQPVVDYGLLQDIVPSMFSKNES
Protein: Polyadenylate-binding protein 2 (PABP-2) (Poly(A)-binding protein 2) (P42731)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the cytoplasm, affects both translation and mRNA decay. Stimulates translation by interaction with translation initiation factor eIF4G, a subunit of the cap-binding complex eIF4F, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. During infection with potyvirus TuMV, acts as a potential integral component of the viral replicase complex that could play an important role in the regulation of potyviral RNA-dependent RNA polymerase (RdRp). Binds to uridylated mRNAs and determines the size of uridine extensions. Limits uridine extension by URT1, likely by binding to the oligo(A) tail and preventing URT1 access.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17670821}. Nucleus {ECO:0000269|PubMed:17670821}. Note=In TuMV-infected plants, partially retargeted in cytoplasmic virus-induced vesicles and in the nucleolus.
Interaction partners:
- Eukaryotic translation initiation factor 4E-1
- Eukaryotic translation initiation factor isoform 4E
- mRNA-decapping enzyme-like protein
- AT3g17750/MIG5_4
- DEAD-box ATP-dependent RNA helicase 52
- Eukaryotic translation initiation factor 4G
- Ubiquitin carboxyl-terminal hydrolase 1
- Protein decapping 5
- Protein ECERIFERUM 16
- Regulator of nonsense transcripts 1 homolog
Sequence:
MAQVQLQGQTPNGSTAAVTSAPATSGGATATQFGNTSLYVGDLDFNVTDSQLFDAFGQMGTVVTVRVCRDLVTRRSLGYGYVNFTNPQDAARAIQELNYIPLYGKPIRVMYSHRDPSVRRSGAGNIFIKNLDESIDHKALHDTFSSFGNIVSCKVAVDSSGQSKGYGFVQYANEESAQKAIEKLNGMLLNDKQVYVGPFLRRQERDSTANKTKFTNVYVKNLAESTTDDDLKNAFGEYGKITSAVVMKDGEGKSKGFGFVNFENADDAARAVESLNGHKFDDKEWYVGRAQKKSERETELRVRYEQNLKEAADKFQSSNLYVKNLDPSISDEKLKEIFSPFGTVTSSKVMRDPNGTSKGSGFVAFATPEEATEAMSQLSGKMIESKPLYVAIAQRKEDRRVRLQAQFSQVRPVAMQPSVGPRMPVYPPGGPGIGQQMFYGQAPPAMIPPQPGYGYQQQLVPGMRPGGGPVPSFFMPMVQPQQQRPGGGRRPGGIQHSQQQNPMMQQQMHPRGRMFRYPQGRGGSGDVPPYDMGNNMPLTIGALASNLSNATPEQQRTMLGEVLYPLVEQVEAESAAKVTGMLLEMDQTEVLHLLESPEALKAKVAEAMDVLRSVAAGGATEQLASLNLS
Protein: UV excision repair protein RAD23 (Q9V3W9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367049}. Cytoplasm {ECO:0000256|RuleBase:RU367049}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
- Peptide-N
- Ubiquitin conjugation factor E4 B
- DNA repair protein complementing XP-C cells homolog
- Proteasomal ubiquitin receptor ADRM1 homolog
- 26S proteasome non-ATPase regulatory subunit 14
- Ubiquitin-ribosomal protein eL40 fusion protein
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 4
- 26S proteasome regulatory complex subunit p50
Sequence:
MIITIKNLQQQTFTIEFAPEKTVLELKKKIFEERGPEYVAEKQKLIYAGVILTDDRTVGSYNVDEKKFIVVMLTRDSSSSNRNQLSVKESNKLTSTDDSKQSMPCEEANHTNSPSSTNTEDSVLSRETRPLSSDELIGELAQASLQSRAESNLLMGDEYNQTVLSMVEMGYPREQVERAMAASYNNPERAVEYLINGIPAEEGTFYNRLNESTNPSLIPSGPQPASATSAERSTESNSDPFEFLRSQPQFLQMRSLIYQNPHLLHAVLQQIGQTNPALLQLISENQDAFLNMLNQPIDRESESGATVPPVSNARIPSTLDNVDLFSPDLEVATSAQRSAAGTSAAHQSGSAADNEDLEQPLGVSTIRLNRQDKDAIERLKALGFPEALVLQAYFACEKNEEQAANFLLSSSFDD
Protein: Hemagglutinin-esterase (HE protein) (EC 3.1.1.53) (E3 glycoprotein) (P0C0V9)
Organism: Breda virus 1 (BRV-1)
Function: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-9-di-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. Also hydrolyzes 5-N-acetyl-4-O-acetylneuraminic acid and N-acetyl-9-O-acetylneuraminic acid, but displays a substrate preference for N-acetyl-9-di-O-acetylneuraminic acid. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture. However, its presence in the virus may alter its pathogenicity. May become a target for both the humoral and the cellular branches of the immune system.
Subcellular location: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MLSLILFFPSFAFAATPVTPYYGPGHITFDWCGFGDSRSDCTNPQSPMSLDIPQQLCPKFSSKSSSSMFLSLHWNNHSSFVSYDYFNCGVEKVFYEGVNFSPRKQYSCWDEGVDGWIELKTRFYTKLYQMATTSRCIKLIQLQAPSSLPTLQAGVCRTNKQLPDNPRLALLSDTVPTSVQFVLPGSSGTTICTKHLVPFCYLNHGCFTTGGSCLPFGVSYVSDSFYYGYYDATPQIGSTESHDYVCDYLFMEPGTYNASTVGKFLVYPTKSYCMDTMNITVPVQAVQSIWSEQYASDDAIGQACKAPYCIFYNKTTPYTVTNGSDANHGDDEVRMMMQGLLRNSSCISPQGSTPLALYSTEMIYEPNYGSCPQFYKLFDTSGNENIDVISSSYFVATWVLLVVVVILIFVIISFFC
Protein: Rho guanine nucleotide exchange factor 18 (A0A087WZG4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Cingulin
- Transforming protein RhoA
- Band 4.1-like protein 4B
- Serine/threonine-protein kinase STK11
- InaD-like protein
- Cingulin-like protein 1
- Rho-associated protein kinase 2
- Rho/Rac guanine nucleotide exchange factor 18
- Junctional adhesion molecule A
- Tight junction protein 1
Sequence:
MVTVGTNILPSRPAASANTAREDAALFSRRIPPRHKNGAAQPGAAPGPGAPGANMGNAHSKSGDRHSALPGRPELSFYGSFPRKWSENVFLDNELLTSKILSVLRPQSERGFRAGDLRYPTHFLSTNSVLASVTASLKEHPRGTLLSDGSPALSRNVGMTVSQKGGPQPTPSPAGPGTQLGPITGEMDEADSAFLKFKQTADDSLSLTSPNTESIFVEDPYTASLRSEIESDGHEFEAESWSLAVDAAYAKKQKREVVKRQDVLYELMQTEVHHVRTLKIMLKVYSRALQEELQFSSKAIGRLFPCADDLLETHSHFLARLKERRQESLEEGSDRNYVIQKIGDLLVQQFSGENGERMKEKYGVFCSGHNEAVSHYKLLLQQNKKFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLVERIIQNTEAGTEDYEDLTQALNLIKDIISQVDAKVSECEKGQRLREIAGKMDLKSSSKLKNGLTFRKEDMLQRQLHLEGMLCWKTTSGRLKDILAILLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLQGPEMYEIYTSSKEDRNAWMAHIQRAVESCPDEEEGPFSLPEEERKVVEARATRLRDFQERLSMKDQLIAQSLLEKQQIYLEMAEMGGLEDLPQPRGLFRGGDPSETLQGELILKSAMSEIEGIQSLICRQLGSANGQAEDGGSSTGPPRRAETFAGYDCTNSPTKNGSFKKKVSSTDPRPRDWRGPPNSPDLKLSDSDIPGSSEESPQVVEAPGTESDPRLPTVLESELVQRIQTLSQLLLNLQAVIAHQDSYVETQRAAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAALEKLQSQLRHEQQRWERERQWQHQELERAGARLQEREGEARQLRERLEQERAELERQRQAYQHDLERLREAQRAVERERERLELLRRLKKQNTAPGALPPDTLAEAQPPSHPPSFNGEGLEGPRVSMLPSGVGPEYAERPEVARRDSAPTENRLAKSDVPIQLLSATNQFQRQAAVQQQIPTKLAASTKGGKDKGGKSRGSQRWESSASFDLKQQLLLNKLMGKDESTSRNRRSLSPILPGRHSPAPPPDPGFPAPSPPPADSPSEGFSLKAGGTALLPGPPAPSPLPATPLSAKEDASKEDVIFF
Protein: Protein SGE1 (10-N-nonyl acridine orange resistance protein) (Crystal violet resistance protein) (P33335)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Drug export permease. Multi-copy suppressor of loss-of-function mutation of GAL11. Involved specifically in transcription of GAL4-dependent genes. Can link GAL4 with the basal transcription machinery if GAL11 is missing. Confers resistance to 10-N-nonyl acridine orange (NAO) and in general to cationic dyes.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized transporter YMR279C
- Aminotriazole resistance protein
Sequence:
MKSTLSLTLCVISLLLTLFLAALDIVIVVTLYDTIGIKFHDFGNIGWLVTGYALSNAVFMLLWGRLAEILGTKECLMISVIVFEIGSLISALSNSMATLISGRVVAGFGGSGIESLAFVVGTSIVRENHRGIMITALAISYVIAEGVGPFIGGAFNEHLSWRWCFYINLPIGAFAFIILAFCNTSGEPHQKMWLPSKIKKIMNYDYGELLKASFWKNTFEVLVFKLDMVGIILSSAGFTLLMLGLSFGGNNFPWNSGIIICFFTVGPILLLLFCAYDFHFLSLSGLHYDNKRIKPLLTWNIASNCGIFTSSITGFLSCFAYELQSAYLVQLYQLVFKKKPTLASIHLWELSIPAMIATMAIAYLNSKYGIIKPAIVFGVLCGIVGSGLFTLINGELSQSIGYSILPGIAFGSIFQATLLSSQVQITSDDPDFQNKFIEVTAFNSFAKSLGFAFGGNMGAMIFTASLKNQMRSSQLNIPQFTSVETLLAYSTEHYDGPQSSLSKFINTAIHDVFYCALGCYALSFFFGIFTSSKKTTISAKKQQ
Protein: Large ribosomal subunit protein uL14m (39S ribosomal protein L14, mitochondrial) (L14mt) (MRP-L14) (Q1JQ99)
Organism: Bos taurus (Bovine)
Function: May form part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1, intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279069}.
Interaction partners:
Sequence:
MAFSSGLWGPCVHMSRAFSQRCFSTTGSLGAIQKMTRVRVVDNSALGNTPYHRPPRCIHVYNKNGVGKVGDRILLAIKGQKKKALIVGHRMPGPTMTPRFDSNNVVLIEDNGNPVGTRIKTPIPTSLRQREGEFSKVLAIAQNFV
Protein: Collagen alpha-1(X) chain (Q05306)
Organism: Mus musculus (Mouse)
Function: Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Aggrecan core protein
- Collagenase 3
- Transcription factor SOX-9
- Collagen alpha-2
- Runt-related transcription factor 2
- Collagen alpha-1
- Integrin-binding sialoprotein
- Collagen, type IV, alpha 6
- Indian hedgehog protein
- Collagen alpha-3
Sequence:
MLPQIPFLLLMFLTLVHGMFYAERYQTPTGIKGPLASPKTQYFIPYAIKSKGIPVRGEQGIPGPPGPTGPRGHPGPSGPPGKPGYGSPGLQGEPGLPGPPGISATGKPGLPGPPGKPGERGPYGHKGDIGPAGLPGPRGPPGPPGIPGPAGISVPGKPGQQGLTGAPGPRGFPGEKGAQGAPGVNGRKGETGYGSPGRPGERGLPGPQGPIGPPGPSGVGRRGENGFPGQPGIKGDRGFPGEMGPSGPPGPQGPPGKQGREGIGKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGFGKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTRGPTGPPGVPGFPGSKGDPGNPGAPGPAGIATKGLNGPTGPPGPPGPRGHSGEPGLPGPPGPPGPPGQAVMPDGFIKAGQRPRLSGMPLVSANHGVTGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYTYDEYSKGYLDQASGSAIMELTENDQVWLQLPNAESNGLYSSEYVHSSFSGFLVAPM
Protein: Rab proteins geranylgeranyltransferase component A 2 (Choroideremia-like protein) (Rab escort protein 2) (REP-2) (P26374)
Organism: Homo sapiens (Human)
Function: Substrate-binding subunit (component A) of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Less effective than CHM in supporting prenylation of Rab3 family.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12356470}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- Opsin-3
- Geranylgeranyl transferase type-2 subunit beta
- Ras-related protein Rab-5A
- Ras-related protein Rab-27A
- Ras-related protein Rab-1A
- Ras-related protein Rab-31
- Ras-related protein Rab-1B
- Ras-related protein Rab-7a
- Ras-related protein Rab-32
Sequence:
MADNLPTEFDVVIIGTGLPESILAAACSRSGQRVLHIDSRSYYGGNWASFSFSGLLSWLKEYQQNNDIGEESTVVWQDLIHETEEAITLRKKDETIQHTEAFCYASQDMEDNVEEIGALQKNPSLGVSNTFTEVLDSALPEESQLSYFNSDEMPAKHTQKSDTEISLEVTDVEESVEKEKYCGDKTCMHTVSDKDGDKDESKSTVEDKADEPIRNRITYSQIVKEGRRFNIDLVSKLLYSQGLLIDLLIKSDVSRYVEFKNVTRILAFREGKVEQVPCSRADVFNSKELTMVEKRMLMKFLTFCLEYEQHPDEYQAFRQCSFSEYLKTKKLTPNLQHFVLHSIAMTSESSCTTIDGLNATKNFLQCLGRFGNTPFLFPLYGQGEIPQGFCRMCAVFGGIYCLRHKVQCFVVDKESGRCKAIIDHFGQRINAKYFIVEDSYLSEETCSNVQYKQISRAVLITDQSILKTDLDQQTSILIVPPAEPGACAVRVTELCSSTMTCMKDTYLVHLTCSSSKTAREDLESVVKKLFTPYTETEINEEELTKPRLLWALYFNMRDSSGISRSSYNGLPSNVYVCSGPDCGLGNEHAVKQAETLFQEIFPTEEFCPPPPNPEDIIFDGDDKQPEAPGTNNVVMAKLESSEESKNLESPEKHLQN
Protein: Solute carrier family 13 member 2 (Na(+)/dicarboxylate cotransporter 1) (NaDC-1) (Renal sodium/dicarboxylate cotransporter) (Q13183)
Organism: Homo sapiens (Human)
Function: Low-affinity sodium-dicarboxylate cotransporter, that mediates the entry of citric acid cycle intermediates, such as succinate, citrate, fumarate and alpha-ketoglutarate (2-oxoglutarate) into the small intestine and renal proximal tubule. Transports the dicarboxylate into the cell with a probable stoichiometry of 3 Na(+) for 1 divalent dicarboxylate, rendering the process electrogenic. Citrate is transported in protonated form as a divalent anion, rather than the trivalent form which is normally found in blood. Has a critical role in renal dicarboxylate transport (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:27927654}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sulfate transporter
- Solute carrier family 26 member 6
- Chloride anion exchanger
- Solute carrier family 15 member 5
Sequence:
MATCWQALWAYRSYLIVFFVPILLLPLPILVPSKEAYCAYAIILMALFWCTEALPLAVTALFPLILFPMMGIVDASEVAVEYLKDSNLLFFGGLLVAIAVEHWNLHKRIALRVLLIVGVRPAPLILGFMLVTAFLSMWISNTATSAMMVPIAHAVLDQLHSSQASSNVEEGSNNPTFELQEPSPQKEVTKLDNGQALPVTSASSEGRAHLSQKHLHLTQCMSLCVCYSASIGGIATLTGTAPNLVLQGQINSLFPQNGNVVNFASWFSFAFPTMVILLLLAWLWLQILFLGFNFRKNFGIGEKMQEQQQAAYCVIQTEHRLLGPMTFAEKAISILFVILVLLWFTREPGFFLGWGNLAFPNAKGESMVSDGTVAIFIGIIMFIIPSKFPGLTQDPENPGKLKAPLGLLDWKTVNQKMPWNIVLLLGGGYALAKGSERSGLSEWLGNKLTPLQSVPAPAIAIILSLLVATFTECTSNVATTTIFLPILASMAQAICLHPLYVMLPCTLATSLAFMLPVATPPNAIVFSFGDLKVLDMARAGFLLNIIGVLIIALAINSWGIPLFSLHSFPSWAQSNTTAQCLPSLANTTTPSP
Protein: Kappa-actitoxin-Bcs4a (Kappa-AITX-Bcs4a) (Potassium channel toxin BcsTx3) (C0HJC4)
Organism: Bunodosoma caissarum (Sea anemone)
Function: Inhibits voltage-gated potassium channels (Kv1/KCNA). Is potent on Drosophila Shaker IR channels (IC(50)=94.25 nM), and rKv1.2/KCNA2 (IC(50)=172.59 nM), and moderately active on hKv1.3/KCNA3 (IC(50)=1006.48 nM), rKv1.6/KCNA6 (IC(50)=2245.93 nM), and Kv1.1/KCNA1 (IC(50) around 3 uM). In vivo, induces a rapid increase in swimming speed on zebrafish larvae, as well as death which occurs between 2 and 18 hours later (By similarity). Also paralyzes swimming crabs (C.danae) when injected at the junction between the body and the walking leg.
Subcellular location: Secreted {ECO:0000269|PubMed:23895459}. Nematocyst {ECO:0000269|PubMed:23895459}.
Interaction partners:
Sequence:
GCKGKYEECTRDSDCCDEKNRSGRKLRCLTQCDEGGCLKYRQCLFYGGLQ
Protein: Autophagy-related protein (Q582K5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Autophagocytosis associated protein, putative
- Cysteine protease
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy-related protein
- Autophagy-related protein
- Cysteine protease
- Protein kinase, putative
- non-specific serine/threonine protein kinase
- Uncharacterized protein
- FUN14 family
Sequence:
MKYNFKDSHSLVKRLNESAKVRKSHPNHFPVICEKVYNSDIGELDRCKFLVPSDLTVGQFVSVLRKRVQLEAESALFVYTNDTVLPSSAQMADIYSKYKDEDGFLYMKYSGEAAFG
Protein: GH26613p (Q961F7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAIENLIGRRLCDMVNSGSSALGQSQSHSQSQHQSVGLFAEWSHLSRDTAEIERSNLVNICKLVVKELLEQSLRYGRMLDSDHLPLQHFFIVIEHVLGHGLRPKKGLLGPRKELWDLLQSVEHYCPEAQDITASVRDLPTVRTHIGRARAWLRIALMQKKLSDYLQALIEHREDSLFDYYEPHALMMSDEIVVIMGILVGLNVIDCNLCVKEEDLDSQQGVIDFSLYLRSSSRNADAAPEDSAPPALLDATGQGNMIAVLDQKNYIEELNRHLNATVGNLQAKVESLTTTNALMKEDLAIARNSLLALQAENQAMRQSTSAGDNNSTGSGGSSDKDKEKASEELVEERRKNSELEKELKLQVSLKAESDMAMKLLEKDIHEKQDTIVSLRRQLDDIKQINLEMYRKLQECEDELTQKGEMVSRLQTKASQIGNILQSLEKKYESKLIDQQHHGPGSGSGTGAGTGAGNGAIGGDRSPNTRRQQNLEKFEALTKKHKQDAGPPMKRMHLKMDAFPPFDPSKYRKSPRQPDAPNTEELQQSKDAKTPTSAKSLNDELAEAAAAVTQHFGVDASQSDYVLCREQAADGET
Protein: RAN binding protein 1 (F6WQW2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGSALGRARRTLSGRPFQRAPCKTRRALSLSAALRNVTKAQGGCPKSLVLWGCRPKRPRKRRTSLKLAWRGTFCSSSLKISEDTHEDHDTSTENTDESNHDPQFEPIVSLPEQEIKTLEEDEEELFKMRAKLFRFASENDLPEWKERGTGDVKLLKHKEKGAIRLLMRRDKTLKICANHYITPMMELKPNAGSDRAWVWNTHADFADECPKPELLAIRFLNAENAQKFKTKFEECRKEIEEREKKAGSGKNDHAEKVAEKLEALSVKEETKEDAEEKQ
Protein: Cytochrome P450 2B1 (EC 1.14.14.1) (CYPIIB1) (Cytochrome P450-B) (Cytochrome P450b) (Cytochrome P450-LM2) (Cytochrome P450-PB1) (Cytochrome P450-PB2) (P00176)
Organism: Rattus norvegicus (Rat)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Mitochondrion inner membrane {ECO:0000305|PubMed:19401463}; Peripheral membrane protein {ECO:0000305|PubMed:19401463}. Note=Post-translationally targeted to mitochondria. Requires the cytosolic chaperones HSP70 and HSP90, for initial targeting to mitochondria, and then requires all three of the receptor proteins in the TOM complex, TOMM70, TOMM20 and TOMM22 for translocation across the mitochondrial outer membrane. After translocation into the matrix, associates with the inner membrane as a membrane extrinsic protein. {ECO:0000305|PubMed:19401463}.
Interaction partners:
- Cytochrome P450 1A1
- Cytochrome P450 1A2
- Bifunctional epoxide hydrolase 2
- Cytochrome P450 2E1
- Cytochrome P450 2U1
- Cytochrome b5 type B
- Cytochrome b5
- Polyunsaturated fatty acid lipoxygenase ALOX15B
- Polyunsaturated fatty acid 5-lipoxygenase
- Arachidonate 12-lipoxygenase, 12R-type
Sequence:
MEPTILLLLALLVGFLLLLVRGHPKSRGNFPPGPRPLPLLGNLLQLDRGGLLNSFMQLREKYGDVFTVHLGPRPVVMLCGTDTIKEALVGQAEDFSGRGTIAVIEPIFKEYGVIFANGERWKALRRFSLATMRDFGMGKRSVEERIQEEAQCLVEELRKSQGAPLDPTFLFQCITANIICSIVFGERFDYTDRQFLRLLELFYRTFSLLSSFSSQVFEFFSGFLKYFPGAHRQISKNLQEILDYIGHIVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHENLMISLLSLFFAGTETSSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRSKMPYTDAVIHEIQRFSDLVPIGVPHRVTKDTMFRGYLLPKNTEVYPILSSALHDPQYFDHPDSFNPEHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVSSHLAPKDIDLTPKESGIGKIPPTYQICFSAR
Protein: Intraflagellar transport protein 81 (Q68RJ5)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region. Required for ciliogenesis.
Subcellular location: Cell projection, cilium {ECO:0000305|PubMed:23990561}.
Interaction partners:
Sequence:
MGDVSYIVDSLGLPPFSYQMSLLSFTEKGPQELLQLLSDVFSTISPKHQKVDVAKEVPDQTADRLIGFLKIIKYRPNVQDPLLFRQLVAAGDRETLYQILRWVVPQAQLLEKRAFVGYYLSFPDMPEEFNFDPDIMELKEEIKAMQQEFIELHKSSDAIKTLSKDTQALKNKIKSLEEEKERLGEKVERAKGAVDKLPDRSSYMEVCTNLRKQQDEEVNLSTAIQTQRALQEKAEASYHRAAARLRELQTSYQEGSAGKLLETLNEDVKNLRAQVNERYPKEVEKRQKRQAALSEALASGISTEMDLQRLQHQATALHNQITEIQERKVAQDKARQGDKAYLQLRQAQQMATVSARKKEELGAKQERLQEKKTALTAQLDKLNAEGGGSGAVFSEEEWRTKYESMKSKLPIYKKMKKELGDLEAEVFVLAHTEELLASQEGGLLEKVKRLEKQQGISGFTETAQHLEKVSEAKSQMDEEKGMTLIEISRTVEEINNAINQRKQQLAPQIKKLRSVRQDFAEFEAKYLEKKTAYDNVVATFEARTSALEGEVSGLKAEVSENETKYHMLHCQLHITDQNIKKVTSGPAAERLRDKYEAKVKEAEDSTKALRDRQREIKDTHSTGLSQIDIMNDMLRLLQLKLNLARGIAVDMSQYGGGGGAAGGANGGMAGQTYDTGSANVLQL
Protein: Decapping mRNA 2 (cDNA FLJ52185, highly similar to mRNA decapping enzyme 2) (B7Z3U5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSDNGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKPYNNHSEMSDLLKGKNQSMRGNGRKQYQDSPNQKKRTNGLQPAKQQNSLMKCEKKLHPRKLQDNFETDAVYDLPSSSEDQLLEHAEGQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL
Protein: Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.27, EC 1.14.11.79) (Q9JJF3)
Organism: Mus musculus (Mouse)
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation. Also catalyzes demethylation of non-histone proteins, such as CGAS: demethylation of monomethylated CGAS promotes interaction between CGAS and PARP1, followed by PARP1 inactivation. Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis (By similarity). Participates in MYC-induced transcriptional activation (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14742713}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19927124}.
Interaction partners:
- PHD finger protein 19
- Large ribosomal subunit protein uL2
- Transcription factor Sp7
- 2-oxoglutarate and iron-dependent oxygenase JMJD4
- Large ribosomal subunit protein uL15
- tRNA wybutosine-synthesizing protein 5
Sequence:
MDELPNGNGAALLKRGRGRRRRHPQSQPRGASVLALPLRPRKIRRHRKSAAASRVAALRARALRSEDSDSKVAVASVRGKRKRPAELLEASRSAEPRPVSARPRSASATLPSRVEGWAALSRNLGTAAPPPPGSHADEPGRPRASPLQQVLTELNGIPSSRRRAARLFEWLLAPLPPDHFYRRLWEREAVLVRRQDRSYYEGLFSTADLDSMLRYEDVQFGQHLDAARYVDGRRETLNPPGRALPAAAWSLYRAGCSLRLLCPQAFSPTVWQFLAVLQEQFGSMAGSNVYLTPPDSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRDPSEELALTSSPNFSQEDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTYQRNTWGDFLEAVLPLAVQAAIEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVHGLPVRWEAGEPVNVGAQLTTETQVHMLQDGVARLVGEGGRLFLYHTVENSRVYHLEEPKCLEIHPQQADAMELLLRSYPEFVRVGDLPCDSVEDQLSLATMLYDKGLLLTKTPLVPS
Protein: Epsin 2 (E9PBC1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTTSSIRRQMKNIVNNYSEAEIKVREATSNDPWGPSSSLMTEIADLTYNVVAFSEIMSMVWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCRENIFAIQTLKDFQYIDRDGKDQGINVREKSKQLVALLKDEERLKAERAQALKTKERMAQVATGMGSNQITFGRGSSQPNLSTSHSEQEYGKAGGSPASYHGSPEASLCPQHRTGAPLGQSEELQPLSQRHPFLPHLGLASRPNGDWSQPCLTCDRAARATSPRVSSELEQARPQTSGEEELQLQLALAMSREVAEQEERLRRGDDLRLQMALEESRRDTVKIPKKKEHGSLPQQTTLLDLMDALPSSGPAAQKAEPWGPSASTNQTNPWGGPAAPASTSDPWPSFGTKPAASIDPWGVPTGATVQSVPKNSDPWAASQQPASSAGKRASDAWGAVSTTKPVSVSGSFELFSNLNGTIKDDFSEFDNLRTSKKTGMQGLTGLLFTMEI