wanglab/gogpt-training-data huggingface dataset:
Protein: Achaete-scute complex protein T4 (Protein scute) (P10084)
Organism: Drosophila melanogaster (Fruit fly)
Function: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system. Also involved in sex determination and dosage compensation.
Interaction partners:
- Achaete-scute complex protein T5
- Protein extra-macrochaetae
- Protein atonal
- Protein daughterless
- Zinc finger protein sens
- Achaete-scute complex protein T3
- Protein sex-lethal
- Enhancer of split m7 protein
- Protein sisterless A
- Basic helix-loop-helix transcription factor amos
Sequence:
MKNNNNTTKSTTMSSSVLSTNETFPTTINSATKIFRYQHIMPAPSPLIPGGNQNQPAGTMPIKTRKYTPRGMALTRCSESVSSLSPGSSPAPYNVDQSQSVQRRNARERNRVKQVNNSFARLRQHIPQSIITDLTKGGGRGPHKKISKVDTLRIAVEYIRRLQDLVDDLNGGSNIGANNAVTQLQLCLDESSSHSSSSSTCSSSGHNTYYQNTISVSPLQQQQQLQRQQFNHQPLTALSLNTNLVGTSVPGGDAGCVSTSKNQQTCHSPTSSFNSSMSFDSGTYEGVPQQISTHLDRLDHLDNELHTHSQLQLKFEPYEHFQLDEEDCTPDDEEILDYISLWQEQ
Protein: Heparan N-sulfatase (N-sulfoglucosamine sulfohydrolase (sulfamidase)) (Q9EQ08)
Organism: Mus musculus (Mouse)
Interaction partners:
- Heparan-alpha-glucosaminide N-acetyltransferase
- Alpha-L-iduronidase
- Alpha-N-acetylglucosaminidase
- Formylglycine-generating enzyme
- Sodium-independent sulfate anion transporter
Sequence:
MHCPGLACCTILLVLGLCGAHSRNVLLIVADDGGFESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFDKVQSLPLLLNQAGVRTGIIGKKHVGPETVYPFDFAFTEENSSVMQVGRNITRIKQLVQKFLQTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFGNGESGMGYIPDWTPQIYDPQDVMVPYFVPDTPAARADLAAQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPQRWGQVSDAYVSLLDLTPTILDWFSIPYPSYAIFGSKTIQLTGRSLLPALEAEPLWATVFSSQSHHEVTMSYPMRSVYHQNFRLIHNLSFKMPFPIDQDFYVSPTFQDLLNRTTTGRPTGWYKDLHRYYYRERWELYDISRDPRETRNLAADPDLAQVLEMLKAQLVKWQWETHDPWVCAPDGVLEEKLTPQCRPLHNEL
Protein: CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (EC 2.4.3.6) (Beta-galactoside alpha-2,3-sialyltransferase 3) (Alpha 2,3-ST 3) (Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (ST3Gal III) (ST3GalIII) (ST3N) (Sialyltransferase 6) (P97325)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc.
Subcellular location: Membrane; Single-pass type II membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Interaction partners:
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Galactoside alpha-
- Beta-1,3-galactosyltransferase 1
- Galactoside alpha-
- Beta-1,3-galactosyltransferase 5
- Beta-galactoside alpha-2,6-sialyltransferase 1
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
- Beta-1,4-galactosyltransferase 3
- Beta-1,3-galactosyltransferase 2
Sequence:
MGLLVFVRNLLLALCLFLVLGFLYYSAWKLHLLQWEDSNSLLLSLDSAGQTLGTEYDRLGFLLKLDSKLPAELATKYANFSEGACKPGYASAMMTAIFPRFSKPAPMFLDDSFRKWARIREFVPPFGIKGQDNLIKAILSVTKEYRLTPALDSLHCRRCIIVGNGGVLANKSLGSRIDDYDIVIRLNSAPVKGFERDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKWLKYIVYKERVSASDGFWKSVATRVPKEPPEIRILNPYFIQEAAFTLIGLPFNNGLMGRGNIPTLGSVAVTMALHGCDEVAVAGFGYDMNTPNAPLHYYETVRMAAIKESWTHNIQREKEFLRKLVKARVITDLSSGI
Protein: ATP synthase F(0) complex subunit f, mitochondrial (ATP synthase membrane subunit f) (Q28851)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion. Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
Sequence:
MASVVPLKEKKLLEVKLGELPSWILMRDFTPSGIAGAFQRGYYRYYNKYVNVKKGSIAGLSMVLAAYVFLNYCRSYKELKHERLRKYH
Protein: Protoporphyrinogen IX dehydrogenase [quinone] (EC 1.3.5.3) (Protoporphyrinogen IX dehydrogenase [menaquinone]) (Protoporphyrinogen IX dehydrogenase [ubiquinone]) (Protoporphyrinogen oxidase) (PPO) (Q4QIU7)
Organism: Leishmania major
Function: In E.coli extracts under anerobic conditions catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX, transferring electrons to fumarate reductase, presumably via menaquinone. In vitro under aerobic conditions forms protoporphyrin IX using ubiquinone as an electron acceptor. Complements an E.coli hemG deletion, allowing normal growth in vivo.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Oxygen-dependent coproporphyrinogen-III oxidase
- Ferrochelatase-like protein
- Transmembrane protein
- Cytochrome b5 heme-binding domain-containing protein
Sequence:
MASQSPKCLMLYSTTDGHTKTIMDTIARQLADETKVRCDVVDIKDGNSYVLADYEKVLLGASIRYGHFSAAFINYVKQHHSELSAMPSAFFSVNLTARKLDKNTATTNVYTRKFLNQSSWSPQLVGVFAGALWYPRYNFFDRVLIQFIMKVTGGETDSTKEIVYTDWAAVRRFASDFAALPLAVPPRPKANTVEKPDGILRSGSGAHCLLAIVGMSAAVIVGIRIIAAKRG
Protein: Prosalusin (Torsin family 2 member A) (Torsin-2A) [Cleaved into: Salusin-alpha; Salusin-beta] (Q8N2E6)
Organism: Homo sapiens (Human)
Function: Salusins -alpha and -beta may be endocrine and/or paracrine factors able to increase intracellular calcium concentrations and induce cell mitogenesis. Salusins may also be potent hypotensive peptides.
Subcellular location: Secreted {ECO:0000269|PubMed:12910263}.
Interaction partners:
Sequence:
MAAATRGCRPWGSLLGLLGLVSAAAAAWDLASLRCTLGAFCECDFRPDLPGLECDLAQHLAGQHLAKALVVKALKAFVRDPAPTKPLVLSLHGWTGTGKSYVSSLLAHYLFQGGLRSPRVHHFSPVLHFPHPSHIERYKKDLKSWVQGNLTACGRSLFLFDEMDKMPPGLMEVLRPFLGSSWVVYGTNYRKAIFIFIRWLLKLGHHGRAPPRRSGALPPAPAAPRPALRAQRAGPAGPGAKG
Protein: Tubulin-folding cofactor B (Cytoskeleton-associated protein 1) (Cytoskeleton-associated protein CKAPI) (Tubulin-specific chaperone B) (Q5E951)
Organism: Bos taurus (Bovine)
Function: Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer. Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99426}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99426}. Note=Colocalizes with microtubules. In differentiated neurons, located in the cytoplasm. In differentiating neurons, accumulates at the growth cone. {ECO:0000250|UniProtKB:Q99426}.
Interaction partners:
- Tubulin-specific chaperone D
- Tubulin-specific chaperone E
- Tubulin-specific chaperone C
- Tubulin-specific chaperone A
- Tubulin-specific chaperone cofactor E-like protein
- Tubulin-specific chaperone A
- ADP-ribosylation factor-like protein 2
- G patch domain-containing protein 4
- AP-2 complex subunit sigma
Sequence:
MEVTGLSAPTVNVFISSSLNSFRSQKRYSRSLTVAEFKCKLQLVVGSPASCMELELYGPDDKFCCKLDQDDALLGSYPVDDGCRIHVIDHSGARLGEYEDISKVEKYEISQEAYEQRQDSIRSFLKRNKLGRFNEEERAQQEAENSQRLIEEEAQASTIPVGSRCEVRTPGQPPRRGTVMYVGLTDFKPGYWIGIRYDEPLGKNDGSVNGKRYFECQAKYGAFVKPSVVTVGDFPEEDYGLDEM
Protein: Sarcalumenin (Q7TQ48)
Organism: Mus musculus (Mouse)
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P13666}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P13666}; Peripheral membrane protein {ECO:0000250|UniProtKB:P13666}. Note=May associate with the sarcoplasmic reticulum membrane, via a calcium-dependent mechanism. {ECO:0000250|UniProtKB:P13666}.
Interaction partners:
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Calsequestrin-1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Ryanodine receptor 1
- Triadin
- Synaptophysin-like protein 2
Sequence:
MKALLLLCCFLASLLLSGQAEVEDASEEAPLRDRSHIDKTLMLNEDKPADDYSAVLQRLRKIYHTSIKPLEQSYKYNELRQHEITDGEITSKPMVLFLGPWSVGKSTMINYLLGLEDTRYQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLIGIEVPHKLLERVTFVDTPGIIENRKQQERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRIILNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQDYKPDTHRELFLKEEISLLEDLNQVIENRLENKIAFIRQHAIRVRIHALLVDRYLQTYKDKMTFFSDGELVFKDIVEDPDKFYIFKTILAKTNVSKFDLPNREAYKDFFGINPISNFKLLSQQCSYMGGCFLEKIERAITQELPSLLGSIGLGKNPGAPNCDKTGCGETPKNRYKKH
Protein: Collagen type VI alpha 2 chain (A0A8I6ALT7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTTTTKMLQGSFSVLLLGGLLGVLHAQQQEAISPDISTTDRNNNCPEKADCPVNVYFVLDTSESVAMQSPTDSLLYHMQQFVPQFISQLQNEFYLEQVALSWRYGGLHFSDQVEVFSPPGSDRASFTKSLQGIRSFRRGTFTDCALANMTQQIRQHVGRGVVNFAVVITDGHVTGNPCGGIKMQAERAREEGIRLFAVAPNRNLNEQGLRDIANTPHELYRNNYATMRPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPHGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKASSLPRTGMGEGKGREFGAVPLGKLGRIGPPGCKGDPGSRGPDGYPGEAGSPGEQGDQGAKVRAWLDGYRGNSGAPGSPGVKGGKGGPGPRGPKGEPVNGSELLLGPNLTRPVFSQGDPGPEGPRGLAGEIGSKGAKGDRGLPGPRGPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYPGPRGTPVSPGGRGDFGLKGAPGRKGEKGEPADPGPPGEPGPRGPRGIPGPEVNPALAPMGVVFQECDVMTYVRETCGCCDCEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRLGAIAKDPKSETGTRVGVVQYSHEGTFEAIRLDDERVNSLSSFKEAVKNLEWIAGGTWTPSALKFAYNQLIKESRRQKTRVFAVVITDGRHDPRDDDLNLRALCDRDVTVTAIGIGDMFHETHESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPELPCQTELYVAQCTQRPVDIVFLLDGSERLGEQNFYKARRFVEEVSRRLTLARRDDDPLNARMALLQYGSQNQQQVAFPLTYNVTTIHEALERTTYLNSFSHVGTGIVHAINNVVRGARGGARRHAELSFVFLTDGVTGNDSLEESVHSMRKQNVVPTVVAVGGDVDMDVLTKISLGDRAAIFREKDFDSLAQPSFFDRFIRWIC
Protein: Arachidonate 12-lipoxygenase, 12R-type (12R-LOX) (12R-lipoxygenase) (EC 1.13.11.-) (Epidermis-type lipoxygenase 12) (O75342)
Organism: Homo sapiens (Human)
Function: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species. In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
Interaction partners:
- Cytochrome P450 4F2
- Cytochrome P450 4F3
- Polyunsaturated fatty acid lipoxygenase ALOX12
- Prostaglandin G/H synthase 2
- Prostaglandin G/H synthase 1
- Magnesium transporter NIPA4
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Cytochrome P450 4A22
- Polyunsaturated fatty acid 5-lipoxygenase
- Cytochrome P450 2J2))
Sequence:
MATYKVRVATGTDLLSGTRDSISLTIVGTQGESHKQLLNHFGRDFATGAVGQYTVQCPQDLGELIIIRLHKERYAFFPKDPWYCNYVQICAPNGRIYHFPAYQWMDGYETLALREATGKTTADDSLPVLLEHRKEEIRAKQDFYHWRVFLPGLPSYVHIPSYRPPVRRHRNPNRPEWNGYIPGFPILINFKATKFLNLNLRYSFLKTASFFVRLGPMALAFKVRGLLDCKHSWKRLKDIRKIFPGKKSVVSEYVAEHWAEDTFFGYQYLNGVNPGLIRRCTRIPDKFPVTDDMVAPFLGEGTCLQAELEKGNIYLADYRIMEGIPTVELSGRKQHHCAPLCLLHFGPEGKMMPIAIQLSQTPGPDCPIFLPSDSEWDWLLAKTWVRYAEFYSHEAIAHLLETHLIAEAFCLALLRNLPMCHPLYKLLIPHTRYTVQINSIGRAVLLNEGGLSAKGMSLGVEGFAGVMVRALSELTYDSLYLPNDFVERGVQDLPGYYYRDDSLAVWNALEKYVTEIITYYYPSDAAVEGDPELQSWVQEIFKECLLGRESSGFPRCLRTVPELIRYVTIVIYTCSAKHAAVNTGQMEFTAWMPNFPASMRNPPIQTKGLTTLETFMDTLPDVKTTCITLLVLWTLSREPDDRRPLGHFPDIHFVEEAPRRSIEAFRQRLNQISHDIRQRNKCLPIPYYYLDPVLIENSISI
Protein: Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) (Q9VYD5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha
- cystathionine gamma-lyase
- hydroxymethylglutaryl-CoA lyase
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- L-serine deaminase
- GCS light chain
- Delta-1-pyrroline-5-carboxylate synthase
- Glutamate--cysteine ligase
- 2-hydroxyacyl-CoA lyase
Sequence:
MTTKMAINAKDIFRNQHRLIRFLEQSIRLCSNQSLKAAQAAQLQQKSSADFEITASLDAQYTSAPEPIKHDKNLGHQFRASQISVRLAAPEQLQPKPDNDEELGFGRLFTDHMLKIYYHKSLGGWQRPEITPLENLVMHPAAKVLHYAVELFEGMKAYRGVDGKIRIFRPDMNMNRMNLAAQRSGLPTFEGKEFVQCLSRLLSIDSEWVPHTDTASLYIRPTLIGIDPTLGVASSDSALLYTILSPVGSYFKTGSSGAVSLLADPSYVRAWPGGVGNRKMGSNYAPTINVQKEAAAKGLQQVLWLYGEDHQLTEVGTMNIFMFFVNDQGEQELVTPPLSGLILPGITRDSILRMTRQWGKFKVSEANITMPMVCELLNQGRLLELFGAGTACVVSPVNRISYLGQDLYIPTMEQEKPVHELIRETLTDIQYGRVDHPWAVVID
Protein: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2) (P12695)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Increased recombination centers protein 15
- 2-oxoglutarate dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Pyruvate dehydrogenase complex protein X component, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Citrate synthase, peroxisomal
- Citrate synthase, mitochondrial
Sequence:
MSAFVRVVPRISRSSVLTRSLRLQLRCYASYPEHTIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKDIPVNKPIAVYVEDKADVPAFKDFKLEDSGSDSKTSTKAQPAEPQAEKKQEAPAEETKTSAPEAKKSDVAAPQGRIFASPLAKTIALEKGISLKDVHGTGPRGRITKADIESYLEKSSKQSSQTSGAAAATPAAATSSTTAGSAPSPSSTASYEDVPISTMRSIIGERLLQSTQGIPSYIVSSKISISKLLKLRQSLNATANDKYKLSINDLLVKAITVAAKRVPDANAYWLPNENVIRKFKNVDVSVAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVNMFTSIINPPQSTILAIATVERVAVEDAAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL
Protein: Probable WRKY transcription factor 34 (WRKY DNA-binding protein 34) (O65590)
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.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9SI37}.
Interaction partners:
- VQ motif-containing protein 20
- Agamous-like MADS-box protein AGL30
- Transmembrane protein, putative
- Agamous-like MADS-box protein AGL65
- Agamous-like MADS-box protein AGL66
- AGAMOUS-like 94
- Agamous-like MADS-box protein AGL104
- Pentatricopeptide repeat-containing protein At3g04760
Sequence:
MAGIDNKAAVMGEWFDCSTTNHRKRSKAELGREFSLNYIKNEDSLQTTFQESSRGALRERIAARSGFNAPWLNTEDILQSKSLTISSPGLSPATLLESPVFLSNPLLSPTTGKLSSVPSDKAKAELFDDITTSLAFQTISGSGLDPTNIALEPDDSQDYEERQLGGLGDSMACCAPADDGYNWRKYGQKLVKGSEYPRSYYKCTHPNCEAKKKVERSREGHIIEIIYTGDHIHSKPPPNRRSGIGSSGTGQDMQIDATEYEGFAGTNENIEWTSPVSAELEYGSHSGSMQVQNGTHQFGYGDAAADALYRDENEDDRTSHMSVSLTYDGEVEESESKRRKLEAYATETSGSTRASREPRVVVQTTSDIDILDDGYRWRKYGQKVVKGNPNPRSYYKCTANGCTVTKHVERASDDFKSVLTTYIGKHTHVVPAARNSSHVGAGSSGTLQGSLATQTHNHNVHYPMPHSRSEGLATANSSLFDFQSHLRHPTGFSVYIGQSELSDLSMPGLTIGQEKLTSLQAPDIGDPTGLMLQLAAQPKVEPVSPQQGLDLSASSLICREMLSRLRQI
Protein: ETS domain-containing protein (LIN-1) (G5EDL0)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
- Mitogen-activated protein kinase mpk-1
- Protein let-418
- Protein lin-9
- Mitogen-activated protein kinase pmk-3
- Mitogen-activated protein kinase pmk-1
- Mitogen-activated protein kinase pmk-2
- GLH-binding kinase 1
- Stress-activated protein kinase jnk-1
- Stress-activated protein kinase JNK
- Probable histone-binding protein lin-53
Sequence:
MNHIDLLKVKKEPPSSSEEAEEEESPKHTIEGILDIRKKEMNVSDLMCTRSSTPPTSSSVDSIITLWQFLLELLQQDQNGDIIEWTRGTDGEFRLIDAEAVARKWGQRKAKPHMNYDKLSRALRYYYEKNIIKKVIGKKFVYRFVTTDAHAPPTADFSSNMNMKMCYVKDEKDIRHEIPSFMTSLQAPPPPPPPPQNPRGNTDFSALSLLGTDSPTTHSVSTPSPTDSVCSPSSSVASSATPSTSSPVDESRQCRKRSLSPSTTSSTTAPPPPPQPPTKKGMKPNPLNLTATSNFSLQPSISSPLLMLQQHHQNSPLFQAQISQLYTYAALASAGLYGPQISPHLASQSPFRSPLVTPKNLGLGELGSSGRTPGLGESQVFQFPPVSAFQATNPLLNTFSNLISPMAPFMMPPSQSSTSFKFPSSTDSLKTPTVPIKMPTL
Protein: Protein Tax-1 (Protein X-LOR) (Protein PX) (Trans-activating transcriptional regulatory protein of HTLV-1) (P14079)
Organism: Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A) (HTLV-1)
Function: Transcriptional activator that activates both the viral long terminal repeat (LTR) and cellular promoters via activation of CREB, NF-kappa-B, SRF and AP-1 pathways. Binds to three 21 bp repeat elements located within the LTRs, referred to as Tax-responsive elements (TRE). Binding to TRE requires the interaction with CREB1 and CREBBP. Also induces chromatin remodeling of proviral LTR-mediated gene expression by recruiting the histone acetyl transferases CREBBP and EP300 to the chromatin, which results in histone acetylation. Via its interaction with IKK regulatory subunit IKBKG, Tax-1 persistently stimulates I-kappa-B kinase (IKK), resulting in constitutive activation of the transcription factor NF-kappa-B. Induction of the nuclear expression of members of the NFkB family of transcription factors, which leads to up-regulated expression of many gene promoters containing NFkB motifs. These genes include those encoding IL2, IL15, IL2RA and IL15RA, leading to autocrine IL2/IL2RA and IL15/IL15RA loops. The resulting T-cell proliferation leads to malignant transformation and to the development of adult T-cell leukemia (ATL). IL13, known to be linked to leukemogenesis, is also up-regulated by Tax-1. Interaction with PDZ domain-containing proteins induce IL2-independent growth, which may be a factor in multi-step leukemogenesis. Inhibits the action of at least three cellular tumor suppressors p53/TP53, RB1 and DLG1, and suppresses their abilities to dictate apoptosis in primary cells. Required for viral replication (By similarity).
Subcellular location: Host nucleus {ECO:0000269|PubMed:14679154}. Host cytoplasm {ECO:0000269|PubMed:14679154}. Note=Shuttles from the host nucleus to the cytoplasm. Found predominantly in the nucleus, where it is equally distributed between the nucleoplasm and the nuclear matrix. {ECO:0000250|UniProtKB:P03409}.
Interaction partners:
Sequence:
MAHFPGFGQSLLFGYPVYVFGDCVQGDWCPISGGLCSARLHRHALLATCPEHQITWDPIDGRVIGSALQFLIPRLPSFPTQRTSKTLKVLTPPITHTTPNIPPSFLQAMRKYSPFRNGYMEPTLGQHLPTLSFPDPGLRPQNLYTLWGGSVVCMYLYQLSPPITWPLLPHVIFCHPGQLGAFLTNVPYKRIEKLLYKISLTTGALIILPEDCLPTTLFQPARAPVTLTAWQNGLLPFHSTLTTPGLIWTFTDGTPMISGPCPKDGQPSLVLQSSSFIFHKFQTKAYHPSFLLSHGLIQYSSFHNLHLLFEEYTNIPISLLFNEKEADDNDHEPQISPGGLEPLSEKHFRETEV
Protein: SET domain-containing protein (Q57ZV3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTGADEKPREVSETTSVRYIDGRRGRGLIAEVDFEADSTILCVPYDIAVLYSPFVRNTCYRCFVSVPKDSRTSQGRGSLQRKRPQQRRPTSQSQRLPLRRSYPQHGRQTSNERNREREEHHYECTDCKHLVLCENCVRELAEGVPRVPVGDEPSKPATSLTWQEQLEVMQQHPLLQAHKQACAWFCSLPESDREGDTDYLRFALQYGSRALLGDTALLLSVGELCTNATQQPPAARQFCTSFARRVADTFAPQGFRVDADHLRDVLFRTKCNSIGYPFNETETLGWMMQEKLCMINHSCDPNAAIVRPRRIEASTSSRSAACSVELLARRRIKAGEEITIAYIDVDRYEDTQIRRRHLLESYWFLCMCSRCEVSANPTAPTRSPPAVPHKGNPTKTKNKKRRNGRQW
Protein: Carbohydrate sulfotransferase 14 (EC 2.8.2.35) (Dermatan 4-sulfotransferase 1) (D4ST-1) (hD4ST1) (Q8NCH0)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. Appears to have an important role in the formation of the cerebellar neural network during postnatal brain development.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Zinc finger protein 469
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- Carbohydrate sulfotransferase 15
- Dermatan-sulfate epimerase
- Beta-1,4-galactosyltransferase 7
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Beta-1,3-galactosyltransferase 6
Sequence:
MFPRPLTPLAAPNGAEPLGRALRRAPLGRARAGLGGPPLLLPSMLMFAVIVASSGLLLMIERGILAEMKPLPLHPPGREGTAWRGKAPKPGGLSLRAGDADLQVRQDVRNRTLRAVCGQPGMPRDPWDLPVGQRRTLLRHILVSDRYRFLYCYVPKVACSNWKRVMKVLAGVLDSVDVRLKMDHRSDLVFLADLRPEEIRYRLQHYFKFLFVREPLERLLSAYRNKFGEIREYQQRYGAEIVRRYRAGAGPSPAGDDVTFPEFLRYLVDEDPERMNEHWMPVYHLCQPCAVHYDFVGSYERLEADANQVLEWVRAPPHVRFPARQAWYRPASPESLHYHLCSAPRALLQDVLPKYILDFSLFAYPLPNVTKEACQQ
Protein: Protein distal antenna (Q9VBW6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable transcription factor with a role in the retinal determination (RD) network. Regulates ato expression and is required for normal R8 induction and differentiation. Danr appears to repress Dan expression, but Dan is required for Danr expression anterior to the morphogenetic furrow (MF). Dan and Danr lie downstream of so and require dac function for highest levels of expression. Contributes to differentiation of antenna-specific characteristics; effector gene that acts downstream of homothorax (hth), Distal-less (Dll), cut (ct) and spineless (ss) genes to control differentiation of distal antennal structures.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000269|PubMed:12571108}.
Interaction partners:
- Protein distal antenna-related
- Paired box protein Pax-6
Sequence:
MNIRMGTKGKRPLRSLTPRDKIHAIQRIHDGESKASVARDIGVPESTLRGWCKNEDKLRFMSRQSATDNLCADALGDKMDGGGGGGGGAGGGGLLGPPEKRQRLDGALPLNFSNKLKFDELAFKRSPLNGLDYSTNKNLADLGYNGLPVDYAAFNGGVKAKVFGADINRPAADPSLNAISPLSSLTHLSGLTGISQSPLAISFNELTTNLNLLAQLNPGLAAMSGLNSFPAGAGNLRTPKPSGQTPLQVQSPRSDSGDRSAQGLSVKNWAKQKPGEGQGSLNLSIKNEGKGGDIKSPSPSIAPSQMGGPMTLSNLAEDPLLYWLKSQQTMLGLNPLYPPTIPMGVTSPPIRSSTPQHMSQLAQTPPIPSAPLTPSSTPSGSLDEKNAAWYNWCKAFGASLHTLNPNAATLAALQANQLQQQVATTAAEGGSMGDPSNILYSHLTKETETPSVRSLSSNEQNPEADEATETDLDGEVEPEASGKPEDLSAAGKVMTPSQSPIAHSSGSRSPEPKAKTKTPETTNSTSECKKILDNMLFKMGGMEATGPLMPEQGSSESEGSFQDTSNPHTNNNDVSASNNNNNNNSNKTDEEEKAKYLDCTADEDIEAIRHGEKFLQWLENCSNPRVTAVQLMQLRFLIAAIKSGNETPMIEKSALPEDSEEHAAEEEGSGRGKSRRRK
Protein: Urocortin-3 (Urocortin III) (Ucn III) (Q924A4)
Organism: Mus musculus (Mouse)
Function: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Corticotropin-releasing factor receptor 2
- Urocortin-2
- Urocortin
- Corticoliberin
- Corticotropin-releasing factor receptor 1
- Corticotropin-releasing factor-binding protein
- Pro-glucagon
Sequence:
MLMPTYFLLPLLLLLGGPRTSLSHKFYNTGPVFSCLNTALSEVKKNKLEDVPLLSKKSFGHLPTQDPSGEEDDNQTHLQIKRTFSGAAGGNGAGSTRYRYQSQAQHKGKLYPDKPKSDRGTKFTLSLDVPTNIMNILFNIDKAKNLRAKAAANAQLMAQIGKKK