wanglab/gogpt-training-data huggingface dataset:
Protein: GLI family zinc finger 2 (F1M2B7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Suppressor of fused homolog
- Kinesin family member 7
- Speckle-type POZ protein, isoform CRA_a.
- Beta-transducin repeat containing E3 ubiquitin protein ligase
- GLI family zinc finger 1
- Protein smoothened
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Kinesin-like protein
- Patched
Sequence:
METSAQAPALEKKEAKSGLLEDSSFPDPGKKACPLAVAAPAAAVAAQGVPQQLLPSFHVPLPIDMRHQEGRYHYDPHPVHGVHGPPTLSGSPVISDISLIRLSPHPAGPGESPFSAHHPYMNPHMEHYLRSVHSSPTLSMISAARGLSPADVAHEHLKERGLFSLAAPGTNPSDYYHQMTLMASHPTPYGDILMQSGGAASAPHLHDYLNPVDASRFSSPRVTPRLSRKRALSISPLSDASLDLQRMIRTSPNSLVAYINNSRSSSAASGSYGHLSAGALSPAFTFPHPINPVAYQQILSQQRGLGSAFGHTPPLIQPSPTFLAQQPMTLTSITVPTQLGSNSSNCISDANQNKQNSESAVSSTVNPITIHKRSKVKTEAEGLRPASPLGLTQEQLADLKEDLDRDDCKQEAEVVIYETNCHWADCTKEYDTQEQLVHHINNEHIHGEKKEFVCRWQACTREQKPFKAQYMLVVHMRRHTGEKPHKCTFEGCSKAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNEKPYICKIPGCTKRYTDPSSLRKHVKTVHGPDAHVTKKQRNDVHLRAPLLKENGDNEAGAEPGGRGPEESVEASSTSHTAEDCLHIKAIKTESSGLCQSSPGAQSSCSSEPSPLGSVPNNDSGVEMPGTGPGSLGDLTALDDTSPGADTSALAVPSTGGLQLRKHMTTMHRFEQLKREKLKSLKDSCSWAGPAPHTRNTKLPPLPVNGSVLENFNNTGGCGPAGLLPNQRLPELTEVTMLSQLQERRDSSTSTMSSAYTVSRRSSGISPYFSSRRSSEASPLGGIRPHNASSADSYDPISTDASRRSSEASQCSGGGPGLLNLTPAQQYSLRAKYAAATGGPPPTPLPGLDRVSLRTRLALLDAPERALPGACPQPLGPRRGSDGPTYNHGHGYVGAAPALPHEGPNGSTRRASDPVRRPDPLVLPRVQRFHSIHNMNPGPLPPCTDRRGLHLQSHPSVDGSLTRHAYSPRPPSINENVVMEAVAAGVEGAGLESDLGLVEDDLVLPDDVVQYIKAHTGGALDDSTRQVYPTEGTGFPENSKLPSPGLQGHRRLAAADSNMSPSAPGLGGCQLSYSPSSSLNKSNMPVQWNEVSSGTVDALPTQVKPPSFPQSNLVQQKPAFAHYPGYSPQALQSGSGGLDSTQPHLQLRGAPSASRGSYTQQPRLPATGSQCLGVTAAMSPQANYSQTHHQLSPNVVSGSLNQFAPSCSNMAAKPSHLGLPQQMEVVPNATIISGHQRELGIASSSLAAVSQPHPVLGYPQQDGYQQVSGLPSSHQPSFMESQQNTGFGLMQPRPPLEPNTASRHRGVRSGQQQQQLYARTAGQAVVTSANQETAEAMPKGTAGTVVSLTPQPSQDTGRSQDQNTLYYYGQIHMYEQNGGCPAMQPQPPQPQGCSDNIQPEPLPSPGVNQVSSTVDSQLLEPPQIDFDAIMDDGDHSSLFSGALSPSLLHNLSQNSSRLTTPRNSLTLPSIPVGISNMAVGDMSSMLTSLAEENKFLNMMT
Protein: E3 ubiquitin-protein ligase ARIH1 (EC 2.3.2.31) (Protein ariadne-1 homolog) (ARI-1) (UbcH7-binding protein) (UbcM4-interacting protein 77) (Ubiquitin-conjugating enzyme E2-binding protein 1) (Q9Z1K5)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets. The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes. Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear. According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest. According to another report EIF4E2 ubiquitination leads to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2. In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, may act in nuclear subcellular localization and nuclear morphology.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9Y4X5}. Note=Mainly cytoplasmic. Present in Lewy body. {ECO:0000250|UniProtKB:Q9Y4X5}.
Interaction partners:
- Cullin-3
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- Ubiquitin-conjugating enzyme E2 L3
- Ubiquitin-like protein NEDD8
- Translation initiation factor eIF2B subunit epsilon
- Cullin-1
- Cyclin-dependent kinase inhibitor 1B
- Ubiquitin-conjugating enzyme E2 N
- E3 ubiquitin/ISG15 ligase TRIM25
Sequence:
MDSDEGYNYEFDEDEECSEEDSGAEEEEDDDEDEPDDDNLDLGEVELVEPGLGVGGERDGLLCGETGGGGGSALGPGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVLLQHVHEGYEKDLWEYIED
Protein: DNA-(apurinic or apyrimidinic site) endonuclease 2 (EC 3.1.11.2) (AP endonuclease 2) (Apurinic-apyrimidinic endonuclease 2) (P87175)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. Provides the majority of the AP-endonuclease (APE) activity. Repairs phleomycin D1-induced DNA damage. Plays a role in oxidative damage repair.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00764}.
Interaction partners:
- Apurinic-apyrimidinic endonuclease 1
- Endonuclease III homolog lyase)
- Probable tyrosyl-DNA phosphodiesterase
- Bifunctional polynucleotide phosphatase/kinase
- Uracil-DNA glycosylase
- DNA repair protein rad16
- UV-damage endonuclease
- Flap endonuclease 1
- Adenine DNA glycosylase
- Cytochrome c oxidase subunit 13, mitochondrial
Sequence:
MRILSWNVNGIQNPFNYFPWNKKNSYKEIFQELQADVICVQELKMQKDSFPQQYAVVEGFDSYFTFPKIRKGYSGVGFYVKKDVAIPVKAEEGITGILPVRGQKYSYSEAPEHEKIGFFPKDIDRKTANWIDSEGRCILLDFQMFILIGVYCPVNSGENRLEYRRAFYKALRERIERLIKEGNRKIILVGDVNILCNPIDTADQKDIIRESLIPSIMESRQWIRDLLLPSRLGLLLDIGRIQHPTRKGMFTCWNTRLNTRPTNYGTRIDYTLATPDLLPWVQDADIMAEVMGSDHCPVYLDLKEEYEGKKLSNFLSHSKEPPLLSTAHHSAYRPSKNIHSMFQHFNSMKKNKNNSPTQSENVSASASSGSSPTVSRANSVIDVDAYPPEKRRRKEQSKLLSFFAKQKEEKEETNKTEDVSIEVLDNNNESDIGLTVKKKVENGNAWKQIFSERAPPLCEGHKEPCKYLTVRKPGINYGRKFWICARPVGELIKNSNAVSEEDTQPFQCRFFIWDSDWRANSKD
Protein: Tyrosine-protein kinase receptor torso (EC 2.7.10.1) (P18475)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable receptor tyrosine kinase which is required for determination of anterior and posterior terminal structures in the embryo. During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to prothoracicotropic hormone Ptth. Binding to Ptth stimulates activation of canonical MAPK signaling leading to ERK phosphorylation (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- DShc protein
- Protein trunk
- Tyrosine-protein phosphatase corkscrew
- Protein daughter of sevenless
- Torso-like protein
- Fibroblast growth factor
Sequence:
MLIFYAKYAFIFWFFVGSNQGEMLLMDKISHDKTLLNVTACTQNCLEKGQMDFRSCLKDCRINGTFPGALRKVQENYQMNMICRTESEIVFQIDWVQHSRGTEPAPNATYIIRVDAVKDDNKETALYLSDDNFLILPGLESNSTHNITALAMHGDGSYSLIAKDQTFATLIRGYQPSKMGAVNLLRFVPQPDDLHHIAAEIEWKPSAESNCYFDMVSYSTNSVNMDEPLEVQFRDRKKLYRHTVDNLEFDKQYHVGVRTVNIMNRLESDLQWLPIAVPSCLDWYPYNYTLCPPHKPENLTVTQKQYLPNILALNITWARPRYLPDNYTLHIFDLFKGGTELNYTLDQNRSHFYVPKITVLGSHFEVHLVAQSAGGKNVSGLTLDKVHRGVLLSEGNMVKLVLFIIVPICCILMLCSLTFCRRNRSEVQALQMDAKDAKASEFHLSLMDSSGLLVTLSANESLEVMDELEVEPHSVLLQDVLGEGAFGLVRRGVYKKRQVAVKLLKDEPNDEDVYAFKCEIQMLKAVGKHPNIVGIVGYSTRFSNQMMLLIEYCSLGSLQNFLREEWKFRQEQNAIGLKKNLEQNVDNRRFNRLPRNSIHDRIEDINNSMLSTVEEESESDQTHSSRCETYTLTRITNAADNKGYGLEDIENIGGSYIPKTAEAPKDRPKRKLKPQPKKDSKQDFKSDNKKRIFENKEYFDCLDSSDTKPRIPLKYADLLDIAQQVAVGMEFLAQNKVVHRDLAARNVLISVDRSIKIADFGLSRDVYHENVYRKSGGSGKLPIKWLALESLTHQVYTSQSDVWSFGVLLYEITTLGGMPYPSVSPSDLLQLLRQGHRMKRPEGCTQEMFSLMESCWSSVPSHRPTFSALKHRLGGMILATNDVPERLKQLQAATESKLKSCDGLNSKVEQVPCEEELYLEPLN
Protein: DNA-directed DNA/RNA polymerase mu (Pol Mu) (EC 2.7.7.7) (Terminal transferase) (Q9JIW4)
Organism: Mus musculus (Mouse)
Function: Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA ligase 4
- DNA repair protein XRCC4
- Non-homologous end-joining factor 1
- X-ray repair cross-complementing protein 6
- X-ray repair cross-complementing protein 5
- DNA-dependent protein kinase catalytic subunit
Sequence:
MLPKRRRVRAGSPHSAVASSTPPSVVRFPDVAIYLAEPRMGRSRRAFLTRLARSKGFRVLDAYSSKVTHVVMEGTSAKEAICWQKNMDALPTGCPQPALLDISWFTESMAAGQPVPEEGRHHLEVAEPRKEPPVSASMPAYACQRPSPLTHHNTLLSEALETLAEAAGFEANEGRLLSFSRAASVLKSLPCPVASLSQLHGLPYFGEHSTRVIQELLEHGTCEEVKQVRCSERYQTMKLFTQVFGVGVKTANRWYQEGLRTLDELREQPQRLTQQQKAGLQYYQDLSTPVRRADAEALQQLIEAAVRQTLPGATVTLTGGFRRGKLQGHDVDFLITHPEEGQEVGLLPKVMSCLQSQGLVLYHQYHRSHLADSAHNLRQRSSTMDAFERSFCILGLPQPQQAALAGALPPCPTWKAVRVDLVVTPSSQFPFALLGWTGSQFFERELRRFSRQEKGLWLNSHGLFDPEQKRVFHATSEEDVFRLLGLKYLPPEQRNA
Protein: Aldo-keto reductase family 1 member C1 (EC 1.1.1.-) (EC 1.1.1.112) (EC 1.1.1.209) (EC 1.1.1.210) (EC 1.1.1.357) (EC 1.1.1.51) (EC 1.1.1.53) (EC 1.1.1.62) (EC 1.3.1.20) (20-alpha-hydroxysteroid dehydrogenase) (20-alpha-HSD) (EC 1.1.1.149) (Chlordecone reductase homolog HAKRC) (Dihydrodiol dehydrogenase 1) (DD1) (High-affinity hepatic bile acid-binding protein) (HBAB) (Q04828)
Organism: Homo sapiens (Human)
Function: Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH. Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens. May also reduce conjugated steroids such as 5alpha-dihydrotestosterone sulfate. Displays affinity for bile acids.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8486699}.
Interaction partners:
- Aldo-keto reductase family 1 member C2
- Aldo-keto reductase family 1 member C3
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- Aldo-keto reductase family 1 member D1
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Polyprenal reductase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
Sequence:
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY
Protein: Large ribosomal subunit protein bL36A (50S ribosomal protein L36) (Ribosomal protein B) (P0A7Q6)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Large ribosomal subunit protein uL13
- Elongation factor G
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS7
- Alternative ribosome-rescue factor A
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL30
- GTP pyrophosphokinase
Sequence:
MKVRASVKKLCRNCKIVKRDGVIRVICSAEPKHKQRQG
Protein: Homeodomain interacting protein kinase 1 (J3KP92)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQANSSHQVANFNIPAYDQGLLLPAPAVEHIVVTAADSSGSAATSTFQSSQTLTHRSNVSLLEPYQKCGLKRKSEEVDSNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDPNLGYPLWRLKTPEEHELETGIKSKEARKYIFNCLDDMAQVNMSTDLEGTDMLAEKADRREYIDLLKKMLTIDADKRITPLKTLNHQFVTMTHLLDFPHSNHVKSCFQNMEICKRRVHMYDTASVLASSSTAAAATLSLANSDVSLLNYQSALYPSSAAPVPGVAQQGVSLQPGTTQICTQTDPFQQTFIVCPPAFQTGLQATTKHSGFPVRMDNAVPIVPQAPAAQPLQIQSGVLTQGSCTPLMVATLHPQVATITPQYAVPFTLSCAAGRPALVEQTAAVLQAWPGGTQQILLPSTWQQLPGVALHNSVQPTAMIPEAMGSGQQLADWRNAHSHGNQYSTIMQQPSLLTNHVTLATAQPLNVGVAHVVRQQQSSSLPSKKNKQSAPVSSKSSLDVLPSQVYSLVGSSPLRTTSSYNSLVPVQDQHQPIIIPDTPSPPVSVITIRSDTDEEEDNKYKPSSSGLKPRSNVISYVTVNDSPDSDSSLSSPYSTDTLSALRGNSGSVLEGPGRVVADGTGTRTIIVPPLKTQLGDCTVATQASGLLSNKTKPVASVSGQSSGCCITPTGYRAQRGGTSAAQPLNLSQNQQSSAAPTSQERSSNPAPRRQQAFVAPLSQAPYTFQHGSPLHSTGHPHLAPAPAHLPSQAHLYTYAAPTSAAALGSTSSIAHLFSPQGSSRHAAAYTTHPSTLVHQVPVSVGPSLLTSASVAPAQYQHQFATQSYIGSSRGSTIYTGYPLSPTKISQYSYL
Protein: Transcriptional regulatory protein TOD6 (PAC-binding factor 1) (Twin of DOT6) (P34219)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the RPD3 histone deacetylase complex RPD3C(L) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. TOD6 binds to sequences containing the core CGATG, which resembles the PAC (Polymerase A and C) motif.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein STB3
- Transcriptional regulatory protein SDS3
- Transcriptional regulatory protein UME1
- Histone deacetylase RPD3
- Protein IFH1
- Histone deacetylase complex subunit CTI6
- Transcriptional regulatory protein RXT2
- Transcriptional regulatory protein DOT6
- Transcription factor SFP1
- Serine/threonine-protein kinase SCH9
Sequence:
MTLPKLSSVSVSSGHVSANSHGFSILSKHPHPNNLVHSHSLSHTNAKSHLPISSTSTKENSTNKEEAESLKKNNPSSWDPSDDIKLRHLKEIKNLGWKEIAHHFPNRTPNACQFRWRRLKSGNLKSNKTAVIDINKLFGVYATGDATPSAGTPSAEEAVKEEAVEDEDITAGSSAIEDSPPDFKPLVKPKYMDRKLITQRSTSTFSDHEPQHTKPRKLFVKPRSFSHSITTNTPNVKTAQQTNLSLYNTTSAKTNKAVNSNDYENIGLVPKIIIRSRRNSFIPSTQIPHSTTKTRKNSHSVISSRRSSFNMMHSRRSSFNSHAPTEPISRRASLVVSPYMSPRRLSTSQSVHYHPQHQYYLNPIASPNCKTDHANDKITHTRTFLDMQKFANKHPWSREDDEVLLNNTKDKQNHLSPLEISIVLPNNRSELEIQQRMDYLKRKGRVSGFHTNEGCKDEEEEDDIDPLHKENGINTPSQQSQNYGMLEAKHDNPKSSELSSMTSANDIRNEQDELPGINSIFKNIF
Protein: Ribonuclease VapC47 (RNase VapC47) (EC 3.1.-.-) (Toxin VapC47) (P9WF49)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits translation and colony formation. Its toxic effect on colony formation is neutralized by coexpression with cognate antitoxin VapB47; the effect on translation has not been tested but is probably neutralized also.
Interaction partners:
- Antitoxin VapB47
- Ribonuclease VapC3
- Ribonuclease VapC12
- Ribonuclease VapC38
- Ribonuclease VapC40
- Antitoxin VapB46
- Ribonuclease VapC30
- Ribonuclease VapC49
- Putative antitoxin VapB5
- Putative antitoxin VapB49
Sequence:
MIYMDTSALTKLLISEPETTELRTWLTAQSGQGEDAATSTLGRVESMRVVARYGQPGQTERARYLLDGLDILPLTEPVIGLAETIGPATLRSLDAIHLAAAAQIKRELTAFVTYDHRLLSGCREVGFVTASPGAVR
Protein: Caskin, isoform B (Caskin, isoform C) (Caskin, isoform E) (LD09801p) (Q7JQG5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHRSLKPHASTAQAKKVQPPTIPGDSPQDLHLYQQPQQLHHHHHQHPNHHHPHHQPSIPLYRLSGPLRHHQNHQADDGISMSGSSIVSSPSLEEGGFNLPRETSVALRLKDEVGGTSTAAPTTGGPGGGGATVVGAPPPGAGKPGVAMVPPPPVFCATLREPLTHKAAVYYHQQLALQEDQGIDLTQSPGRDSPGSSSGSAGSGSRHSTASLDSGRASSYLTGVSSSGASIRAPLSSPRCSSVSSCSIGSVDRQRNDELIIDWLLEMKHEEYAQLFIAAGYDLPTIARMTPEDLTAIGIKNPHHRERIKQRIDKLQVLDNLPHFVPGSIEEWLQLLRLEEYIQPLLEQNYKTVRDVTQVTWEDLEDIGIVKLGHQKKILLAIKRVKDIISGKWNPGGANAYQQQEYQRKPWQFNVPIPSTPSYVPTTRVSWDDTKIYATSSVLNSTAPSGSSCLNSSLANGDAYYCTGSNHECCSGNDVVLIKVRQPRGKSLESLEDIHDNSTRSHLTFSHYTTTDYGHFGPPTTAAAAAAMAAAATLQQQHHHQQLLHQQQQQAAAARLLGNNAPGIGWRRSYDDGDITPTNDATRELLYEQEGGGTLPRQQRGILQRAVLNTMPPLEHHHYMNAAAAAEYGAASGVEGGANYMGGSPLTGKKIAPEPPRRHCSIRNSRTLSGEGVPSGAAAQAHQQAAQQQQGQHMFYGHTAQHWQQQQQQAGAGTGQQPIYANYATIQQTTAEIHCEKYHDSKSTSSIDSIDTIPFANENTGTIKQRLLNRQELQGGGAGNNNVPGGGHPAHLHSSSSSSSSSSTNTIANIAHSFHSLKSSSSLHDATLARSESMGSTASGGSALHLRSPTLDMSNAGGSTAEPASSPEAAVPTVAINNGVPPKVSVNVLNDIGNMLANLTDELDAMLEEEKRVGLNIDSE
Protein: Zinc finger and BTB domain-containing protein 7B (Krueppel-related zinc finger protein cKrox) (c-Krox) (T-helper-inducing POZ/Krueppel-like factor) (Zinc finger protein 67) (Zfp-67) (Zinc finger protein Th-POK) (Q64321)
Organism: Mus musculus (Mouse)
Function: Transcription regulator that acts as a key regulator of lineage commitment of immature T-cell precursors. Exerts distinct biological functions in the mammary epithelial cells and T cells in a tissue-specific manner. Necessary and sufficient for commitment of CD4 lineage, while its absence causes CD8 commitment. Development of immature T-cell precursors (thymocytes) to either the CD4 helper or CD8 killer T-cell lineages correlates precisely with their T-cell receptor specificity for major histocompatibility complex class II or class I molecules, respectively. Cross-antagonism between ZBTB7B and CBF complexes are determinative to CD4 versus CD8 cell fate decision. Suppresses RUNX3 expression and imposes CD4+ lineage fate by inducing the SOCS suppressors of cytokine signaling. induces, as a transcriptional activator, SOCS genes expression which represses RUNX3 expression and promotes the CD4+ lineage fate. During CD4 lineage commitment, associates with multiple sites at the CD8 locus, acting as a negative regulator of the CD8 promoter and enhancers by epigenetic silencing through the recruitment of class II histone deacetylases, such as HDAC4 and HDAC5, to these loci. Regulates the development of IL17-producing CD1d-restricted naural killer (NK) T cells. Also functions as an important metabolic regulator in the lactating mammary glands. Critical feed-forward regulator of insulin signaling in mammary gland lactation, directly regulates expression of insulin receptor substrate-1 (IRS-1) and insulin-induced Akt-mTOR-SREBP signaling. Transcriptional repressor of the collagen COL1A1 and COL1A2 genes. May also function as a repressor of fibronectin and possibly other extracellular matrix genes. Potent driver of brown fat development, thermogenesis and cold-induced beige fat formation. Recruits the brown fat lncRNA 1 (Blnc1):HNRNPU ribonucleoprotein complex to activate thermogenic gene expression in brown and beige adipocytes.
Subcellular location: Nucleus {ECO:0000269|PubMed:22730529, ECO:0000269|PubMed:29420538}.
Interaction partners:
- Membrane progesterone receptor epsilon
- Heterogeneous nuclear ribonucleoprotein U
- Runt-related transcription factor 3
- Histone deacetylase 3
Sequence:
MGSPEDDLIGIPFPDHSSELLSCLNEQRQLGHLCDLTIRTQGLEYRTHRAVLAACSHYFKKLFTEGGGGTVMGTGGGGTASGGAGAGVCELDFVGPEALGALLEFAYTATLTTSSANMPAVLQAARLLEIPCVIAACMEILQGSGLEAPSPDEDDCERARQYLEAFATATTTASTSGMPNGEDSPPQVPLLPPPPPPPRPVARRSRKPRKAFLQTKGARANHLVPEAPTVLTHPLTYEEEEMVGRLGNSGGSGLGDSYSPPTGAASPAEGPLNYEVFEGEEEEEEMAYPPGYGLAQSNEPSLSPEELGSDEDPIDPDLMAYLSSLHQDALTPGLDGQDKLVRKRRSQMPQECPVCHKIIHGAGKLPRHMRTHTGEKPFACEVCGVRFTRNDKLKIHMRKHTGERPYSCPHCPARFLHSYDLKNHMHLHTGDRPYECHLCHKAFAKEDHLQRHLKGQNCLEVRTRRRRKDDVAAPHYPPPSTTTSSPAGLDLSNGHLDTFHLSLARFWEQSATTGPPVTTQGPPEEEEEEGTPTTPQAEGAMESS
Protein: Endosome/lysosome-associated apoptosis and autophagy regulator family member 2 (Estrogen-induced gene 121-like protein) (Q3UZV7)
Organism: Mus musculus (Mouse)
Function: Functions as a regulator of the BMP signaling pathway and may be involved in epidermal differentiation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6DDW2}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLLLTLRRAKGRDRGRPAGGPRRALSLPWSPAWICCWALAGCQAVWAGDSSSSGRPLPACQEKDYHFEYTECDSTGSRWRVAIPNSAVDCSGLPDPVKGKECTFSCASGEYLEMKNQVCSKCVEGTYSLGSGIKFDEWDELPAGFSNVATFMDTVVGPSDSRPDGCNNSSWLPRGNYIESNRDDCTVSLIYAVHLKKSGYVFFEYQYVDNNIFFEFFIQNDQCQEMDATTDKWVKLTDNGEWGSHSVMLKSGTNILYWRTTGILMGSKAVKPVLVKNITIEGVAYTSECFPCKPGTFSNKPGSFNCQMCPRNTYSEKGAKECIRCKEDSQFSEEGASECVDRPPCTTKDYFQIHTPCDEEGKTQIMYKWIEPKICREDLTDAIRLPPSGEKKDCPPCNPGFYNNGSSSCHPCPPGTFSDGTKECKSCPAGTEPALGFEYKWWNVLPANMKTSCFNVGNSKCDGMNGWEVAGDHIRSGAGGSDNDYLILNLHIPGFKPPTSMTGATGSELGRITFVFETLCSADCVLYFMVDINRKSTNVVESWGGTKEKQAYTHVIFKNATFTFTWAFQRTNQGQDNRRFINDVVKIYSITATNAVDGVAASCRACALGSEQSASSCVPCPPGHYIEKETNQCKECPADTYLSIHQVYGKEACIPCGPGSKSTQDHSLCYSDCFFYHEKENQTLHYDFRNLSSVGSLMNGPSFTSKGTKYFHFFNISLCGHEGRKMALCTNNISDFTVKEMVTGSDDYTNLVGAFVCQSTIIPSESKGFRAALSSQSIILADMFLGVTVDTALQNVNIKEDMFPVSPSQVPDVHFFYKSSTATTSCINGRSTAVKMRCNPMRPGAGVISVPSKCPAGTCDGCTFYFLWESAEACPLCTEHDFHEIEGACKRGLQEILYVWNEPKWCIKGISLPEKKLSTCETVDFWLKVGAGVGAFTAVLLVALTCYFWKKNQKLEYKYSKLVMTTNSKECELPAADSCAIMEGEDNEEDVVYSNKQSLLGKLKSLATKEKDDHFESVQLKSSRCPNI
Protein: Testis-specific serine/threonine-protein kinase 2 (TSK-2) (TSK2) (TSSK-2) (Testis-specific kinase 2) (EC 2.7.11.1) (Serine/threonine-protein kinase 22B) (O54863)
Organism: Mus musculus (Mouse)
Function: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-281' of TSKS and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Present in the cytoplasm of elongating spermatids. In spermatozoa, localizes in the equatorial segment, neck, the midpiece and in a specific sperm head compartment. In spermatids, concentrates in centrioles during flagellogenesis. Localizes in the tail and acrosomal regions of epididymal sperm.
Interaction partners:
Sequence:
MDDAAVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHRSIIKTYEIFETSDGRIYIVMELGVQGDLLEFIKCRGALHEDVARKMFRQLSSAVKYCHDLDVVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDGSGRIVLSKTFCGSAAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIKKMLRIQKEHRVDFPRSKNLTGECKDLIYRILQPDVNRRLHIDEILSHSWLQPPKPKAMSSASFKREGEGKYRADCKLDTRPGSRPEHRPDHKLATKPQQRMLVTPENEDRMEDRLAETSRAKDHHISGAEVEKAST
Protein: Tubulin alpha-8 chain (EC 3.6.5.-) (Alpha-tubulin 8) (Tubulin alpha chain-like 2) [Cleaved into: Dephenylalaninated tubulin alpha-8 chain] (Q9NY65)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-2A chain
- Tubulin beta chain
- Tubulin beta-4A chain
- Tubulin beta-6 chain
- Tubulin beta-8 chain
- Tubulin beta-1 chain
- Tubulin beta-2B chain
- Tubulin beta-3 chain
- Tubulin beta-4B chain
- Microtubule-associated protein tau
Sequence:
MRECISVHVGQAGVQIGNACWELFCLEHGIQADGTFDAQASKINDDDSFTTFFSETGNGKHVPRAVMIDLEPTVVDEVRAGTYRQLFHPEQLITGKEDAANNYARGHYTVGKESIDLVLDRIRKLTDACSGLQGFLIFHSFGGGTGSGFTSLLMERLSLDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPIISAEKAYHEQLSVAEITSSCFEPNSQMVKCDPRHGKYMACCMLYRGDVVPKDVNVAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGTDSFEEENEGEEF