wanglab/gogpt-training-data huggingface dataset:
Protein: At1g80480 (Plastid transcriptionally active 17) (Q9M8L6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Chloroplast envelope quinone oxidoreductase homolog
- Probable transmembrane ascorbate ferrireductase 3
- Probable transmembrane ascorbate ferrireductase 4
- Transmembrane ascorbate ferrireductase 1
- Transmembrane ascorbate ferrireductase 2
Sequence:
MATLSTLEIATTFLSFTAPRSSAAFNYRFSSAAVSVLSRPRATTVSVRTTPSFFYSPVVRRQRFSSVSASATQTEDSDVTTKIPPDNRIPATIITGFLGSGKTTLLNHILTRDHGKRIAVIENEFGEVDIDGSLVASKSIGAEDIVMLNNGCLCCTVRGDLVRMIGELVNTKKGKFDHIVIETTGLANPAPIIQTFYAEEEIFNDVKLDGVVTLVDAKHARLHLDEVKPEGVVNEAVEQIAYADRIIVNKTDLVGEAELGSVVQRIKTINSMAQMTRTKYGNVDLDYVLGIGGFDLERIESSVNEDDKGDHHDHDHDHHHDHNHDHDHHHHDGHDHHHHSHDHTHDPGVSSVSIVCEGSLDLEKANMWLGTLLMERSEDIYRMKGLLSVHTMEERFVFQGVHDIFQGSPDRLWGREEERVNKIVFIGKNLNREELEKGFKACLI
Protein: Cinnamyl alcohol dehydrogenase (Mannitol dehydrogenase) (C1IC54)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MAKSAEEENQQKAFGWAATDNSGILSPFNFSRRENGDDDVTLKILYCGVCHSDLHTLRNDWGFSFYPVVPGHEISGVVTKVGKNVTKFNIGDRVGVGVLVGSCKTCECCEQDLENYCPRIIFTYNSYNPDGTKNYGGYSDMIVVDQRYVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGMTEAGKHLGVSGLGGLGHVAVKIGKAFGLKVTAISSSPQKESEAINRLGADSFLVSNDPEKMKSAIGTMDYIIDTVSAVHPLLPLLSLLKVNGKLVTVGLPNKPLELPVFPLVMGRKLIGGSDVGGMKETQEMLDFCAKHNITADIELIRIEEINTAMERLAKSDVRYRFVIDVANSLSQ
Protein: Mitochondria-eating protein (Spermatogenesis-associated protein 18) (Q8TC71)
Organism: Homo sapiens (Human)
Function: Key regulator of mitochondrial quality that mediates the repairing or degradation of unhealthy mitochondria in response to mitochondrial damage. Mediator of mitochondrial protein catabolic process (also named MALM) by mediating the degradation of damaged proteins inside mitochondria by promoting the accumulation in the mitochondrial matrix of hydrolases that are characteristic of the lysosomal lumen. Also involved in mitochondrion degradation of damaged mitochondria by promoting the formation of vacuole-like structures (named MIV), which engulf and degrade unhealthy mitochondria by accumulating lysosomes. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21264228, ECO:0000269|PubMed:22292033, ECO:0000269|PubMed:22532927}. Mitochondrion outer membrane {ECO:0000269|PubMed:21264228, ECO:0000269|PubMed:22292033}. Mitochondrion matrix {ECO:0000269|PubMed:22532927, ECO:0000269|PubMed:38322995}. Note=Localizes to the cytosol under normal conditions (PubMed:21264228, PubMed:22532927). Relocalizes to mitochondrion outer membrane following cellular stress. May form molecular condensates in the mitochondrial matrix (PubMed:38322995). Colocalizes with BNIP3 and BNIP3L at the mitochondrion outer membrane (PubMed:22292033). {ECO:0000269|PubMed:21264228, ECO:0000269|PubMed:22292033, ECO:0000269|PubMed:22532927}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol {ECO:0000269|PubMed:22532927}. Mitochondrion matrix {ECO:0000269|PubMed:22532927}. Note=Appears to predominantly remain in the cytosol following induction of MALM (mitochondrial protein catabolic process). {ECO:0000269|PubMed:22532927}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:22532927}. Mitochondrion matrix {ECO:0000269|PubMed:22532927}. Note=Appears to predominantly localize to the mitochondrial matrix following induction of MALM (mitochondrial protein catabolic process). {ECO:0000269|PubMed:22532927}.
Interaction partners:
- Beta-sarcoglycan
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
Sequence:
MAENLKRLVSNETLRTLQEKLDFWLKEYNTNTCDQNLNHCLELIEQVAKVQGQLFGILTAAAQEGGRNDGVETIKSRLLPWLEASFTAASLGKSVDSKVPSLQDTFDRERHKDPSPRDRDMQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRSAISLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRRSEPWSLEERKREQWNSLKQNADQQDTEAMSDYKKQLRNLKEEIAVLSAEKSALQGRSSRSRSPSPAPRSRSCSRSRSASPSTAVKVRRPSPNRSKLSNVARKAALLSRFSDSYSQARLDAQCLLRRCIDKAETVQRIIYIATVEAFHVAKMAFRHFKIHVRKSLTPSYVGSNDFENAVLDYVICHLDLYDSQSSVNDVIRAMNVNPKISFPPVVDFCLLSDFIQEICCIAFAMQALEPPLDIAYGADGEVFNDCKYRRSYDSDFTAPLVLYHVWPALMENDCVIMKGEAVTRRGAFWNSVRSVSRCRSRSLSPICPRSQIGLNTMSRSRSPSPIRCGLPRF
Protein: Anthocyanin regulatory Lc protein (P13526)
Organism: Zea mays (Maize)
Function: Putative transcriptional activator. Control tissue-specific synthesis of anthocyanin pigments in various parts of the maize plant.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Sulfotransferase
Sequence:
MALSASRVQQAEELLQRPAERQLMRSQLAAAARSINWSYALFWSISDTQPGVLTWTDGFYNGEVKTRKISNSVELTSDQLVMQRSDQLRELYEALLSGEGDRRAAPARPAGSLSPEDLGDTEWYYVVSMTYAFRPGQGLPGRSFASDEHVWLCNAHLAGSKAFPRALLAKSASIQSILCIPVMGGVLELGTTDTVPEAPDLVSRATAAFWEPQCPSSSPSGRANETGEAAADDGTFAFEELDHNNGMDDIEAMTAAGGHGQEEELRLREAEALSDDASLEHITKEIEEFYSLCDEMDLQALPLPLEDGWTVDASNFEVPCSSPQPAPPPVDRATANVAADASRAPVYGSRATSFMAWTRSSQQSSCSDDAAPAAVVPAIEEPQRLLKKVVAGGGAWESCGGATGAAQEMSGTGTKNHVMSERKRREKLNEMFLVLKSLLPSIHRVNKASILAETIAYLKELQRRVQELESSREPASRPSETTTRLITRPSRGNNESVRKEVCAGSKRKSPELGRDDVERPPVLTMDAGTSNVTVTVSDKDVLLEVQCRWEELLMTRVFDAIKSLHLDVLSVQASAPDGFMGLKIRAQFAGSGAVVPWMISEALRKAIGKR
Protein: Aquaporin (Q41372)
Organism: Spinacia oleracea (Spinach)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSKEVSEEAQAHQHGKDYVDPPPAPFFDLGELKLWSFWRAAIAEFIATLLFLYITVATVIGHSKETVVCGSVGLLGIAWAFGGMIFVLVYCTAGISGGHINPAVTFGLFLARKVSLLRALVYMIAQCLGAICGVGLVKAFMKGPYNQFGGGANSVALGYNKGTALGAEIIGTFVLVYTVFSATDPKRSARDSHVPILAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIFNSNKVWDDQWIFWVGPFIGAAVAAAYHQYVLRAAAIKALGSFRSNPTN
Protein: Protein PAT1 homolog 1 (PAT1-like protein 1) (Protein PAT1 homolog b) (Pat1b) (hPat1b) (Q86TB9)
Organism: Homo sapiens (Human)
Function: RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:17936923, ECO:0000269|PubMed:20543818, ECO:0000269|PubMed:20584987, ECO:0000269|PubMed:20826699, ECO:0000269|PubMed:20852261, ECO:0000269|PubMed:22090346, ECO:0000269|PubMed:32354837}. Nucleus {ECO:0000269|PubMed:22090346}. Nucleus, PML body {ECO:0000269|PubMed:22090346}. Nucleus speckle {ECO:0000269|PubMed:22090346}. Note=Predominantly cytoplasmic (PubMed:22090346). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (PubMed:22090346). Enriched in splicing speckles. Localization to nuclear foci and speckles requires active transcription. Excluded from the nucleolus (PubMed:22090346). {ECO:0000269|PubMed:22090346}.
Interaction partners:
- Probable ATP-dependent RNA helicase DDX6
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm1
- 5'-3' exoribonuclease 1
- Enhancer of mRNA-decapping protein 4
- mRNA-decapping enzyme 1A
- Enhancer of mRNA-decapping protein 3
- m7GpppN-mRNA hydrolase
- CCR4-NOT transcription complex subunit 6
- CCR4-NOT transcription complex subunit 8
Sequence:
MFRYESLEDCPLDEDEDAFQGLGEEDEEIDQFNDDTFGSGAVDDDWQEAHERLAELEEKLPVAVNEQTGNGERDEMDLLGDHEENLAERLSKMVIENELEDPAIMRAVQTRPVLQPQPGSLNSSIWDGSEVLRRIRGPLLAQEMPTVSVLEYALPQRPPQGPEDDRDLSERALPRRSTSPIIGSPPVRAVPIGTPPKQMAVPSFTQQILCPKPVHVRPPMPPRYPAPYGERMSPNQLCSVPNSSLLGHPFPPSVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKLLQGRVGQMLPPAPGFRAFFSAPPSATPPPQQHPPGPGPHLQNLRSQAPMFRPDTTHLHPQHRRLLHQRQQQNRSQHRNLNGAGDRGSHRSSHQDHLRKDPYANLMLQREKDWVSKIQMMQLQSTDPYLDDFYYQNYFEKLEKLSAAEEIQGDGPKKERTKLITPQVAKLEHAYKPVQFEGSLGKLTVSSVNNPRKMIDAVVTSRSEDDETKEKQVRDKRRKTLVIIEKTYSLLLDVEDYERRYLLSLEEERPALMDDRKHKICSMYDNLRGKLPGQERPSDDHFVQIMCIRKGKRMVARILPFLSTEQAADILMTTARNLPFLIKKDAQDEVLPCLLSPFSLLLYHLPSVSITSLLRQLMNLPQSAATPALSNPHLTAVLQNKFGLSLLLILLSRGEDLQSSDPATESTQNNQWTEVMFMATRELLRIPQAALAKPISIPTNLVSLFSRYVDRQKLNLLETKLQLVQGIR
Protein: E3 ubiquitin protein ligase RIE1 (EC 2.3.2.27) (Protein RING-FINGER FOR EMBRYOGENESIS 1) (RING-type E3 ubiquitin transferase RIE1) (Q8GUU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable E3 ubiquitin-protein ligase required for embryo development.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- F-box protein At4g02733
- Defensin-like protein 8
- Putative defensin-like protein 3
- F-box protein At4g00893
- RING-finger, DEAD-like helicase, PHD and SNF2 domain-containing protein
- At5g63780
- ECA1 gametogenesis related family protein
- ECA1 gametogenesis related family protein
- Putative F-box protein At1g59675
- RNA-binding
Sequence:
MSSYSSDSTAARDQHAPLLRPRHDGSFSSSSSSARPTALAVLLGRITGHRAPSMLVRETAARALEERRIDWGYSKPVVAADILWNAALVLASAVMLVGTVEERPNEPIRVWICVYGLQCLFHVVLVWSEYWRRNSTRRARDLESYDHEDYNIEYDYEQDSDDNSTTYSFVKRCESINTVISFIWWIIGFYWVVEGGDKLLGEAPNLYWLSVIFLAIDVFFAVFCVVLACLVGIALCCCLPCIIALLYAVAGTEGVSEAELGVLPLYKFKAFHSNEKNITGPGKMVPIPINGLCLATERTLLAEDADCCICLSSYEDGAELHALPCNHHFHSTCIVKWLKMRATCPLCKYNILKGTTDQS
Protein: Sarcospan (K-ras oncogene-associated protein) (Kirsten-Ras-associated protein) (Q62147)
Organism: Mus musculus (Mouse)
Function: Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also found in myotendinous junctions and in the postsynaptic membrane of neuromuscular junctions. {ECO:0000250}.
Interaction partners:
- Dystrophin
- Dystroglycan 1
- Dystrobrevin alpha
- Delta-sarcoglycan
- Alpha-sarcoglycan
- Beta-sarcoglycan
- Utrophin
- Gamma-sarcoglycan
- Epsilon-sarcoglycan
- Zeta-sarcoglycan
Sequence:
MGRKPSPRAQELPEEEARTCCGCRFPLLLALLQLALGIAVTVLGFLMASISPSLLVRDTPFWAGSIVCVVAYLGLFMLCVSYQVDERTCVQFSMKVFYFLLSALGLMVCMLAVAFAAHHYSLLAQFTCETSLDSCQCKLPSSEPLSRAFVYRDVTDCTSVTGTFKLFLIIQMVLNLVCGLVCLLACFVMWKHRYQVFYVGVGLRSLMASDGQLPKA
Protein: Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41)] (A0A1D8PK65)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Acetyl-CoA carboxylase
- Long-chain fatty acid-CoA ligase
- 3-oxoacyl-[acyl-carrier-protein] synthase
- [acyl-carrier-protein] S-malonyltransferase
- Faa2p
- Faa2-3p
- Faa2-1p
- Medium-chain fatty acid-CoA ligase
- 3-oxoacyl-[acyl-carrier-protein] reductase
Sequence:
MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERIIEIGPSPTLAGMANRTIKAKYESYDAALSLQRQVLCYSKDAKEIYYKPDPADLAPKETPKQEESTPSAPAAATPTPAAAAAAAPTPAPASAGPVESIPDEPVKANLLIHVLVAQKLKKPLDAVPMTKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEDTPLEELAEQFQDSFSGQLGKTSTSLIGRLMSSKMPGGFSITTARKYLESRFGLGAGRQDSVLLMALTNEPANRLGSEADAKAFFDGIAQKYASSAGISLSSGAASGAGAANSGGAVVDSAALDALTAENKKLAKQQLEVLARYLQVDLNKGAKSFIKEKEASAVLQKELDLWEAEHGEFYAKGIQPTFSALKSRTYDSYWNWARQDVLSMYFDIIFGKLTSVDRETINQCIQIMNRANPTLIKFMQYHIDHCPEYKGETYKLAKRLGQQLIDNCKQVLTEDPVYKDVSRITGPKTKVSAKGNIEYEETQKDSVRKFEQYVYEMAQGGAMTKVSQPTIQEDLARVYKAISKQASKDSKLELQRVYEDLLKVVESSKEIETEQLTKDILQAATVPTTPTEEVDDPCTPSSDDEIASLPDKTSIIQPVSSTIPSQTIPFLHIQKKTKDGWEYNKKLSSLYLDGLESAAINGLTFKDKYVLVTGAGAGSIGAEILQGLISGGAKVIVTTSRFSKKVTEYYQNMYARYGAAGSTLIVVPFNQGSKQDVDALVQYIYDEPKKGGLGWDLDAIIPFAAIPENGNGLDNIDSKSEFAHRIMLTNLLRLLGAVKSKKTTDTRPAQCILPLSPNHGTFGFDGLYSESKISLETLFNRWYSEDWGSKLTVCGAVIGWTRGTGLMSANNIIAEGIEKLGVRTFSQKEMAFNILGLLTPEIVQLCQEEPVMADLNGGLQFIDNLKDFTSKLRTDLLETADIRRAVSIESAIEQKVVNGDNVDANYSKVMVEPRANMKFDFPTLKSYDEIKQIAPELEGMLDLENVVVVTGFAEVGPWGNSRTRWEMEAYGEFSLEGAIEMAWIMGFIKYHNGNLKGKPYSGWVDAKTQTPIDEKDIKSKYEEEILEHSGIRLIEPELFNGYDPKKKQMIQEVVVQHDLEPFECSKETAEQYKHEHGEKCEIFEIEESGEYTVRILKGATLYVPKALRFDRLVAGQIPTGWDARTYGIPEDTISQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSSSGPIKTPVGACATAVESVDIGIETILSGKAKVVLVGGYDDFQEEGSYEFANMNATSNSIEEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMTADLALKMGVPIHAVLAMTATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNIEYRKRQLNKRLEQIKSWEETELSYLQEEAELAKEEFGDEFSMHEFLKERTEEVYRESKRQVSDAKKQWGNSFYKSDPRIAPLRGALAAFNLTIDDIGVASFHGTSTVANDKNESATINNMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGLVPGNRNADNVDKLLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVHPDYLFAVLDRSTYEEYATKVSARNKKTYRYMHNAITRNTMFVAKDKAPYSDELEQPVYLDPLARVEENKKKLVFSDKTIQSSQSYVGEVAQKTAKALSSLNKSSKGVGVDVELLSAINIDNETFIERNFTGNEVEYCLNTAHPQASFTGTWSAKEAVFKALGVESKGAGASLIDIEITRDVNGAPKVILHGEAKKAAAKAGVKNVNISISHDDFQATAVALSEF
Protein: Dynein axonemal assembly factor 3 (Q3UYV8)
Organism: Mus musculus (Mouse)
Function: Required for the assembly of axonemal inner and outer dynein arms. Involved in preassembly of dyneins into complexes before their transport into cilia (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q32NQ7}.
Interaction partners:
- Dynein axonemal assembly factor 4
- Dynein axonemal assembly factor 1
- Dynein axonemal assembly factor 5
- Zinc finger MYND domain-containing protein 10
- Dynein axonemal intermediate chain 2
- Dynein axonemal assembly factor 6
- Sperm-associated antigen 1
- Dynein axonemal assembly factor 11
- Axonemal dynein light intermediate polypeptide 1
- Coiled-coil domain-containing protein 39
Sequence:
MTTPAGSGTGYGSVSWWGLSPALDLQAESPPVDPDSQSKTERKVPELDALLLGSVDGRHMLRTLARAALWPLRSFNFYVLENNLEAVARHMLIFSLALEEPEKMGLQERSETFLELWGNALLRPSVAAFLRAQASHLANLVLEPDRLEEQLPWLSLRLLKFRERDALEAVFRFWSGGEKGPEVFPMSRLWDSRLRHYLGSRYDARRGVADWDLRMKLHDRGAQVIHIQEFRRWRDTGVAFELRDLSAYHVPNRTLASGRLLSHRGERVAARGYWGDIATGPFMAFGIEADDQSLLRTRNGQPVKTASEITQHNVTELFREVAAWRGPRAIQGNVEETESPEPDVPAQEPFTIHFLPLDSSQTLHHKTCYQGRFQLLYVSCGMVHLLSPELGACVAPGGNLVVELARYLVDLRPKELKAFSDRVVEIARVAGFAPHTATKPSETFARFYKLGDSTPGGGDSAVESGPAPSKVESTRAPLPESISPPQANQAPSLEAMSPPLADLAPPLETMCPPQANQAPPLEALSPSKADQIPPLEAMSPPQAKLVLPVEAISLPQADLASPPEVISPLQEAMATSWVNAPPKHVT
Protein: Ubiquinone biosynthesis protein UbiV (P45475)
Organism: Escherichia coli (strain K12)
Function: Required for O(2)-independent ubiquinone (coenzyme Q) biosynthesis. Together with UbiU, is essential for the C6-hydroxylation reaction in the oxygen-independent ubiquinone biosynthesis pathway.
Interaction partners:
- Ubiquinone biosynthesis protein UbiU
- Ubiquinone biosynthesis accessory factor UbiT
- tRNA hydroxylation protein P
- 23S rRNA 5-hydroxycytidine C2501 synthase
- Putative NAD
Sequence:
MKYSLGPVLWYWPKETLEEFYQQAATSSADVIYLGEAVCSKRRATKVGDWLEMAKSLAGSGKQIVLSTLALVQASSELGELKRYVENGEFLIEASDLGVVNMCAERKLPFVAGHALNCYNAVTLKILLKQGMMRWCMPVELSRDWLVNLLNQCDELGIRNQFEVEVLSYGHLPLAYSARCFTARSEDRPKDECETCCIKYPNGRNVLSQENQQVFVLNGIQTMSGYVYNLGNELASMQGLVDVVRLSPQGTDTFAMLDAFRANENGAAPLPLTANSDCNGYWRRLAGLELQA
Protein: Serine/threonine-protein kinase NLK (EC 2.7.11.24) (Nemo-like kinase) (Protein LAK1) (Q9UBE8)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000250|UniProtKB:O54949}.
Interaction partners:
- Lymphoid enhancer-binding factor 1
- Transcription factor 7-like 2
- Mitogen-activated protein kinase kinase kinase 7
- Forkhead box protein O1
- Transcription factor 7-like 1
- Transcription factor 7
- Forkhead box protein O3
- Forkhead box protein O4
- Catenin beta-1
- E3 ubiquitin-protein ligase RNF138
Sequence:
MSLCGARANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPVTNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE
Protein: Apoptosis inhibitor Rv3654c (O69622)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Effector protein that participates in the suppression of macrophage apoptosis by blocking the extrinsic pathway. Recognizes the host polypyrimidine tract binding protein-associated splicing factor (PSF), which probably leads to its cleavage, diminishing the level of caspase-8 in macrophages.
Subcellular location: Secreted {ECO:0000269|PubMed:20454556}. Host cytoplasm {ECO:0000269|PubMed:20454556}. Note=Is secreted into the macrophage cytoplasm. Might be secreted via a type IV pili apparatus that seems to be encoded in the same operon. {ECO:0000269|PubMed:20454556}.
Interaction partners:
- DUF4244 domain-containing protein
- Putative conjugal transfer protein Rv3659c
- Possible conserved alanine rich membrane protein
- Apoptosis inhibitor Rv3655c
- Uncharacterized protein Rv3660c
- Probable conserved transmembrane protein
Sequence:
MVARHRAQAAADLASLAAAARLPSGLAAACARATLVARAMRVEHAQCRVVDLDVVVTVEVAVAFAGVATATARAGPAKVPTTPG
Protein: 18 kDa Sin3-associated polypeptide (H7BZW6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSGFAAGVFNFCPSVFSLPQTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFTDVKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPP
Protein: E3 ubiquitin-protein ligase UBR2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase UBR2) (Ubiquitin-protein ligase E3 component N-recognin-1 homolog) (Q07963)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E3 ubiquitin-protein ligase which probably functions outside the N-end rule pathway, since it lacks the residues essential for the degradation of N-end rule substrates. Mediates RPN4 ubiquitination and subsequent degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 2
- MYND-type zinc finger protein MUB1
- Protein RPN4
- Arginyl-tRNA--protein transferase 1
- Ubiquitin fusion degradation protein 4
- Kinetochore-associated protein DSN1
- E3 ubiquitin-protein ligase listerin
- E3 ubiquitin-protein ligase UBR1
- E3 ubiquitin-protein ligase TOM1
- Protein SAN1
Sequence:
MEDSDLSITNIRDFLTELPKLAKCEYSETTSYLLWKTLNLRLKHSDNDINWRSLVSILNSEAWENEKYRDILNGRKWRTLEFENDHHSVGNMHIGTACTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYVAKVVMRPEGRICHCGDPFAFNDPSDAFKCKNELNNIPISNDNSNVTDDENVISLLNYVLDFLIDVTVSYKEEAEAHSSERKASSLMHPNQNSITDDIMEKHECEPLVNDENFVFFDNNWSNTRKEAHMEWAIQIEEEECNVHYMDLASTITRILNTPVEYAISITKALEDSHDVVTVLQSENFFEIDQIAKEFQKENIVVHVRKADDIFKRKLTDDLTDWLYSLCFKAATSLQNKYALRISMLDVWYSHFSKMRVSPTNTNPDFSKINLLGGFLISNEDSDESWFKPWSLENIEDERISKILTNYNERLIRAHSPNTVSHFYNFYGSRFQYIIINSINILSKKSKFKMLKIMASLFSLRDESRKFLAAQYIDVYLSVLYDAVASDAKECQVTLMSILGQYTFQDPSIANMTISSGFIERTIRFAFTLMAFNPEDLMSYLPISLYNGFKLPTETIRNRRTIICFKDLCTIMSANTVPEELLSNEAIFNAIIESFSEFSNVLPLKRETKEHVEVENFDFSAFYFFFSSILIMTDGYTRSISLVKDAAFRKQIVLKLLDVAQTREFESLTNSRKAISPDNASTNENDSNKATLSTVRETICNYVAETINFQVGVNTQYFFNPMSYLFKFVIQWSQCGRYEPIPASLTNYINLFEVFQDKQKALYISESALSTLVLIGQINVGFWVRNGTPITHQARMYTKYSMREFTYISDIFNVQFSMAMCNPDELMVTYLSRWGLKHWANGVPMYDYPDTETTVAVVNECILLLIQLLTEVRSLVMKSSKEGFERTFKSEIIHALCFDTCSYAQIVNCIPEHITKHPSFDIYLEKYANYTSPVSLTDNGIFVLKEKYKDEIDPYYIGLSSSRRYDVEKNIRLNMANLKKMKYEDTFVPAKKVKDLLKNTLFSGLYSISSVNTFGLFLKNTLDHIIKYDYDNLLPRVVHLIHLCVVNNLNEFMGILWHEYAIVDTEFCHYHSIGSILYYCLLKDNFSESHGKIREIFRYLMETAPHVNVNSYLREQTTSYTPGILWPTKEDKSHKDKEFERKKHLARLRKKKLMKKLAQQQMKFMENNSVDTSDISTPRTTSPSLSPTRINAENSSNTINSCCDDDCVFCKMPKDDDVFVYFSYQERNICDHGIDFTNPTDVNRINSLFSGKQTKDSAIQENPQDDDGTRLKFTSCEPVLRACGHGSHTKCLSGHMKSIRGIQNQTTKNIPLSYGSGLIYCPVCNSLSNSFLPKTNDIDKRTSSQFFMCIEKRSEAEENLDPMSSICIKAAMILGDLQGKKVTTIEDAYKVVNSVFINTISNTELRLRSHKKEGKIVNMERISSQCILTLHLVCELKSFIYKKFVNSKTFSSEISRKIWNWNEFLIKGNNVNLLLYMSQNFDNIDGGKTPQPPNLCIYEMFKRRFHQLLLLLARDMMRVNFYKDCRNKIKISSNGSEEPSTSFSYLFNTFKKYVDLFKPDDVRFDFTSLEKIKDFICSLLLESLSIFCRRTFLLFNIQYDDDGDGDNNNNRSNNFMDVKQREIELIFRYFKLPNLTHFLKDFFYNELTQNIERYNDGNDNLRIQQVIYDMVQNINTRAYPSPEHIQLIELPLNLSKFSLDNDEISNKCDKYEIAVCLLCGQKCHIQKSIALQGYLQGECTDHMRNGCEITSAYGVFLMTGTNAIYLSYGKRGTFYAAPYLSKYGETNEDYKFGTPVYLNRARYANLANEIVFGNMIPHIVFRLTDGSADLGGWETM
Protein: Zinc fingers and homeoboxes protein 1, isoform 2 (ZHX1-C8orf76 readthrough transcript protein) (Q96EF9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLRKLWQWFYEETESSDDVEVLTLKKFKGDLAYRRQEYQKALQEYSSISEKLSSTNFAMKRDVQEGQARCLAHLGRHMEALEIAANLENKATNTDHLTTVLYLQLAICSSLQNLEKTIFCLQKLISLHPFNPWNWGKLAEAYLNLGPALSAALASSQKQHSFTSSDKTIKSFFPHSGKDCLLCFPETLPESSLFSVEANSSNSQKNEKALTNIQNCMAEKRETVLIETQLKACASFIRTRLLLQFTQPQQTSFALERNLRTQQEIEDKMKGFSFKEDTLLLIAEVSVSLGFM
Protein: Leucine zipper transcription factor-like protein 1 (Q9JHQ5)
Organism: Mus musculus (Mouse)
Function: Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:22093827}.
Interaction partners:
- BBSome complex member BBS2
- BBSome complex member BBS7
- BBSome complex member BBS5
- BBSome complex member BBS4
- Protein PTHB1
- BBSome complex member BBS1
- Tetratricopeptide repeat protein 8
- Sodium- and chloride-dependent transporter XTRP3A
- FYVE and coiled-coil domain-containing protein 1
- Sodium- and chloride-dependent transporter XTRP3B
Sequence:
MAELGLNEHHQNEVINYMRFARSKRGLRLKTVDSCFQDLKDSRLVEETFTIDEVSEVLNGLQAVVHSEVESELINTAYTNVLLLRQLFSQAEKWYLKLQTDISELENRELLEQVAEFEKAEFVSSSKKPIIDITKPKLVPINEGGTTELLNKEILRLQQENEKLKSRLKTIEIQAVNALDEKSKLERVLQDLQLDQENQQDLLKAQDLDDLENTVATLRSEFQKTLNDKTENQKSLEENLAAAKHDLLRVQEQLSMAEKELEKKFQQTAAYRNMKEILTKKNDQIKDLRKRLAKYESED