wanglab/gogpt-training-data huggingface dataset:
Protein: Aryl hydrocarbon receptor nuclear translocator 2 (ARNT protein 2) (Q78E60)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that plays a role in the development of the hypothalamo-pituitary axis, postnatal brain growth, and visual and renal function. Specifically recognizes the xenobiotic response element (XRE).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9HBZ2, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Hypoxia-inducible factor 1-alpha
- Endothelial PAS domain-containing protein 1
- Neuronal PAS domain-containing protein 4
- Aryl hydrocarbon receptor nuclear translocator
- Hypoxia-inducible factor 3-alpha
- Aryl hydrocarbon receptor
- SIM bHLH transcription factor 1
- Aryl hydrocarbon receptor repressor
- SIM bHLH transcription factor 2
- Neuronal PAS domain-containing protein 1
Sequence:
MATPAAVNPPEMASDIPGSVTLPVAPMAATGQVRMAGAMPARGGKRRSGMDFDDEDGEGPSKFSRENHSEIERRRRNKMTQYITELSDMVPTCSALARKPDKLTILRMAVSHMKSMRGTGNKSTDGAYKPSFLTEQELKHLILEAADGFLFVVAAETGRVIYVSDSVTPVLNQPQSEWFGSTLYEQVHPDDVEKLREQLCTSENSMTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGNAPLDHLPLNRITTMRKRFRNGLGPVKEGEAQYAVVHCTGYIKAWPPAGMSIPEEDADVGQGSKYCLVAIGRLQVTSSPVCMDMSGMSVPTEFLSRHNSDGIITFVDPRCISVIGYQPQDLLGKDILEFCHPEDQSHLRESFQQVVKLKGQVLSVMYRFRTKNREWLLIRTSSFTFQNPYSDEIEYVICTNTNVKQLQQQQAELEVHQRDGLSSYDLSQVPVPNLPTGVHEAGKPVEKADAIFSQERDPRFAEMFAGISASEKKMMSSASASGSQQIYSQGSPFPAGHSGKAFSSSVVHVPGVNDIQSSSSTGQNISQISRQLNQGQVAWTGSRPPFPGQPSKTQSSAFGIGSSHPYPADPSSYSPLSSPAASSPSGNAYPSLANRTPGFAESGQSGGQFQGRPSEVWSQWQSQHHGQQSGEQHSHQQPGQTEVFQDMLPMPGDPTQGTGNYNIEDFADLGMFPPFSE
Protein: SH2 domain-containing protein 1B (EWS/FLI1-activated transcript 2) (EAT-2) (O35324)
Organism: Mus musculus (Mouse)
Function: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244. In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through CD244/2B4. However, conflicting results are reported which may reflect the use of different strain backgrounds. Proposed to act as an inhibitor of CD244-mediated NK cell function including cytotoxicity and IFN-gamma production, the latter found also by triggering KLRA4 and KLRK1 next to CD244. Seems to positively regulate CD244- and CD84-dependent NK cell functions implicating CD244-mediated phosphorylation of VAV1. Activation of SLAMF7-mediated NK cell function does not effect receptor tyrosine phosphorylation but distal signaling. In the context of NK cell-mediated cytotoxicity does not enhance conjugate formation with target cells but stimulates polarization of the microtubule-organizing center and cytotoxic granules toward the NK cell synapse. Negatively regulates CD40-induced cytokine production in dendritic cells downstream of SLAM family receptors probably by inducing activation of the PI3K pathway to inhibit p38 MAPK and JNK activation.
Interaction partners:
- Natural killer cell receptor 2B4
- SH2 domain-containing protein 1B2
- Signaling lymphocytic activation molecule
- SLAM family member 7
- T-lymphocyte surface antigen Ly-9
- SLAM family member 5
- SLAM family member 6
Sequence:
MDLPYYHGCLTKRECEALLLKGGVDGNFLIRDSESVPGALCLCVSFKKLVYSYRIFREKHGYYRIETDAHTPRTIFPNLQELVSKYGKPGQGLVVHLSNPIMRNNLCQRGRRMELELNVYENTDEEYVDVLP
Protein: Protein-arginine deiminase type-3 (EC 3.5.3.15) (Peptidylarginine deiminase III) (Protein-arginine deiminase type III) (P70708)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the deimination of arginine residues of proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9ULW8}.
Interaction partners:
Sequence:
MSLQRTVRVSLEHPTSAVCVAGVETIVDIYGSVPEGTDMFEVYGTPGVDIYVSPSMERNRERADTRRWCFNKGLEIIVVMNSPSNDLNDSHVQIAYHSSHEHLPLAYAVLYLTCVDITLDCDMNCADRQDRSFVDKRQWMWGPDGYGAILLVNCDRDEVSSDAQDNCDQCVRCLQDLEDMSVMVLRTQGPESLFDDHRLILHTSSCDAERARVFHVCGPEDSCEAYRCVLGPDRMSYEVPRLKGYEERFYVEGLSFPDAGFPGILSFHITLLDDSNEDYSETPIFTDTVVFRVAPWIMTPSTLPPLEVYVCQVRNNTCFVEAVEELARKAGCKLTICPQAENRNDRWIQDEMELGYTQAPHKTLPVVFDSPRNGELQGFPYKRILGLDFGYVTREPPDSSVSGLDSFGNLEVSPPVVANGKEYPLGRILIGGNLPGSRGRRVTQVVRDFLHAQKVQPLVELFVDWLAVGHVDEFLSFVPAPDGKGFRLLLASPGACFRLFQEKQKWGHGRSLLFEGVIGDRRVQTISINQVLSNQSLINFNKFAQSCIDWNREVLKRELGLGESDIIDIPQLFKSEKRKAVAFFPDLVNMLVLGKHLGIPKPFGPIINGRCCLEEKVRSLLEPLGLHCTFIDDFTPYHMLHGEVHCGTNVRREPFAFKWWHMVP
Protein: E3 ubiquitin-protein ligase UPL5 (Ubiquitin-protein ligase 5) (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase UPL5) (Q9SU29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin protein ligase that regulates leaf senescence through ubiquitination and subsequent degradation of WRKY53.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20409006}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin-ribosomal protein eL40z fusion protein
- Ubiquitin-ribosomal protein eS31x fusion protein
- Ubiquitin-ribosomal protein eS31z fusion protein
- Ubiquitin-ribosomal protein eS31y fusion protein
- DNA-directed RNA polymerase V subunit 1
- High mobility group B protein 6
- Ubiquitin carboxyl-terminal hydrolase 14
- Ubiquitin-conjugating enzyme E2 27
Sequence:
MTLSRSSADDSTNNANRSYSAVAGTDNKRKRDEDSSDYVGVAESLEMLKKQEIDADHMAASAQQTLISWRSGENSRSLSSSGECSSSNRPESTRLQIFVRMMSGGKTIVIHAEKYDTVEKLHQRIEWKTKIPALEQRVIYKGKQLQRENSLTYYSIEQDASLQLVARMQSTEHPVAWQTIDDIMYTISRMYKGENLQSNINEKIVTFFAMIPVESDESIAKYLNIFSNSSVPAALVMLYASSLERNKSCAKSSVKLFLSNCVALPKNQKNYCLPIVLEFCKLLRKVCPDQKLYVTCRNTLGSMLETFDNPHGVYNDQYETFGVEIFPFFTELTGLLLNELAQNSGPSFCDFQKVSSFWQQLRKVIELKVAFPIPIVLPMQSTALEAEIRHLHRLFGSLLTTMDLCMCRVESSLADKEVGNSETMSSSWSQYLSILKIINSMSNIYQGAKGQLAVMLNKNKVSFSALVVKFAKRGDDHQWIFEYKEATNFEARRHLAMLLFPDVKEDFEEMHEMLIDRSNLLSESFEYIVGASPEALHGGLFMEFKNEEATGPGVLREWFYLVCQEIFNPKNTLFLRSADDFRRFSPNPASKVDPLHPDFFEFTGRVIALALMHKVQVGVLFDRVFFLQLAGLKISLEDIKDTDRIMYNSCKQILEMDPEFFDSNAGLGLTFVLETEELGKRDTIELCPDGKLKAVNSKNRKQYVDLLIERRFATPILEQVKQFSRGFTDMLSHSVPPRSFFKRLYLEDLDGMLRGGENPISIDDWKAHTEYNGFKETDRQIDWFWKILKKMTEEEQRSILFFWTSNKFVPVEGFRGLSSKLYIYRLYEANDRLPLSHTCFYRLCIPRYPTITLMEQRLRLIAQDHVSSSFGKW
Protein: SLIT and NTRK-like protein 3 (O94933)
Organism: Homo sapiens (Human)
Function: Suppresses neurite outgrowth.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Neuroligin-2
- Interleukin-1 receptor accessory protein-like 1
Sequence:
MKPSIAEMLHRGRMLWIILLSTIALGWTTPIPLIEDSEEIDEPCFDPCYCEVKESLFHIHCDSKGFTNISQITEFWSRPFKLYLQRNSMRKLYTNSFLHLNNAVSINLGNNALQDIQTGAFNGLKILKRLYLHENKLDVFRNDTFLGLESLEYLQADYNVIKRIESGAFRNLSKLRVLILNDNLIPMLPTNLFKAVSLTHLDLRGNRLKVLFYRGMLDHIGRSLMELQLEENPWNCTCEIVQLKSWLERIPYTALVGDITCETPFHFHGKDLREIRKTELCPLLSDSEVEASLGIPHSSSSKENAWPTKPSSMLSSVHFTASSVEYKSSNKQPKPTKQPRTPRPPSTSQALYPGPNQPPIAPYQTRPPIPIICPTGCTCNLHINDLGLTVNCKERGFNNISELLPRPLNAKKLYLSSNLIQKIYRSDFWNFSSLDLLHLGNNRISYVQDGAFINLPNLKSLFLNGNDIEKLTPGMFRGLQSLHYLYFEFNVIREIQPAAFSLMPNLKLLFLNNNLLRTLPTDAFAGTSLARLNLRKNYFLYLPVAGVLEHLNAIVQIDLNENPWDCTCDLVPFKQWIETISSVSVVGDVLCRSPENLTHRDVRTIELEVLCPEMLHVAPAGESPAQPGDSHLIGAPTSASPYEFSPPGGPVPLSVLILSLLVLFFSAVFVAAGLFAYVLRRRRKKLPFRSKRQEGVDLTGIQMQCHRLFEDGGGGGGGSGGGGRPTLSSPEKAPPVGHVYEYIPHPVTQMCNNPIYKPREEEEVAVSSAQEAGSAERGGPGTQPPGMGEALLGSEQFAETPKENHSNYRTLLEKEKEWALAVSSSQLNTIVTVNHHHPHHPAVGGVSGVVGGTGGDLAGFRHHEKNGGVVLFPPGGGCGSGSMLLDRERPQPAPCTVGFVDCLYGTVPKLKELHVHPPGMQYPDLQQDARLKETLLFSAGKGFTDHQTQKSDYLELRAKLQTKPDYLEVLEKTTYRF
Protein: RNA-directed RNA polymerase (EC 2.7.7.48) (Q9MC15)
Organism: Pseudomonas phage phi8
Interaction partners:
Sequence:
MASFVPLVGDPKLEGSYFSWVNNQPSAMDDYSLVKTVAAIRTAFGPSINRAPSFKDVTQLVVVTRTGVKHYKANDPQYLRFQKELADALQQFEPSKQLTLGVTGLGLTRDFGTMYTHGAVFMNPTLSPRVDRLGETGGELPSDYMLALSIMSEIYFEEFKPAKVRTNGKSKTGLPNNTKDAREKKKFFMSLMDHGTGWSSALAKGDYSYSAKYYGSAPITLPTYRDQLEKPGKKRDGYDFLGNAVVAADKSIPSKYSQGVDGLHALRRRTAYAVSYAAATPMQCFVAGCRHIALERYGETWHEHDAEDIIRRIYKYGFYELYDASAFDTGFSWKEITTMIDAIPGITDLARDYMRSVHRLPLLITSDVRGVKGAYLLNMDKYSPGLQSGVPSVSDFGKIRGAAQWSYGLMVLGAIRYQSRAQLKTEFKTLLKHGRPDFAMQNRGDDTMPLAARQKDLQKWCEIVEGFKFCKWEKDTGKKFIGRVLYQRTPESKVVAYSDIVTMLEKTFINERSMFSAHRPFAATGNVMRYEMNMAHPAFGAVMDVVDTIMLKHFGVTYKECFVGAQALEKELNNGVELPDYAGLNQATRDFILDPDVIHYKWRESDIDPRVLDMVMPTSLEPDLCEEAVHKFGFVK
Protein: Dof zinc finger protein DOF5.8 (AtDOF5.8) (Q9FGD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 36
- NAC domain-containing protein 69
Sequence:
MPSEFSESRRVPKIPHGQGGSVAIPTDQQEQLSCPRCESTNTKFCYYNNYNFSQPRHFCKSCRRYWTHGGTLRDIPVGGVSRKSSKRSRTYSSAATTSVVGSRNFPLQATPVLFPQSSSNGGITTAKGSASSFYGGFSSLINYNAAVSRNGPGGGFNGPDAFGLGLGHGSYYEDVRYGQGITVWPFSSGATDAATTTSHIAQIPATWQFEGQESKVGFVSGDYVA
Protein: Secreted protein PRY1 (PRY family protein 1) (Pathogenesis-related protein 1) (Q59PV6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted protein that acts as a virulence factor during infections.
Subcellular location: Secreted {ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:22997008}.
Interaction partners:
- Opaque-phase-specific protein OP4
Sequence:
MKQNYILSIILCYLLANVHSAPAIITVWQTVTDAQVAAGPTAAAPAANANANVQQAAAASAPAPAPVASPAAPAPASSAPQSSTPSSSGWLSNLFNSFFGGSDSDSSSGSDTASAAPASTSPQSSSSSSSSSGNSFLSFLSGLFGSGSSSSTPSSISQQQQQQQGSPASGSNSPNSAQPDAAAASNPVPQSNNNQGSGLGSGFGSGFGSGSGSDSDSGSGLPSASSSTIIQQQPSSSNIGSSSTSSSSSSSSSSSSSSSSSGDIYAAISQCDGIDASFASEILDAHNKYRAQHKVGDLSWDVDTYNYAKNNADNYDCSGVLTHTHGKFGENLAAGFKDGASTVAAWVDEPISYSDASFVYNHFTQVIWKGSTKVGCAYKDCRKSNWGLYVVCEYDPYGNVIGQGSKNVFP
Protein: Lactoylglutathione lyase (EC 4.4.1.5) (Glyoxalase I) (X5DNM4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM
Protein: Clathrin light chain A (Lca) (P08081)
Organism: Rattus norvegicus (Rat)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (By similarity).
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P09496}. Note=Cytoplasmic face of coated pits and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250|UniProtKB:P09496}.
Interaction partners:
- Clathrin heavy chain 1
- Clathrin light chain B
- AP-2 complex subunit alpha
- AP-2 complex subunit beta
- AP-2 complex subunit mu
- Cyclin-G-associated kinase
- AP-2 complex subunit sigma
- Epsin-2
- AP-2 complex subunit alpha-2
- Huntingtin-interacting protein 1
Sequence:
MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGPQAHGEPPGGPDAVDGVMNGEYYQESNGPTDSYAAISEVDRLQSEPESIRKWREEQTERLEALDANSRKQEAEWKEKAVKELEEWYARQDEQLQKTKASNRVADEAFYKQPFADVIGYVTNINHPCYSLEQAAEEAFVNDIDESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH
Protein: Sperm-associated microtubule inner protein 5 (Q8WW14)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9CQT6}. Cytoplasm {ECO:0000269|PubMed:25609838}. Nucleus {ECO:0000250|UniProtKB:Q9CQT6}. Note=Localizes to the A-tubules of DMTs (By similarity). Located in the cytoplasm of spermatocytes and the nuclei of round spermatids and elongated spermatids (By similarity). {ECO:0000250|UniProtKB:A6QPC0, ECO:0000250|UniProtKB:Q9CQT6}.
Interaction partners:
Sequence:
MEPSKTFMRNLPITPGYSGFVPFLSCQGMSKEDDMNHCVKTFQEKTQRYKEQLRELCCAVATAPKLKPVNSEETVLQALHQYNLQYHPLILECKYVKKPLQEPPIPGWAGYLPRAKVTEFGCGTRYTVMAKNCYKDFLEITERAKKAHLKPYEEIYGVSSTKTSAPSPKVLQHEELLPKYPDFSIPDGSCPALGRPLREDPKTPLTCGCAQRPSIPCSGKMYLEPLSSAKYAEG
Protein: Sorbitol dehydrogenase (Polyol dehydrogenase) (O96299)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Sorbitol dehydrogenase
- BcDNA.GH10614
- LD24696p
- AT18092p
- Uncharacterized protein, isoform A
- FI19917p1
- Aldo-keto reductase on Y, isoform D
- NADP-dependent oxidoreductase domain-containing protein
- Hexokinase type 2
- Phosphotransferase
Sequence:
MATDNLTAVLHGIEDLRLEQRPIPEIADDEVLLAMDSVGICGSDVHYLAHGRIGDFVLTKPMIIGHEAAGVVAKLGKKVTTLKVGDRVAIEPGVPCRYCDHCKQGRYNLCADMVFCATPPYDGNLTRYYKHAADFCFKLPDHVSMEEGALLEPLSVGVHACRRAGVGLGSKVLILGAGPIGLVTLLAAQAMGASEILITDLVQQRLDVAKELGATHTLLLQRDQSAEETVKVVHQTMSEVPDKSIDCCGAESSARLAIFATRSGGVVVVVGMGAPEVKLPLINALAREIDIRGVFRYCNDYSAALALVASGKVNVKRLVTHHYDITETAEAFETSRRGTGGAIKVMIHVQPRDANNKVKF
Protein: Uncharacterized protein, isoform M (M9PF57)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI19480p1
- Z band alternatively spliced PDZ-motif protein 66, isoform E
- Uncharacterized protein, isoform B
- PDZ and LIM domain protein Zasp
Sequence:
MAALQRKLVHKQFNSPMGLYSQENVKATLNRELKAFGGEGIEVDDQITKPLNLANSAVLRAVEEEEQQAKCGDFPHKDFYPTERQSRPRQRGEVDALHHTLHQQLLNQIKTDYLSHQQDITIDRDTVLKINRLATKRHLLKRDHSWPPAEQDQPTINPEQSHQISCSPSHSIEALREKFQSPTLVIEPTANEVREQRRRDGGSKERSKTLQKHTKEPDLAEVFHQTPISKGFSAPETKAADVDLGLVAPRCEYYEQLAHKRSATPTLPTQITPYRPRYKRQAHSLDRSRSRKRTVGAPELPPPKPRTSKPKVQRRCIKLATEVKISYGHDGDSEDDPNSGQDVDLETLPLPPTPVSPAAANLNQAKTAGRMVIDNVAVKQQQQMALALATNGSISPVNPSPSPLANTRIVPIRVEASADQLKLSAQQIYDDACSYLQDHQEMEDIQPRTESPTYVSATGGIKLLQRQSSSTPSTPVPPPLPSPIMRSKSGQDSQAKENQTKRQGRIYSLETATEKQHEAHVEIAQLEAKYAHIQQSIAEHLLQIDAYMENAKQALQRSAQTTPVSTPVPIPPTATATPPPPPPPPPTALPARPISSASNEAWDIFAHRQSPILAVESPLQAILRQIYTRAAGLPKRLSKEIKEDADAEAEEESLTENVPIVERALEDLHKIAVALEQKSEPAKLMHVELRTTPAVSEAEHVVIKDEEQDADMEYRHVSDVIANYEQLAKKEFEEWKEEQVVNSEEMLPKTELRKAIEEQLAKKGLRGGKKVLEGEEKPVTKLDVEKDVKKDAKAVAASKEELVEDKSAIQKESKKDLGTSEAPADLTKDADAVEETERSCGHGDSSVYCPVCDEMRCSPNTWGKLNKADQWRIANLHNEPLKNYKATYEIRSPYISRQISWEDMQSAKENVPPEKLQRQRSFVEIVTTPATESPPPSTPPPPPPPPPRQLALQKPETEVTWERSRSPSPLPSRKYPAPLIEAPQRSSSPYGLNPVQTKAPPSPVNLPAKFTHVPQLEGHNIGLLVKTATEPLQQSMSASSTMLAATPPRSAAQPTPFEFPSLEQAEEQHKFKSLASFDEVQRDFGVNRSFDNVSPRPYLGIEGYKRVAWPPASEERIIREFTPQPQTQSPAPGAGGYYPQAHAPTAAAAAPPQQQYGAPSYDGQQPGAQWQQQQQQQQVPQQQYQPQSQAQAPYQPPQWNQPQQQQQQPSYQASPYQQQQQQQPSYYPQQNGGSTYAQPPYNSYSQPQLPYSQDQTDLQQQQQQQQQQYPGAYAGQDSYRGASPGIITLRKEAPVSQKPAPVYTSQPAAVSYQGGSKLRGDLKWPPPEYKEAAARENEERRQLALGPVCRPRRVNRDYTPFFAKHQLNNGYPSYKVPPGTQHIFG
Protein: Ack-related non-receptor tyrosine kinase (EC 2.7.10.2) (EC 2.7.11.1) (Ras-regulating kinase ark-1) (G5EBZ8)
Organism: Caenorhabditis elegans
Function: Probable tyrosine protein kinase which plays a role in vulva development, probably by acting as a negative regulator of the let-23/EGFR and let-60/ras pathway. Involved in the negative regulation of germline development.
Interaction partners:
- Sex muscle abnormal protein 5
- Dual specificity protein phosphatase lip-1
- E3 ubiquitin-protein ligase CBL
- Sorting nexin lst-4
- Lateral signaling target 1 protein
- Lateral signaling target protein 2
Sequence:
MREEPTAGTADATLNKLLQAADLSGYESDLRRKLKLRNAADLQYVEEVDLLSVGMSRPEQKRLRKEYTKMFPSGIFGKVKKAFKRAESLDRKTSNSVANQDDNDHHVIPIEKITLCKELGQGEFGSVWQAGWKNSAGSDVIQVAVKCVGSDKLLATSSSFLQEAAIMTRMRHEHVVRLYGVVLDTKKIMLVSELATCGSLLECLHKPALRDSFPVHVLCDYAEQIAMGMSYLELQRLIHRDLAARNVLVFSPKLVKISDFGLSRSLGIGEDYYRSEFTPNLKLPIAWCAPECINFLKFTSKSDVWAYGVTIWEMFSYGEMPWKGRSGAQILELVDRKKELLTRPKACPEDIYDMLKETWTHQVQDRPTFSDIVAKFPERRAQSVRAVVDCKDSAADHLHFKKDDLIVVISRSPAQYPDGYYWFGSLRNGKLGLFRPTDTVAHLGSEPPCSNGTIENGFSEKEKGGKKNKKAEKESERERKKLLISEPVGDVRHTCHVGIDGTAFGLLQLDKKAMCPTSSSPSTSRGSQASPAPSHTSSSTTSSVHLRETVARNGVPIKETMSLRDVGPLSRDALNLRDTVSPPVARAPSQPPSYSQPRPPPRSVSSVSSGNQHSVQVHDQFSSLDRSRGSLTPTAPPLTASAANSLKDPLTGISLSIPSNNLISYMDDQEDDHRWTRSPGAISQSTTLTALSSSRKDPIPAPRGPVAAVYARGKDIPTPASKSDIALCEKIEDLNRDLTNYSIGTICDYSEDRPLLDSMNRTISSSTTHQPPPQSSEARIRFMTEQEVRKINEKSAREHRKTEDLLREERQKEQKPGEIEEPQQPAESLYSTRTPQQEGWSSAAQEAYKLLVECGTNLKQASVSPPPMSPTSSRLSTLDRSSISPAPPRPVTPPLSVRNETISMRKSQQEEMEHVTVEENSPKRVHIIETKLIDGPARGMSPIQDRHIPAFTTPMSNGSFRKAPAPTPVSPAPAGSTDQKPPPCRPPKTRQFPLVIDERNLAYDNLNGFGAGARVAPPVPPKPKVRTIFSFADDQKKQKEVAN
Protein: Death-associated protein kinase 3 (DAP kinase 3) (EC 2.7.11.1) (DAP-like kinase) (Dlk) (MYPT1 kinase) (ZIP-kinase) (O54784)
Organism: Mus musculus (Mouse)
Function: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation; in vitro phosphorylates PAWR (By similarity). Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates STAT3 and enhances its transcriptional activity. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis (By similarity). Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition.
Subcellular location: Nucleus {ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9488481}. Nucleus, PML body {ECO:0000269|PubMed:12917339}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O88764}. Chromosome, centromere {ECO:0000250|UniProtKB:O88764}. Cytoplasm {ECO:0000250|UniProtKB:O88764}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43293}. Midbody {ECO:0000250|UniProtKB:O43293}. Note=Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments. Associated with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis (By similarity). {ECO:0000250|UniProtKB:O88764}.
Interaction partners:
- Beclin-1
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Death-associated protein kinase 1
- Death-associated protein kinase 2
- Kalirin
Sequence:
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRAAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR
Protein: Ascaphin-8 (P0CJ32)
Organism: Ascaphus truei (Coastal tailed frog)
Function: Antimicrobial peptide that shows similar potency against Gram-negative bacteria and Gram-positive bacteria. Has a high hemolytic activity.
Subcellular location: Secreted.
Interaction partners:
Sequence:
GFKDLLKGAAKALVKTVLF
Protein: ARS-binding protein 1 (P49777)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds, preferentially, to the Maundrell ARS consensus sequence within ARS3002.
Subcellular location: Nucleus.
Interaction partners:
- CENP-B homolog protein 1
- Switch-activating protein 1
- CENP-B homolog protein 2
Sequence:
MGKIKRRAITEHEKRALRHYFFQLQNRSGQQDLIEWFREKFGKDISQPSVSQILSSKYSYLDNTVEKPWDVKRNRPPKYPLLEAALFEWQVQQGDDATLSGETIKRAAAILWHKIPEYQDQPVPNFSNGWLEGFRKRHILHAINEQPTESVVLNNTEPPNDPLSRVYDVTRLTNINDIFTMQETGLFWKLVPNGTPEVEDIKGITRFKARITLTVCCNASGTERLPLWVIGYSQSPRVFRAANVKPEVMNFKWRSNGKASMTTAIMEEWLRWFDACMEGRKVILLIDSYTPHLRAVENIRNSGNDLRNTTVITLPSTSASISQPCSEGVIYALKACYRKHWVQYILEQNELGRNPYNTTNVLRAILWLVKAWTTDISPEIIENAFNLSGVLGLFNESAVTSRALDEMIHPLRELVSEFSVQAAMRIEDFISPSEENIVDSSEDIINQIASQYMDDRAFETDEEESTEFQITTKDAMKAIELLLNYEAQQPDGNPAITISLLNYQKLLEARGGNVNLSRLRST
Protein: Actin-related protein 6 (gArp6) (gARPX) (Q9DEE9)
Organism: Gallus gallus (Chicken)
Function: Required for formation and/or maintenance of the proper nucleolar structure and function (By similarity). Plays a dual role in the regulation of ribosomal DNA (rDNA) transcription. In the presence of high glucose, it maintains active rDNA transcription through H2A.Z deposition and under glucose starvation, is required for the repression of rDNA transcription, and this function may be independent of H2A.Z.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P45890}. Nucleus {ECO:0000269|PubMed:16487625}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9GZN1}. Note=Colocalizes with HP1 family proteins at pericentric heterochromatin. {ECO:0000269|PubMed:16487625}.
Interaction partners:
- RuvB-like helicase
- E1A binding protein p400.
- RuvB-like helicase
- DNA methyltransferase 1 associated protein 1.
- Vacuolar protein sorting-associated protein 72 homolog
- Histone H2A.Z
- Histone H2A.V
- Coiled-coil domain containing 170.
- YEATS domain-containing protein 4
- Splicing factor 3B subunit 4
Sequence:
MATLVLDNGAYNAKIGYSHAHVSVIPNCQFRSKTARLKTFTANQLDEIKDPSGLFYILPFQKGYLVNWDVQRQVWDYLFGKEMYQVDFVDTNIIITEPYFNFSSIQESMNEILFEEYQFQAVLRVNAGALSAHRYFRDNPSELCCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDFYKDMEIAKLKGEENTVMVDYVLPDFSTIKKGFCKPREEMVLSGKYKTGEQILRLTNERFAVPEILFHPSDIGIQEMGIPEAIVDSIQNLPEEMQPHFFKNIVLTGGNTLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYSWEGGKLISENDDFEDLVVTREDYEEHGHNICEEKFDI
Protein: Asator, isoform D (EC 2.7.11.1) (Q9V4D6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFWHLLCVPNDENASAPDDGNQSCQPSSKQDQYLSPNRNCQKNLLRLYPPPPSKPPPLVGAILQTRLLHQISPSAIADADADLNAVGELLYPNVLQRSATLPAKHNRLGVRSRVTFKVPSSNLPAQDSYSHQPRNQVAVAAKDGILVDVKAKESVKMTSEDLLQPGHVVKERWKVVRKIGGGGFGEIYEGQDLITREQVALKVESARQPKQVLKMEVAVLKKLQGKEHVCRFIGCGRNDRFNYVVMQLQGKNLAELRRAQPRGAFSLSTTLRLGLQILKAIESIHSVGFLHRDIKPSNFSVGRLPYNCRRVYMLDFGLARQYTTGTGEVRCPRAAAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVNGQLPWRKIKDKEQVGLTKEKYDHRILLKHLPSDLKQFLEHIQSLTYGDRPDYAMLIGLFERCMKRRGVKESDPYDWEKVDSTAIGNISATGNPSIPIKSDYMHGNITQMTVAASNASGTEYIRKRAEIETAHITATDPLNIKEKVDKNCNATSLAQPAKGSGEPMVQHGNAANNQNITSKGLQQQSTLTNSQVAIANIQSAPSMIEREDVQYTKLEEGAPTKFITMKPNGECDNVDIAAKCIFEQKHVEANDDIVGRASLSGVEQHYKSQIKKHNSPEIANKQIQRTGTVTNDKTSEVNRSTEEQKSTFGRLRVLTAPPMSVHDLPSGGGHSHQVSDLSGKQDPYAATSNAAPIGINSSSTKFGSQHGQIFGLAAMPPINRRSATSTNLRPSSSASQRINSGSTIGGAVGNGSNTARSSVAGDHSVTQFALIDDENVSALQQVTKGGALTLASQWKSQFDDSEDTTDNEWNREHQLQPNLEQLIKLDISLPLNEAKPFPQHGVAGTGKLINPPGEAKGRPKRYTLNITGIENYEALRISIPNCWSEPAMGNVLRKGLEPPAVQQAAFDDTVYRMDIARNVCVRETYSEITHLARPSTSSVLRNRLPSPFKKDSALQLNSTNDSLDKSRHRNSLPNVSVNDIFDDLQMKLNLDLGSAIQENNCCISGRLEIRVIPKDTSHPDDSVYYDAMGAVKNTPTANEGHDHSDQAVNNCDEMEATSAVIAFPNKSISKIMSPPGRDATEERTGASLCSLYSAGVNKLKLNGNTAPRTQFKKGSTDGFGENESEFDFPLLNPSKIPVRQSKCASWAGADFISASKPLESAEVPQEIPYHPQSDTTYSVIDSIPVRKTTYSIALECPPNISDLTPGLRRRRESTEGKYVTDPTQLPLKFQRPRSRTSSRTRGIPNAMLENSDDNGTVMSAEKTGHGHVVKTEGVKNFTTSENSSEVNPKCTISPPPGDPKIENSARLRRYRHNID