wanglab/gogpt-training-data huggingface dataset:
Protein: Cryptochrome photolyase family 1 (B7FZ64)
Organism: Phaeodactylum tricornutum (strain CCAP 1055/1)
Interaction partners:
Sequence:
MAKSEEKKHDVAIHWFRNGLRFHDNPCLLDACQKSESLLPIYVVDPEFPFAQTAGCRAGTIRANFLLESINEVDEKLRKMGSQLVVVLGKSHEVLPEIVATTQAKALFYEQEAAAPVREQDAETIQAIKNRLKRDGKNYECKFEAYATHTLHPMERYLAQCKDHTAPSTYGSFTKIFNKMSVAKEVNEVKEVPSLPNKSVKLLEKSFAEALRMPTLKDLGYAAAADDMKNSGKGGYAFAGGENAAIELLAKNMARSQWVATFEKPKTSPNDATRPSTTALSPYVKHGCISPRRFYHELSKVYSKYNSKETSKPPVSLHGQLMWRDFNYLVGYSTPNFDKMIDNPIARQIPWDDDPDLLLAWKMSKTGYPYIDAIMTQLRETGWIHHLARHSVACFLTRGDLWQSWEDGATVFEEYLIDADWSINNFNWQWLSCTAHFYQYFRCYSPIAFGKKTDPNGDYIRKWLPQFKDMPAKYIYEPWEAPIELQKKVGVIVGENYPHPIVDHKLVSKNNMSRMKEAYDAQKNREPMPANESHSSGLNRDTSPKRQRRN
Protein: Uncharacterized protein C1orf105 (O95561)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKRELKASVPKFDKIPWLSEASLVNKPLVLSLPRRYPHTSATFLTSSKKNMNLPILFQVPDVLSKARRNQCDSMLLRNQQLCSTCQEMKMVQPRTMKIPDDPKASFENCMSYRMSLHQPKFQTTPEPFHDDIPTESIHYRLPILGPRTAVFHGLLTEAYKTLKERQRSSLPRKEPIGKTTRQ
Protein: Contactin-6 (Neural recognition molecule NB-3) (mNB-3) (Q9JMB8)
Organism: Mus musculus (Mouse)
Function: Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus (By similarity). Involved in motor coordination.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Neural cell adhesion molecule L1-like protein
- Receptor-type tyrosine-protein phosphatase gamma
Sequence:
MRLLWKLVILLPLINSCAGEGRFSRPIFIQEPQDVIFPLDLSRSEIILTCTANGYPSPHYRWKQNGTDIDFGMTYHYRLDGGSLAISSPRTDQDIGIYQCLATNPVGTILSRKAKLQFAYIEDFETKTRSTVSVREGQGVVLLCGPPPHFGELSYAWTFNDSPLYVQEDKRRFVSQDTGNLYFAKVEPSDVGNYTCFVTNKEAHRSVQGPPTPLVLRTDGVMGEYEPKIEVRFPETIQAAKDSSIKLECFALGNPVPDISWKRLDGSPMPGKIKYSKSQAILEIPKFQQEDEGFYECIAGNLRGRNLAKGQLIFYAPPEWEQKIQNTYLSIYDSLFWECKASGNPNPSYTWLKNGQRLNTEERIQIENGTLIITMLNISDSGIYQCAAENKYQTIYANAELRVLASAPDFSKNPIKKISVVQVGGDISIECKPNAFPKASISWKRGTENLKQSKRVLFLEDGSLKICNVTRADAGSYTCVATNQFGNGKSSGGLVVKERTIITVPPSKMDVTVGESIVLPCQVSHDPTMEVLFVWYFNGDIIDLKKGVAHFERIGGESVGDLMIRNIQLGHSGKYLCTVQTTLERLSAVADIIVRGPPGPPEDVKVEHISSTTSQLSWRPGPDNNSPIQIFTIQTRTPFSVGWQAVATVPEILNGQTYNATVVGLSPWVEYEFRVVAGNNIGIGEPSKPSELLRTKASVPNVAPGNINGGGGSRSELVITWEAIPEELQNGEGFGYIVMFRPVGTTAWMKERVALVESSKFIYRNESIMPLSPFEVKVGVYNNEGEGSLSTVTIVYSGEDEPQLAPRGTSVQSFSASEMEVSWNAIAWNRNTGRVLGYEVLYWTDNSKESMIGKIRVSGNVTTKNITGLRANTIYFASVRAYNTAGTGPSSLPVNVTTKKSPPSQPPANIAWKLSNSKLCLNWEHVKTMENESEVLGYKILYRQNRQSKTHILETNNTSAELLVPFEEDYLIEIRTVSDGGDGSSSEEIRIPKMSSLSSTGVQISKPSTQSLSMVGVFYCFAIHPLSR
Protein: Protein TraB (P41067)
Organism: Escherichia coli (strain K12)
Function: Involved in F pilus assembly.
Interaction partners:
Sequence:
MASINTIVKRKQYLWLGIVVVGTASAIGGALYLSDVDMSGNGETVAEQEPVPDMTGVVDTTFDDKVRQHATTEMQVTAAQMQKQYEEIRRELDVLNKQRGDDQRRIEKLGQDNAALAEQVKALGANPVTATGEPVPQMPASPPGPEGEPQPGNTPVSFPPQGSVAVPPPTAFYPGNGVTPPPQVTYQSVPVPNRIQRKVFTRNEGKQGPSLPYIPSGSFAKAMLIEGADANASVTGNESTVPMQLRITGLVEMPNSKTYDATGCFVGLEAWGDVSSERAIVRTRNISCLKDGKTIDMPIKGHVSFRGKNGIKGEVVMRNGKILGWAWGAGFVDGIGQGMERASQPAVGLGATAAYGAGDVLKMGIGGGASKAAQTLSDYYIKRAEQYHPVIPIGAGNEVTVVFQDGFQLKTVEEMALERTQSRAEEDNPESPVPVPPSAESHLNGFNTDQMLKQLGNLNPQQFMSGSQGGGNDGK
Protein: tRNA-splicing endonuclease subunit Sen2 (EC 4.6.1.16) (H7C2Z3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR011789}.
Interaction partners:
Sequence:
MAEAVFHAPKRKRRVYETYESPLPIPFGQDHGPLKEFKIFRAEMINNNVIVRNAEDIEQLYGKGYFGKGILSRSRPSFTISDPKLVAKWKDMKTNMPIITSKRYQHSVEWAAELMRRQGQDESTVRRILKDYTKPLEHPPVKRNEEAQVHDKLNSGMVSNMEGTAGGERPSVVNGDSGKSGGVGDPREPLGCLQEGSGCHPTTESFEKSVREDASPLPHVCCCKQDALILQRGLHHEDGSQHIGLLHPGDRGPDHEYVLVEEAECAMSEREAAPNEEAFFLVYALGCLSIYYEKEPLTIVKLWKAFTVVQPTFRTTYMAYHYFRSKGWVPKVGLKYGTDLLLYRKGPPFYHASYSVIIELVDDHFEGSLRRPLSWKSLAALSRVSVNVSKELMLCYLIKPSTMTDKEMESPECMKRIKVQSRSVVQAGVQCCDLGSLQPLPAGFKRFSCLSLLSSWDYRHAPPHTANFCIFSRDGVSLCWPGWSGTPDLK
Protein: Voltage-dependent calcium channel beta subunit-associated regulatory protein (Q8N350)
Organism: Homo sapiens (Human)
Function: Negatively regulates voltage-gated calcium channels by preventing the interaction between their alpha and beta subunits. Thereby, negatively regulates calcium channels activity at the plasma membrane and indirectly inhibits calcium-regulated exocytosis.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q66L44}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:Q66L44}. Cell membrane {ECO:0000250|UniProtKB:Q66L44}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:Q66L44}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q66L44}.
Interaction partners:
Sequence:
MQPTATMATAATTTTTTTATVALTTSWDNATGRPTAEPDPILDNYVLLVVVMSLFVGGTLVVLSGVLLLCKRCWDVHQRLNRAMEEAEKTTTTYLDNGTHPAQDPDFRGEDPECQDAETERFLSTSSTGRRVSFNEAALFEQSRKTQDKGRRYTLTEGDFHHLKNARLTHLHLPPLKIVTIHECDSGEASSATTPHPATSPKATLAIFQPPGKALTGRSVGPSSALPGDPYNSAAGATDFAEISPSASSDSGEGTSLDAGTRSTKAGGPGAAAGPGEAGPGSGAGTVLQFLTRLRRHASLDGASPYFKVKKWKLEPSQRAASLDTRGSPKRHHFQRQRAASESTEQEEGDAPQEDFIQYIARAGDAVAFPHPRPFLASPPPALGRLEAAEAAGGASPDSPPERGAGSAGPEQQQPPLEPDAERDAGPEQAQTSYRDLWSLRASLELHAAASDHSSSGNDRDSVRSGDSSGSGSGGAAPAFPPPSPPAPRPKDGEARRLLQMDSGYASIEGRGAGDDTEPPAAPARPRSPRAWPRRPRRDYSIDEKTDALFHEFLRHDPHFDDTPAAARHRARAHPHARKQWQRGRQHSDPGARAAPALAGTPAPPAGAARPARAPLRRGDSVDGPPDGRTLGGAGDDPAIPVIEEEPGGGGCPGSGLCVLPSGSVLDKLAAGLDERLFPPRLAEPVVATPALVAAAPTSPDHSPA
Protein: Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49) (Q75JD5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable malate dehydrogenase 1
- Probable malate dehydrogenase 3
- Probable malate dehydrogenase 2, mitochondrial
- Enolase B
- Enolase A
- phosphoenolpyruvate carboxylase
- Probable ATP-citrate synthase
- Pyruvate kinase
- Citrate synthase, mitochondrial
- Citrate synthase
Sequence:
MNQAVAESINKSLKSSTADYTPKGYHITELESDSIYLDEHFSGNAKIFHNPAVAVLYEQALAFEHGSAITSTGALVTRSGVKTGRSPKDKRIVKEPSSQDDIWWGPVNIAMDDLSFMINRERAIDYLNTQEKIYVIDGYAGWDPKYRIKVRVICARAYHALFMHNMLIRPANREELRNFGEPDYTIYNAGQFPANRYTKGMSSSSSIAIDFARKEMVILGTQYAGEMKKGILTIMMYLMPKMGVLPLHSSCNQARNNGDTTLFFGLSGTGKTTLSADINRELIGDDEHVWTDTGCFNIEGGCYAKCIDLSREKEPEIFDAIKFGAVLENVVYNEYSRKVDYNDVSITENTRCAYPLEHIPNAKFPAIAGHPKNIIMLTCDAFGILPPVSRLDANQVMYHFIQGYTAKVAGTEVGVTEPTATFSSCYGEPFIVWHPTKYAEMLASQLHKHSARAWLINTGWTGGSHGVGSRIKLAYTRAIIDAIHSGELEKIPTTKMDVFGFQVPNSCPGVPSEILMPINGWADKEKYVSTMHKLAKLFIENFKKFQDKASPELVAAGPILPQ
Protein: Homeobox protein extradenticle (Dpbx) (P40427)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription factor which acts with the selector homeodomain proteins altering the regulation of downstream target genes such as wingless (wg), teashirt (tsh) and decapentaplegic (dpp), thus affecting segmental identity. Delimits the eye field and prevent inappropriate eye development. Required for proper localization of chordotonal organs within the peripheral nervous system.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:9346235, ECO:0000269|PubMed:9450936, ECO:0000269|PubMed:9463350}. Note=Nuclear translocation requires interaction with hth.
Interaction partners:
- Homeobox protein homothorax
- Homeobox protein abdominal-B
- Homeobox protein abdominal-A
- Homeotic protein ultrabithorax
- Homeotic protein Sex combs reduced
- Homeotic protein deformed
- Homeotic protein antennapedia
- Homeotic protein distal-less
- Homeotic protein labial
- Protein teashirt
Sequence:
MEDPNRMLAHTGGMMAPQGYGLSGQDDGQNAGSENEVRKQKDIGEILQQIMSISEQSLDEAQARKHTLNCHRMKPALFSVLCEIKEKTVLSIRNTQEEEPPDPQLMRLDNMLIAEGVAGPEKGGGGAAAASAAAASQGGSLSIDGADNAIEHSDYRAKLAQIRQIYHQELEKYEQACNEFTTHVMNLLREQSRTRPITPKEIERMVQIIHKKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQASEILNEYFYSHLSNPYPSEEAKEELARKCGITVSQVSNWFGNKRIRYKKNIGKAQEEANLYAAKKAAGASPYSMAGPPSGTTTPMMSPAPPQDSMGYPMGSGGYDQQQPYDNSMGGYDPNLHQDLSP
Protein: Uncharacterized membrane protein At1g75140 (Q9FRK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MADSQNGKSAFFFFFVSLILLFLSPSYSDVTASESDPIPYENSDASPGVVTSSESDRQGVSLHRLEELVRNLTELVARLDAKLSETPFKVKKEITRDEIEEKAKAFSVTKYSPFWSERFEFTSAVKLDSEATCINVLPFRDHEGLSKYFAVGDSSGRVFVFLRNGDVLVEFFTTCDSPITAMVSYMSVYKNESFVVTGHQSGVILLHRLREGSIGEDLNSAVMENVGKFDGTEDGLQVTLLEVHHVGRVRYILATDLSGKLTVFTENRTVYGSVSPTSRPLVFLKQRLLFLTETGAGSLDLRSMKIRESECEGLNHSLARSYVFDASERAKAYGFTSEGEIIHVLLLGDIMNFKCRVRSKKKVQMEEPVALQAIKGYLLIVNQEKVFVYNVSTQHYVRTTGPRLLFPAALEDIRSTFLSHRESTKTTDHQKLEKVTPLIASDREKLLVMGLGDGYVATYKSKLPISKAEFNTMLWSSPVFFFILFLFGAWHFFSKKKESLTAWGPDDPFSSTTMSSSSTTTAQNSSAFSESTRRNDDHMDLRRRYVSPSRYPPGAATGAYRSVGSNDPSSRAPVETTNYRTTAQEMKYRGGSGLDSGGFGKRRESLFGNNKALDDES
Protein: Transcriptional activator Myb isoform 1 (V-myb avian myeloblastosis viral oncogene homolog) (F1QP24)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Runt-related transcription factor
- GATA-binding protein 1a.
- V
- histone acetyltransferase
- CREB-binding protein b.
- CCAAT/enhancer-binding protein.
- SI:bY184L24.2.1
- Endothelial transcription factor GATA-2b
- Rhombotin-2
- Plastin-2
Sequence:
MARRHRHSVYSSDEDDDDVEIYDHDYDGPHAKTGKRHLGKTRWTREEDEKLKRLVEHHGSEDWKVIASFLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDQIIYQAHEKLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQHAAKVSPTPLNNSYSKPHLLNYNHTPSNTSMPASSMSNQYPYYTESSRVPFPLALQLNILNFPQHGTAAIQRHYSDEDPEKEKRVKEIEMLLMSTENELKGQQALPISMNGYGGWNRGSLADSSVGIVVSVPAPSLEQGCLPEESAHGNTNSPNNDSSSTLPEFIDAIDSAPSVWANKHPKTECQTGQGSPANNGNRSAPTFLCSTPKYSSVRHLPFSPTQFFNASVSPDSDSQNIPVTPSPVCSQKALQQDLALRPQKENELFRTPNLRRSIMECSPRTPTPFKSTLTMQDSKYGPLKRVHSPSLDSGVVGTIKQEPQECEISVGGVHLDQPPLKKIKQEVESVCLQWEGQDLHTQLFPSNGPAHDMPDLLTSSVLMLPNTEKTEDGHKAAQLPRRPIGSPLQQLNTWEQVLCGKTEEQTIPSEATHKYLSNYSSRALVI
Protein: E3 ubiquitin-protein ligase MARCHF9 (EC 2.3.2.27) (Membrane-associated RING finger protein 9) (Membrane-associated RING-CH protein IX) (MARCH-IX) (RING finger protein 179) (RING-type E3 ubiquitin transferase MARCHF9) (Q86YJ5)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I, CD4 and ICAM1, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17174307}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 H
Sequence:
MLKSRLRMFLNELKLLVLTGGGRPRAEPQPRGGRGGGCGWAPFAGCSTRDGDGDEEEYYGSEPRARGLAGDKEPRAGPLPPPAPPLPPPGALDALSLSSSLDSGLRTPQCRICFQGPEQGELLSPCRCDGSVRCTHQPCLIRWISERGSWSCELCYFKYQVLAISTKNPLQWQAISLTVIEKVQIAAIVLGSLFLVASISWLIWSSLSPSAKWQRQDLLFQICYGMYGFMDVVCIGLIIHEGSSVYRIFKRWQAVNQQWKVLNYDKTKDIGGDAGGGTAGKSGPRNSRTGPTSGATSRPPAAQRMRTLLPQRCGYTILHLLGQLRPPDARSSSHSGREVVMRVTTV
Protein: DNA mismatch repair protein Msh2 (MutS protein homolog 2) (P54275)
Organism: Rattus norvegicus (Rat)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containing DNA strand. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P43246}. Chromosome {ECO:0000250|UniProtKB:P43246}.
Interaction partners:
- DNA mismatch repair protein Mlh1
- DNA mismatch repair protein
- DNA mismatch repair protein
- Mismatch repair endonuclease PMS2
- MutL homolog 3
- PMS1 homolog 1, mismatch repair system component
- DNA polymerase delta catalytic subunit
- Exonuclease 1
- DNA excision repair protein ERCC-1
- Breast cancer type 1 susceptibility protein homolog
Sequence:
MAVQPKETLQLEGAAEVGFVRFFEGMPEKPSTTVGLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKTLQTVVLSKMNFESFVKDLLLVRHYRVEVYKNKAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMATSIGIMGIKLSTVDGQRQVGVGDVDSTQRKLGLCEFPDNDQFSNLEALLIQIGPKECILPGGETAGDMGKLRQVIQRGGILITERKRIDFSTKDIYQDLNRLLKGRKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELATFDFSQYMKLDMAAVRALNLFQGSVEDTTGSQSLAAFLNKCKTAQGQRLVSQWIKQPLMDKNRIEERLNLVEAFVEDSELRRALQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGVKQLPNVIQALEKYQGRHQALLLAVFVTPLTDLRSDFSKFQEKIETTLDMDQVENHEFLVKPSFDPNLSELREVMDGLEKKMQSTLISAARGLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSELSSLNEEYTKNKGEYEEAQDAIVKEIVNISSGYVEPMQTVNDVLAHLDAVVSFAHVSNAAPVPYVRPVILEKGKGRIIVKASRHACVEVQHDVAFIPNDVHFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATNIGAFCMFATHFHELTALASQIPTVNNLHVTALTTEETLTMLYQVKTGVCDQSFGIHVAELANFPRHVIECAKQKALELEEFQSIGTSQGHDETQPAAKRRCLEREQGEKIILEFLSKVKQVPFTDLSEESVSVKLKQLKAEVLAKNNSFVNEIISRVKAP
Protein: Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha) (Q14012)
Organism: Homo sapiens (Human)
Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-694', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation (By similarity). Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}.
Interaction partners:
- Calmodulin-1
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Calmodulin-like protein 6
- Nitric oxide synthase 3
- Cyclic AMP-responsive element-binding protein 1
- Protein phosphatase 1F
- Neuronal migration protein doublecortin
Sequence:
MLGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKEALEGKEGSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAKSKWKQAFNATAVVRHMRKLQLGTSQEGQGQTASHGELLTPVAGGPAAGCCCRDCCVEPGTELSPTLPHQL
Protein: LD40380p (Q8SX63)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFMCLSRTQEMSMSCFPPGTMARYFCGTSSRGVCVANFLNDIDGQGHGSVFDAKWSPDGTMIAATDSHGHILIFGLGVCIEKYKMLPTELFFHTDFRPLLRDAQHHVVDEQTQIMPHLMPPPFLVDADGNPHPSRFQRFVPGRESCSLDQLIPNLTVGVDGVVIDDGGAGGDAVVAAAPAEAPPAALPPAAAGGPQGANYSHIDRMIAALANRQSVNVNANDANPTNGNQSFERLTNRQMPDSNGRQSSRGNVLGSRLSTPRQGWGAAAAAPVEDQAGPSQPPAEPAAEPGQAQVQQALPLKFIRRTYVRPMKYPQLQNLKQTIYSAGQFEKQEYKREMRRRPIMINTASAASSQQPGSVGRPRNTRGNGGGARAGRRRGPQPAGGQPQPAYRTRAVRDQEPEHYDEVAPPPEEEEEDVSSNSSGDTSYSNVEENLEDSSDESETDSSDYSDWVADTPGPNLEPPKRSKRKPLSRRPRSSDDSSDDERAGRSRGGQVTARKVGRKTVLFPPTDANGEIPELYRPAEWLSEVIPRKAPYYPQMGDEVVYFRQGHAKYLDAVRLKKVYKLSHSSEPWNFHTLRDHELVRVIGIKYEIRPPRLCCLKLAIIDEEGNMTGTTFKIKYHDMPDVLDFLVLRQTFDLAVQRNWSIGDRFRCMIVDGWWMGQIESRHALSADFPDSSFMCFRVRWDNGEYEFMSPWDMEPIDQQRVPDEVGGAVPVLPEEIRATLYQPKSEEWHRGDRDGTCRRIINGLEQVMRLSIAEHFLAPVDLNIYPDYAYLIEYPIDLTTIKSRFENHFYRRITSAQFDVRYLATNAEQYNRRHAIIVKHSRIVTDLCLRIIREPDEIDVAAVYHQLADVYHSSESENEVDSDVVPSTSTGPTTSAAAAAARQRVSSARRSTRIHSEGDWRADCRQLLDLMWARTDSAPFREPVDTIDFPDYLEIIATPMDLRTVKEDLLGGNYDDPLDFAKDVRLIFQNSKNYNTNKRSRIYAMTLRLSALFESHIKTVVTSWKAALRRANKNKSGSSGGGRGGSSSSPNKRVKKERSTRRNQKPTAAARRLPVANSSEDEDEEDDDDDDDDDDEEEASTRGRSRRRNGVAVSASSSGSNRVTSSSAAQQRRGKSSSSEEEEEEETSAQATSDASSDEEERAQSNDSSPQQTRTRRARQRQRLSDDSNINDSEDSYNPNEGRGSRRRPGAARPSSNRQTNGHSSKRRRLNKSPANAAPGPSLPRRTRRIAGSSAEEAASHSQHDESTQDSQIGRRKGRSASSRSIGNGPSTSAAAAANSSLESPSRNTRANGTRTSSHLGAENDHSYHLPVRNGRIIESDTDSPVIRPTRQSAKRALMDWGRGSDIEEEEEEEEEDSEEAEEILPTPTKDDLPSTSRAALAQAAAGPSRQLRTNRNTVVRPAQSDDDDDDDSDNEPLANNQQKNYQSPAKSSSTATVAPHPLSLRRRLASPPERNTHMTRSHATSTTSSAAASRAEQQPAVSTHDHNYLGNVNSSRAPRRILSRHQRNADELDTSLDVLENSRLLSAIANHRRPTSTTNSNSASNVVTRRLRGRASQANSHDEDHEEEEAAASDEGTDGGSSSQSYEDEDEDSDSEDNQPLTSYVSPSNGRPRRKAKTSSSSATTQERPLRRTRRPPSNNSIANDNDDDDDYVVPRSRRANRGGNQRAGRNQKRPRYNEQSEEEEAAAGYSHRSKRIRNGDAHASSQERSQASTERDQEEEEDGTSVDSEEQQVNVSSRGRVRKPSAKARGIFKE
Protein: Spondin-1 (F-spondin) (O42114)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MMDKDGLVVLLVFLNVFLIHSDAFKRDTAERHSRSEGGFCRILRTQARSARRDGQNEFRLKVEGEPETYQPGSTYRVSLYASSPSYFRGFTLIALKEGREGVSPDDYAGTFKLIDESDTQFMTNCPPAVTESIPRRRTRIQVFWTAPPSGSGCVTLKASVVQRRIIFFQDEGSLTKRLCEKDPVAITEKPAQECCACGTAKYRVTFYGNWSEKLDPKDYPRRANHWSALIGASHTRSYVLWEYGGFASEGVKQVSEYGSPVKMEEEIRQKGDDVMTVIKTKAQWPAWQPLNIRAAPSAEFSVDRVRHLISFLTMLGPSPDWNVGLSGEDLCTRDCGWVQKLVKDLVPWDAGTDSGVSYESPNKPSIPQERIRPLTSLDHPQSPFYDPSGGPMTPLGRVVVERIARKGEQCNTVPDTIDDIVADIAQEEKEEGDNTPETCIYSNWSPWSACSSSTCDKGRRMRQRMLKAQLDPNLPCLHTQDFEPCMGPGCSEEEASTCMMSEWISWSPCSASCGMGMRSRERYVKQFPEDGSSCTLPTEETEKCVVNDDCSPSSCVVTEWGEWEPCSVSCGLGMRRRERMMKMDASDGSPCRVQMAEAEKCMMPECNAVVCMLSPWSDWGECSVSCGVGMRTRQRMLKTPVKPGQCPDELEQVEKCMLPECPTDCMLSEWSAWSECNKSCGKGHMIRSRMVKLEPQFGGLPCPETVQRKKCKIRKCSRGSRASEKRKRQEVSDRRRAKQSRESVAEESTVCPIRPWSSWTECTKPCDGGTQERVMTIKKKGKSSQHNHCKNKKEIRACNVHPC
Protein: Beta-amyrin 28-monooxygenase (EC 1.14.14.126) (Beta-amyrin 28-oxidase) (Cytochrome P450 716A12) (MtCYP716A12) (Protein LACKING HEMOLYTIC ACTIVITY) (Q2MJ20)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Catalyzes the carboxylation of beta-amyrin at the C-28 position to form oleanolic acid. Involved in an early step in the hemolytic saponin biosynthetic pathway. Catalyzes the carboxylation of alpha-amyrin and lupeol at the C-28 position to form ursolic acid and betulinic acid respectively.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Beta-amyrin synthase
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
Sequence:
MEPNFYLSLLLLFVTFISLSLFFIFYKQKSPLNLPPGKMGYPIIGESLEFLSTGWKGHPEKFIFDRMRKYSSELFKTSIVGESTVVCCGAASNKFLFSNENKLVTAWWPDSVNKIFPTTSLDSNLKEESIKMRKLLPQFFKPEALQRYVGVMDVIAQRHFVTHWDNKNEITVYPLAKRYTFLLACRLFMSVEDENHVAKFSDPFQLIAAGIISLPIDLPGTPFNKAIKASNFIRKELIKIIKQRRVDLAEGTASPTQDILSHMLLTSDENGKSMNELNIADKILGLLIGGHDTASVACTFLVKYLGELPHIYDKVYQEQMEIAKSKPAGELLNWDDLKKMKYSWNVACEVMRLSPPLQGGFREAITDFMFNGFSIPKGWKLYWSANSTHKNAECFPMPEKFDPTRFEGNGPAPYTFVPFGGGPRMCPGKEYARLEILVFMHNLVKRFKWEKVIPDEKIIVDPFPIPAKDLPIRLYPHKA
Protein: Diacylglycerol O-acyltransferase 2 (RcDGAT2) (EC 2.3.1.20) (A1A442)
Organism: Ricinus communis (Castor bean)
Function: Involved in triacylglycerol (TAG) synthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diricinolein using ricinoleoyl-CoA.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ASU1}; Multi-pass membrane protein {ECO:0000255}. Lipid droplet {ECO:0000250|UniProtKB:Q9ASU1}.
Interaction partners:
- O-acyltransferase
- Phosphatidylcholine: Diacylglycerol Acyltransferase
- phospholipid:diacylglycerol acyltransferase
- phospholipid:diacylglycerol acyltransferase
- Phosphatidic acid phosphatase, putative
- ER Phosphatidate Phosphatase
- Phosphatidic acid phosphatase, putative
- Phosphatidic acid phosphatase, putative
- phosphatidate phosphatase
- phosphatidate phosphatase
Sequence:
MGEEANHNNNNNNINSNDEKNEEKSNYTVVNSRELYPTNIFHALLALSIWIGSIHFNLFLLFISYLFLSFPTFLLIVGFFVVLMFIPIDEHSKLGRRLCRYVCRHACSHFPVTLHVEDMNAFHSDRAYVFGYEPHSVFPLGVSVLSDHFAVLPLPKMKVLASNAVFRTPVLRHIWTWCGLTSATKKNFTALLASGYSCIVIPGGVQETFYMKHGSEIAFLKARRGFVRVAMEMGKPLVPVFCFGQSNVYKWWKPDGELFMKIARAIKFSPIVFWGVLGSHLPLQRPMHVVVGKPIEVKQNPQPTVEEVSEVQGQFVAALKDLFERHKARVGYADLTLEIL
Protein: Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Allergen Scy p 8) (Methylglyoxal synthase) (EC 4.2.3.3) (Triose-phosphate isomerase) (allergen Scy p 8.0101) (A0A1L5YRA2)
Organism: Scylla paramamosain (Mud crab)
Function: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
Interaction partners:
Sequence:
MANQRKFFVGGNWKMNGDKAAIDGIISFMKGPLNADTEVVVGCPQCYLMYTREHMPANIGVAAQNCYKTAKGAFTGEISPAMIKDCGCEWVILGHSERRNVFGEPDQLISEKVGHALEAGLKVIPCIGEKLEERESNRTEEVVFAQMKALVPNISDWSRVVIAYEPVWAIGTGKTATPEQAQDVHAKLRQWLRDNVSPQVAESTRIIYGGSVSAGNCKELAKTGDIDGFLVGGASLKPDFVTIINARA
Protein: Uncharacterized protein MJ0480 (Q57904)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Adenylate kinase
- Uncharacterized protein MJ0606
- Protein translocase subunit SecY
Sequence:
MFGSIFDIYYKTLDAIFMPIIKVLHPALAILIIAIIVSLIINIATKLLVDQKRVAELKKEIQEFQVKFKKMSKNPEMMEKLQEEQQRIMQLNAELMKMSFRPMIYTWVPIILIFIYLRHVYGFGGVYQELNPGWNGVVVYLPIILSKILFIDFWHWLGSIFYKGGFKIVSNTALGWLGWYILCSFATSTVLRKILGIK