wanglab/gogpt-training-data huggingface dataset:
Protein: Rho GTPase-activating protein 15 (ArhGAP15) (Rho-type GTPase-activating protein 15) (Q53QZ3)
Organism: Homo sapiens (Human)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12650940}. Membrane {ECO:0000269|PubMed:12650940}; Peripheral membrane protein {ECO:0000269|PubMed:12650940}.
Interaction partners:
- tRNA-queuosine alpha-mannosyltransferase
Sequence:
MQKSTNSDTSVETLNSTRQGTGAVQMRIKNANSHHDRLSQSKSMILTDVGKVTEPISRHRRNHSQHILKDVIPPLEQLMVEKEGYLQKAKIADGGKKLRKNWSTSWIVLSSRRIEFYKESKQQALSNMKTGHKPESVDLCGAHIEWAKEKSSRKNVFQITTVSGNEFLLQSDIDFIILDWFHAIKNAIDRLPKDSSCPSRNLELFKIQRSSSTELLSHYDSDIKEQKPEHRKSLMFRLHHSASDTSDKNRVKSRLKKFITRRPSLKTLQEKGLIKDQIFGSHLHKVCERENSTVPWFVKQCIEAVEKRGLDVDGIYRVSGNLATIQKLRFIVNQEEKLNLDDSQWEDIHVVTGALKMFFRELPEPLFPYSFFEQFVEAIKKQDNNTRIEAVKSLVQKLPPPNRDTMKVLFGHLTKIVAKASKNLMSTQSLGIVFGPTLLRAENETGNMAIHMVYQNQIAELMLSEYSKIFGSEED
Protein: Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1) (P91079)
Organism: Caenorhabditis elegans
Function: Component of the serine palmitoyltransferase (SPT) that catalyzes the first committed step in sphingolipid biosynthesis, which is the condensation of an acyl-CoA species and L-serine. The catalytic core is composed of a heterodimer of sptl-1 and sptl-2 or sptl-1 and sptl-3 (By similarity). Required for the specification of abicobasal polarity and development of the gut lumen.
Interaction partners:
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 3
- 3-dehydrosphinganine reductase
- Sphingosine kinase 1
- Alkaline ceramidase
- Ceramide kinase 1
- Ceramide glucosyltransferase 3
- Ceramide synthase hyl-2
- Serine hydroxymethyltransferase
- Probable acid ceramidase
Sequence:
MGFLPDSWHFYIETLLVALLAYVVMRNRSKRQQEKLSKKLTERQKDELIADWTPEPLVPETPQDHPVLNPKYADGKMTKDVSIDGEKYLNMASTNFLSFIGVKRIEDRAKQTIFKYGVGSCGPRGFYGTVDVHLDLEKELAKFMGCEEAVLYSYGFATVSSAIPAYAKKGDVIFVDEGVNFAIQKGLQASRSRVEYFKHNDMEHLERLLLEQEQRDKKDPKKAKSVRRFIVVEGLYVNYADLCPLPKIIEFKWRFKVRVFIDESWSFGVIGKTGRGVTEHFNVPMEDVDMVMASLENALASTGGFCVGRSYVVGHQRLSGLGYCFSASLPPLLATAASEAISIIDEEPSRVQKVTEMAINGQKKLQDALSGSKFSLQGCPESPMKHIYYNGEDEEKQLDTFVETVFTKNHLLLTRARYLDKDELFKIRPSIRVMFQHDLTEEEIQRAVDAIRVVAHKF
Protein: Checkpoint protein HUS1 (hHUS1) (O60921)
Organism: Homo sapiens (Human)
Function: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase.
Subcellular location: Nucleus {ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:11077446}. Cytoplasm, cytosol {ECO:0000269|PubMed:11077446}. Note=In discrete nuclear foci upon DNA damage (PubMed:11077446). According to PubMed:11077446, localized also in the cytoplasm (PubMed:11077446). DNA damage induces its nuclear translocation (PubMed:11077446). Shuttles between the nucleus and the cytoplasm (PubMed:11077446). {ECO:0000269|PubMed:11077446}.
Interaction partners:
- Cell cycle checkpoint control protein RAD9A
- Cell cycle checkpoint protein RAD17
- Cell cycle checkpoint protein RAD1
- DNA topoisomerase 2-binding protein 1
- Serine/threonine-protein kinase ATR
- Replication factor C subunit 2
- Cell cycle checkpoint control protein RAD9B
- Replication factor C subunit 4
- RAD9, HUS1, RAD1-interacting nuclear orphan protein 1
- Replication factor C subunit 5
Sequence:
MKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSMWCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLTVSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMKNISNHLVIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDIRKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS
Protein: GDP/UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolyzing) (EC 3.2.1.184) (Q0P8T0)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into flagellin via O-linkage to Ser/Thr. Catalyzes the conversion of GDP-N,N'-diacetylbacillosamine (Bac2Ac4Ac) into 2,4-diacetamido-2,4,6-trideoxymannose and GDP. It can also use UDP-N,N'-diacetylbacillosamine however it generates small quantities of 2,4-diacetamido-2,4,6-trideoxymannose.
Interaction partners:
- N,N'-diacetyllegionaminic acid synthase
- Sugar-phosphate nucleotide transferase
- CMP-N,N'-diacetyllegionaminic acid synthase
- Nucleotide sugar dehydratase
- Uncharacterized protein
- Oxidoreductase
- 6-hydroxymethylpterin diphosphokinase MptE-like domain-containing protein
- PseE protein
- Aminotransferase
- PseD protein
Sequence:
MSKRKICIVSATRAEWYLLRNLCHEIQNDKDLSLQIIATGAHLSPEFGLTYKEIEKEFKITKKIPILLANDDKISLCKSMSLAFSAFSDAFEDLKPDMVVILGDRYEMLSVASVCLLMHIPLVHLCGGELTLGAIDDSIRHSISKMSHLHFVSHEIYKKRLLQLGEEEKRVFNIGSLASTIIKNMNFLNKKDLEKALEMKLDKELYLITYHPLTLNVKNTQKEIKTLLKKLDTLKNASLIFTKANADENGLLINEILQNYCQKNSHKAKLFDNLGSQKYLSLMKIAKAMIGNSSSGISESPFFKTPCINIGDRQKGRLRTQNIIDSEINDLDQAFEKLESKEFKQNLKNFKNPYDNGKNPNKIIKTCLKNVNLDTILHKNFIDL
Protein: T. brucei spp.-specific protein (Q4GZD8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNSHIFHFPSPSSVCVCVCTPSAAAIVCACNKIFFLVRMMCPLLLRFSCYSVQLQFCYLCSLPLFFFLFPLLFYSLIFSFVFTAGCWTSTTHLRP
Protein: Lethal(2) giant larvae protein homolog SRO7 (Polarity protein SRO7) (Sodium protection protein 1) (Suppressor of RHO3 protein 7) (Q12038)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as an allosteric regulator of polarized exocytosis by promoting the targeted fusion of vesicles with the plasma membrane. Coordinates the spatial and temporal nature of both Rab-dependent tethering and SNARE-dependent membrane fusion of exocytic vesicles with the plasma membrane. Required for targeting of the sodium pumping ATPase ENA1 to the Cell Surface, thus being involved in maintenance of ion homeostasis in cells exposed to NaCl stress. May be involved in the targeting of the myosin proteins to their intrinsic pathways. Multicopy suppressor of RHO3. May also participate in the maintenance of cell polarity and bud growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10402465, ECO:0000269|PubMed:9837945}. Cell membrane {ECO:0000269|PubMed:10402465}; Peripheral membrane protein {ECO:0000269|PubMed:10402465}; Cytoplasmic side {ECO:0000269|PubMed:10402465}.
Interaction partners:
- Protein transport protein SEC9
- Ras-related protein SEC4
- Exocyst complex component EXO84
- Protein SSO1
- Exocyst complex component SEC15
- Myosin-2
- GTP-binding protein RHO3
- Exocyst complex component SEC8
- Exocyst complex component SEC3
- Exocyst complex component EXO70
Sequence:
MFGSKRLKNVKEAFKSLKGQNSETPIENSKASFKSKNSKTSTISKDAKSSSSLKIPISSNNKNKIFSLAETNKYGMSSKPIAAAFDFTQNLLAIATVTGEVHIYGQQQVEVVIKLEDRSAIKEMRFVKGIYLVVINAKDTVYVLSLYSQKVLTTVFVPGKITSIDTDASLDWMLIGLQNGSMIVYDIDRDQLSSFKLDNLQKSSFFPAARLSPIVSIQWNPRDIGTVLISYEYVTLTYSLVENEIKQSFIYELPPFAPGGDFSEKTNEKRTPKVIQSLYHPNSLHIITIHEDNSLVFWDANSGHMIMARTVFETEINVPQPDYIRDSSTNAAKISKVYWMCENNPEYTSLLISHKSISRGDNQSLTMIDLGYTPRYSITSYEGMKNYYANPKQMKIFPLPTNVPIVNILPIPRQSPYFAGCHNPGLILLILGNGEIETMLYPSGIFTDKASLFPQNLSWLRPLATTSMAASVPNKLWLGALSAAQNKDYLLKGGVRTKRQKLPAEYGTAFITGHSNGSVRIYDASHGDIQDNASFEVNLSRTLNKAKELAVDKISFAAETLELAVSIETGDVVLFKYEVNQFYSVENRPESGDLEMNFRRFSLNNTNGVLVDVRDRAPTGVRQGFMPSTAVHANKGKTSAINNSNIGFVGIAYAAGSLMLIDRRGPAIIYMENIREISGAQSACVTCIEFVIMEYGDDGYSSILMVCGTDMGEVITYKILPASGGKFDVQLMDITNVTSKGPIHKIDAFSKETKSSCLATIPKMQNLSKGLCIPGIVLITGFDDIRLITLGKSKSTHKGFKYPLAATGLSYISTVEKNNDRKNLTVIITLEINGHLRVFTIPDFKEQMSEHIPFPIAAKYITESSVLRNGDIAIRVSEFQASLFSTVKEQDTLAPVSDTLYINGIRIPYRPQVNSLQWARGTVYCTPAQLNELLGGVNRPASKYKESIIAEGSFSERSSDDNNANHPEHQYTKPTRKGRNSSYGVLRNVSRAVETRWDAVEDRFNDYATAMGETMNEAVEQTGKDVMKGALGF
Protein: Calcium/calmodulin-dependent protein kinase II inhibitor 1 (calcium/calmodulin-dependent protein kinase II inhibitor alpha) (CaM-KIINalpha) (CaMKIINalpha) (Q9JI15)
Organism: Rattus norvegicus (Rat)
Function: Potent and specific inhibitor of CaM-kinase II (CAMK2). Plays a role in the maintenance of long-term retrieval-induced memory in response to contextual fear (By similarity). Modulates blood pressure and vascular reactivity via regulation of CAMK2 activity in addition to regulation of left ventricular mass. Mediates the NLRP3 inflammasome in cardiomyocytes via acting as an inhibitor of the MAPK14/p38 and MAPK8/JNK pathways, thereby regulating ventricular remodeling and cardiac rhythm post-myocardial infarction (By similarity). Negatively effects insulin sensitivity and promotes lipid formation in adipose tissues independent of CAMK2 signaling.
Subcellular location: Synapse {ECO:0000250|UniProtKB:Q6QWF9}. Cell projection, dendrite {ECO:0000269|PubMed:11182241}. Postsynaptic density {ECO:0000250|UniProtKB:Q6QWF9}.
Interaction partners:
Sequence:
MSEVLPYGDEKLSPYGDGGDVGQIFSCRLQDTNNFFGAGQSKRPPKLGQIGRSKRVVIEDDRIDDVLKTMTDKAPPGV
Protein: AFG3 like matrix AAA peptidase subunit 2 (F1LN92)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- AFG3
- ATP-dependent clpX-like chaperone, mitochondrial
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Prohibitin 1
- Prohibitin-2
- Single-pass membrane protein with aspartate-rich tail 1.
- Mitochondrial-processing peptidase subunit alpha
- ATP-dependent Clp protease proteolytic subunit
- Lon protease homolog, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
Sequence:
MAHRCLLLWGRGGCRRGLPPLLVPSGCLGPGRRPCLRTLYQYATVQTANSRSSLLRDVIAAYQRFCSRPPKGFEKYFPNGKNGKKASESKEAVGEKKESQLSGPQSSGGASGGGGKRRGKKEDSHWWSRFQKGDFPWDDKDFRMYFLWTALFWSGVMIYFLFKSSGREITWKDFVNNYLSKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPTVLIIAFLLYTIRRGPAGIGRTGRGMGGLFSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARMIDDEVRILISEAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGPRPFTEKSTYEEFVEGTGSLDEDTSLPEGLQDWNKEREKEKKEKKEKEEPVNEKVVS
Protein: Complement C1q tumor necrosis factor-related protein 6 (Q9BXI9)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Complement C1q tumor necrosis factor-related protein 1
Sequence:
MQWLRVRESPGEATGHRVTMGTAALGPVWAALLLFLLMCEIPMVELTFDRAVASGCQRCCDSEDPLDPAHVSSASSSGRPHALPEIRPYINITILKGDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAPCQKRFFAFSVGRKTALHSGEDFQTLLFERVFVNLDGCFDMATGQFAAPLRGIYFFSLNVHSWNYKETYVHIMHNQKEAVILYAQPSERSIMQSQSVMLDLAYGDRVWVRLFKRQRENAIYSNDFDTYITFSGHLIKAEDD
Protein: Alpha-S1-casein (Alpha-casein) (P02661)
Organism: Rattus norvegicus (Rat)
Function: Important role in the capacity of milk to transport calcium phosphate.
Subcellular location: Secreted.
Interaction partners:
- Beta-casein
- Kappa-casein
- Alpha-S2-casein-like B
- Alpha-lactalbumin
- Alpha-S2-casein-like A
- Whey acidic protein
- Glycosylation-dependent cell adhesion molecule 1
Sequence:
MKLLILTCLVAAALALPRAHRRNAVSSQTQQENSSSEEQEIVKQPKYLSLNEEFVNNLNRQRELLTEQDNEIKITMDSSAEEQATASAQEDSSSSSSSSEESKDAIPSATEQKNIANKEILNRCTLEQLQRQIKYSQLLQQASLAQQASLAQQASLAQQALLAQQPSLAQQAALAQQASLAQQASLAQQASLAQKHHPRLSQVYYPNMEQPYRMNAYSQVQMRHPMSVVDQAQFSVQSFPQLSQYGAYPLWLYFPQDMQYLTPEAVLNTFKPIAPKDAENTNVW
Protein: GDNF family receptor alpha-2 (GDNF receptor alpha-2) (O35977)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- Neurturin
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Artemin
- Glial cell line-derived neurotrophic factor
- Persephin
Sequence:
MILANAFCLFFFLDETLRSLASPSSLQGSELHGWRPQVDCVRANELCAAESNCSSRYRTLRQCLAGRDRNTMLANKECQAALEVLQESPLYDCRCKRGMKKELQCLQIYWSIHLGLTEGEEFYEASPYEPVTSRLSDIFRLASIFSGTGTDPAVSTKSNHCLDAAKACNLNDNCKKLRSSYISICNREISPTERCNRRKCHKALRQFFDRVPSEYTYRMLFCSCQDQACAERRRQTILPSCSYEDKEKPNCLDLRSLCRTDHLCRSRLADFHANCRASYRTITSCPADNYQACLGSYAGMIGFDMTPNYVDSNPTGIVVSPWCNCRGSGNMEEECEKFLRDFTENPCLRNAIQAFGNGTDVNMSPKGPSLPATQAPRVEKTPSLPDDLSDSTSLGTSVITTCTSIQEQGLKANNSKELSMCFTELTTNISPGSKKVIKLNSGSSRARLSAALTALPLLMLTLAL
Protein: Protocadherin 9 (F1LS01)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MDLRDFYLLAALIACLRLDSAIAQELIYTIREELPENVPIGNIPKDLNISHINAATGTSASLVYRLVSKAGDAPLVKVSSSTGEIFTTSNRIDREKLCAGASYAEENECFFELEVVILPNDFFRLIKIKIIVKDTNDNAPMFPSPVINISIPENTLINSRFPIPSATDPDTGFNGVQHYELLNGQSVFGLDIVETPEGEKWPQLIVQQNLDREQKDTYVMKIKVEDGGTPQKSSTAILQVTVSDVNDNRPVFKEGQVEVHIPENAPVGTSVIQLHATDADIGSNAEIRYIFGAQVAPATKRLFALNNTTGLITVQRSLDREETAIHKVTVLASDGSSTPARATVTINVTDVNDNPPNIDLRYIISPINGTVYLSEKDPVNTKIALITVSDKDTDVNGKVICFIEREVPFHLKAVYDNQYLLETSSLLDYEGTKEFSFKIVASDSGKPSLNQTALVRVKLEDENDNPPIFNQPVIELSVSENNRRGLYLTTISATDEDSGKNADIVYQLGPNASFFDLDRKTGVLTASRVFNREEQERFIFTVTARDNGTPPLQSQAAVIVTVLDENDNSPKFTHNHFQFFVSENLPKYSTVGVITVTDEDAGENKAVTLSILNDNENFVLDPYSGVIKSNVSFDREQQSSYTFDVKATDGGQPPRSSTAKVTINVMDVNDNSPVVISPPSNTSFKLVPLSAIPGSVVAEVFAVDIDTGMNAELKYTIVSGNNKGLFRIDPVTGNITLEEKPAPTDVGLHRLVVNISDLGYPKALHTLVLVFLYVNDTAGNASYIYDLIRRTMETPLDRNIGDSGQPYQNEDYLTIMIAIVAGAMVVIVVIFVTVLVRCRHASRFKAAQRSKQGAEWMSPNQENKQNKKKKRKKRKSPKSSLLNFVTIEESKPDDAVHEPINGTISLPAELEEQSIGRFDWGPAPPTTFKPNSPDLAKHYKSASPQPAFHLKPDTPVSVKKHHVIQELPLDNTFVGGCDTLSKRSSTSSDHFSASECSSQGGFKTKGPLHTRQSQRRVTFHLPDGSQESCSDSGLGDHEPVGSGTLISHPLPLVQPQDEFYDQASPDKRTEADGNSDPNSDGPLGPRGLAEATEMCTQECLVLGHSDNCWMPPGLGPYQHPKSPLSTFAPQKEWIKKDKLVNGHTLTRAWKEDTNRNQFNDRKQYGSNEGHFSNGSHMADIPLANLKSYKQAGGTIESPKEHQL
Protein: Moesin (Membrane-organizing extension spike protein) (P26041)
Organism: Mus musculus (Mouse)
Function: Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (By similarity). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (By similarity). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (By similarity). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs. Modulates phagolysosomal biogenesis in macrophages. Participates also in immunologic synapse formation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:9856983}; Peripheral membrane protein {ECO:0000269|PubMed:9856983}; Cytoplasmic side {ECO:0000269|PubMed:9856983}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9856983}. Apical cell membrane {ECO:0000269|PubMed:9856983}; Peripheral membrane protein {ECO:0000269|PubMed:9856983}; Cytoplasmic side {ECO:0000269|PubMed:9856983}. Cell projection, microvillus membrane {ECO:0000269|PubMed:9856983}; Peripheral membrane protein {ECO:0000269|PubMed:9856983}; Cytoplasmic side {ECO:0000269|PubMed:9856983}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Note=Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment (By similarity). Localizes at the uropods of T lymphoblasts (By similarity). {ECO:0000250|UniProtKB:P26038, ECO:0000269|PubMed:9856983}.
Interaction partners:
- Na
- Radixin
- Ezrin
- CD44 antigen
- Sodium/hydrogen exchanger 1
- Intercellular adhesion molecule 1
- Vascular cell adhesion protein 1
- Membrane cofactor protein
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
Sequence:
MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERALLENEKKKRELAEKEKEKIEREKEELMEKLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLASEMAELTARISQLEMARKKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEHDEQDENGAEASAELRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM
Protein: Protein kinase, putative (Q57UD5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- SAM domain-containing protein
Sequence:
MEPADGLKRCGASTDTIIEEIKALAKSMLESTEAIRRRSRNVESCKSYDALLSVLESTAPLTKHPARQQRTQGHNDVICEFPVTRGGGISGGATANNAKPGNCYAKKVSGDAAEFCESELDDTEAEVTSCSPEACGEDGHDLGGFYPNSKAQLFSACTMGADFSADSDDNVYDGVKTQVVFKAVDPALYQDISGCTWQPEPLLLHSETGEAVEDSSEDKDEDKESDYMDDAAVVGTKKVYRVPSFPFGGGITEGQARFLSKTFSETIRRGGLSSSKRPAHVTVKDFVGYKYDECATTDAERSRFKPVSPFEFVVELERGVMFDAVRAREERRQEFRRLAKEGKAPVTMGSFNLRVIMDPIKTGFEEEKTFPIERGTIVADRYQIVEMLGKATFSRAVRCYDLSQPIYEDDVKVEDKDRTATTDAQNRCVDTENGGVSNDAKKRKVVGYVEVCLKIINNSKDFFDQSLDEIRLLTLINKYKDPDKAHVIRLIDSFYYKEHTMLVTELLSDNLYEYSKYNREEEETFYFTIPRLRRIARQITEALTYVHSLSLIHADLKPENILFVSHRRCLIKVIDFGSSCFLSDHLSSYIQSRSYRAPEVILGCDYDGRIDVWSLGAILAELVTGEVLFTSETVPEMLARIVYVCGRPFPRRMLWEGRHTSKFINKFGCIYEQGNKDGDDPGEDSSYYYLYTPVPQSSGIKNPDAEGTDAENNGTRDTESLISEERPYRVLREKLAAHNVTDSAFISFVEACLTLDHKARPRSKDLLSHPFLAQVD
Protein: TATA-box-binding protein (TATA sequence-binding protein) (TBP) (TATA-binding factor) (TATA-box factor) (Transcription initiation factor TFIID TBP subunit) (P17871)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Subcellular location: Nucleus.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit Taf12
- Transcription initiation factor TFIID subunit 2
- SAGA complex/transcription factor TFIID complex subunit Taf6
- Putative transcription initiation factor TFIID 111 kDa subunit
- SAGA complex/transcription factor TFIID complex subunit Taf10
- SAGA complex/transcription factor TFIID complex subunit Taf9
- Transcription factor IIIB 60 kDa subunit
- Transcription initiation factor TFIID subunit 7
- TATA-binding protein-associated factor mot1
- Transcription initiation factor TFIID subunit 13
Sequence:
MDFALPTTASQASAFMNNSSLTFPVLPNANNEATNETADSGDAEVSKNEGVSGIVPTLQNIVATVNLDCRLDLKTIALHARNAEYNPKRFAAVIMRIREPKSTALIFASGKMVVLGGKSEDDSKLASRKYARIIQKLGFNAKFTDFKIQNIVGSCDVKFPIRLEGLAYSHGTFSSYEPELFPGLIYRMVKPKVVLLIFVSGKIVLTGAKVREEIYQAFEAIYPVLSEFRKH
Protein: Histone deacetylase 1 (HD1) (EC 3.5.1.98) (Protein deacetylase HDAC1) (EC 3.5.1.-) (Protein deacylase HDAC1) (EC 3.5.1.-) (Q4QQW4)
Organism: Rattus norvegicus (Rat)
Function: Histone deacetylase that catalyzes 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. Histone deacetylases act via the formation of large multiprotein complexes. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). Also functions as deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (By similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:30980393}.
Interaction partners:
- Chromodomain-helicase-DNA-binding protein 4
- Histone deacetylase 2
- Nuclear receptor corepressor 1
- Methyl-CpG-binding protein 2
- Paired amphipathic helix protein Sin3a
- RB-binding protein 4, chromatin-remodeling factor.
- DNA helicase
- Transcription factor YY2
- DNA
- Sin3A associated protein 30
Sequence:
MAQTQGTKRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEEDPDKRISICSSDKRIACEEEFSDSDEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKMA