wanglab/gogpt-training-data huggingface dataset:
Protein: Mediator of RNA polymerase II transcription subunit 17 (Mediator complex subunit 17) (Suppressor of RNA polymerase B 4 homolog) (P87306)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 14
Sequence:
MAEEANKDADISSLSLSLDPEIIGGQNNFLENNLQQIFQKIIQERGPFRDLKEEDLQKELQKESIKDESSAKSSETENVLEFATLDSKRNVNDTEVESMDSQAYKKELIEQIMIAQTECSLALDMTSLLLSKFKENSIETISPFLKSTVPPSSLQFSRSQPPESKESDATLAKCWKEKSLTSSCKFLFEAKERLTSVVETEHEYYTELVKVKEASWPLFNSQGSNHLSVQYSCLGGISLGLGLIRMKPESKSFEVQSSLLYSQAALKISILNKDRDEIGSSTWSWPSQNCNSVLLKDIYKLQEILFEMDIWNSLLQEAQSCGNQGVNFTGDEILVPISDDHVVRITLETSSKNTESGFTEDKKSNEDTSTNFVTIKQEKELLKCLCDTLNAIAHILFLKHCRKSDRRSQQPELYMAIDANAPLILRPLIFYYNLNQESLEFQRWLKQRDISFKFMPNYPWEKAKDFLELENSLSINRLSISWRIMVSNFEPAIFIQHTPTLHGTDKSVWRCKDQYSSNQFSSLKNVCQYIEHHINSLSRRSKKTE
Protein: Dystrobrevin alpha (DTN-A) (Alpha-dystrobrevin) (Dystrophin-related protein 3) (Q9Y4J8)
Organism: Homo sapiens (Human)
Function: May be involved in the formation and stability of synapses as well as being involved in the clustering of nicotinic acetylcholine receptors.
Subcellular location: Cytoplasm. Synapse. Cell membrane {ECO:0000250}. Note=In peripheral nerves, colocalizes with MAGEE1 in the Schwann cell membrane. {ECO:0000250}.
Interaction partners:
- Sarcospan
- Dystrophin
- Syncoilin
- Alpha-1-syntrophin
- Beta-2-syntrophin
- Dystroglycan 1
- Beta-1-syntrophin
- Gamma-2-syntrophin
- Utrophin
- Alpha-sarcoglycan
Sequence:
MIEDSGKRGNTMAERRQLFAEMRAQDLDRIRLSTYRTACKLRFVQKKCNLHLVDIWNVIEALRENALNNLDPNTELNVSRLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTLMSDPPPQCLVWLPLLHRLANVENVFHPVECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEYTSWKSPAKKLTNALSKSLSCASSREPLHPMFPDQPEKPLNLAHIVDTWPPRPVTSMNDTLFSHSVPSSGSPFITRSSPPKDSEVEQNKLLARAAPAFLKGKGIQYSLNVADRLADEHVLIGLYVNMLRNNPSCMLESSNRLDEEHRLIARYAARLAAESSSSQPPQQRSAPDISFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKTQGAGSPRSSPSHTISRPIPMPIRSASACSTPTHTPQDSLTGVGGDVQEAFAQSSRRNLRNDLLVAADSITNTMSSLVKELNSEVGSETESNVDSEFARTQFEDLVPSPTSEKAFLAQIHARKPGYIHSGATTSTMRGDMVTEDADPYVQPEDENYENDSVRQLENELQMEEYLKQKLQDEAYQVSLQG
Protein: Uncharacterized protein (Q580H6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MERGMCLVERDVDGLSCKTMLAPQGWVQRVHHDVRDKCSVNVTHFTSLDSLSTSLYVTEYFLPRPTSVESGSSAGVTPEALAASLAQLLDPSKFSLCTAWEVPQSAPTESCGPLGKLLCKYVLLVSVALSTRERDATYARCSFDAVVYDLKERYLQLSRGSDVVGLSSTEWVAGNSAVCTRRGCCVIHVTAPPGRNICWHPQLGGEATCKLGEAAKELGLVSENLNFLLYEDAAGSVEVMFALLPLTPGVCIMKRGDLQRAWLRRTRGSRWRSLRLPTPRLTTGVVDPCNSLYDVRPPGSFYLLVRGEGGTARSVIAWLMEPRVGSDSSIVLLTTFHTARGGAVSATASVVATDAAITVDTAAVDPATAAQCLKHCKWLRSTFCASVGMTFSWSALCVGKSPGLLFRQGNLVIQLPSESTRYASASAVAAASAVSRGNESAALGSITVEAVDRADGTERRATITLLREFRCAIDFMDYVVTEFTYEAHVDRRSAVMRRCKAPLALLPGGGQGTGKCPEAYSFWIRLGERDAIHYVVRECGIGRLLLAQACVTDCSPFSDVVAERWESWVGGIGVASIL
Protein: Nitric oxide synthase (EC 1.14.13.39) (A0A0R4IQG7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004468}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004468}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}.
Interaction partners:
- Argininosuccinate lyase
- Calmodulin
- Arginase
- Arginase
- non-specific serine/threonine protein kinase
- V-akt murine thymoma viral oncogene homolog 2,-like.
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Non-specific serine/threonine protein kinase.
- Calmodulin-like protein 4
Sequence:
MQESEPSVCQLQPNIISVRLFKRKIGGLGFLVKQRVCKPPVIVSDLIRGGAAEECGLVQVGDIVLAVNNKPLVDMSYERALETLKNVSPESHAVLILRGPEGFTTHLETTLSSDGKTKTIRVTRPVNPAQSRPCERCSPLTPNMTKELRAIENLSSSSTPRKESRDDKPLIPLLSQDSLLREGGHAGLLLNGVEDNNDLLKEIEPVLKLIKNSKKEINGEGQRVIDRKDAEVQVERDLGVGNGQNAQLASDNDRVFDDLWRKDNMPTVLNNPYSESDKPQSYERVSPTKAVQNGSPSKCPRFMKVKNWETGALYNDTLHHSSSKVPICTEHVCIGSIMVPNQHAHKPDEDRRKEELLPLATDFIDQYYTSIKRCCSKAHVDRLEEVKKEIETSGTYQLKDTELIYGAKHAWRNAARCVGRIQWSKLQVFDARDCTTAHGMFNYICNHIKYATNKGNLRSAITIFPQKTDGKHDFRVWNSQLIRYAGYKQPDGSILGDPASVELTEICMQQGWKAPKGRFDVLPLLLQANGNDPELFEIPDDLVLEVPIIHPKFEWFKELNLKWYGLPAVSNMLLEIGGLEFTACPFSGWYMGTEIGVRDFCDSSRYNILEEVATMMGLDTRKTSSLWKDQALVEINIAVLYSYQMSKVTIVDHHSATESFMKHMENEYRVRGGCPGDWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGVNGTPTKKRAIGFKKLAKAVKFSAKLMGQAMAKRVKATILFATETGKSQDYAKTLCEIFKHAFDAKVMSMDEYDTVDLEHETLVIVVTSTFGNGDPPENGEKFGAALMEMRHPTTSVEDRKTYKVRFNSVSSYSDTRKSSSDEPESKANFESTGPLANVRFSVFGLGSRAYPHFCAFAHAVDTLFEELGGERILRMGEGDELCGQEESFRTWAKKVFKAACDVFCVGDDVNIEKANDSLISNDRSWKKSKFRMTYTAEAPTLTQALYSIHKKKVYGAKVVQRQNLQSARSNRLTIFVRLDANNHESLKYLPGDHLGVFPGNNEDLVTTLIEKLEDAPPVNQIVKVEFLEERNTALGVISNWTDESRIPPCTIYQAFKYFLDITTPPSPVLLQQFAPLATNEKQRKRLEVLSKGLQEYEEWKWYNNPTMVEVLEEFPSLQIPSTLLLTQLPLLQPRYYSISSSPDLYPGEIHLTVAVVSYRPRDGEGPIHHGVCSSWLNSLDEGDTVPCFVRGAPSFRMPKDSQVPCILIGPGTGIAPFRAFWQQRQYDVENKGIKACPMILVFGCRQSQIDHIYKEQTIQAKNKEVFKELYTAYSREPGRPKKYVQDVLREQLSETVYKCLREEGGHIYVCGDVTMAGDVLKTVQQIFKLHGNMSLEDAGFYISKLRDENRYHEDIFGVTLRTYEVTNRLRSESIAYIEESKKDIDEVFCS
Protein: Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Dolichol-phosphate mannose synthase subunit 1) (DPM synthase subunit 1) (Dolichyl-phosphate beta-D-mannosyltransferase subunit 1) (Mannose-P-dolichol synthase subunit 1) (MPD synthase) (O70152)
Organism: Mus musculus (Mouse)
Function: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex.
Subcellular location: Endoplasmic reticulum.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol kinase
- Dol-P-Man:Man
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichyldiphosphatase 1
- Dolichyl-phosphate beta-glucosyltransferase
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
Sequence:
MASTGASRSLAASPRPPQGRSSRQDKYSVLLPTYNERENLPLIVWLLVKSFSESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLGTAYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFITQILLRPGASDLTGSFRLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT
Protein: Uncharacterized zinc protease Rv2782c (EC 3.4.24.-) (P9WHT5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Cytochrome bc1 complex cytochrome b subunit
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit D
- Conserved protein
- NADH-quinone oxidoreductase subunit C
- Polyribonucleotide nucleotidyltransferase
Sequence:
MPRRSPADPAAALAPRRTTLPGGLRVVTEFLPAVHSASVGVWVGVGSRDEGATVAGAAHFLEHLLFKSTPTRSAVDIAQAMDAVGGELNAFTAKEHTCYYAHVLGSDLPLAVDLVADVVLNGRCAADDVEVERDVVLEEIAMRDDDPEDALADMFLAALFGDHPVGRPVIGSAQSVSVMTRAQLQSFHLRRYTPERMVVAAAGNVDHDGLVALVREHFGSRLVRGRRPVAPRKGTGRVNGSPRLTLVSRDAEQTHVSLGIRTPGRGWEHRWALSVLHTALGGGLSSRLFQEVRETRGLAYSVYSALDLFADSGALSVYAACLPERFADVMRVTADVLESVARDGITEAECGIAKGSLRGGLVLGLEDSSSRMSRLGRSELNYGKHRSIEHTLRQIEQVTVEEVNAVARHLLSRRYGAAVLGPHGSKRSLPQQLRAMVG
Protein: A-factor receptor protein (A-factor-binding protein) (Q9ZN78)
Organism: Streptomyces griseus
Function: Represses adpA expression by binding to the promoter region in the absence of A-factor, causing repression of streptomycin production and of sporulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:2502536}.
Interaction partners:
Sequence:
MAKQARAVQTWRSIVDAAASVFDDYGYERAAISEILRRAKVTKGALYFHFASKEAIAQAIMDEQTSTVEFEQEGSPLQSLVDGGQQFAFALRHNSMARAGTRLSIEGVFLGGPHPWGDWIDATARMLELGQERGEVFPQIDPMVSAKIIVASFTGIQLVSEADSGRADLRGQVAEMWRHILPSIAHPGVIAHIKPEGRVDLAAQAREKAEREEQEARIAAEAKGAGSDAATDSGSRSGGSGLRGGGSGRGPRAGGAGDEGDEEPAGAGVAAGGVVA
Protein: Ferric-mycobactin receptor, FemA (Q9I2J4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Sigma factor regulator, FemR
- Probable sigma-70 factor, ECF subfamily
- Ferric enterobactin receptor
- ECF sigma factor, FemI
- PepSY domain-containing protein
- Probable sigma-70 factor, ECF subfamily
- Probable transmembrane sensor
- Probable tonB-dependent receptor
- Anti-sigma factor FoxR
- Probable transmembrane sensor
Sequence:
MPVRTLRPRSLSLAIHAAAMTLALAGAAPALLAAEAPAASSARSYDIAPGPLGRTLSAFASDNGVSLAFDPALTEGRRSAALRGRYAPVEALHRLLLGSGLELQQRSDGSYTLVPAATDGALELQSSLITAQAAGAETLPAEYAGGQVARGARLGMLGNADVMDAPFSITSYTARTIEQQQARSVADLLQANDPSVRVVGGRGDLVDSYTIRGFSVQNADVAFNGLYGLLPFWRVPIEFAERVEVLKGPNALLGGISPGGSVGGTINLVPKRADDQPLTRVSVDWTQRGQLGTHLDIGRRFGENNAFGVRFNGVYRNGDTAVDHQSREFPMLSLGLDFRGERLRLSSDLLYQKESLEGVVRPLLTGPGTTHIPHAPDSKTRFGLRDSYLDQEDYSMVNRGEYDLADNLTAFASIGGRQSNYETIAANSILVGNQGDIVNSLARQRGDRRTYSAEVGLRGNFDTGPLRHDWTLSANRLHERLGMVYAFTGMQSGNLYQTSPHTPLPDFSSLDGSIPKTNETDLGGVALADRLSFLEDRVQVTLGVRRQQIESRNYDQTSGARTSHDKRHVWTPMASVLVKPLQDLSLYANYIQGLSQGEAAPMTAANAGQVLAPYKAEQYEIGAKYDLGGFTTTLALFEIRKPNAYTDASNVFRADGEQRNRGVELSLYGEPLDGVRVMAGATYIKPEQNKTGDPASEGKDAPGVARRQANLGVSWDTPFVDGLTLDSRWIYTGSAYVDSANALAVPHWNRVDLGAAYAFQVAGKPLVARANLENALGKDYWTAANGYLSISSPRTLSLSLTADF
Protein: Baseplate puncturing device gp5.4 (Gene product 5.4) (gp5.4) (P39234)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Baseplate central spike complex-associated protein. Makes the tip of the central spike which probably punctures the host outer membrane, a necessary step for viral DNA ejection into the host cell.
Subcellular location: Virion {ECO:0000269|PubMed:27193680}. Note=Present in the baseplate. {ECO:0000269|PubMed:27193680}.
Interaction partners:
Sequence:
MSGLSYDKCVTAGHEAWPPTVVNATQSKVFTGGIAVLVAGDPITEHTEIKKPYETHGGVTQPRTSKVYVTGKKAVQMADPISCGDTVAQASSKVFIK
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 3) (1-AGP acyltransferase 3) (1-AGPAT 3) (Lysophosphatidic acid acyltransferase gamma) (LPAAT-gamma) (Q9NRZ7)
Organism: Homo sapiens (Human)
Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA. Has a preference for arachidonoyl-CoA as a donor (By similarity). Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20537980, ECO:0000269|PubMed:21173190}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:21173190}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phosphatidate cytidylyltransferase 2
- Phosphatidate cytidylyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase MBOAT7
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Phospholipid phosphatase 5
Sequence:
MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSLLGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE
Protein: Mix-type homeobox gene 2 (Q1RM27)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- PAK4-inhibitor inka1
- Eukaryotic translation initiation factor 4, gamma 2a.
- Calmodulin-regulated spectrin-associated protein family, member 2a.
- Nodal-related 1.
- Nanog
- Sulfate anion transporter 1
- SRY-box transcription factor 32.
Sequence:
MKDMWTDCIAQDGNSQASKIAGRRKRTSFTKEHLELLKMAFNVDPYPGISVRESLSQATGLPESRIQVWFQNKRARTLKNRAIQSSPQLDNKSPLPSPFLPPHMASVGVSAQQRGIQESPFNIQMSQTSPQHFTFPPSDYSTPVVKPRQTRLMGTSSCSPSDLQATPDSWSYAGSTQISPESWDVAAENFGNSYKDESPFFLYPPPPYPYGSTRVGCPSSMESLSTSPASSDSAFWDMGLENCSPSVPYTSCGSPWDRLTEEQPVAPLPDLSSQCLEDVLGEMEPAWWSFNGQMDL
Protein: Gem-associated protein 4 (Gemin-4) (Component of gems 4) (p97) (P57678)
Organism: Homo sapiens (Human)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
Subcellular location: Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, gem. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs and in the nucleolus.
Interaction partners:
- Probable ATP-dependent RNA helicase DDX20
- Gem-associated protein 5
- Gem-associated protein 2
- Protein argonaute-2
- Gem-associated protein 6
- Gem-associated protein 7
- Survival motor neuron protein
- Gem-associated protein 8
- Serine-threonine kinase receptor-associated protein
- Small nuclear ribonucleoprotein-associated proteins B and B'
Sequence:
MDLGPLNICEEMTILHGGFLLAEQLFHPKALAELTKSDWERVGRPIVEALREISSAAAHSQPFAWKKKALIIIWAKVLQPHPVTPSDTETRWQEDLFFSVGNMIPTINHTILFELLKSLEASGLFIQLLMALPTTICHAELERFLEHVTVDTSAEDVAFFLDVWWEVMKHKGHPQDPLLSQFSAMAHKYLPALDEFPHPPKRLRSDPDACPTMPLLAMLLRGLTQIQSRILGPGRKCCALANLADMLTVFALTEDDPQEVSATVYLDKLATVISVWNSDTQNPYHQQALAEKVKEAERDVSLTSLAKLPSETIFVGCEFLHHLLREWGEELQAVLRSSQGTSYDSYRLCDSLTSFSQNATLYLNRTSLSKEDRQVVSELAECVRDFLRKTSTVLKNRALEDITASIAMAVIQQKMDRHMEVCYIFASEKKWAFSDEWVACLGSNRALFRQPDLVLRLLETVIDVSTADRAIPESQIRQVIHLILECYADLSLPGKNKVLAGILRSWGRKGLSEKLLAYVEGFQEDLNTTFNQLTQSASEQGLAKAVASVARLVIVHPEVTVKKMCSLAVVNLGTHKFLAQILTAFPALRFVEEQGPNSSATFMVSCLKETVWMKFSTPKEEKQFLELLNCLMSPVKPQGIPVAALLEPDEVLKEFVLPFLRLDVEEVDLSLRIFIQTLEANACREEYWLQTCSPFPLLFSLCQLLDRFSKYWQLPKEKRCLSLDRKDLAIHILELLCEIVSANAETFSPDVWIKSLSWLHRKLEQLDWTVGLRLKSFFEGHFKCEVPATLFEICKLSEDEWTSQAHPGYGAGTGLLAWMECCCVSSGISERMLSLLVVDVGNPEEVRLFSKGFLVALVQVMPWCSPQEWQRLHQLTRRLLEKQLLHVPYSLEYIQFVPLLNLKPFAQELQLSVLFLRTFQFLCSHSCRDWLPLEGWNHVVKLLCGSLTRLLDSVRAIQAAGPWVQGPEQDLTQEALFVYTQVFCHALHIMAMLHPEVCEPLYVLALETLTCYETLSKTNPSVSSLLQRAHEQRFLKSIAEGIGPEERRQTLLQKMSSF
Protein: GRIP and coiled-coil domain-containing protein 2 (185 kDa Golgi coiled-coil protein) (GCC185) (Q8CHG3)
Organism: Mus musculus (Mouse)
Function: Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-6A
- CLK4-associating serine/arginine rich protein
- Ras-related protein Rab-9A
- Syntaxin-16
- Ras-related protein Rab-9B
- Golgin subfamily A member 1
- Vesicle transport through interaction with t-SNAREs homolog 1A
- Ras-related protein Rab-6B
- ADP-ribosylation factor-like protein 1
- Ran GTPase-activating protein 1
Sequence:
MEDSAPDAVAAAPSGTPKSKLETLPREDLIKFAKKQMMLLQKAKARCTELDKEVEELKSKPVDGGTDDIIKVLTERLDALLLEKAETEQQCLCLKKENVKMKQEVEDSVTKLEETHKEFEQSHRNYVKEIESCKNELMAVHSEHSKETAILQKELEEAVHKQVELREQLKSQSDSEDNVRKLQEEIQNITAAFEEQISCLEKKLEATSDEKQQEIIHLQKVIEDKAQHYQKDINTFQAEILQLRATHKEEVTELMSQIETSAKEHEAEINKLKENRVTQCEASENIPEKYQCESENLNEVASDASPESQNCSVALQEDPSAEQTVCDKVRQLEDSLKELESQHSILKDEVTYMNNLKLKLEMDAQHIKDEFFHEREDLEFKINELLLAKEEQGYVVEKLKYEREDLNRQLCCAVEQHNKEIQRLQEHHQKEVSELSETFISGSEKEKLALMFEIQGLKEQCENLQHEKQEVVLNYESLREMMEILQTELGESAGKISQEFETMKQQQASDVHELQQKLRSAFNEKDALLETVNRLQGENEKLLSQQELVPELESTIKNLQADNSMYLASLGQKDTMLQELEAKISSLAKEKDDFISKIKTSHEEMDDLHQKWEREQRLSVELREAAGQAAQHNSELRQRVSELTGKLDELVREKSQNDQSITVQMKTMTEDQEALSSKIKSLYEENNRLHSEKAQLSRDLEALQAQQDFAHKEHVAEFEKKLQLMVEERDDLNKLLENEQVQKSFVKTQLYEYLKQLRASILEENEEEDVVKLIQAVGESLVKVKEEEHNLVFEYDARVLELENKIKCLQEDSAVQCEELRTLVRDSEQEKILLRKELDAVTSAKEALQLDLLEMKNTNEKASLENQTLSTQVEELSQTLHSRNEVHDEKVLVIEHENLRLLLKQRESELQDVRAELILLKDSLEKSPSVKNDQLSLVKELEEKIESLEKESKDKDEKISKIKLVAVKAKKELDSNRKEAQTLREELESVRSEKDRLSASMKEFLQGAESYKSLLLEYDKQSEQLDVEKERAHNFERHIEDLTKQLRNSTCQYERLTSDNEDLLARIETLQANAKLLEAQILEVQKAKGVVEKELDAEKLQKEQKIKEHVSTVNELEELQLQFQKEKKQLQKTMQELELVKKDAQQTTLMNMEIADYERLMKELNQKLTNKNSTIEDLEQEMKIQKEKQETLQEEITSLQSSVQHYEEKNTKIKQLLVKTKKELADAKQAETDHLLLQASLKGELEASQQQVEVYKIQLAEMTSEKHKIHEHLKTSAEQHQRTLSAYQQRVVALQEESRAAKAEQAAVTSEFESYKVRVHNVLKQQKNKSVSQVETEGAKQEREHLEMLIDQLKIKLQDSQNSLQISVSEYQTLQAEHDTLLERHNRMLQETVTKEAELREKLCSVQSENTMMKSEHSQTMCQLTSQNEALRTSFRDQVRHLQDEHRKTVETLQHQLSKLEAQLFQLKSEPSTRSPASSHQPSKSLRERRTTDLPLLDMHTVAREEGEGMETTDSESVSSAGTHIQSLEQLLSSPDTKLERLAETSLWHNEFTKEELAEKLSSTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQEREKSVANLEYLKNVLLRFIFLKPGSERERLLPVIDTMLQLSPEEKGKLATVAQGEEESASRSSGWASYLHSWSGLR
Protein: Protein phosphatase 2C 56 (AtPP2C56) (EC 3.1.3.16) (Protein ABSCISIC ACID-INSENSITIVE 1) (Protein phosphatase 2C ABI1) (PP2C ABI1) (P49597)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1. Represses MAPKKK18 activity and promotes MAPKKK18 degradation by the proteasome pathway upon abscisic acid (ABA) treatment. Represses KIN10 activity by the specific dephosphorylation of its T-loop Thr-198, leading to a poststress inactivation of SnRK1 signaling. Restricts MAPKKK20 activity by dephosphorylation.
Subcellular location: Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein. Note=Associated to the plasma membrane when in complex with PA, subsequently to ABA signaling.
Interaction partners:
- Abscisic acid receptor PYL1
- Serine/threonine-protein kinase SRK2E
- Abscisic acid receptor PYR1
- Serine/threonine-protein kinase SRK2D
- Serine/threonine-protein kinase SRK2I
- Abscisic acid receptor PYL9
- Abscisic acid receptor PYL4
- Abscisic acid receptor PYL5
- Abscisic acid receptor PYL8
- Abscisic acid receptor PYL2
Sequence:
MEEVSPAIAGPFRPFSETQMDFTGIRLGKGYCNNQYSNQDSENGDLMVSLPETSSCSVSGSHGSESRKVLISRINSPNLNMKESAAADIVVVDISAGDEINGSDITSEKKMISRTESRSLFEFKSVPLYGFTSICGRRPEMEDAVSTIPRFLQSSSGSMLDGRFDPQSAAHFFGVYDGHGGSQVANYCRERMHLALAEEIAKEKPMLCDGDTWLEKWKKALFNSFLRVDSEIESVAPETVGSTSVVAVVFPSHIFVANCGDSRAVLCRGKTALPLSVDHKPDREDEAARIEAAGGKVIQWNGARVFGVLAMSRSIGDRYLKPSIIPDPEVTAVKRVKEDDCLILASDGVWDVMTDEEACEMARKRILLWHKKNAVAGDASLLADERRKEGKDPAAMSAAEYLSKLAIQRGSKDNISVVVVDLKPRRKLKSKPLN
Protein: Uncharacterized protein (Q586S4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEERKGHDRTLVKRHAFGVKADVSGCVCWVEEGTLLYPIGKTAAMHNLNTNTQRFFETSQRSGGITALAVSANKKFIAMAESGAAPQVQVFDTVTRKRRKVLTVPDLEGDRFTALDFSADGRHLVTQGGAPQWRLFFWNWERSKPLASTSVVADFGLQEICEAHNESDAAPGSLSSGARTTAAQSSTTSMSHVTCVTVCPSDPLLIGVSGFGFMYFYRYQEGVLRIQPHISFARERTSNFLTHSWVGRDRVVASTQNGELLLIEAGVFRRILPVPPSTTEGAVNPAVLAIVPTRNGFIAGSDQGTVAIYETIGSANESYAIVYNVPVPSEKPGEVKSDDLGVASRPVATNKLRASIISDGQTEGEGGQDAPAKPLFVINDVTQGKISSTTESSPTVSGKGIRPAQLRLEAGRPEPRKDNSVVHLCIDQTEETVAMVTHGGQILAFNFASDWSKVSAEEPPTVLHVCQPFHIGGIIGLDCSVKKPYLATSGVDQSVRIWNTSTHRLETCEYFTSQPGALAIHPNGLYLVVCFPDKVRVLSILWNGLRERRVINLRNTTDVKYSVGGSYFAVAHGNIIHLYNSLTCDVHGQLRGHPQKINCFQWCATSPYPTDNSIISSSLDGIVINWNISEMRKETEYADKKHQFRYITADDRTLWAVSEPTSIAMDVQWKSTLHEMDRYTTSDIAANAAVTEYEFVESKVTSLLIAPKQRMLFGGMDDGSVKFMSFPLQVGVQEVPIVAHMGPVGRMVLSHDESTLYTISSDGTLFIFDAREDGRPLQRDLGYFSDDVLVLASEVEDHDITIESLRHTTEKLRTDIESDEKRRNHEQNTRLRERADEFKNELDTLDAEYEALLNAKAEQERAFVAVKLEKEGESAPQLEGLEREGQAEVQRLEDLCAELQHKLDQSTFVYEREVEDLLAEIQRHQEEDHDRFKDVVSKREKGLQKLEQQVQRTKANNAEVRQRLELDTDAEVMNVEKQNQAELNAIRERYLRMKGEGAIMRKNTLRMQKETDVHNSELQVLDNAKATLTEQLSELNETMAQLHQDIDERDAIIGEKERKIYDLKKLNQELEKHKFVLDYRIRQLKSQMEPRQREIAREHQRISERNVELDNLHGNNIALRQNIEELKAELAQQQQQIKQTLSHMKDFETYKSRVKRDIGEIAPAMQDAAMLRDVVERLYQRHVVARDGQRAAQVGQEIKDEFKSQVEYLSTSVEALSRKCEADQEQHRCEVSAMMMENLTLIREIHELRAELADLRNVSVTVADEGKRHAMLEERGKQGPPGRVALPTGLAGVKRPELLWELEENRKALKSIRDHVESLQQMLASLAPPKSAIVSLPPLV