wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerase II subunit RPB2 (EC 2.7.7.6) (3'-5' exoribonuclease) (EC 3.1.13.-) (DNA-directed RNA polymerase II 140 kDa polypeptide) (DNA-directed RNA polymerase II subunit B) (RNA polymerase II subunit 2) (RNA polymerase II subunit B2) (RNA-directed RNA polymerase II subunit RPB2) (EC 2.7.7.48) (P30876)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9852112}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB4
- General transcription factor IIF subunit 2
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB11-a
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVEDAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTYSAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLDPGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSMLARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEMVKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETKKAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQKFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLSHLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSPILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSEVSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASGVVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSPRNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIVAIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGMRHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSETGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEGITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGYHLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSRDGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGCRNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (O96660)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
- Mothers against decapentaplegic homolog
- Zinc finger FYVE domain-containing protein
- E3 ubiquitin-protein ligase Smurf1
- Sno oncogene, isoform B
- receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
- Forkhead box protein O
- Cullin homolog 1
- GEO01111p1
- Serine/threonine-protein kinase receptor
Sequence:
MLPFTPQVVKRLLALKKGNEDNSVEGKWSEKAVKNLVKKIKKNSQLEELERAISTQNCQTRCVTVPRSKPAPAGEHLRKGLPHVIYCRLWRWPDLQSQNELKPLDHCEYAFHLRKEEICINPYHYKKIELSILVPKSLPTPPDSIVDYPLDNHTHQIPNNTDYNAAIIRSASLSPPQYMELGGAGPVSVSSSASSTPATAAGGGGGPSSSSSSSSSAASAYQQQQQQLSFGQNMDSQSSVLSVGSSIPNTGTPPPGYMSEDGDPIDPNDNMNMSRLTPPADAAPVMYHEPAFWCSISYYELNTRVGETFHASQPSITVDGFTDPSNSERFCLGLLSNVNRNEVVEQTRRHIGKGVRLYYIGGEVFAECLSDSSIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLSQSVSQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDRVLTQMGSPRLPCSSMS
Protein: Nitrophorin-7 (NP7) (EC 1.7.6.1) (Nitrite dismutase) (Q6PQK2)
Organism: Rhodnius prolixus (Triatomid bug)
Function: Converts nitrite as the sole substrate to form nitric oxide gas (NO). NO(2-) serves both as an electron donor and as an electron acceptor. Binds to negatively charged cell surfaces of activated platelets; binds to L-a-phosphatidyl-L-serine (PS)-bearing phospholipid membranes. Once bound on an activated platelet, NP7 releases its stored nitric oxide gas (NO) into the victim's tissues while feeding, resulting in vasodilation and inhibition of platelet aggregation. Also acts as an anticoagulant by blocking coagulation-factor binding sites. Has antihistamine activity; binds histamine with high affinity.
Subcellular location: Secreted {ECO:0000269|PubMed:15170336, ECO:0000269|PubMed:17428677}.
Interaction partners:
Sequence:
MELYTALLAVTILSPSSIVGLPGECSVNVIPKKNLDKAKFFSGTWYETHYLDMDPQATEKFCFSFAPRESGGTVKEALYHFNVDSKVSFYNTGTGPLESNGAKYTAKFNTVDKKGKEIKPADEKYSYTVTVIEAAKQSALIHICLQEDGKDIGDLYSVLNRNKNALPNKKIKKALNKVSLVLTKFVVTKDLDCKYDDKFLSSWQK
Protein: Ankyrin repeat domain-containing protein 45 (Q5TZF3)
Organism: Homo sapiens (Human)
Function: May play a role during cell division.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31208154}. Midbody, Midbody ring {ECO:0000269|PubMed:31208154}. Cleavage furrow {ECO:0000269|PubMed:31208154}. Note=Distribution is highly dynamic during mitosis. Not detected during interphase, localized to cytoplasm during metaphase, to cleavage furrow during anaphase and telophase, and to midbody ring during cytokinesis. {ECO:0000269|PubMed:31208154}.
Interaction partners:
- Hypoxia up-regulated protein 1
- Endoplasmin
- Sodium/hydrogen exchanger 11
Sequence:
MESEGPPESESSEFFSQQEEENEEEEAQEPEETGPKNPLLQPALTGDVEGLQKIFEDPENPHHEQAMQLLLEEDIVGRNLLYAACMAGQSDVIRALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARDVAARYSQTECVEFLDWADARLTLKKYIAKVSLAVTDTEKGSGKLLKEDKNTILSACRAKNEWLETHTEASINELFEQRQQLEDIVTPIFTKMTTPCQVKSAKSVTSHDQKRSQDDTSN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (O22764)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Pyruvate, phosphate dikinase regulatory protein 1, chloroplastic
- Protein kinase superfamily protein
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase UCN
- AT3g24190/MUJ8_17
- Uncharacterized aarF domain-containing protein kinase At1g71810, chloroplastic
- Uncharacterized aarF domain-containing protein kinase At5g05200, chloroplastic
- Serine/threonine-protein kinase STN8, chloroplastic
- Protein KINASE OF THE OUTER CHLOROPLAST MEMBRANE 1
Sequence:
MADSHSVNNQLSRHTSIFGLRLWVVLGVCVGAAIVLLLVLISLWFIYRRSNKNKSLESSSKSNHTIVPVVSKEIQEIRPPIQPDPTPEPHQNQQREDDNKIHIEIGKDHRIAYPERGGWTGSGSGSGSGDQGLLMLSGPEVSHLGWGHWYTLRELEVSTNGFADENVIGQGGYGIVYRGVLEDKSMVAIKNLLNNRGQAEKEFKVEVEAIGRVRHKNLVRLLGYCVEGAHRMLVYEYVDNGNLEQWIHGGGLGFKSPLTWEIRMNIVLGTAKGLMYLHEGLEPKVVHRDIKSSNILLDKQWNSKVSDFGLAKLLGSEMSYVTTRVMGTFGYVAPEYASTGMLNERSDVYSFGVLVMEIISGRSPVDYSRAPGEVNLVEWLKRLVTNRDAEGVLDPRMVDKPSLRSLKRTLLVALRCVDPNAQKRPKMGHIIHMLEAEDLVSKDDRRNSGGGGGGIEQGRSPRRKTNVNESEDESGNSVLINNDQLALENKQN
Protein: Tyrosine-protein phosphatase non-receptor type (EC 3.1.3.48) (Q53XS4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR000929}.
Interaction partners:
Sequence:
MLSRGWFHRDLSGLDAETLLKGRGVHGSFLARPSRKNQGDFSLSVRVGDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGVLQDRDGTIIHLKYPLNCSDPTSERWYHGHMSGGQAETLLQAKGEPWTFLVRESLSQPGDFVLSVLSDQPKAGPGSPLRVTHIKVMCEGGRYTVGGLETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEDTAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKGKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYIKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGDLIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEVLQSQKGQESEYGNITYPPAMKNAHAKASRTSSKHKEDVYENLHTKNKREEKVKKQRSADKEKSKGSLKRK
Protein: mRNA clone with similarity to L-glycerol-3-phosphate:NAD oxidoreductase and albumin gene sequences (Q13138)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVLMGANIASEVADEKFCETTIGESPLAPAYTVHLVASPPQTAPTPLSHLFPIRQRKENTSIRGEGGWDTPREGASGPCLGKHSDEPSLRVGAVAHLWSQLLKRLRWEDRLSPGV
Protein: ATP-dependent RNA helicase DHX8 (EC 3.6.4.13) (DEAH box protein 8) (RNA helicase HRH1) (Q14562)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as component of the spliceosome. Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome.
Subcellular location: Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:28062851, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
Interaction partners:
- SNW domain-containing protein 1
- Cell division cycle 5-like protein
- U4/U6 small nuclear ribonucleoprotein Prp3
- Crooked neck-like protein 1
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor SLU7
- Pre-mRNA-splicing factor SYF1
- RNA helicase aquarius
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing factor 19
Sequence:
MAVAVAMAGALIGSEPGPAEELAKLEYLSLVSKVCTELDNHLGINDKDLAEFVISLAEKNTTFDTFKASLVKNGAEFTDSLISNLLRLIQTMRPPAKPSTSKDPVVKPKTEKEKLKELFPVLCQPDNPSVRTMLDEDDVKVAVDVLKELEALMPSAAGQEKQRDAEHRDRTKKKKRSRSRDRNRDRDRDRERNRDRDHKRRHRSRSRSRSRTRERNKVKSRYRSRSRSQSPPKDRKDRDKYGERNLDRWRDKHVDRPPPEEPTIGDIYNGKVTSIMQFGCFVQLEGLRKRWEGLVHISELRREGRVANVADVVSKGQRVKVKVLSFTGTKTSLSMKDVDQETGEDLNPNRRRNLVGETNEETSMRNPDRPTHLSLVSAPEVEDDSLERKRLTRISDPEKWEIKQMIAANVLSKEEFPDFDEETGILPKVDDEEDEDLEIELVEEEPPFLRGHTKQSMDMSPIKIVKNPDGSLSQAAMMQSALAKERRELKQAQREAEMDSIPMGLNKHWVDPLPDAEGRQIAANMRGIGMMPNDIPEWKKHAFGGNKASYGKKTQMSILEQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDAVKFSQYFYEAPIFTIPGRTYPVEILYTKEPETDYLDASLITVMQIHLTEPPGDILVFLTGQEEIDTACEILYERMKSLGPDVPELIILPVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLVVTPISQAQAKQRAGRAGRTGPGKCYRLYTERAYRDEMLTTNVPEIQRTNLASTVLSLKAMGINDLLSFDFMDAPPMETLITAMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRPKDKQALADQKKAKFHQTEGDHLTLLAVYNSWKNNKFSNPWCYENFIQARSLRRAQDIRKQMLGIMDRHKLDVVSCGKSTVRVQKAICSGFFRNAAKKDPQEGYRTLIDQQVVYIHPSSALFNRQPEWVVYHELVLTTKEYMREVTTIDPRWLVEFAPAFFKVSDPTKLSKQKKQQRLEPLYNRYEEPNAWRISRAFRRR
Protein: Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1) (Lipid raft adaptor protein p18) (Q9CQ22)
Organism: Mus musculus (Mouse)
Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes. May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes. May also play a role in RHOA activation. Involved in the control of embryonic stem cells differentiation; together with FLCN it is necessary to recruit and activate RRAGC/RagC and RRAGD/RagD at the lysosomes, and to induce exit of embryonic stem cells from pluripotency via non-canonical, mTOR-independent TFE3 inactivation.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:30020076}; Lipid-anchor {ECO:0000269|PubMed:30020076}; Cytoplasmic side {ECO:0000269|PubMed:30020076}. Late endosome membrane {ECO:0000269|PubMed:19177150}; Lipid-anchor {ECO:0000250|UniProtKB:Q6IAA8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q6IAA8}. Note=Recruited to lysosome and endosome membranes through N-terminal myristoylation and palmitoylation. {ECO:0000269|PubMed:30020076}.
Interaction partners:
- Neutral amino acid transporter 9
- Ragulator complex protein LAMTOR4
- Ragulator complex protein LAMTOR3
- Ragulator complex protein LAMTOR2
- Ragulator complex protein LAMTOR5
- Ras-related GTP-binding protein C
- Regulatory-associated protein of mTOR
- Ras-related GTP-binding protein D
- Ras-related GTP-binding protein A
- V-type proton ATPase subunit B, brain isoform
Sequence:
MGCCYSSENEDSDQDREERKLLLDPSSTPTKALNGAEPNYHSLPSARTDEQALLSSILAKTASNIIDVSAADSQGMEQHEYMDRARQYSTRLAVLSSSLTHWKKLPPLPSLTSQPHQVLASEPIPFSDLQQVSRIAAYAYSALSQIRVDAKEELVVQFGIP
Protein: Cell cycle checkpoint protein RAD17 (hRad17) (RF-C/activator 1 homolog) (O75943)
Organism: Homo sapiens (Human)
Function: Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination.
Subcellular location: Nucleus {ECO:0000269|PubMed:10232579, ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:12400013}. Chromosome {ECO:0000269|PubMed:24534091}. Note=Phosphorylated form redistributes to discrete nuclear foci upon DNA damage (PubMed:11799063). Localizes to DNA double-strand breaks (DSBs) (PubMed:24534091). {ECO:0000269|PubMed:11799063, ECO:0000269|PubMed:24534091}.
Interaction partners:
- Replication factor C subunit 5
- Replication factor C subunit 4
- Cell cycle checkpoint control protein RAD9A
- Replication factor C subunit 2
- Checkpoint protein HUS1
- Replication factor C subunit 3
- Serine/threonine-protein kinase ATR
- Cell cycle checkpoint protein RAD1
- Cell cycle checkpoint control protein RAD9B
- Serine-protein kinase ATM
Sequence:
MSKTFLRPKVSSTKVTDWVDPSFDDFLECSGVSTITATSLGVNNSSHRRKNGPSTLESSRFPARKRGNLSSLEQIYGLENSKEYLSENEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKQGGSILLITGPPGCGKTTTLKILSKEHGIQVQEWINPVLPDFQKDDFKGMFNTESSFHMFPYQSQIAVFKEFLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLRKYVRIGRCPLIFIISDSLSGDNNQRLLFPKEIQEECSISNISFNPVAPTIMMKFLNRIVTIEANKNGGKITVPDKTSLELLCQGCSGDIRSAINSLQFSSSKGENNLRPRKKGMSLKSDAVLSKSKRRKKPDRVFENQEVQAIGGKDVSLFLFRALGKILYCKRASLTELDSPRLPSHLSEYERDTLLVEPEEVVEMSHMPGDLFNLYLHQNYIDFFMEIDDIVRASEFLSFADILSGDWNTRSLLREYSTSIATRGVMHSNKARGYAHCQGGGSSFRPLHKPQWFLINKKYRENCLAAKALFPDFCLPALCLQTQLLPYLALLTIPMRNQAQISFIQDIGRLPLKRHFGRLKMEALTDREHGMIDPDSGDEAQLNGGHSAEESLGEPTQATVPETWSLPLSQNSASELPASQPQPFSAQGDMEENIIIEDYESDGT
Protein: Tubulin delta chain (Delta-tubulin) (Q9R1K7)
Organism: Mus musculus (Mouse)
Function: Acts as a positive regulator of hedgehog signaling and regulates ciliary function.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:29290584}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:10753753}. Cytoplasm {ECO:0000269|PubMed:10753753}. Nucleus {ECO:0000269|PubMed:10753753}. Note=Associated with centrioles (PubMed:10753753). Both cytoplasmic and nuclear (PubMed:10753753). In the elongating spermatid it is associated with the manchette, a specialized microtubule system present during reshaping of the sperm head (PubMed:10753753). {ECO:0000269|PubMed:10753753}.
Interaction partners:
- Gamma-tubulin complex component 2
- Tubulin epsilon chain
- Gamma-tubulin complex component 5
- Gamma-tubulin complex component 4
Sequence:
MSIVTVQLGQCGNQIGFEVFDALFRDSHCSQGLCSKRDNEAYQASCRERFFREEENGVPVARAVLVDMEPKVINQTLSKAAQSGRWNYGQHTSFCQKQGSGNNWAYGYSVHGPKHEESIMNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFVTQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLIHENDAVHKICAKRMNIKQISFRDLNQVLAHQLGSVFQPTYSEDSSFHYRRNPLGDLMEHLVPHPEFKMLGVRNIPQMSAASLAYSAFTWAGLLKHLRQMLISSAKMEEGINWQVRPPLTGLPPIGKASAHKEHHFNTSLANLVVLRGREVHSADVEGFKDPALYTSWLEPVDAFSVWKTQRAFDKYEKSAALVSNSQLLVKPLDMIVGKAWNMFSSKAFIHQYTKFGMEEEDFLDSFALLEQVVASYGSLGP
Protein: Transforming acidic coiled-coil containing protein 2 (Q4VXL8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGGSQSLQPAPASDLNLEASEAMSSDSEEAFETPESTTPVKAPPAPPPPPPEVIPEPEVSTQPPPEEPGCGSETVPVPDGPRSDSVEGSPFRPPSHSFSAVFDEDKPIASSGTYNLDFDNIELVDTFQTLEPRASDAKNQEGKVNTRRKSTDSVPISKSTLSRSLSLQASDFDGASSSGNPEAVALAPDAYSTGSSSASSTLKRTKKPRPPSLKKKQTTKKPTETPPVKETQQEPDEESLVPSGENLASETKTESAKTEGPSPALLEETPLEPAVGPKAACPLDSESAEGVVPPASGGGRVQNSPPVGRKTLPLTTAPEAGEVTPSDSGGQEDSPAKGLSVRLEFDYSEDKSSWDNQQENPPPTKKIGKKPVAKMPLRRPKMKKTPEKLDNTPASPPRSPAEPNDIPIAKGTYTFDIDKWDDPNFNPFSSTSKMQESPKLPQQSYNFDPDTCDESVDPFKTSSKTPSSPSKSPASFEIPASAMEANGVDGDGLNKPAKKKKTPLKTMVEDVMSVCSLFDTFRVKKSPKRSPLSDPPSQDPTPAATPETPPVISAVVHATDEEKLAVTNQKWTCMTVDLEADKQDYPQPSDLSTFVNETKFSSPTEELDYRNSYEIEYMEKIGSSLPQDDDAPKKQALYLMFDTSQESPVKSSPVRMSESPTPCSGSSFEETEALVNTAAKNQHPVPRGLAPNQESHLQVPEKSSQKELEAMGLGTPSEAIEITAPEGSFASADALLSRLAHPVSLCGALDYLEPDLAEKNPPLFAQKLQEELEFAIMRIEALKLARQIALASRSHQDAKREAAHPTDVSISKTALYSRIGTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGKS
Protein: Cyclin-dependent kinase-like 1 (EC 2.7.11.22) (Q66HE7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVSLLEVFRRKRRLHLVFEYCHHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKHSVIKLCDFGFARLLTGPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGVKIPDPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIRDVGELARPHDKPTRKTLRQSRKHLTGLQHLPQLTSSSVLPALDRKKYHCGTRNFNYHFPNI
Protein: Gag polyprotein [Cleaved into: Matrix protein p17 (MA)] (Q79791)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
Subcellular location: [Matrix protein p17]: Virion membrane {ECO:0000256|RuleBase:RU004487}; Lipid-anchor {ECO:0000256|RuleBase:RU004487}. Host nucleus {ECO:0000256|RuleBase:RU004487}. Host cytoplasm {ECO:0000256|RuleBase:RU004487}.; SUBCELLULAR LOCATION: Host cell membrane {ECO:0000256|ARBA:ARBA00004425}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004425}. Host endosome, host multivesicular body {ECO:0000256|ARBA:ARBA00004560}. Virion membrane {ECO:0000256|ARBA:ARBA00037826}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037826}. Virion {ECO:0000256|RuleBase:RU004487}. Host cytoplasm {ECO:0000256|RuleBase:RU004487}. Host nucleus {ECO:0000256|RuleBase:RU004487}.
Interaction partners:
Sequence:
MGARASVLSGGELDKWEKIRLRPGGKKQYRLKHIVWASRELERFAVNPGLLETSEGCRQILRQLQPSLQTGSEERRSLFNTVAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPATIMIQRGNFRNQKKTVKCFNCGKEGHIAKNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSHKGRPGNFLQSRPEPTAPPEESFRFGEETTTPSQKQEPIDKELYPLASLRSLFGSDPSSQ
Protein: Uncharacterized protein (Q386B0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRASVLLLKSSIRTSGLLLPWKIRPVADTMERRDAWKELEQLLTSITRLSNEEAIEKMTEFCPRLAICDIEYPVETLQRKRRLEERRMLRQHHENRSRNGKKKGEREQVTETVTLADDEATRKLMKSTLRILVARAQKNSGTSDREVVRDKMKKSSSKIIVSSSSATPAPLPSKSDEGKRSGADKKANRGEVDGTQNSKRKGEVEKSSDLVSSPTTTTTGATAAAAAAAMNVSSSSTFPSGETPFRASSTASTAGVKGADTSSGGGSACKTGKGK
Protein: Adenosylhomocysteinase (EC 3.13.2.1) (Q6FWX3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Cystathionine beta-synthase
- Cystathionine beta-lyase
- Candida glabrata strain CBS138 chromosome F complete sequence
- cystathionine gamma-synthase
- Candida glabrata strain CBS138 chromosome H complete sequence
- cystathionine gamma-lyase
- Homocysteine/cysteine synthase
- S-adenosylmethionine synthase
- Threonine dehydratase
Sequence:
MSAPAQNYKIADISLAAFGRKEIELAENEMPGLMAIRKAYAEAQPLKGARIAGCLHMTIQTAVLIETLVALGAEVTWTSCNIYSTQDHAAAAIAASGVPVFAWKGETEEEYMWCIEQQLFAFKDNKKLNLILDDGGDLTSFVHEKYPEMLTDCFGLSEETTTGVHHLYRMMREGKLKVPAINVNDAVTKSKFDNLYGCRESLVDGIKRATDVMLAGKVAVVAGFGDVGKGCAASLRGMGARVLVTEIDPINALQAAMEGYEVTTMEDAASVGQVFVTTTGCRDIIKGEHFEKMPEDAIVCNIGHFDIEIDVAWLKENAKECINIKPQVDRYLLSSGRHVILLANGRLVNLGCATGHSSFVMSCSFSNQVLAQIALFKSDDKAFRTKFVEFEKTGPFEVGVHVLPKILDEAVAKFHLEKLGVKLTTLSDVQSEYLGIPQQGPFKADHYRY
Protein: Regulating synaptic membrane exocytosis protein 4 (RIM4 gamma) (Rab3-interacting molecule 4) (RIM 4) (Q8CIX1)
Organism: Rattus norvegicus (Rat)
Function: Regulates synaptic membrane exocytosis.
Subcellular location: Synapse {ECO:0000250}.
Interaction partners:
Sequence:
MERSQSRLSLSASFEALAIYFPCMNSFDDEDAADSRRLKGAIQRSTETGLAVEMPSRTLRQASHESIEDSMNSYGSEGNLNYGGVCLASDAQFSDFLGSMGPAQFVGRQTLATTPMGGVEIGLQERNGQLEVDIIQARGLTAKPGSKTLPAAYIKAYLLENGVCIAKKKTKVARKSLDPLYNQVLLFPESPQGKVLQVIVWGNYGRMERKQFMGVARVLLEELDLTTLAVGWYKLFPTSSMVDPATGPLLRQASQLSLESTVGPCGERS
Protein: Calcium/calmodulin-dependent protein kinase Ib (Calcium/calmodulin-dependent protein kinase type 1 isoform X2) (Calcium/calmodulin-dependent protein kinase type 1-like isoform X2) (E7F1H0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Doublecortin-like kinase 2b.
- BRISC and BRCA1-A complex member 2
- Calmodulin
- Calmodulin-like protein 4
- Anaphase-promoting complex subunit 5.
Sequence:
MPLGEDGPSWKKKTANIKDIYDFKEVLGTGAFSEVMLAEEKRTRKLVAVKCIAKKALEGKENSIENEIAVLHKIKHANIVSLEDIFESKSHLYLVMQLVSGGELFDRIVEKGFYTEKDASKLIQQILDAVKYLHDMGIVHRDLKPENLLYYSMDEESKIMISDFGLSKIEGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILRAEYEFDSPYWDDISDSAKDFIVHLMEKDPNQRYTCEQALQHPWIAGDTALDKNIHESVSAQIKKNFAKSKWKQAFNATAVVRHMRRLQLGTSQEGPPQNTLPSPCHGHLLLPEGDEDDSVRENSGCSEGVSDGNDIQNCSYHLHPTSRV
Protein: Chitin synthase regulator SKT5 (P34226)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Activator of the chitin synthase CHS3 which polymerizes chitin, a structural polymer of the fungal cell wall.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17142567}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Farnesylation is not required for cellular membrane localization. {ECO:0000269|PubMed:17142567}.
Interaction partners:
- Chitin synthase 3
- Protein BNI4
- Chitin synthase export chaperone
- Chitin synthase 2
- Chitin synthase 1
- Chitin biosynthesis protein CHS5
- Chitin biosynthesis protein CHS6
- 1,3-beta-glucan synthase component FKS1
- Protein OS-9 homolog
- Covalently-linked cell wall protein 12
Sequence:
MASSPQVHPYKKHLMQSQHINFDNRGLQFQNSSLKVGQDFSDNKENRENRDNEDFSTADLPKRSANQPLINEHLRAASVPLLSNDIGNSQEEDFVPVPPPQLHLNNSNNTSLSSLGSTPTNSPSPGALRQTNSSTSLTKEQIKKRTRSVDLSHMYLLNGSSDTQLTATNESVADLSHQMISRYLGGKNNTSLVPRLKTIEMYRQNVKKSKDPEVLFQYAQYMLQTALTIESSNALVQDSDKEGNVSQSDLKLQFLKEAQSYLKKLSIKGYSDAQYLLADGYSSGAFGKIENKEAFVLFQAAAKHGHIESAYRASHCLEEGLGTTRDSRKSVNFLKFAASRNHPSAMYKLGLYSFYGRMGLPTDVNTKLNGVKWLSRAAARANELTAAAPYELAKIYHEGFLDVVIPDEKYAMELYIQAASLGHVPSATLLAQIYETGNDTVGQDTSLSVHYYTQAALKGDSVAMLGLCAWYLLGAEPAFEKDENEAFQWALRAANAGLPKAQFTLGYFYEHGKGCDRNMEYAWKWYEKAAGNEDKRAINKLRSRDGGLASIGKKQHKKNKSISTLNLFSTVDSQTSNVGSNSRVSSKSETFFTGNPKRDREPQGLQINMNSNTNRNGIKTGSDTSIRKSSSSAKGMSREVAEQSMAAKQEVSLSNMGSSNMIRKDFPAVKTESKKPTSLKNKKDKQGKKKKDCVIM