wanglab/gogpt-training-data huggingface dataset:
Protein: Agamous-like MADS-box protein AGL1 (Protein SHATTERPROOF 1) (P29381)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor. Interacts genetically with TT16/AGL32 in a partially antagonistic manner during flower development. Is essential for the coordination of cell divisions in ovule, seed coat development and endosperm formation.
Subcellular location: Nucleus.
Interaction partners:
- Developmental protein SEPALLATA 3
- BEL1-like homeodomain protein 9
- At1g27000/T7N9_6)
- Homeobox protein BEL1 homolog
- Large ribosomal subunit protein uL14my
- F-box protein 7
- Floral homeotic protein APETALA 2
- B3 domain-containing protein At5g18000
- Protein SPOROCYTELESS
- MADS-box protein
Sequence:
MEEGGSSHDAESSKKLGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALVIFSTRGRLYEYANNSVRGTIERYKKACSDAVNPPSVTEANTQYYQQEASKLRRQIRDIQNSNRHIVGESLGSLNFKELKNLEGRLEKGISRVRSKKNELLVAEIEYMQKREMELQHNNMYLRAKIAEGARLNPDQQESSVIQGTTVYESGVSSHDQSQHYNRNYIPVNLLEPNQQFSGQDQPPLQLV
Protein: Serine/threonine-protein kinase Doa (EC 2.7.12.1) (Protein darkener of apricot) (P49762)
Organism: Drosophila melanogaster (Fruit fly)
Function: Negative regulator of the copia retrotransposon element of the white (w) gene. In the eye, it is required for normal pigmentation, photoreceptor cell development and for organization of interommatidial bristles. Also essential for embryonic segmentation and differentiation of the nervous system. Functions in the control of alternative splicing by phosphorylating the arginine/serine-rich splicing factors, SR proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17828581}.; SUBCELLULAR LOCATION: [Isoform K]: Cytoplasm, cytosol {ECO:0000269|PubMed:11014821}.; SUBCELLULAR LOCATION: [Isoform A]: Nucleus {ECO:0000269|PubMed:11014821}. Note=Mainly nuclear with only low levels present in the cytoplasm. {ECO:0000269|PubMed:11014821}.
Interaction partners:
- Uncharacterized protein, isoform F
- LD29830p
- Serine/arginine-rich splicing factor x16
- RNA-binding protein 1
Sequence:
MVAANLEVPTSSSSSAATKRQKDVDNKLEKCLNDMLKLKTSSNNNSTSNSNNNAIMSHSLTGEHKDPKTALEGPTSSSSSSSSKYIGESQIPVPVQLYDPQKPLLQQQQQQQRICYPIGKSNSTSQLPMGGYQRLLQHQQQQHHQQQQQQHQEQQQYPQHKRPFLNWNSFACSAMNGASDPFMQQQHMPAHQQQQHLPHKLQQSYSSSHVPKQAPKSGLAMFLQKNTNKENKFGQPMQQQPPGMMPQMYGYQAPQQQSKIGYPRTGAPLTHSASFSSAQRPTALQFHQQHQQQQHLQQQQQHPQQQQHQHSSFGVGMMSRNYYNMPKQPERKPLQTFDPYAYPKPNQMQPVKYQQQQQHPHTQFQNASAGGGGGGAAGLQYDPNTNTQLFYASPASSSSNKQPQQPQQQQQQQQSQLQQSNSVIFNHSGQQHQPHQQQQNEMSKSALGLHFIETAKPVIQDDADGHLIYHTGDILHHRYKIMATLGEGTFGRVVKVKDMERDYCMALKIIKNVEKYREAAKLEINALEKIAQKDPHCDHLCVKMIDWFDYHGHMCIVFEMLGLSVFDFLRENNYEPYPLDQVRHMAYQLCYSVKFLHDNRLTHTDLKPENILFVDSDYTSHYNHKINREVRRVKNTDVRLIDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCILFELYLGITLFQTHDNREHLAMMERILGQIPYRMARNHTLYSKTKTKYFYHGKLDWDEKSSAGRYVRDHCKPLFLCQLSDSEDHCELFSLIKKMLEYEPSSRITLGEALHHPFFDRLPPHHRVGEVSNKQPLSSGSSSRERSHSLSR
Protein: LD40728p (RluA pseudouridine synthase 2, isoform A) (RluA pseudouridine synthase 2, isoform D) (Q9VKU8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pseudouridylate synthase 7 homolog
- RE57978p
- Mitochondrial assembly of ribosomal large subunit protein 1
- rRNA methyltransferase 3, mitochondrial
- Acyl carrier protein, mitochondrial
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL3m
Sequence:
MESSKLLRNAQTQHGDASSVDVENIFLHRHMLYTNPTSDGNLHDREDSPECVWCPDDKDGSPAESKDPPISISEEKSETQSKEVLSEKRKASSTDDEGHVKKVKLEANSLKTKRPGFSDERYDETSYYFENGLRKVYPYFFTFTTFAKGRWVDEKILDVFVREFRAAPPEEYERSLEAGKLTVNSEKVPKDYKIKHNDLLANVVHRHEVPVTSQPIKIVYMDKDIVVVNKPASIPVHPCGRYRHNTVVFILAKEHNLKNLRTIHRLDRLTSGLLLFGRTAEKARELELQIRTRQVQKEYVCRVEGRFPDGIVECNEKIDVVSYKIGVCKVSPKGKDCKTTFKRIGEVGSDSIVLCKPLTGRMHQIRVHLQFLGYPISNDPLYNHEVFGPLKGRGGDIGGITEEQLISNLISIHNAENWLGLEGDQIVSGEIKDVAASTSVVEAPSVVQAPINSETEKPVISKNLEPSNDATAQIATQTCYEEPDRSFDSKKTTSDPQCSECKINYRDPGTKDLIMYLHAWKYKGVGWEYETELPEWACNSNIDYDKV
Protein: Acetyl-coenzyme A synthetase, cytoplasmic (EC 6.2.1.1) (Acetate--CoA ligase) (Acetyl-CoA synthetase) (ACS) (AceCS) (Acetyl-CoA synthetase 1) (AceCS1) (Acyl-CoA synthetase short-chain family member 2) (Acyl-activating enzyme) (Propionate--CoA ligase) (EC 6.2.1.17) (Q9NR19)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Acetate is the preferred substrate. Can also utilize propionate with a much lower affinity (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10843999, ECO:0000269|PubMed:28003429, ECO:0000269|PubMed:28552616}. Cytoplasm {ECO:0000250|UniProtKB:Q9QXG4}. Nucleus {ECO:0000269|PubMed:28552616}. Note=Glucose deprivation results in its AMPK-dependent phosphorylation and subsequent nuclear translocation (PubMed:28552616). Phosphorylation at Ser-659, leads to exposure of its nuclear localization signal which is required for its interaction with KPNA1 and subsequent translocation to the nucleus (PubMed:28552616). Found in the cytoplasm in undifferentiated neurons and upon differentiation, translocates to nucleus (By similarity). {ECO:0000250|UniProtKB:Q9QXG4, ECO:0000269|PubMed:28552616}.
Interaction partners:
- Citrate synthase, mitochondrial
- Acetyl-CoA carboxylase 1
- Acetyl-CoA carboxylase 2
- Acetyl-CoA acetyltransferase, mitochondrial
- Acetyl-coenzyme A thioesterase
- Peroxisomal acyl-coenzyme A oxidase 1
- Acetyl-CoA acetyltransferase, cytosolic
- Peroxisomal acyl-coenzyme A oxidase 3
- Aldehyde dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MGLPEERVRSGSGSRGQEEAGAGGRARSWSPPPEVSRSAHVPSLQRYRELHRRSVEEPREFWGDIAKEFYWKTPCPGPFLRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ
Protein: Putative anti-sigma regulatory factor (Serine/threonine protein kinase) (Q2RIF6)
Organism: Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Interaction partners:
- Anti-sigma-factor antagonist
- Anti-sigma-factor antagonist
- Serine phosphatase
- Diguanylate cyclase
- Anti-sigma factor antagonist
- RNA polymerase sigma factor
- Anti-sigma factor antagonist
- Serine phosphatase
- Flagellar hook-associated protein 1
- Flagellar basal body rod protein FlgB
Sequence:
MNLKQTLPITSEYDIITARQAAREIARQIGFNTVDQVRIATAVSELTRNVVLYAGFGKVDIEVVTRGERQGIEITVSDQGPGIADIELALRDGYSSSNGLGAGLSGARRLMDTFFIESRVGQGTTVRIGKWKNWK
Protein: Mitoferrin-1 (Mitochondrial iron transporter 1) (Mitochondrial solute carrier protein) (Solute carrier family 25 member 37) (Q9NYZ2)
Organism: Homo sapiens (Human)
Function: Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q287T7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family B member 10, mitochondrial
- Ferrochelatase, mitochondrial
- Asparaginyl-tRNA synthetase
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- Frataxin, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Mitochondrial potassium channel ATP-binding subunit
- Zinc fingers and homeoboxes protein 2
- Hemoglobin subunit gamma 1
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
Sequence:
MELRSGSVGSQAVARRMDGDSRDGGGGKDATGSEDYENLPTSASVSTHMTAGAMAGILEHSVMYPVDSVKTRMQSLSPDPKAQYTSIYGALKKIMRTEGFWRPLRGVNVMIMGAGPAHAMYFACYENMKRTLNDVFHHQGNSHLANGIAGSMATLLHDAVMNPAEVVKQRLQMYNSQHRSAISCIRTVWRTEGLGAFYRSYTTQLTMNIPFQSIHFITYEFLQEQVNPHRTYNPQSHIISGGLAGALAAAATTPLDVCKTLLNTQENVALSLANISGRLSGMANAFRTVYQLNGLAGYFKGIQARVIYQMPSTAISWSVYEFFKYFLTKRQLENRAPY
Protein: Pre-protein VI (pVI) [Cleaved into: Endosome lysis protein; Protease cofactor (pVI-C)] (P24937)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: During virus assembly, promotes hexon trimers nuclear import through nuclear pore complexes via an importin alpha/beta-dependent mechanism. By analogy to herpesviruses capsid assembly, might act as a chaperone to promote the formation of the icosahedral capsid.
Subcellular location: [Pre-protein VI]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04048, ECO:0000269|PubMed:14633984}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04048, ECO:0000269|PubMed:14633984}. Note=Shuttles between host cytoplasm and nucleus. {ECO:0000255|HAMAP-Rule:MF_04048, ECO:0000269|PubMed:14633984}.; SUBCELLULAR LOCATION: [Endosome lysis protein]: Virion {ECO:0000255|HAMAP-Rule:MF_04048, ECO:0000269|PubMed:25071205}. Note=Associates with the base of each peripentonal hexon on the capsid interior. Present in around 360 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04048, ECO:0000269|PubMed:25071205}.
Interaction partners:
Sequence:
MEDINFASLAPRHGSRPFMGNWQDIGTSNMSGGAFSWGSLWSGIKNFGSTVKNYGSKAWNSSTGQMLRDKLKEQNFQQKVVDGLASGISGVVDLANQAVQNKINSKLDPRPPVEEPPPAVETVSPEGRGEKRPRPDREETLVTQIDEPPSYEEALKQGLPTTRPIAPMATGVLGQHTPVTLDLPPPADTQQKPVLPGPTAVVVTRPSRASLRRAASGPRSLRPVASGNWQSTLNSIVGLGVQSLKRRRCF
Protein: Leukocyte cell derived chemotaxin 2 (F1NEF7)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MPALSLIALLSLVSTAFARQWEVHPPQQQGRHWAQICSGNPFNRIRGCDRYGCGNYGASRQGKGEKHKGVDVICTDGSIVYAPFSGQLSGPIRFFHNGNAIDDGVQISGSGYCVKLVCIHPIRYHGQIQKGQQLGRMLPMQKVFPGIVSHIHVENCDQSDPTHLLRPIPDISPPFPQQDAHWAVVCAGNPTNEIRGCDKYGCGYFGAPRRNGKGEKHKGVDVICADGATVYAPFSGELSGPVKFFHNGNAIDDGVQIRGSGFCVKLLCIHPIRYNGRISKGQVLGRMLPMQRVFPGIISHIHVENCDRSDPTSNLERGKGRK
Protein: 3-phosphoinositide-dependent protein kinase 1 (EC 2.7.11.1) (Pdk-class protein kinase 1) (Q9Y1J3)
Organism: Caenorhabditis elegans
Function: Involved in the daf-2/insulin receptor-like transduction pathway, which controls longevity and prevents developmental arrest at the dauer stage. Phosphorylates and activates sgk-1, akt-1 and akt-2.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase sgk-1
- Serine/threonine-protein kinase akt-2
- Serine/threonine-protein kinase akt-1
- Phosphatidylinositol 3-kinase age-1
- Forkhead box protein O
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase daf-18
- Phosphoinositide 3-kinase adapter subunit
Sequence:
MEDLTPTNTSLDTTTTNNDTTSDREAAPTTLNLTPTASESENSLSPVTAEDLIAKSIKEGCPKRTSNDFMFLQSMGEGAYSQVFRCREVATDAMFAVKVLQKSYLNRHQKMDAIIREKNILTYLSQECGGHPFVTQLYTHFHDQARIYFVIGLVENGDLGESLCHFGSFDMLTSKFFASEILTGLQFLHDNKIVHRDMKPDNVLIQKDGHILITDFGSAQAFGGLQLSQEGFTDANQASSRSSDSGSPPPTRFYSDEEVPEENTARRTTFVGTALYVSPEMLADGDVGPQTDIWGLGCILFQCLAGQPPFRAVNQYHLLKRIQELDFSFPEGFPEEASEIIAKILVRDPSTRITSQELMAHKFFENVDWVNIANIKPPVLHAYIPATFGEPEYYSNIGPVEPGLDDRALFRLMNLGNDASASQPSTFRPSNVEHRGDPFVSEIAPRANSEAEKNRAARAQKLEEQRVKNPFHIFTNNSLILKQGYLEKKRGLFARRRMFLLTEGPHLLYIDVPNLVLKGEVPWTPCMQVELKNSGTFFIHTPNRVYYLFDLEKKADEWCKAINDVRKRYSVTIEKTFNSAMRDGTFGSIYGKKKSRKEMMREQKALRRKQEKEEKKALKAEQVSKKLSMQMDKKSP
Protein: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2 (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase 2) (Glutamine:fructose-6-phosphate amidotransferase 2) (GFAT 2) (GFAT2) (Hexosephosphate aminotransferase 2) (O94808)
Organism: Homo sapiens (Human)
Function: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
Interaction partners:
- Glucosamine 6-phosphate N-acetyltransferase
- Glucose-6-phosphate isomerase
- N-acetylglucosamine-6-phosphate deacetylase
- Glutamine--fructose-6-phosphate aminotransferase 1
- Glucosamine-6-phosphate deaminase 1
- Glutamine synthetase
- Glucosamine-6-phosphate deaminase 2
- Mannose-6-phosphate isomerase
- Amidophosphoribosyltransferase
- Glutaminase kidney isoform, mitochondrial
Sequence:
MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKRGKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMKRLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSASDDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE
Protein: Biotin synthase auxiliary protein (P9WLT7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Biotin synthase
- Uncharacterized protein Rv1591
Sequence:
MVEIVAGKQRAPVAAGVYNVYTGELADTATPTAARMGLEPPRFCAQCGRRMVVQVRPDGWWARCSRHGQVDSADLATQR
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 (Complex I-B22) (NADH-ubiquinone oxidoreductase B22 subunit) (E7EWZ0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
Sequence:
MAFLASGPYLTHQQKVLRLYKRALRHLESWCVQRDKYRYFACLMRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHPQPYIFPDSPGGTSYERYDCYKVPEWCLDDWHPSEKAMYPDYFAKREQWKKLRRESWEREVRSTCTSLFLSYVDGVKFCSPQAEVQIPAMTVTLGPCFSDIL
Protein: Cell division control protein 4 (E3 ubiquitin ligase complex SCF subunit CDC4) (F-box protein CDC4) (P07834)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. Directs ubiquitination of the phosphorylated CDK inhibitor SIC1. Involved in the degradation of CDC6 together with CDC34/UBC3 and CDC53, and in restricting the degradation of FAR1 to the nucleus. Is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. Required for HTA1-HTB1 locus transcription activation. Required for G1/S and G2/M transition.
Subcellular location: Nucleus {ECO:0000269|PubMed:11080155}.
Interaction partners:
- Protein SIC1
- Suppressor of kinetochore protein 1
- RING-box protein HRT1
- Cell division control protein 53
- Cell division control protein 6
- Ubiquitin-conjugating enzyme E2-34 kDa
- SCF E3 ubiquitin ligase complex F-box protein GRR1
- Cyclin-dependent kinase inhibitor FAR1
- F-box protein MET30 subunit MET30)
- Anaphase-promoting complex subunit CDC23
Sequence:
MGSFPLAEFPLRDIPVPYSYRVSGGIASSGSVTALVTAAGTHRNSSTAKTVETEDGEEDIDEYQRKRAAGSGESTPERSDFKRVKHDNHKTLHPVNLQNTGAASVDNDGLHNLTDISNDAEKLLMSVDDGSAAPSTLSVNMGVASHNVAAPTTVNAATITGSDVSNNVNSATINNPMEEGALPLSPTASSPGTTTPLAKTTKTINNNNNIADLIESKDSIISPEYLSDEIFSAINNNLPHAYFKNLLFRLVANMDRSELSDLGTLIKDNLKRDLITSLPFEISLKIFNYLQFEDIINSLGVSQNWNKIIRKSTSLWKKLLISENFVSPKGFNSLNLKLSQKYPKLSQQDRLRLSFLENIFILKNWYNPKFVPQRTTLRGHMTSVITCLQFEDNYVITGADDKMIRVYDSINKKFLLQLSGHDGGVWALKYAHGGILVSGSTDRTVRVWDIKKGCCTHVFKGHNSTVRCLDIVEYKNIKYIVTGSRDNTLHVWKLPKESSVPDHGEEHDYPLVFHTPEENPYFVGVLRGHMASVRTVSGHGNIVVSGSYDNTLIVWDVAQMKCLYILSGHTDRIYSTIYDHERKRCISASMDTTIRIWDLENIWNNGECSYATNSASPCAKILGAMYTLQGHTALVGLLRLSDKFLVSAAADGSIRGWDANDYSRKFSYHHTNLSAITTFYVSDNILVSGSENQFNIYNLRSGKLVHANILKDADQIWSVNFKGKTLVAAVEKDGQSFLEILDFSKASKINYVSNPVNSSSSSLESISTSLGLTRTTIIP
Protein: Kinesin light chain 1 (KLC 1) (Q07866)
Organism: Homo sapiens (Human)
Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity.
Subcellular location: Cell projection, growth cone {ECO:0000250|UniProtKB:P37285}. Cytoplasmic vesicle {ECO:0000269|PubMed:21385839}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:14970196}.
Interaction partners:
- Kinesin heavy chain isoform 5A
- Kinesin heavy chain isoform 5C
- Kinesin-1 heavy chain
- Kinesin light chain 2
- Kinesin light chain 4
- C-Jun-amino-terminal kinase-interacting protein 3
- C-Jun-amino-terminal kinase-interacting protein 1
- Kinesin light chain 3
- Calsyntenin-1
- Amyloid-beta precursor protein
Sequence:
MYDNMSTMVYIKEDKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSNMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDTDSTKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGTSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPENMEKRRSRESLNVDVVKYESGPDGGEEVSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR
Protein: Glutamine synthetase 2 cytoplasmic (EC 6.3.1.2) (Glutamate--ammonia ligase 2) (P20478)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm.
Interaction partners:
- Glutamate dehydrogenase, mitochondrial
- Glutamate synthase
- Multifunctional protein r
- Amidophosphoribosyltransferase
- Delta-1-pyrroline-5-carboxylate synthase
- glutamine--fructose-6-phosphate transaminase
- glutamine--fructose-6-phosphate transaminase
- Multifunctional fusion protein
- Amidophosphoribosyltransferase
- glutaminase
Sequence:
MSARILEDSPNARINKTILDRYLSLPLQENIVQATYVWIDGTGEDLRCKDRTLDFIPQSPKELPVWNYDGSSCYQAEGSNSDTYLYPVAIYKDPFRRGNNILVMCDTYKFDGTPTDTNKRKTCLEVANKCAAEEPWFGIEQEYTFLDFDGHPLGWPKNGFPGPQGPYYCGVGANKVYARDIVDAHYRACLYAGIKVSGTNAEVMPAQWEFQVGPCEGISIGDDLWMARFLLHRISEEFGIVSTLDPKPMPGDWNGAGAHTNVSTKAMREDGGIRDIEKAVAKLSKCHERHIRAYDPKQGQDNARRLTGKHETSSINDFSAGVANRGCSIRIPRGVNDDGKGYFEDRRPSSNCDPYSVVEAILRTICLDE
Protein: Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) (P00817)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- V-type proton ATPase subunit c''
- Inorganic pyrophosphatase, mitochondrial
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit c
- Plasma membrane ATPase 1
- Plasma membrane ATPase 2
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit gamma, mitochondrial
- RHO1 GEF localizing protein 1
Sequence:
MTYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKENNIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFVRNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPIDVLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDINDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPENQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGIDLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWFFISGSV
Protein: Endothelial differentiation-related factor 1 (EDF-1) (Multiprotein-bridging factor 1) (MBF1) (O60869)
Organism: Homo sapiens (Human)
Function: Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. May function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism.
Subcellular location: Cytoplasm. Nucleus. Note=Also nuclear upon binding to NR5A1 and treatment of cells with TPA or forskolin.
Interaction partners:
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS7
Sequence:
MAESDWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQHSITKNTAKLDRETEELHHDRVTLEVGKVIQQGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLRGKDIGKPIEKGPRAK
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IBW9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MAPGGRQGDGGEDIDHQSAKHLLDSIGKIVHDQMKKEAEQRSKGELEGKLSFATVSGETGATDKPCNFDYDKLIGANDGKRHPCKKDGKGEEVPRFSDKQGAECANNRIQGNNKNSHYKDFGACAPFRRLNLCNKNFPNMNSNDSSKAKHDLLVDVCLAAKYEGDSLKHYSEKLNLTYTDSPSQLCTELARSFADIGDIIRGKDLYLGYNRKEKAQKEKLEQNLKKFFQNIDEKLPLKAKNYYTKEKDPNFLKLREDWWTANRETVWEALTCDAHGTYFHATCSDLNGDCSQAHEKCRCPKTSGGKAIKAGGDVTIVPTYFDYVPQYLRWFEEWAEDFCRKKKKYVDIVKTYCREQDKSGNQRYCSRNGYDCTKTVRARGKYRMGNQCTKCLFACNPYVEWIENQRKQFDKQVKKYKTEISDGGGRQKRDAGGTTKYEGYEKKFYDELKGNYSDVNAFLGLLNNEKACTAVKDNDGGTIHFETVGTTTTIGENGGTSDTSGTNNENEGTFYRSKYCQPCPHCGVKREGNEWKEKKKNTDQCTSGKRYKPKNNAEATNIRILKSGDGQTEIENKLNEFCDQINLDTLNSGVNSAGGGGGGRSGSQELYQEWKCYKGDDVVKVENKDEEEDEEENVQKVKDAGGLCILKNERSETNSQNHPYDIQKTYNDFFNFWVAHVLKDSIHWRTKKIKGCLSNGAKIRCNKKNKCNNDCGCFERWVKQKKDEWKPIKQHFYTQEDIVKKGPFMTLTHDYVLEGVLELEFLKGDSEEDFEADSSEDSQSRDEDAQETKRIKDMFEKKKKKNKDEVASNEETIIDFMLDEELNDAKQCIEKHTCPPQEGLARSESDTQRDTHSDDVEAEEEDEEEEEDDVGAEGESETVKDTEAPVETKKDVDVCKIVEQALNNMENLNAACTLKYGPKAPTSWKCIPSGSDSSSSGAICVPPRRRRLYVGKLEQWANKHNTDASEARGSEAPSPSGTDTHTQPDPQKALLKAFVESAAVETFFLWHRYKEEKKKPQEGGLPLLGTGDSVDGEEEEQPPQNELNGGKIPNDFLRQMFYTLADYKDILDGKNIVADILNGSSGSDKDMVEREKTIKEKIKIFFEQNGNKEAAPRGSTQTQPSEKLKSWWSQNGEYIWKGMVCALTYEENGARGTDGKTTLKRNDDVYEKFFGKPSDSSILPVTGSTPTGTAATPNGTTGTYTTQYQYDSVTIGASGTGAKSDDTINNPTLKDFVLRPPYFRYLEEWGETFCRQRTRMLEKIKDDCKVGQGNGKNGDKVCSGYGEECKIEDISKEGLFADLKCPSCAISCSSYRKWIKGKKTQYEKQKDRYKTEIDQAKSDNEFCATLKSLSDAAQFLERLGPCKKDNASGEGKKFFENEGEAFTPATNCKPCPEFKINCKNGKCKSGDGDTKEKCNEKTTIDVNDIENKTDVNNIVMLVSDDNKNKSETVLEACIEAGIFKGIRKEEWKCRNECGLDVCGLKKGDNNGKLDDKQIILIRALIKRWLEYFLEDYNKIRKKLKSCTEKGEGSPCIKDCKKKCDCVKAWINLKTKEWEEIKKPYLEQYKNGYGENYNVKTILEKFQDQPEFKKAIGPCPNLGQFEDSIHCNGAARSENGKKRDIVECLLQKLEKKAEKCQNQNETACDTPSTCDKNLTPDVEDDDEEPYEDLLLQETEEKPEEAKKKMMPKICEGVIPKEEVKDKDGCKPAAAPSAETDKEKPVPKPPSQPTNPPNPFEHPAVIPALMSSTIMWSVGIGFAAFTYFYLKKKTKASVGNLFQILQIPKGDYDIPTLKSSNRYIPYASDRYKGKTYIYMEGDSSGDEKYAFMSDTTDVTSSESEYEELDINDMYVPGSPKYKTLIEVVLEPSKRDTMSTQSDIPLNDKLDSNKLTDEEWNKLKQDFISILQNPQNDLPQNNISGNIQMDTHPSVSILHDDMEEKPFITSIHDRDLHNGEEVTYNINLDDHKNMNFSTNHDNIPPKNNQNDLYTGIDLINDSISGNHNVDIYDELLKRKENELFGTNHTKHTTTNSITKKTHNDPIVNQINLFHKWLDRHKNMCEQWDKHKKEELLDKLKKEWEQDYNNNSDDIHTSDNNIVSTVNHVFNTDVSIQIDMDDPNPVNPFTNMYTNSDNSTMDNILNGMEKHREPYFYDIYEDDITYFDIDDEKTPMGDIYVDHNNVNSNNMDVPNKVHIEMNIVNNKKEIFEEEYPISDIWNI
Protein: Lateral muscles scarcer, isoform B (Lateral muscles scarcer, isoform C) (RE33150p) (Q8MZ02)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Tektin
- AT25567p
- Homeobox protein goosecoid
- EG:115C2.6 protein
- RH05790p
- AT08210p
- LP04777p
- Dystrobrevin, isoform F
- RE31520p
- GH23506p
Sequence:
MNSQSAVRRYPHSFSIEQILAKPEMRSSTSFEDSVQDESGRGGNCLGASRASSPATSSCLDDNMDDGKSDIDLASDDGNGLGDDRKKRPRTAFSAAQIKALETEFERGKYLSVAKRTALAKQLQLTETQIKIWFQNRRTKWKRKYTSDVETLASHYYAQLGIGGLARPMVVGDRLWLFSQTPTGPTPIQSIMLNGSGSAAPMASATTATGSPMRPYATSGGMPPLPGPSVMESARNAILARGQPLNFALPFGVAKPPAGGVPAASYIPRCKPYATSYVDYAASLPTNESYLQMKYATLPPEAESGASNGLAELERVFGDANANFLQQRSTPVAGTATAYGHDGLNQAQRSRRPTQSESECSDIDCEHLDEDEEPPAAE