wanglab/gogpt-training-data huggingface dataset:
Protein: Inactive GDSL esterase/lipase-like protein 23 (GDSL-like lipase 23) (Probable myrosinase-associated protein GLL23) (Q8W4H8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the control of the PYK10 complex size and possibly substrate specificity. May be exported from the endoplasmic reticulum upon interaction with MVP1.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:24330158}. Note=Only transiently resident in a specific ER subcompartment and is either post-translationally modified prior to export or targeted for degradation.
Interaction partners:
- F5A9.16
- TSA1-like protein
- Beta-glucosidase 23
- MD-2-related lipid-recognition protein 3
- Membrane protein of ER body 1
- PYK10-binding protein 2
- Transmembrane emp24 domain-containing protein p24delta8
- At1g72640
- Classical arabinogalactan protein 10
- Myrosinase 2
Sequence:
MMAKNCNLVSVLCVFLVLTLFNKPITVAGQNIPAVGLFTFGDSNFDAGNKQTLTKTLLPQTFWPYGKSRDDPNGKFSDGLIAPDFLAKFMRIPIVIPPALQPNVNVSRGASFAVADATLLGAPVESLTLNQQVRKFNQMKAANWNDDFVKKSVFMIYIGANDYLNFTKNNPNADASTQQAFVTSVTNKLKNDISLLYSSGASKFVIQTLAPLGCLPIVRQEFNTGMDQCYEKLNDLAKQHNEKIGPMLNELARTAPASAPFQFTVFDFYNAILTRTQRNQNFRFFVTNASCCGVGTHDAYGCGFPNVHSRLCEYQRSYLFFDGRHNTEKAQEMFGHLLFGADTNVIQPMNIRELVVYPADEPMRESWVPPTSATVQLRESRGYEYY
Protein: LIM domain kinase 1 (LIMK-1) (EC 2.7.11.1) (P53669)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15660133}. Nucleus {ECO:0000269|PubMed:15660133}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P53667}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P53668}. Note=Predominantly found in the cytoplasm. Localizes in the lamellipodium in a CDC42BPA, CDC42BPB and FAM89B/LRAP25-dependent manner. {ECO:0000250|UniProtKB:P53667, ECO:0000250|UniProtKB:P53668}.
Interaction partners:
- Cofilin-1
- Cofilin 2
- Bone morphogenetic protein receptor type-2
- Ras-related C3 botulinum toxin substrate 1
- non-specific serine/threonine protein kinase
- Rho-associated protein kinase 1
- Serine/threonine-protein kinase PAK 1
- Rho-associated protein kinase 2
- Serine/threonine-protein kinase PAK 5
- Serine/threonine-protein kinase PAK 3
Sequence:
MRLTLLCCTWREERMGEEGSELPVCASCSQSIYDGQYLQALNADWHADCFRCCECSTSLSHQYYEKDGQLFCKKDYWARYGESCHGCSEHITKGLVMVGGELKYHPECFICLACGNFIGDGDTYTLVEHSKLYCGQCYYQTVVTPVIEQILPDSPGSHLPHTVTLVSIPASAHGKRGLSVSIDPPHGPPGCGTEHSHTVRVQGVDPGCMSPDVKNSIHIGDRILEINGTPIRNVPLDEIDLLIQETSRLLQLTLEHDPHDSLGHGPVSDPSPLASPVHTPSGQAGSSARQKPVLRSCSIDTSPGAGSLVSPASQRKDLGRSESLRVVCRPHRIFRPSDLIHGEVLGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSQYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENRNVVVADFGLARLMIDEKGQSEDLRSLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVRGFLDRYCPPNCPPSFFPITVRCCDLDPEKRPSFVKLEQWLETLRMHLAGHLPLGPQLEQLERGFWETYRRGESSLPAHPEVPD
Protein: E3 ubiquitin ligase rnf-5 (EC 2.3.2.27) (RING finger protein 5) (Q09463)
Organism: Caenorhabditis elegans
Function: E3 ubiquitin ligase that plays a role in the maintenance of muscle cell boundaries and muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix. Ubiquitinates the LIM domain protein unc-95, thereby regulating its dislocalization from muscle dense bodies and weakening the link between the muscle cells and the hypodermis. Regulation of unc-95 dissociation from muscle dense bodies by ubiquitination plays an important role in ecdysis during molting. Plays a role in the cessation of distal tip cell migration at the end of larval morphogenesis. Acts as a negative regulator of autophagy.
Subcellular location: Cell junction {ECO:0000269|PubMed:15210732}. Cell junction, focal adhesion {ECO:0000269|PubMed:15210732}. Cell membrane {ECO:0000269|PubMed:15210732}. Note=Colocalizes with deb-1/vinculin in muscle dense bodies. {ECO:0000269|PubMed:15210732}.
Interaction partners:
- E3 ubiquitin ligase rnf-121
- S5 DRBM domain-containing protein
- Derlin-1
- LIM domain-containing protein unc-95
- Derlin-2
- RING-type E3 ubiquitin transferase
- Erlin
- Nuclear speckle splicing regulatory protein 1 homolog
- Exportin-T
Sequence:
MASETKAPSEEPTSSSNKDESARFECNICLDAAKDAVVSLCGHLFCWPCLSQWLDTRPNNQVCPVCKSAIDGNKVVPIYGRGGDSSDPRKKVPPRPKGQRSEPPPQSFAGFNWGGDGGMMGGGGPNVHFSFGIGTVNGLFPLMFMLPFIQGIFPLSFVASFFGNGNQGAAAAGGGNGGGNDGNDGTHAHTHGHTHGPRGHGESAAPGSRMAQEEEYLSNIFKYIGFFMLFWLLFV
Protein: Checkpoint protein (Q9XTN5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKFRALMQDPLYMKEFQAIVATLTKLAKDCVMILGSRQMHFIVNEDQSSAASPLVWAGITAEEYFPEYRMEAAHPDQEYIVLGVSSANLGRALSVLRGGGVNSCKLKLQRIQFPCISVIASVLTSSSTEAREVVHDVPVTIIPGSDWSAYVVPRVPNSQLALGLPSLRLLKSLIDKLKNISPSLDFQVNVDGELNVIATSEMSTVTSRFQKLLIRTVSGSQQEASCSVDSRKASAFFGALQLPNEELTIGIDREHSIHLQIDVRQDVVLHSILPAVCM
Protein: 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily protein (F4IV21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 2-oxoglutarate
- At5g01740 family protein)
- Oil body-associated protein 2A
Sequence:
MEETKMSLLDDSFTSAMTLTNSGVPQVPDRYVLPPSQRPALGSSLGTSETTLPVIDLSLLHQPFLRSLAIHEISMACKEFGFFQVINHGIPSSVVNDALDAATQFFDLPVEEKMLLVSANVHEPVRYGTSLNHSTDRVHYWRDFIKHYSHPLSKWIDMWPSNPPCYKDKVGKYAEATHLLHKQLIEAISESLGLEKNYLQEEIEEGSQVMAVNCYPACPEPEMALGMPPHSDFSSLTILLQSSKGLQIMDCNKNWVCVPYIEGALIVQLGDQVEVMSNGIYKSVIHRVTVNKEVKRLSFASLHSLPLHKKISPAPKLVNPNNAPAYGEFSFNDFLNYISSNDFIQERFIDTIKKSSS
Protein: Sugar transporter ESL1 (Protein EARLY-RESPONSIVE TO DEHYDRATION 6-LIKE 1) (ERD six-like 1) (Sugar transporter ERD6-like 3) (Sugar transporter-like protein 2) (Q94KE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sugar transporter. Transports monosaccharides across the vacuolar membrane independently from a proton gradient. May function coordinately with the vacuolar invertase to regulate osmotic pressure by affecting the accumulation of sugar in the cells under abiotic stress conditions.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:19901034}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000269|PubMed:19901034}.
Interaction partners:
- Amino acid transporter AVT1E
- Sucrose transport protein SUC4
- Cyclin-dependent protein kinase inhibitor SMR10
- Bidirectional sugar transporter SWEET17
Sequence:
MTMSENSRNLEAGLLLRKNQNDINECRITAVVLFSTFVSVCGSFCFGCAAGYSSVAQTGIINDLGLSVAQYSMFGSIMTFGGMIGAIFSGKVADLMGRKGTMWFAQIFCIFGWVAVALAKDSMWLDIGRLSTGFAVGLLSYVIPVYIAEITPKHVRGAFVFANQLMQSCGLSLFYVIGNFVHWRNLALIGLIPCALQVVTLFFIPESPRLLGKWGHEKECRASLQSLRGDDADISEEANTIKETMILFDEGPKSRVMDLFQRRYAPSVVIGVGLMLLQQLSGSSGLMYYVGSVFDKGGFPSSIGSMILAVIMIPKALLGLILVEKMGRRPLLLASTGGMCFFSLLLSFSFCFRSYGMLDELTPIFTCIGVVGFISSFAVGMGGLPWIIMSEIFPMNVKVSAGTLVTLANWSFGWIVAFAYNFMLEWNASGTFLIFFTICGAGIVFIYAMVPETKGRTLEDIQASLTDFLQ
Protein: Chaperone protein DnaJ (P95830)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01152}.
Interaction partners:
Sequence:
MNNTEFYDRLGVSKNASADEIKKAYRKLSKKYHPDINKEPGAEDKYKEVQEAYETLSDDQKRAAYDQYGAAGANGGFGGAGGFGGFNGAGGFGGFEDIFSSFFGGGGSSRNPNAPRQGDDLQYRVNLTFEEAIFGTEKEVKYHREAGCRTCNGSGAKPGTSPVTCGRCHGAGVINVDTQTPLGMMRRQVTCDVCHGRGKEIKYPCTTCHGTGHEKQAHSVHVKIPAGVETGQQIRLAGQGEAGFNGGPYGDLYVVVSVEASDKFEREGTTIFYNLNLNFVQAALGDTVDIPTVHGDVELVIPEGTQTGKKFRLRSKGAPSLRGGAVGDQYVTVNVVTPTGLNDRQKVALKEFAAAGDLKVNPKKKGFFDHIKDAFDGE
Protein: Excitatory amino acid transporter 4 (High-affinity neuronal glutamate transporter) (Sodium-dependent glutamate/aspartate transporter) (Solute carrier family 1 member 6) (O35544)
Organism: Mus musculus (Mouse)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:9379843}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Excitatory amino acid transporter 3
- Histone acetyltransferase KAT5
- Nuclear receptor ROR-alpha
Sequence:
MSSHGNSLFLRESGAGGGCLQGLQDSLQQRALRTRLRLQTMTREHVRRFLRRNAFILLTVSAVIIGVSLAFALRPYQLSYRQIKYFSFPGELLMRMLQMLVLPLIVSSLVTGMASLDNKATGRMGMRAAVYYMVTTVIAVFIGILMVTIIHPGKGSKEGLHREGRIETVPTADAFMDLVRNMFPPNLVEACFKQFKTQYSTRVVTRTIVRTDNGSELGASMSPTSSVENETSILENVTRALGTLQEVISFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIAGKILEMEDMAVLGGQLGMYTLTVIVGLFLHAGGVLPLIYFLVTHRNPFPFIGGMLQALITAMGTSSSSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQEKGASRGRGGNESVM
Protein: GTP-binding protein Rheb homolog (EC 3.6.5.-) (Q9VND8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds GTP and exhibits intrinsic GTPase activity (By similarity). Activates the protein kinase activity of TORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K through activation of TORC1 signaling. May also have a role in activating TORC2 signaling.
Subcellular location: Endomembrane system {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15382}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}.
Interaction partners:
- LD23779p
- Raptor, isoform B
- Gigas, isoform A
- Serine/threonine-protein kinase mTor
- Protein LST8 homolog
- TBC1 domain family member 7
- BNIP3, isoform A
- Ribosomal protein S6 kinase
- GH04846p
- GH16429p
Sequence:
MPTKERHIAMMGYRSVGKSSLCIQFVEGQFVDSYDPTIENTFTKIERVKSQDYIVKLIDTAGQDEYSIFPVQYSMDYHGYVLVYSITSQKSFEVVKIIYEKLLDVMGKKYVPVVLVGNKIDLHQERTVSTEEGKKLAESWRAAFLETSAKQNESVGDIFHQLLILIENENGNPQEKSGCLVS
Protein: UDP-Glycosyltransferase superfamily protein (F4J962)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Acyl-CoA N-acyltransferase with RING/FYVE/PHD-type zinc finger domain-containing protein
- Rop guanine nucleotide exchange factor 2
- Glucan endo-1,3-beta-glucosidase 6
- Alpha/beta-Hydrolases superfamily protein
- Glucan endo-1,3-beta-glucosidase 10
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- Glycosyltransferase)
- Kanadaptin-like protein
- Putative F-box protein At1g32420
- Putative F-box/kelch-repeat protein At1g32430
Sequence:
MEKKMEAKRRIVLVPIPAQGHVTPLMQLGKVLNSKGFSITVVEGHFNQVSSSSQHFPGFQFVTIKESLPESEFEKLGGIESMITLNKTSEASFKDCISQLLLQQGNDIACIIYDEYMYFCGAAAKEFSIPSVIFSTQSAANYVSHPDMQDKVVENLYPLRYKDLPTSGMGPLDRFFELCREVANKRTASAVIINTVSCLESSSLSWLEQKVGISVYPLGPLHMTDSSPSSLLEEDRSCIEWLNKQKPKSVIYISIGTLGQMETKEVLEMSWGLCNSNQPFLWVIRAGSILGTNGIESLPEDVNKMVSERGYIVKRAPQIEVLGHPAVGGFWSHCGWNSILESIGEGVPMICKPFHGEQKLNAMYLECVWKIGIQVEGDLERGAVERAVKRLTVFEEGEEMRKRAVTLKEELRASVRGGGSLHNSLKEFEHFMMTL
Protein: ATP-sensitive inward rectifier potassium channel 1a.1 (Novel protein (Zgc:63534)) (Potassium channel ROMK2) (Potassium inwardly-rectifying channel, subfamily J, member 1) (Q7SY43)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
Sequence:
MTRSLREWFKEYMSERRGRKNRLVTKDGRCNIEFGNVMHRNRFAYVLDFWTTFVETRWRFILLYFVASFTLSWFIFGLIWYWLARNNGDLLWQNPPPGHKPCAFSVNDMTYAFLFSLETQSTIGFGNIYVTDQCPGGVALIVIQTIIGLFINIFWCGIVMTKISLPKKRAKTITFSESAVICPKKGTLCLQIRVANLRKTLMIGSQIYGKLLRTTVTGGETVILDQVSIDFMVDAGKDNLFFVCPLTLYHIIDKSSPFFNMAVDTMHQQDFELVVFLDGMAESTSSACQVRTSYIPQEIMWGYDFLPIISRSKEGRYRVDFSNFAKVVPVPTAHCSHCYHNEPGNHLHLKGIDNKGFEVIDIEPPNGTKM
Protein: Sirohydrochlorin cobaltochelatase (EC 4.99.1.3) (CbiXS) (O29537)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Interaction partners:
- Cobalamin biosynthesis precorrin-2 methyltransferase
- precorrin-2 dehydrogenase
- Cobalamin biosynthesis protein CbiHC
- Cobalamin biosynthesis precorrin-6Y methylase
- Cobalamin biosynthesis precorrin-3 methylase
- Glutamyl-tRNA reductase
- Cobalamin biosynthesis precorrin methylase
- Cobalt-precorrin-5B C
- Cobalt transport protein CbiN
- Putative cobalt transport protein CbiM
Sequence:
MRRGLVIVGHGSQLNHYREVMELHRKRIEESGAFDEVKIAFAARKRRPMPDEAIREMNCDIIYVVPLFISYGLHVTEDLPDLLGFPRGRGIKEGEFEGKKVVICEPIGEDYFVTYAILNSVFRIGRDGKGEE
Protein: Mitochondrial zinc maintenance protein 1, mitochondrial (Altered inheritance of mitochondria protein 8) (Found in mitochondrial proteome protein 36) (Q03429)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:20404342, ECO:0000269|PubMed:21807901}.
Interaction partners:
- Succinate dehydrogenase assembly factor 3, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Succinate dehydrogenase assembly factor 1, mitochondrial
- ATP synthase assembly factor FMC1, mitochondrial
- Mitochondrial chaperone BCS1
- Protein ISD11
- Protein CBP3
- mRNA-binding protein PUF3
- Assembly factor CBP4
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
Sequence:
MSTRTKALNAYRHGLRATRIAFRNDAEVLLAARAKMRSGMLCPPDPKLTTEDQIQHLEDVAVFLRRNLVQGKKVDGSSTKEPRYHLNIHKDTELGDNETIADPTARVKTNLKARPFKCSDKKQ
Protein: Ced-12 (FI01538p) (Q9VKB2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Myoblast city, isoform B
- Adapter molecule Crk
- PTB domain-containing adapter protein ced-6
- Sponge, isoform E
- Protein draper
- AT17867p
- Ras-related protein Rac1
- LD47387p
- Ras-like GTP-binding protein Rho1
- Cdc42 homolog
Sequence:
MIPKKTTVKDSHIVKIAVEREDHIAQLINLDQRHPLASKIQEICNGWSISDHQNYALQFYEPTNRKYVTEKNRNEIKNGSVLQLQYSPSKTACDAMEVLLNGSPQEKALRLKELTSLSTDHTFALEFIKEKGLDTLIKMIEDGGQTNEDILKYSLASFVELMEHGTVSWEVPENSFVARNIEIVRNFQKYPTNCGESALSNLENIVMCSNKHVLVAEDIKLQDILRLLQDVNSPVMRQNAIALLNALFVKADEGRRRTIAQTISAKQFRLALIGNGLGTEMTHQLYVLQTLTLGLLEKRMRMKMNAQDQDAHEKIKELRRIAFDDNTNALNQNDDHIRRGGGSGAGNVNFSQYYKKLGFKCDINPAQDFIETPPGILALDCMVYFARNYTQQYAKIVRENSCRADEHECPFGRTSIELVKVLCDILRIGEPPAEQSGDFQPMFFTHDSPFEEFFCICVITLNRTWKDMRATAEDFSTTFSVVREQIQRTLKGRPENLDDFRNKIALLTYQQITTLRQQERTSKEECDSTASAIVKLKEKISPQILELIKQQRLSFLVEGTHFAKYLRGTRTKDKFWYARLSPNHKVIHYGDCDEKTIPTMEELPKKLPISEIKQLLEGKECPHMKETRIRKSAVNLAFSITFENMEHSTLDFVAPDESIFNYWTDGINALLGQPMVSKQKNEDFDTLLSMEIKLRLLDTEGVDISKDPPPIPEDPENYDFCFES
Protein: Histone acetyltransferase (EC 2.3.1.48) (A0A3B3ITI3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU361211}.
Interaction partners:
Sequence:
XFRDIQEQALQTCAVVVMCKQLYWNWISTFTSGIRLEEQRAADGKTLKQQTVPQQKVGVTGPPDPQVRCPSVIEFGKYEIHTWYSSPYPQEYSRLPKLYLCEFCLKYMKSRTILQQHMKKCGWFHPPANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTQNDVKGCHLVGYFSKEKHCQQKYNVSCIMILPQYQRKGYGRFLIDFSYLLSKREGQAGSPEKPLSDLGRLSYMAYWKSVILECLYHQNDKQISIKKLSKLTGICPQDITSTLHHLRMLDFRSDQFVIIRREKLIQDHMAKLQLNLRPVDVDPECLRWTPVIVSNSVVSEEEEEEAEEGENEEPQCQERELEISVGKSVSHENKEQDSYSVESEKKPEVMAPVSSTRLSKQVLPHDSLPANSQPSRRGRWGRKNRKTQERFGDKDSKLLLEETSSAPQEQYGECGEKSEATQEQYTESEEQLVASEEQPSQDGKPDLPKRRLSEGVEPWRGQLKKSPEALKCRLTEGSERLPRRYSEGDRAVLRGFSESSEEEEEPESPRSSSPPILTKPTLKRKKPFLHRRRRVRKRKHHNSSVVTETISETTEVLDEPFEDSDSERPMPRLEPTFEIDEEEEEEDENELFPREYFRRLSSQDVLRCQSSSKRKSKDEEEDEESDDADDTPILKPVSLLRKRDVKNSPLEPDTSTPLKKKKGWPKGKSRKPIHWKKRPGRKPGFKLSREIMPVSTQACVIEPIVSIPKAGRKPKIQESEETVEPKEDMPLPEERKEEEEMQAEAEEAEEGEEEDAASSEVPAASPADSSNSPETETKEPEVEEEEEKPRVSEEQRQSEEEQQELEEPEPEEEEDAAAETAQNDDHDADDEDDGHLESTKKKELEEQPTREDVKEEPGVQESFLDANMQKSREKIKDKEETELDSEEEQPSHDTSVVSEQMAGSEDDHEEDSHTKEELIELKEEEEIPHSELDLETVQAVQSLTQEESSEHEGAYQDCEETLAACQTLQSYTQADEDPQMSMVEDCHASEHNSPISSVQSHPSQSVRSVSSPNVPALESGYTQISPEQGSLSAPSMQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNSSSQSSCSYGGLSSSSSLTQSSCVVTQQMASMGSSCSMMQQSSVQPAANCSIKSPQSCVVERPPSNQQQQPPPPPPQQPQPPPPQPQPAPQPPPPQQQPQQQPQPQPQQPPPPPPPQQQPPLSQCSMNNSFTPAPMIMEIPESGSTGNISIYERIPGDFGAGSYSQPSATFSLAKLQQLTNTIMDPHAMPYSHSPAVTSYATSVSLSNTGLAQLAPSHPLAGTPQAQATMTPPPNLASTTMNLTSPLLQCNMSATNIGIPHTQRLQGQMPVKGHISIRSKSAPLPSAAAHQQQLYGRSPSAVAMQAGPRALAVQRGMNMGVNLMPTPAYNVNSMNMNTLNAMNSYRMTQPMMNSSYHSNPAYMNQTAQYPMQMQMGMMGSQAYTQQPMQPNPHGNMMYTGPSHHSYMNAAGVPKQSLNGPYMRR
Protein: Membrane steroid-binding protein 1 (AtMP1) (Membrane-associated progesterone-binding protein 5) (AtMAPR5) (Q9XFM6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: MSBP1 can bind to multiple steroid compounds with different affinities. Negatively regulates cell elongation and brassinosteroid signaling. May act as a coreceptor with BAK1 and enhances its endocytosis.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Endosome membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- ATG8-interacting protein 1
- Cysteine/Histidine-rich C1 domain family protein
- Glutamyl-tRNA
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Nicastrin
- Rac-like GTP-binding protein ARAC8
- Bet1-like SNARE 1-2
Sequence:
MALELWQTLKEAIHAYTGLSPVVFFTALALAFAIYQVISGWFASPFDDVNRHQRARSLAQEEEPPIPQPVQVGEITEEELKQYDGSDPQKPLLMAIKHQIYDVTQSRMFYGPGGPYALFAGKDASRALAKMSFEEKDLTWDVSGLGPFELDALQDWEYKFMSKYAKVGTVKVAGSEPETASVSEPTENVEQDAHVTTTPGKTVVDKSDDAPAETVLKKEE
Protein: MAM and LDL-receptor class A domain-containing protein 1 (A2AJX4)
Organism: Mus musculus (Mouse)
Function: Enhances production and/or transport of FGF15 and thus has a role in regulation of bile acid synthesis.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23747249}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MFLPKAAVSAFSMHGSLCFLWTVCLSISPLSQQGVQAFQCSNGVSLPSDYVCDFTDHCGDNSEEQQCWSYGRCNFEDRLCSMTEDQTLQPGWTRRSGIISNSPPFWDHNGNISAHFLALVSRVDSISSNLRSRIFLPTNDQQVCQITFYNFSSNQNGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQSSQQFQVIFQAQMLATHGQEEVIAIDDISFSSGCLPADVCQTCGFDLDTCGLATEASAGRTSWMCTKVREIPSLDSVPWQDQRGHDEGSFVWMRAGHASVSRLVESSAYLNSSVCHCMDGNCRLQFNYTMENSILRVRLYNDKEEKKTWTFNTSTYSTWMKADVLIPEDLKAFKVVLEGTVLSQKSFIGIDQLLVYNFGQTHSQKLCSVNEYTPASRQCLTHSSVCDSGMDHSNGIDEDSEACASLLTWDFESGFCGWEPFPTEDSHWEVVRGLSNGEHLFLEAGHTVSRNQGSFIYFGPQKSTAVARLGSPILTKSLTTFTPCQVRFWYHLSEHSSLSVFTRTSVDGSLLKQSEVTQFSDSQWSQAKVDLHAKAEESTLPFQLVLEATILSSNATVAVDDISISHECEISYKSLRSTSIQNKVADCDFEANSCGWFEASGGDHFDWVWSSQSNLSADLEQQAPPRDHTHGTAQGHFMFILKTSNSLFQTAKLQSPTFSQTGPGCTMSFWFYNYGLSVGAAELQLHLENSRDTTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDDIHFENCALPPPVESCDEPDHFWCRQTKACIGRHQLCDLVDDCGDYTDETGCAPGLQCNFENGICNWEQSTKDDFNWTRYQGPTSTMNTGPMKDHTLGTAKGHYLYIETSGPQGFQDKAVLLSPILNATEAKVCTFRLYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSITSRKPFQILIMASVGDGFTGDIAIDDLSFMDCTLYPDNLPMDIPSPPETSVPVTLPPNNCTDDQFVCRSNGHCVGNIQKCDFRYDCIDKSDESSCVLEVCTFEERKLCKWYQPIPANSLHDSNTFRWGLGNGISIHHGEENHRPSVDHTKNTTDGWYLYADSSNGKFGDLADIVTPVISLMGPRCTLVFWTYMNGATVGSLQVLIKMGNTISKVWAQSGQQGPQWKKAEVFLGIHSHVEIVFRAKRGVSYIGDVAVDDVSFQNCSPLLSTNRKCTTDEFMCANKHCIEKDKLCDFVNDCADNSDETTFICGTSSGRCDFEFDLCTWEQDQDEDIDWNLKASNIPATSTEPAVDHTLGNSSGHYIILKSFFPQQPVKTGRISSPVISKRSKDCKIIFNYHMYGSGIAALLLLQVTVTNHTRVLLNLTKEQGNFWQRKELSLSSDEDFRVKFEGRVGEGIRGNIALDDIVLTKSCLPSHHSTREEPAFPLPTGFCPRGYEECQNGRCYSPEQRCNFVDDCGDNSDENECGGSCTFEKGWCGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNEHGHFMYLEATPVGLHGDKAHFKSATWQESSAACTMSFWYFISAKATGSIQILIKTDKGLWEVWQQSKPDPGNHWRRATILLGKLRNFEVIFQGIRTRDLGGGAAIDDIEFNNCTTVGETTDICSEETDFLCQDKKCIASHLVCDYKPDCSDTSDEAHCGYYTSTAGSCNFETTSGDWTVECGLTQDPEDDLDWSIGSIIPTEGLSRDSDHTPGSGRHFLYVNTSLAEEGSTARIITSHFFPASLGICTVRFWFYMVDPHIVGILKVYLIEKSGLNILMWSMMRNKNTGWTYAHVPLSSNSPFKVAFEADLGGKEDIFIALDDITFTPTCASGGPALPQPPLCEEGQFACIYALQCVSASEKCDGQEDCIDGSDEMNCSLGPSPQPCSDTEFQCFESQCIPSLLLCDGVADCQFNEDESSCVNQSCPSGALACNSSGLCIPAHQRCDGTAHCKDIQVDESSCSECPIHYCRNGGTCVIENIGPTCRCVQGWTGNRCHIRSNLSTEGSVHTQNYIWTLLGIGLGFLLTHIAVAILCSLGIRRRPMRKSEGVGNHSFINPVYRNCINQEKTQSSIYSFPNPFYGAASGSLETVSHHLKS
Protein: Transcriptional adapter (A0A0B4KFU2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR025024}.
Interaction partners:
Sequence:
MTTIADLFTKYNCTNCQDDIQGIRVHCAECENFDLCLQCFAAGAEIGAHQNNHSYQFMDTGTSILSVFRGKGAWTAREEIRLLDAIEQYGFGNWEDISKHIETKSAEDAKEEYVNKFVNGTIGRATWTPAQSQRPRLIDHTGDDDAGPLGTNALSTLPPLEINSDEAMQLGYMPNRDSFEREYDPTAEQLISNISLSSEDTEVDVMLKLAHVDIYTRRLRERARRKRMVRDYQLVSNFFRNRNYAQQQGLTKEQREFRDRFRVYAQFYTCNEYERLLGSLEREKELRIRQSELYRYRYNGLTKIAECTHFEQHAATATHRSTGPYGHGKTLHCIINAPNNERSNGSIRQCLTTGPHAYLQWKSSAAKLFLALPTTESQKGRNVKRRRGKFKFNRTKKHAPHRRPDLLRRIIAQQKLLG
Protein: Protein CutA, chloroplastic (Copper-binding protein CutA) (AtCUTA) (P93009)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in metal homeostasis. Specifically binds Cu(2+). The truncated isoform has less specificity in metal binding.
Subcellular location: Plastid, chloroplast intermembrane space {ECO:0000269|PubMed:12795705}.
Interaction partners:
- Polyadenylate-binding protein-interacting protein 11
- Polyadenylate-binding protein-interacting protein 13
- Heavy metal-associated isoprenylated plant protein 25
- Heavy metal-associated isoprenylated plant protein 21
- UTP:RNA uridylyltransferase 1
Sequence:
MASSLTTRLSAVIGSRRSFPIVGAFCVLSTLSISSLSSSSPFKSGCAQSFSVVPLLRSKFSSKAFSSSIRMEESSKTVPSIVVYVTVPNREAGKKLANSIVQEKLAACVNIVPGIESVYEWEGKVQSDSEELLIIKTRQSLLEPLTEHVNANHEYDVPEVIALPITGGSDKYLEWLKNSTRN
Protein: Nicotinamide nucleotide adenylyltransferase 3 (A0A8I5ZM75)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKNRIPVVLLACGSFNPITNMHLRLFEVARDHLHQTGKYQVIEGIISPVNDSYGKKDLVASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHGELLRSVAQMDGPDPSKIPSASADAW