wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor SOX-6 (A0A0G2JTZ2)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that plays a key role in several developmental processes, including neurogenesis, chondrocytes differentiation and cartilage formation (By similarity). Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis (By similarity). Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate SOX9's ability to transactivate. Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5, required to form and maintain a pool of highly proliferating chondroblasts between epiphyses and metaphyses, to form columnar chondroblasts, delay chondrocyte prehypertrophy but promote hypertrophy, and to delay terminal differentiation of chondrocytes on contact with ossification fronts (By similarity). Binds to the proximal promoter region of the myelin protein MPZ gene, and is thereby involved in the differentiation of oligodendroglia in the developing spinal tube (By similarity). Binds to the gene promoter of MBP and acts as a transcriptional repressor (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P40645, ECO:0000255|PROSITE-ProRule:PRU00267}. Cytoplasm {ECO:0000250|UniProtKB:P40645}.
Interaction partners:
- Transcription factor SOX-5
- Histone deacetylase 1
- Transcription factor SOX-9
- Catenin beta-1
- BCL11 transcription factor A
- Forkhead box J3
- Aggrecan core protein
Sequence:
MSSKQATSPFACTVDGEETMTQDLTSREKEEGSDQHPASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLCSLYSFRNTSTSPHKPDEGSREREIMNSVTFGTPERRKGSLADVVDTLKQKKLEEMTRTEQEDSSCMEKLLSKDWKEKMERLNTSELLGEIKGTPESLAEKERQLSTMITQLISLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARQQQQLLQQQHKINLLQQQIQVQGHMPPLMIPIFPHDQRTLAAAAAAQQGFLFPPGITYKPGDNYPVQFIPSTMAAAAASGLSPLQLQKGHVSHPQINPRLKGISDRLGRNLDPYEHGGGHSYNHKQIEQLYAAQLASMQVSPGAKMPSTPQPPNSAGAVSPTGIKNEKRGTSPVTQVKDETTAQPLNLSSRPKTAEPVKSPTSPTQSLFPASKTSPVNLPNKSSIPSPIGGSLGRGSSLDILSSLNSPALFGDQDTVMKAIQEARKMREQIQREQQQQPHGVDGKLSSMNSMGLSNCRNEKERTRFENLGPQLTGKSSEDGKLGPGVIDLTRPEDAEGSKAMNGSAAKLQQYYCWPTGGATVAEARVYRDARGRASSEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKSMSNQEKQPYYEEQARLSKIHLEKYPNYKYKPRPKRTCIVDGKKLRIGEYKQLMRSRRQEMRQFFTVGQQPQIPITTGTGVVYPGAITMATTTPSPQMTSDCSSTSASPEPSLPVIQSTYGMKMDGASLAGNDMINGEDEMEAYDDYEDDPKSDYSSENEAPEPVSAN
Protein: Transmembrane anterior posterior transformation protein 1 homolog (A2BIE7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in primary cilia formation. Involved in cartilage and bone development. May play a role in the differentiation of cranial neural crest cells. May act as a downstream effector of hoxc8 during development (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6NXT6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6NXT6}. Membrane {ECO:0000250|UniProtKB:Q6NXT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6NXT6}.
Interaction partners:
- Zinc finger SWIM domain-containing protein 7
- Major facilitator superfamily domain-containing protein 6-like
- GPN-loop GTPase 2
Sequence:
MADSVAAGLGDENETENEDKEREKRLFSGVKKMEKQAAASDVTETLGFYERKAKCKDRKTNVSDLSLVRFISAELTRGYFLEHNEAKYTERRERVYTCLRIPKELEKLMIFGYFLCLDVFLYVFTLLPLRVLLALVRLLTLPCCGLSGSRILQPAQVCDVLKGFIMVLCYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYTLLLIVCLRNMEQFSWNPDHLWVLFPDVCMVIASEIAVDVVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDYSDSVSRRMGFIPLPLALLLIRVVTSSVKIQGSLSIVCVLLFYLGMITLKVLNSIVLLGKSCMYVKEANMEEKLFQNPPSAAPSRVSSRAHRTKHTREPPGDPAEEGMSASVTTQPTQQDECPAPQIPTSESDQFLTTPDESEEKSLIQDDSELKHRAPKKDLLEIDRFTICGNRID
Protein: A-kinase anchor protein 10, mitochondrial (AKAP-10) (Dual specificity A kinase-anchoring protein 2) (D-AKAP-2) (Protein kinase A-anchoring protein 10) (PRKA10) (O43572)
Organism: Homo sapiens (Human)
Function: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11248059}. Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but also membrane associated and cytoplasmic.
Interaction partners:
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- Na
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase type II-beta regulatory subunit
- Ras-related protein Rab-4A
- Ras-related protein Rab-11A
- A-kinase anchor protein 1, mitochondrial
Sequence:
MRGAGPSPRQSPRTLRPDPGPAMSFFRRKVKGKEQEKTSDVKSIKASISVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLHDTIVLPYFIQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKKHETTASFLTDSLDKRLEDSGSAQLFMTHSEGIDLNNRTNSTQNHLLLSQECDSAHSLRLEMARAGTHQVSMETQESSSTLTVASRNSPASPLKELSGKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIARICGEDGQVDPNCFVLAQSIVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLTAPGSVGPPDESHPGSSDSSASQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMTFGRVSDLGQFIRESEPEPDVRKSKGSMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDIMQQAQYDQPLEKSTKL
Protein: SET domain-containing protein (Q55FF7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone H4
- DNA-directed RNA polymerase II subunit rpb3
- Histone H2B.v3
- DNA-directed RNA polymerase II subunit rpb2
- Probable E3 ubiquitin-protein ligase bre1
- Histone H3.3 type b
- Histone-lysine N-methyltransferase set1
- Histone H3.3 type c
- Histone H3.3 type a
- Histone H2A.z
Sequence:
MNKKVFLNNYLNERKQLNGNEINNNNNNNNNNNYNNNNNNNNLNKDKDKDKDKERDKDRERIKERTKERGDKERDRDKERDRERKKEKVEKPQVAVLKQSAQHVKQQRLKEKEKGKEKEKDKEKDKEKDKEREREKEKEKEKVKDREKEKEKEKEKEKEKVKDREKVKDREKEKEKEKERDKLKPKDSKIKERDIEKEKVRDREKEREKIRDREKDKNSNNNIIKPKEKKDESIAKTQKNITIKENGNITSSSSISNSSSINNNNNNKIINKSVSTNGNGNSSNSTNNNNSNGSNGVDIKKKPILDSKKRALPSSSSKSQTTSTSTSTSTSKLSKPIVKKKKDSNLKRIKLSNGGVVTKYKRKKSNNDSGSDDSSYDSSDDSSGNDSSSSGSSSSSGSDDSDNSSDDDSDSSDGDSSSDNDDDNDKNSSGSDDDEDGDSSSFDSNYSGSYDSFSDSSECDDSDCSCGKKRKNKPDSSNSKLTNLKKPITNGNTTDNLDNGLTTSSIVVDDQQKITNEYIEKHLNSGKANPDYSDIAVLIQKSRNKKFGFISRNFFIERTEKILYEIDDIDICNCSKSSGSVCGDDCLNRESYVECNIEHCELGKKCTNQRFQRKQYSNIKPAFTGKKGWGLIANEDIEEKQFIMEYCGEVISKQTCLRRMKEAENEKFFYFLTLDSKECLDASKRGNLARFMNHSCDPNCETQKWTVGGEVKIGIFAIKPIPKGTELTFDYNYERFGAQKQECYCGSVNCRGYLGQKSKSSTSTTRPKQITRWKNSIVLNHNHHVKYFLGEPIIPHSNPSSSSSSRSVSTLYNSELSPEMELQLINSKRIFLHRNVRKLKSFYFNVFNYYSSGGGSGGNNKKLINITSTSTSNSSLNSSLNSNIKLKRKNKISDIFNI
Protein: Oleosin H1 (Allergen Ses i 4) (Oleosin 17 kDa) (allergen Ses i 4.0101) (Q9FUJ9)
Organism: Sesamum indicum (Oriental sesame) (Sesamum orientale)
Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Subcellular location: Lipid droplet {ECO:0000255|RuleBase:RU000540, ECO:0000269|PubMed:12450125, ECO:0000269|PubMed:16436145}. Membrane {ECO:0000255|RuleBase:RU000540}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU000540}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}.
Interaction partners:
Sequence:
MADRDRPHPHQIQVHPQHPHRYEGGVKSLLPQKGPSTTQILAIITLLPISGTLLCLAGITLVGTLIGLAVATPVFVIFSPVLVPAAILIAGAVTAFLTSGAFGLTGLSSLSWVLNSFRRATGQGPLEYAKRGVQEGTLYVGEKTKQAGEAIKSTAKEGGREGTART
Protein: Sidestep, isoform B (B7Z0R1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MQLLLPTSGMPTNTLETETPAMQTTYWPRQTGNSKSKSNTNCKCNINTHRKSRTRCPDNGKTIWAVGFTLVLLTCLQQLKSVSADEESQDFQKNIPARLVWAALGKTVELPCDLTPPTSQDSVKLLLWFKDTTGIPLYSLDSRGGNVKLAPHAAIASDLGQRLFFSIGDNPKDSRLQINDVKPEDGGVYRCRVDFFNSPTRNFRHNLTLVVPPEEPRIFDAQGKEISQMAGPFREGYELFLCCQVRGGRPPPKVTWWRDDTELIGTSHTSVEEGATVMVNQLLIGTTTRDFYGIRIECRAQGTRLVDPVRKDVTVQVYLKPVRVKIATPNELLTAGQPMPIRCESWGSYPAAKITWLLDGEPIRNAEVTVHSDKEDGNITTSILTLKVTSENDNAELTCRATNPWFSGGAIEDKRIIRVAYPPTVSVHLANEDPSRLVTRAEGQNVTFKCRADARPPVTSYSWFKNGMRMSGESTEIMHLTQLERESAGAYACGATNTEGETRSSSLTLKVQFSPRCKSGTEQTSIGAVSLHSILVKCEVDADPPDSVRFSWTYNNTRNVSPVLNSRIQSNGLASTVTYLPQTDSELITLACWASNAVGRQTTPCLVHILPANTPEAPKACELRNDTVLEVVCVAGSDGGLSQYFMLEVVGGDPLYSGDPGGSAGQGRGQFSEAIGLGDNEISTLNDQATSAPIFRMQENSPQFRLNNLEPGREYQFLVYAVNAKGRSEPPVVIENVRVAAQLGPYDESILSEDPTPAETTHHGGGGVGGSGSSSGLGTGASTGSGPEKQSTLLILAAVVVIGAVVVTSIIVAGIVVVCRHRPRPPEPQEVRKSMRPARNDVPSMYIEEDELNELEEGGGRAADIRARVAPPNSHLCGGGGMPMPGGVGSSGGAIVGVAGPHHYISESFIQYAQPSLNGTIPKSILNKL
Protein: 26S proteasome regulatory subunit rpn11 (Protein pad1) (P41878)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit rpn502
- 26S proteasome regulatory subunit rpn7
- Probable proteasome subunit alpha type-3
- 26S proteasome regulatory subunit rpn10
- 26S proteasome regulatory subunit 6B homolog
- Probable proteasome subunit alpha type-5
- 26S proteasome regulatory subunit rpn12
- Probable 26S proteasome regulatory subunit rpn6
- 26S proteasome regulatory subunit rpn1
Sequence:
MESLQRLLQGARMGTGMMGDQPLVDNSECVYISSLALLKMLRHGRHGTPMEVMGLMLGEFVDDFTVRVVDVFAMPQSGTGVSVEAVDPVFQKNMMDMLKQTGRPEMVVGWYHSHPGFGCWLSSVDINTQQSFEQLTPRAVAVVVDPIQSVKGKVVIDAFRLINPSTLMMGQEPRQTTSNLGHINKPSIQALIHGLGRHYYSLRINYKKTELEEIMLLNLHKQPWAHGLLLENFNSAAEKNHASIDKMKSLSEQYTERVQNEVTLSPEQLRIQYVGKQDPKKHLDAEVQKCIDNNISSMLACMLDSVAF
Protein: Guanine nucleotide-binding protein G(o) subunit alpha (EC 3.6.5.-) (P59215)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P18872}. Membrane {ECO:0000250|UniProtKB:P09471}; Lipid-anchor {ECO:0000250|UniProtKB:P09471}.
Interaction partners:
- D
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 16
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein subunit gamma
- Gamma-aminobutyric acid type B receptor subunit 1
Sequence:
MGCTLSAEERAALERSKAIEKNLKEDGISAAKDVKLLLLGAGESGKSTIVKQMKIIHEDGFSGEDVKQYKPVVYSNTIQSLAAIVRAMDTLGVEYGDKERKADSKMVCDVVSRMEDTEPFSAELLSAMMRLWGDSGIQECFNRSREYQLNDSAKYYLDSLDRIGAADYQPTEQDILRTRVKTTGIVETHFTFKNLHFRLFDVGGQRSERKKWIHCFEDVTAIIFCVALSGYDQVLHEDETTNRMHESLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYEDAAAYIQTQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY
Protein: Geranylgeranyl pyrophosphate synthase 10, mitochondrial (GGPP synthase 10) (GGPS10) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 10) (Dimethylallyltranstransferase 10) (EC 2.5.1.1) (Farnesyl diphosphate synthase 10) (Farnesyltranstransferase 10) (EC 2.5.1.29) (Geranyltranstransferase 10) (EC 2.5.1.10) (Q9LJY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Dehydrodolichyl diphosphate synthase 2
- Phytoene synthase 1, chloroplastic
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Isopentenyl phosphate kinase
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Ent-copalyl diphosphate synthase, chloroplastic
- Farnesyl pyrophosphate synthase 2
Sequence:
MENREVFVYIVISIFRSLQFLFWRFRPRYNDVTSALTRPLTSAASYDFKFMSYMVNKAKSVNKALEEAVPLREPELKIREAMRYTLLSDGKRVRPMLCLAACELVGGQESTAMSAACAIEMLHASSLILDDLPCMDNDSLRRGKPTNHIVFGESIAILASQALIALAVQKTTSSTFADVPPERILKTVQEMVKAVEGLVAGQQADLAGEGMRFDSDTGLEHLEFIHIHKTAALLEAAAVMGAIMGGGSDEEIERLRSYARCIGLMFQVVDDVLDVTKSSEELGKTAGKDLIAGKLTYPRLMGVEKSKEYAERLNIEAREHLLGFDIDKVAPLVSLADYIVNRQN
Protein: Two pore channel protein 2 (Two pore calcium channel protein 2) (Voltage-dependent calcium channel protein TPC2) (A0JMD4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Intracellular channel initially characterized as a non-selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid adenine dinucleotide phosphate), it is also a highly-selective Na(+) channel activated directly by PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate). Localizes to the lysosomal and late endosome membranes where it regulates organellar membrane excitability, membrane trafficking, and pH homeostasis.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q8NHX9}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8NHX9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein.
- Voltage-dependent calcium channel protein TPC1
- Cation/H+ exchanger protein 2
- Sodium/potassium/calcium exchanger 5
- Oculocutaneous albinism II.
- Solute carrier family 45 member 2.
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Glutamine-dependent NAD
- Sodium/potassium/calcium exchanger 4
Sequence:
MEEEPLLAGSINQGSGDYGAHSESCLHYPDEHTPRSRRLSYSVTDDSCNVEEDADADLYVQQAVVFIEDAIKYRSINHRVDSGSLRLYRWYYSNLCQWGLGLTIAVVLALAFIERPSSLTYTSDIRVKPKPWEPPCGMTEGIEIVCLCIFILDVTAKGYLIGWEEFRMNKWLLAYLIVITASVIDWMLSISMLCDENLRVRRLIRPFFLLQNSSLMKKTLKCIKRTLPEIASVILLLALHICLFTMIGMLIFAKSDDPKQNGEWQTYFRNLPKALSSLLVLLTTANNPDVMIPAYSLNRGYSIFFILFSVFGTYLLMNLMTAIIYNQFRGYLLMSVQTSIIRRRLGIRAAFEVLCCPGRGHTSTQAEGHVERVAVSMFLKVMERVHMKSYCRQAIVKAARRFPDGFISGEDFQRLFNELDKDFVKEHPPKPEYSSSGLQHIQYVYSHYYISVLGNAVALANVICICTVLVLNAEKSASEKNYFYMEIINCIFILYYLIEMLLKIVAFGWKGYLSYRNNIFDGFLTVLLLAIQIVIFITFKIPYVDVDPVPRHVMALWEMIRLVNMLIVFRFLRIIPEIKLMAVVASTIVDLVKNLRAFAGILLVVYYMFAVLGIWLFQGAISPPSNMSLVSNSSLENITGPYSMECGTFEQLEYWPNNFDDFASSLILLYNIMVVNNWHVFTDAYARYTTDWSLVYFVVWWLTSSVMWVNLFVALILENFTYKWDRSNGLSVEDVERIAYQSTVQLMFKEHVKEPTEEELLAQLHQHPHLHLSW
Protein: Neuroendocrine protein 7B2 (Q9XTY3)
Organism: Caenorhabditis elegans
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Neuroendocrine convertase 2
- Carboxypeptidase E
Sequence:
MIGAVSLVFFTVGVAAIYGLDLENAGDFVLPSGDFIDLISRDSENLPDLSSFGVKHISGGAGEGEQKLLEEDNFQERQEVKVDNVLPAYCEPPNPCPVGFTKEHGCLEEFENSAEFSRNYQADQHCICDQEHMFNCAEKEAQDVSESLQKILEENNMHANTIAKKFHDKRSSDEYVPRRKRSIPSSAHKVNPYLQGEPLRSMQKKNGKHSW
Protein: Ankyrin repeat-containing protein (Q54WI0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Paxillin-B
- Phospholipase D B
- LMBR1 domain-containing protein 2 homolog B
- SAP DNA-binding domain-containing protein
- LIM domain-containing protein D
- Calponin-homology
- Uncharacterized protein
- LIM domain-containing protein C
- Calcium-regulated actin-bundling protein
Sequence:
MSGQQPTTEMLESTPKNEQSTVVIPSNLTLTTTTITGNTITNTTTTQPTPQQHTGIKVIAPSTMNLNTATTQQHQQQQQITPTSSNSAVPISSSNNNNNITATSSTSTTPLTGSVNTAVSSSSSPNTPSSPSVSRQQPTPTPTPTTTTTTTTTAAATTTGSTTATSTTTPSLSASITLPPNSLTSGNNITSTSHIEYQNAMENKKTLKKIIKSSKHWSESVKAYCTTASQFSEELLKHSEQLSPSPKKETHLNVALLSFGHTLKSVNSINDQMLNEVQDVFYTPLNNFVDYDFAEVVESNKRVTKAKDDYDQSLGKISASIKKSKQGIDEGRLFLYEQELEKLKEQYEGSNKDLEIKLAELEHKNETKYLKSLILFINSQYHFYNRASKLFANLKPKLDNIEKYLEEIQPPKVVEGHLMKKSKQVMGGWNKCWYVLKDGMLYCYKGKKEFHPENALNILLCSVRVPQVISTSSPMTQQPPTKEKDINLGSNQDFRFEILHPRKKQPIVLQAENEEERDRWVQAIQDAISNSLNCQSVGSGSSSVSSYQLGKSLSQSTTGAGGVNANIGGSGSGVGGGGGGQSIQADEVNQQVLRILQKVGGNTCCADCNQPDPDWASINLGIIICKVCSGVHRSLGTHISKVRSLTLDKWSPENILFMKEVGNTRFNLLFEHHVSPDVPKPSPQSDRMAKEQWIRAKYKNKEFIIKSTLSNEELSKTMQKNIHDGKKDVLTYLKLLAQGAEINYSGGDDGRSPLHQSIFKCDDVLIPELLLQNGADITLVDPRGWTSMHYAAFFNRPRCANLLMKRGFESVKTKYRDHLSRLAVDLASLNRSKETEKILRGEEIDTGLNMDNIENNTIPLFEPTVPLSIDFPVVNQEILSDDEEEDQNNNNEPEIQSWSENESSIGRSSFSDTNNPGSNVQQQQQEQQQEQQTSNTNQIQTINNNNNNNNNNNNNNNNNNNNNNNNVVPTLTTTHVLNSSNSINNLSNSLANNVNNSASNSSSSLVSLTNYSSTGNISNSWVTGSQPNSSNNLSLDDSGFEGGSESLAPPTAATTSDKKQKVEKDKDYKNTRPKSKRRPSILGKGKNTLRLMRNKWGKKESDSEDSESESEEAEVSKESPPHPPTSSSNTTLPPQQSLQATSDNVNNKSTSNLLSSSRDPNIKDSQSSSSSQQQHSPSLQSQQQQQSTHTSESPVLSSSKQSPDQTISHTQSSSSLINDDQSSQVGSEEKSPSKNSKEGSPTPFKMFLKKLKINKKKDGNGNTVSTAGEKRDPSVEDIAELNDIPDNISVGTNDDSLVSDDSSTSNNTANNKKPKKSKKSKPLENHSDANTNE
Protein: Myosin phosphatase Rho interacting protein (A0A494BZV2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAAKENPCRKFQANIFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEGRTGQKFSLCILTPEKEHFIRAETKEIVSGWLEMLMVYPRTNKQNQKKKRKVEPPTPQEPGPAKVAVTSSSSSSSSSSSIPSAEKVPTTKSTLWQEEMRTKDQPDGSSLSPAQSPSQSQPPAASSLREPGLESKEEESAMSSDRMDCGRKVRVESGYFSLEKTKQDLKAEEQQLPPPLSPPSPSTPNHRYSCPESPSQELGGPLPSPGPRLPHQMVCSISLSSLDVASQPPAYVDSGSTRGRGTERLGSAFAFKASRQYATLADVPKAIRISHREAFQVERRRLERRTRARSPGREEVARLFGNERRRSQVIEKFEALDIEKAEHMETNAVGPSPSSDTRQGRSEKRAFPRKRDFTNEAPPAPLPDASASPLSPHRRAKSLDRRSTEPSVTPDLLNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEIDLSACYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVHPTTAPDVTSSLPEEKNKSSCSFETCPRPTEKQEAELGEPDPEQKRSRARERRREGRSKTFDWAEFRPIQQALAQERVGGVGPADTHEPLRPEAEPGELERERARRREERRKRFGMLDATDGPGTEDAALRMEVDRSPGLPMSDLKTHNVHVEIEQRWHQVETTPLREEKQVPIAPVHLSSEDGGDRLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQTEVAASPSGAWQRLHRVNQDLQSELEAQCQRQELITHQIQTLKRSYGEAKDTIRHHEAEIRSLQARLSNAAAELAIKEQALAKLKGDLKREQGRVREQLEERQHSEAALSSQLRASEQKLKSAEALLLEKTQELRGLETQQALQRDRQKEVQRLQERIADLSQQLGASEQAQRLMEEKLQRNYELLLESCEKEKQALLQNLKEVEDKASAYEDQLQGQAQQVETLQKEKLSATFEGSEQVHQLEEQLEAREASVRRLAEHVQSLCDERDLLRQRFQELTERVATSDEDVAELREKLRRREADNQSLEHSYQRVSSQLQSMHTLLREKEEELERIKEAHEKVLEKKEQDLNEALVKMVALGSSLEETEIKLQAKEEILRKFASESPKDMEEPRSTPEETERDGTLLPGQPVQATRAPLGLPHTRLEDEDEDLGAPPGEEYGDGSPSREDSMVPPKSVEVLDREGHQQGTAKLDQGAPGVKRQRIRFSTIQCQRYIHPEGSEKTWTSSTSSDTSQDRSPSEESMSSEPAPSVLPATGDSDTYLSIIHSLETKLYVTEEKLKDVTVRLESQQGQSREALLALHHQWAGTEAQLREQLRASLLQVGALASQLEQERQERARRVEGHVGELGDFQVKNSQALMCLENCREQLRSLPRASQEDEQDARAASLASVESALVSAIQALQHWPAPAHGGARAQLETGGTEENGKPASLQQCSQSELTEQEQVRLLSDQIALEASLISQIADSLKNTTSDVSRMLHEISWSGQPPMESAGAPVDTWARKVLVDGEFWSQVESLRKHLGTLGGEAVGASGDGQQSIPQGLAPILANATWVRAELSFATQSVRESFHRRLQSIQETLRGTQTALRQHKCLLREILGAYQTPDFERVMQQVLEALRLPAGHEDGVQLSWDLSPLGEVLGRDSDSSQEPFDVSDQSPGAFVAIQEELAQQLKEKASLLEEIAAALPSLPPVESLRDCQKLLQVSQSLSYNTCLGGLGQYSSLLVQDAIIQAQVCYASCRIRLEYEKELQLCKESWQTREPSCSEQAQAARALREEYEELLRKQKSEYLDVIAIVERENAELKAKAAQLDHQQQCLEDAESKHSMSMFTLRGRYEEEIRCVVEQLTRTESTLQAERSRVLSQLDASVRDRQDMERHHGEQIQTLEDRFQLKVRELQTIHEEELRTLQEHYSQSLRCLQDTLCLHQGPHPKALPAPAPNWQATQGEADSMTGLRERIQELEAQMDVMREELGHKDLEGDAATLREKYQRDLESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSVNSDVEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGEATGSPLAQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPDSATVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSLKEGLTVQERLKLFESRDLKKD
Protein: DNA-binding protein RFX6 (Regulatory factor X 6) (Q5RJA1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor required to direct islet cell differentiation during endocrine pancreas development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8HWS3}.
Interaction partners:
- Paired box 4.
- Neurog3 protein
- Homeobox protein HB9
- Neurogenic differentiation factor 1
- ATP-binding cassette sub-family C member 8 isoform X1, member 8)
- Homeobox protein Nkx-2.2a
- NK6 homeobox 1.
Sequence:
MYVIHLAEADESNASISSEEDLGHLDYSKPFAAKQTQPKKSISQIIKDKKKQTQLTLQWLEDNYIVCEGVCLPRCILYAHYLDFCRKEKLDPACAATFGKTIRQKFPLLTTRRLGTRGHSKYHYYGIGIKESSAYYHSVYSGKGLTRFSGSKLKNEGGFTRKYSLSSKTGTLLPEFPSAQHLVLQDSVSKEKVDTLIMMYKTHCQCILDNAINVNFEEIQNFLLHFWQGMPEHLLPLLENPVIVDIFCVCDSILYKVLTDVLIPATMQDMPESLLADIRNFAKHWEHWMLSSLENLPEILSEKKVPIARRFVSSLKRQTSFLHLAQIARPALFDQIVVTSMVNDIDKVDLNSIGSQALLSVTNDQDSDFYSEYDSISVFQELKDLLRKNATVESFIEWLDSVVEQKVIKPSKQNGRSVKKRAQDFLLKWSFFGARVMHNLTLNNATSFGSFHLIRMLLDEYILLAIETQFNNDKEQDLQNLLEKYMRSADASKATFTASPSSCFLANRNKPGVSSSDSAVKDEIPPEDDYLTLAAAQQGLGAGTVVYHSADPDNFTIAGQMDFSQNSAPLMTPPISPAMMNRSSVINQGPMAMRPQTSCPIQGQLPCQTFPEPLYQSLHNPPSGSYPNASYYQPMFRTQTHTESGRYAFSGHHLSKDCFSNSCTASPYGTRGSSGGYTAAGDAGMETEAVQMLESSGFGFGGTTGAADGCSGPVCSSGHRYYGSSSGYVDAPRMGTFIDQHVSVISSVSSIRSVSAYAEAHDPLNILDDTSRKTRPYYTELSAMGTHTAGSSIAHSCSVSAPCMYGAPAPYHSQNTLLPLQGATEIREMMSSLPPINTVFMGSTSGPP
Protein: WASH complex subunit 4 (Strumpellin and WASH-interacting protein) (SWIP) (WASH complex subunit SWIP) (Q2M389)
Organism: Homo sapiens (Human)
Function: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting.
Subcellular location: Early endosome {ECO:0000269|PubMed:23676666}.
Interaction partners:
- WASH complex subunit 3
- WASH complex subunit 5
- WASH complex subunit 1
- WASH complex subunit 2C
- WASH complex subunit 2A
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit beta
- FK506-binding protein 15
- Vacuolar protein sorting-associated protein 35
- F-actin-capping protein subunit alpha-2
Sequence:
MAVETLSPDWEFDRVDDGSQKIHAEVQLKNYGKFLEEYTSQLRRIEDALDDSIGDVWDFNLDPIALKLLPYEQSSLLELIKTENKVLNKVITVYAALCCEIKKLKYEAETKFYNGLLFYGEGATDASMVEGDCQIQMGRFISFLQELSCFVTRCYEVVMNVVHQLAALYISNKIAPKIIETTGVHFQTMYEHLGELLTVLLTLDEIIDNHITLKDHWTMYKRLLKSVHHNPSKFGIQEEKLKPFEKFLLKLEGQLLDGMIFQACIEQQFDSLNGGVSVSKNSTFAEEFAHSIRSIFANVEAKLGEPSEIDQRDKYVGICGLFVLHFQIFRTIDKKFYKSLLDICKKVPAITLTANIIWFPDNFLIQKIPAAAKLLDRKSLQAIKIHRDTFLQQKAQSLTKDVQSYYVFVSSWMMKMESILSKEQRMDKFAEDLTNRCNVFIQGFLYAYSISTIIKTTMNLYMSMQKPMTKTSVKALCRLVELLKAIEHMFYRRSMVVADSVSHITQHLQHQALHSISVAKKRVISDKKYSEQRLDVLSALVLAENTLNGPSTKQRRLIVSLALSVGTQMKTFKDEELFPLQVVMKKLDLISELRERVQTQCDCCFLYWHRAVFPIYLDDVYENAVDAARLHYMFSALRDCVPAMMHARHLESYEILLDCYDKEIMEILNEHLLDKLCKEIEKDLRLSVHTHLKLDDRNPFKVGMKDLALFFSLNPIRFFNRFIDIRAYVTHYLDKTFYNLTTVALHDWATYSEMRNLATQRYGLVMTEAHLPSQTLEQGLDVLEIMRNIHIFVSRYLYNLNNQIFIERTSNNKHLNTINIRHIANSIRTHGTGIMNTTVNFTYQFLKKKFYIFSQFMYDEHIKSRLIKDIRFFREIKDQNDHKYPFDRAEKFNRGIRKLGVTPEGQSYLDQFRQLISQIGNAMGYVRMIRSGGLHCSSNAIRFVPDLEDIVNFEELVKEEGLAEETLKAARHLDSVLSDHTRNSAEGTEYFKMLVDVFAPEFRRPKNIHLRNFYIIVPPLTLNFVEHSISCKEKLNKKNKIGAAFTDDGFAMGVAYILKLLDQYREFDSLHWFQSVREKYLKEIRAVAKQQNVQSASQDEKLLQTMNLTQKRLDVYLQEFELLYFSLSSARIFFRADKTAAEENQEKKEKEEETKTSNGDLSDSTVSADPVVK
Protein: DnaJ heat shock protein family (Hsp40) member B2 (C9JRD2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASYYEILDVPRSASADDIKKAYRRKALQWHPDKNPDNKEFAEKKFKEVAEAYEVLSDKHKREIYDRYGREGLTGTGTGPSRAEAGSGGPGFTFTFRSPEEVFREFFGSGDPFAELFDDLGPFSELQNRGSRHSGPFFTFSSSFPGHSDFSSSSFSFSPGAGAFRSVSTSTTFVQGRRITTRRIMENGQERVEVEEDGQLKSVTINGVPDDLALGLELSRREQQPSVT