wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VJC2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Armadillo segment polarity protein
- Axin
- FI08533p
- Protein smoothened
- Transcriptional activator cubitus interruptus
- Kinesin-like protein costa
- V-type proton ATPase proteolipid subunit
- Mitochondrial 2-oxodicarboxylate carrier
- Dynein axonemal light chain 1
Sequence:
MAKQEATNGKVRNASLHLEKLLIGGKYRLVKPIGSGSFGDIYLGLSITDGSEVAIKVEKNDAKYPQLIYEAKVYEQLARCPGFPTLLHYGCEKNYNAMVMDLLGPSLEELFNLCKRRFSLKTVLMLTDQLLMRIECVHERGFIHRDIKPDNFLMGLDRHCNKLYLIDFGLSKRYKDIESEIHIPYRTDRNLTGTVRYASINAQIGVEQSRRDDMESMSYCLMYFNLGKLPWQGITAANKKQKYEKILEKKTSVTIAQLCKGFPSEFCLLMTYVRNLGFKEPPDHTYLRQIFRILFRSLNHHYDYIYDWTALQQQKDQICRSREQILESEREEVRKRDGERGCEPQRDKERHKDLELDRLHKTSTQQAKCSNGHLTNRYDRIGDGGISKRK
Protein: OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1 (OTU domain-containing protein 1) (EC 3.4.19.12) (Deubiquitinating enzyme OTU1) (Q8LG98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Cysteine protease with a preference for Met-1 and 'Lys-48' over 'Lys-63'-linked ubiquitin (UB) tetramers (e.g. Ub2, Ub3 and Ub4) as substrates.
Interaction partners:
- F5D14.24 protein
- Ubiquitin-ribosomal protein eL40z fusion protein
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin-ribosomal protein eS31y fusion protein
- Ubiquitin-ribosomal protein eS31z fusion protein
- Ubiquitin-ribosomal protein eS31x fusion protein
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 11
- T-complex protein 11
- Ubiquitin C-terminal hydrolase 22
- Ubiquitin-conjugating enzyme E2 36
Sequence:
MQNQIDMVKDEAEVAASISAIKGEEWGNCSSVEDQPSFQEEEAAKVPYVGDKEPLSSLAAEYQSGSPILLEKIKILDSQYIGIRRTRGDGNCFFRSFMFSYLEHILESQDRAEVDRIKVNVEKCRKTLQNLGYTDFTFEDFFALFLEQLDDILQGTEESISYDELVNRSRDQSVSDYIVMFFRFVTAGDIRTRADFFEPFITGLSNATVDQFCKSSVEPMGEESDHIHITALSDALGVAIRVVYLDRSSCDSGGVTVNHHDFVPVGITNEKDEEASAPFITLLYRPGHYDILYPKPSCKVSDNVGK
Protein: Somatostatin receptor subtype 4 (Q6YEY0)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
RYAKMKTATNIYLLNLAVADELFMLSVPFVASSAALRHWPFGSVLCRAVLSVDGLNMFTSVFCLTVLSVDRYVAVVHPLRAATYRRPSVAKLINLGVWLASLLVTLPIAIFADTRPARGGQAVACNLQWPHPAWSAVFVVYTFLLGFLLPVLAIGLCYLLIVGKMRAVALRAGWQQRRRSGKKITRLVLMVVVVFVLCWMPFYVVQLLNLFVTSLDATVNHVSLILSYANSCANPILYGFLSDNSRRSFQRVL
Protein: Coiled-coil domain-containing protein 43 (Q96MW1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAPSEVAAIAPGEGDGGGGGFGSWLDGRLEALGVDRAVYGAYILGILQEEEEEEKLDALQGILSAFLEEDSLLNICKEIVERWSETQNVVTKVKKEDEVQAIATLIEKQAQIVVKPRMVSEEEKQRKAALLAQYADVTDEEDEADEKDDSGATTMNIGSDKLLFRNTNVEDVLNARKLERDSLRDESQRKKEQDKLQRERDKLAKQERKEKEKKRTQRGERKR
Protein: Differentially expressed in FDCP 6 homolog (Q7SYB5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDLRSELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLKIPHEAAALEEHFRDDDDGPVSSQGYMPYLNKYILDKVVEGTFVKENVDELCWTLTAKKNYRPEGKSILPAKDAFRLWCLFIFLSEDRYPLVMIPDEVEYLLKKFCMAMSVELNYVELEDFISQDSVQQNGFTVWTFLEMMNSGKLTRGIAKETVSMAIEEVYREIVGDVLKEGYLWKKGQLRRNWTERWFTLRPSTLLYFTSEDRKDHKGNIQLDGNCCVEVLPDRDGKRCMFCLKTLTKTYELSASDTKQRQEWTTAIQTAIRLYVEGKTSLHKDLKLKRRDQREQREKRREAKEQELQRLRALQEERERKMAELELLKEAQRQAQAMLEQDEQRRRQQHEQLHQALEIQLKEAEEARASMQAEMALKEAEAEKQRTRIRELEAMQQRLEDALQQEIKARQDEEAFRYAQARLLAEEEEKMKALMGLREEQEEYIQRAQREKQELRQEMESKSRALEEAQRQLEETRANRYRVDQDVVAAQRKLRQASTNVKHWNVQMNRLMHPIGPGEKRSSGGSFSSFRIPSQKDPALRQKQKSEEQDEESKENMESRGGCEADRRLSTNGQMEIP
Protein: Nucleoside diphosphate kinase IV, chloroplastic/mitochondrial (NDK IV) (NDP kinase IV) (NDPK IV) (EC 2.7.4.6) (Nucleoside diphosphate kinase 4) (Q8LAH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Shows the highest specificity towards GDP (By similarity).
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}.
Interaction partners:
- Thymidylate kinase
- Inosine triphosphate pyrophosphatase
- At5g66005
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- UMP kinase
- Guanylate kinase 2
- Guanylate kinase 1
- Guanylate kinase 3, chloroplastic
- Probable UMP-CMP kinase 2
- Probable UMP-CMP kinase 1
Sequence:
MSSQICRSASRAARSLLSSAKNARFFSEGRAIGAASVVHATGKVPQYASNFGKSGSGFVSNSWITGLLALPAAAFMLQDQEALAAEMERTFIAIKPDGVQRGLISEIITRFERKGYKLVGIKVMVPSKGFAQKHYHDLKERPFFNGLCNFLSSGPVVAMVWEGEGVIRYGRKLIGATDPQKSEPGTIRGDLAVVVGRNIIHGSDGPETAKDEISLWFKPEELVSYTSNAEKWIYGQN
Protein: Ribosome-inactivating protein luffin P1 (EC 3.2.2.22) (Arginine/glutamate-rich polypeptide) (AGRP) [Cleaved into: Luffin P1a; Luffin P1b; Luffin P1c] (P56568)
Organism: Luffa aegyptiaca (Sponge gourd) (Luffa cylindrica)
Function: Inhibits protein synthesis in animal cells.
Interaction partners:
Sequence:
PRGSPRTEYEACRVRCQVAEHGVERQRRCQQVCEKRLREREGRREVD
Protein: Microtubule-associated protein RP/EB family member 1C (APC-binding protein EB1C) (End-binding protein 1C) (AtEB1C) (Protein ATEB1 homolog 1) (AtEB1H1) (Q9FGQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant-specific EB1 subtype that functions preferentially at early stages of plant mitosis by regulating spindle positioning and chromosome segregation. Accumulates in the prophase nucleus and is required to maintain spindle bipolarity during premetaphase and/or metaphase and for efficient segregation of chromosomes at anaphase. May play a role in the dynamics of microtubule network in elongating pollen tubes.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=During mitosis, accumulates in the prophase nucleus, and after the nuclear envelope disintegration is associated with whole spindle microtubules, plus end of microtubules, phragmoplast and finally is actively recruited to the nucleus. Localizes in the microtubule network in elongating pollen tubes.
Interaction partners:
- Mitotic spindle checkpoint protein MAD2
- Serine/threonine-protein kinase Aurora-2
- CLIP-associated protein
- Mitotic spindle checkpoint protein BUBR1
- Serine/threonine-protein kinase Aurora-1
- Mitotic checkpoint protein BUB3.2
- Kinesin-like protein KIN-14D
- Mitotic checkpoint protein BUB3.1
- 65-kDa microtubule-associated protein 3
- 65-kDa microtubule-associated protein 4
Sequence:
MATNIGMMDSAYFVGRSEILAWINSTLQLNLSKVEEACSGAVHCQLMDSVHPGTVPMHKVNFDAKSEYEMIQNYKVLQDVFNKLKITKHIEVSKLVKGRPLDNLEFMQWMKKYCDSVNGGQHNYHALERREASKGGKEATKRAAATQQSGKSSSSSAPPRPSSSNGTRKHEPQSNNTGTHHSSTGNHHHSSKPSAKQSKPVPAYDEKITELKLYIDSLEKERDFYFSKLRDVEILCQNPDTEHLPLVGSIKRILYAADGEDVGAAETQTLSPIAEGSEERRNSVTESQKRKLIVNLDVDVAAITTLSPRQRLSDASDVKCSGSSPLLTC
Protein: Stress-responsive DNAJB4-interacting membrane protein 1 (Q6ZPB5)
Organism: Homo sapiens (Human)
Function: Promotes neuronal cells survival to stress conditions.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MWPAPCSVGRLLIFFMCSSSGYVVQGCGPSPGARTTLGSPLSLWSIKTPSHIFCTRRAINLGFPSPPLVQLIFWSLNAGLDLYLCLISSCGFSQVFWPVEAFCSFSLSFFALALSHKFVICRLDQHIFSGFTKSLKNLPPCHRTDI
Protein: GH06923p (RALBP1 associated Eps domain containing, isoform A) (Q8MQS4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RalA-binding protein 1
- Dynamin associated protein 160, isoform D
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- AP-2 complex subunit alpha
- Adaptor protein complex 2, mu subunit, isoform A
- AP complex subunit sigma
- Protein cappuccino
- AP complex subunit beta
- Cyclin-G-associated kinase
- non-specific serine/threonine protein kinase
Sequence:
MDVSLTEPETRFYSELFQCCDVEKTGKVPMLKATELFRSADIANETVIEITGLAGIPSTALHISRTQFYSCLKLIAAHQAAMPLRQELILATFPLPLPHFSWKEAVTAPVAVENGLTALPPPPPTDRRNSLRRNSQQEQLQDTSDVPSTDSEVEQNESVDDATGHGRGTDGCGVVSSSSRENVGRRRGGGTGGGSPEAWSTNSDSPTPTNSVAERPWAQDTLWQGLLGDEHRQLLGTEEESSDRHSSDDDDNESELVTIYQITPEQREYYNKQFRTVQRDPHGLLSGQAARNFFEKSRIPVEELRHIWQLCDVTRDGALSLSEFTAAMHLVVLRRNNIPLPTSLPHCLHPNVLQAAASGSGQGVTSSSSAALPQEPPEADLLHLNDDDEDDHTDNTIIAGNLSGSSTTSKPRPNVPSDKNIMNLSSISTSSQASNSSKREATPQNSLGKNRSISNSPNVEKPVSGTVSSTASAVDSTNVSSQWTKFSESPTTSAVSVQSTTGAAPVVAAGAAASGASSPGLKPVLFDMKRSAQDVVSNPQILHPVPLRVTPIGTAIASSAESSNENESAVAQREDSPKAISSTTVNNQSSAVVPGISGVAGSSHRDSSDLRAIQRPQAKKLPAKNSALPPPPQREPSIGSTGPSESQEPQAAYVASSLASKKEPPPLPPPRPHRHARSSSLDLNKFKIGATGGAQQAEITAQASFDMQTSTGFADFTHFADEGAANVVDEQQLHSLPPAAPPPQAAVVPPTRITLQQAQQRVSAFEVYRKPQTPRGSQSPPQQPPPPAPAVGLTTQTGQLPSAESFEKRVTAISDSLRHVSFKQGQANTTEVLQRLREQNNSLLHLCNDLSDELLSVQTRKEEMRLKLEGLNASDSTGRTSSSICAPVTANVTGGSSGSAGAAYTNV
Protein: 25-hydroxyvitamin D3 24-hydroxylase (O73684)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MGGCSILLRSSALTCGRPRSSPPGAEVRCRGRRPLCALRGRGHPLAALPGPPSWPLMGSLPDVLWKGGLKRQHETLAEYHRRFGKIFRMKLGAFDSVHIGAPCLLESLYRRESSCPQRLEIKPWKAYRDYRDEGYGLLILEGKDWQRVRSAFQKKLMKPKEVVKLDNTINEVLEDFMHRIDEICNHNGQMEDVYSEFNKWSFESICLVLYGKRFGLLQQDVEEESLNFIKAVKTMMATFGMMMVTPVELHKGLNTKVWQAHTKAWDDIFKTAKHSIDSRLQRHSANPQEDFLCDIYSGGQLSKKELYATIAELQIAGVETTANSLLWALYNISRNPHVQQKLLQEIQSVLAANESPTAESIKNMPYLKACLKESMRLTPSVPFTTRTIDTEMVLGDYVLPEGTVLMINSYALGCNEEYFNGWTQFKPERRWLQKHSINPFSHVPFGIGKRMCIGRRLAELQLHLALCWIIRKYQLVATDDNPVETLHSGILIPSRELPIAFHRRLQLD
Protein: Alpha/beta hydrolase domain-containing protein 17C (Abhydrolase domain-containing protein 17C) (EC 3.1.2.22) (Q6PCB6)
Organism: Homo sapiens (Human)
Function: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards NRAS and DLG4/PSD95.
Subcellular location: Recycling endosome membrane {ECO:0000250|UniProtKB:B5DFK7}; Lipid-anchor {ECO:0000250|UniProtKB:B5DFK7}; Cytoplasmic side {ECO:0000250|UniProtKB:B5DFK7}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:B5DFK7}. Postsynaptic density membrane {ECO:0000250|UniProtKB:B5DFK7}.
Interaction partners:
Sequence:
MPEPGPRMNGFSLGELCWLFCCPPCPSRIAAKLAFLPPEPTYTVLAPEQRGAGASAPAPAQATAAAAAAQPAPQQPEEGAGAGPGACSLHLSERADWQYSQRELDAVEVFFSRTARDNRLGCMFVRCAPSSRYTLLFSHGNAVDLGQMCSFYIGLGSRINCNIFSYDYSGYGVSSGKPSEKNLYADIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYECAAVILHSPLMSGLRVAFPDTRKTYCFDAFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDIELYAQYLERLKQFISHELPNS
Protein: Prefoldin subunit 5 (EIG-1) (Myc modulator 1) (c-Myc-binding protein Mm-1) (Q9WU28)
Organism: Mus musculus (Mouse)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Prefoldin subunit 1
- Prefoldin subunit 3
- Prefoldin subunit 4
- Prefoldin subunit 2
- Prefoldin subunit 6
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit beta
Sequence:
MAQSINITELNLPQLEMLKNQLDQEVEFLSTSIAQLKVVQTKYVEAKDCLNVLNKSNEGKELLVPLTSSMYVPGKLHDVEHVLIDVGTGYYVEKTAEDAKDFFKRKIDFLTKQMEKIQPALQEKHAMKQAVMEMMSQKIQQLTALGAAQATVKA
Protein: Reticulophagy regulator 2 (Q6NS82)
Organism: Mus musculus (Mouse)
Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress. When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins. Required for collagen quality control in a LIR motif-independent manner.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NC44}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 60S ribosomal export protein NMD3
- Gamma-aminobutyric acid receptor-associated protein
- Proliferation-associated protein 2G4
- Eukaryotic translation initiation factor 6
Sequence:
MASSGGGNTGAGGTSGLGLGLGLSLGMGEATGDAEEEAAAAEAVGRLATSLWLRLRGWEAVLAAAQRLLVWEKPLHSLVTAATLNGLFWLLSSSSLRPFFLLSISLLTYFLLDLWHPRFLPDVSAPPPEEPHSDSEGAGSGAQPHLLSVPELCRYLAESWLTFQIHLQELLQYKRQNPAQFCARGCAACAVLAVLGHYVPGVMISYIVLLSILLWPLVVYHELIQRMYTRLEPLLMQLDYSMKAEADALHHKHDKRKRQGKSAPPAGDEPLAETESESEAELAGFSPVVDVKKTALALAITDSELSDEEASILESGGFSVSRATTPQLTDVSEDLDQQSLPSEPEEALNRELGEGEETELASPEDLLSAPPALSKQALDTEEEGAADKEALLQLSSPLHFVNTHFNGAGSPQDGVKCPPGAPVKTLSPEAVSGDLMAPSSTLSPQLCLAESGPVTPLSPSVLPSLPQDSPQPLAAPEEEEALTTEDFELLDQGELEQLNAELGLGPEMPPKPPDVLPPPPLGADSHSLVQSDQEAHAEVEP
Protein: Dynein regulatory complex protein 9 (IQ domain-containing protein G) (Q9H095)
Organism: Homo sapiens (Human)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Binds calmodulin when cellular Ca(2+) levels are low and thereby contributes to the regulation of calcium and calmodulin-dependent protein kinase IV (CAMK4) activity; contributes to the regulation of CAMK4 signaling cascades. Required for normal axoneme assembly in sperm flagella, normal sperm tail formation and for male fertility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24787902}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q80W32}. Cell projection, cilium {ECO:0000250|UniProtKB:Q80W32}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q80W32}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8HQ54}. Note=First detected in the cytoplasm of pachytene spermatocytes. Colocalizes with alpha-tubulin at the manchette in developing spermatids. Detected in the flagellum of mature testicular spermatozoa, and in the flagellum and post-acrosomal region of the head of epididymal spermatozoa. Detected in cilia in trachea and oviduct. {ECO:0000250|UniProtKB:Q80W32}.
Interaction partners:
- Calmodulin-1
- Calmodulin-1
- Dynein regulatory complex subunit 7
- Dynein regulatory complex subunit 5
Sequence:
MEEDSLEDSNLPPKVWHSEMTVSVTGEPPSTVEEEGIPKETDIEIIPEIPETLEPLSLPDVLRISAVLEDTTDQLSILNYIMPVQYEGRQSICVKSREMNLEGTNLDKLPMASTITKIPSPLITEEGPNLPEIRHRGRFAVEFNKMQDLVFKKPTRQTIMTTETLKKIQIDRQFFSDVIADTIKELQDSATYNSLLQALSKERENKMHFYDIIAREEKGRKQIISLQKQLINVKKEWQFEVQSQNEYIANLKDQLQEMKAKSNLENRYMKTNTELQIAQTQKKCNRTEELLVEEIEKLRMKTEEEARTHTEIEMFLRKEQQKLEERLEFWMEKYDKDTEMKQNELNALKATKASDLAHLQDLAKMIREYEQVIIEDRIEKERSKKKVKQDLLELKSVIKLQAWWRGTMIRREIGGFKMPKDKVDSKDSKGKGKGKDKRRGKKK
Protein: Serine/arginine-rich splicing factor 3 (Pre-mRNA-splicing factor SRP20) (Splicing factor, arginine/serine-rich 3) (P84103)
Organism: Homo sapiens (Human)
Function: Splicing factor that specifically promotes exon-inclusion during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing. Also functions as export adapter involved in mRNA nuclear export. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. Involved in nuclear export of m6A-containing mRNAs via interaction with YTHDC1: interaction with YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export. RNA-binding is semi-sequence specific.
Subcellular location: Nucleus {ECO:0000269|PubMed:11336712}. Nucleus speckle {ECO:0000269|PubMed:26876937}. Cytoplasm {ECO:0000269|PubMed:11336712}. Note=Recruited to nuclear speckles following interaction with YTHDC1. {ECO:0000269|PubMed:26876937}.
Interaction partners:
- Serine/arginine-rich splicing factor 2
- Transformer-2 protein homolog beta
- Eukaryotic initiation factor 4A-III
- Protein mago nashi homolog
- RNA-binding protein 8A
- Nuclear RNA export factor 1
- Serine/arginine-rich splicing factor 7
- Poly
- YTH domain-containing protein 1
- Serine/arginine-rich splicing factor 1
Sequence:
MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKRSRNRGPPPSWGRRPRDDYRRRSPPPRRRSPRRRSFSRSRSRSLSRDRRRERSLSRERNHKPSRSFSRSRSRSRSNERK
Protein: Leucine-rich repeat and calponin homology domain-containing protein 2 (Q5VUJ6)
Organism: Homo sapiens (Human)
Function: May play a role in the organization of the cytoskeleton.
Interaction partners:
- Dedicator of cytokinesis protein 8
Sequence:
MAASQGGGGNSGGGGCGGGGSSGGCGTAGGGGGGAGGGGGGGGGTLVVPIPVPTLFGQPFPNGPPWNPGSLQPQHTVRSLDRALEEAGSSGILSLSGRKLRDFPGSGYDLTDTTQADLSRNRFTEIPSDVWLFAPLETLNLYHNCIKTIPEAIKNLQMLTYLNISRNLLSTLPKYLFDLPLKVLVVSNNKLVSIPEEIGKLKDLMELDISCNEIQVLPQQMGKLHSLRELNIRRNNLHVLPDELGDLPLVKLDFSCNKVTEIPVCYRKLHHLQVIILDNNPLQVPPAQICLKGKVHIFKYLNIQACCRMDKKPDSLDLPSLSKRMPSQPLTDSMEDFYPNKNHGPDSGIGSDNGEKRLSTTEPSDDDTVSLHSQVSESNREQTSRNDSHIIGSKTDSQKDQEVYDFVDPNTEDVAVPEQGNAHIGSFVSFFKGKEKCSEKSRKNEELGDEKRLEKEQLLAEEEDDDLKEVTDLRKIAAQLLQQEQKNRILNHSTSVMRNKPKQTVECEKSVSADEVNSPLSPLTWQPLENQKDQIDEQPWPESHPIIWQSEERRRSKQIRKEYFKYKSMRKSSSGNENDEQDSDNANMSTQSPVSSEEYDRTDGFSHSPFGLKPRSAFSRSSRQEYGAADPGFTMRRKMEHLREEREQIRQLRNNLESRLKVILPDDIGAALMDGVVLCHLANHIRPRSVASIHVPSPAVPKLSMAKCRRNVENFLDACKKLGVSQERLCLPHHILEERGLVKVGVTVQALLELPTTKASQLSVA
Protein: Mediator of RNA polymerase II transcription subunit 22 (Mediator complex subunit 22) (Suppressor of RNA polymerase B 6) (P32570)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 6
Sequence:
MSNQALYEKLEQTRTILSVKLAELINMTTIADRNDDDEGSFAQENSELAVATTSVMMVNNQTMQLIKNVQDLLILTRSIKEKWLLNQIPVTEHSKVTRFDEKQIEELLDNCIETFVAEKTT
Protein: Outer membrane lipoprotein DolP (P64596)
Organism: Escherichia coli (strain K12)
Function: Plays an important role in maintaining outer membrane integrity. Supports proper folding and function of BamA under envelope stress conditions. Binds specifically to anionic phospholipids via the BON 2 domain. This interaction is essential for function and guides the protein to the cell division site. It was reported that DolP is a potential upstream regulator of the amidase activator NlpD. However, later studies suggest that DolP affects cell division and may impact daughter cell separation, but likely not as a regulator of NlpD.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:28708841, ECO:0000269|PubMed:33315009}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:33315009}; Periplasmic side {ECO:0000269|PubMed:33315009}. Note=Localizes to the cell division site (PubMed:28708841, PubMed:33315009). Localization to the division site is dependent upon interaction with anionic phospholipids (PubMed:33315009). Upon envelope stress, loses its association with the mid-cell (PubMed:33847565). {ECO:0000269|PubMed:28708841, ECO:0000269|PubMed:33315009, ECO:0000269|PubMed:33847565}.
Interaction partners:
- DnaA initiator-associating protein DiaA
- Penicillin-binding protein activator LpoA
- UPF0102 protein YraN
- Outer membrane protein assembly factor BamD
Sequence:
MKALSPIAVLISALLLQGCVAAAVVGTAAVGTKAATDPRSVGTQVDDGTLEVRVNSALSKDEQIKKEARINVTAYQGKVLLVGQSPNAELSARAKQIAMGVDGANEVYNEIRQGQPIGLGEASNDTWITTKVRSQLLTSDLVKSSNVKVTTENGEVFLMGLVTEREAKAAADIASRVSGVKRVTTAFTFIK
Protein: Rhodanese-like domain-containing protein 4, chloroplastic (Protein THYLAKOID RHODANESE-LIKE) (Sulfurtransferase 4) (AtStr4) (Q9M158)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Rhodanese domain-containing protein required for anchoring ferredoxin--NADP reductase to the thylakoid membranes and sustaining efficient linear electron flow (LEF).
Subcellular location: Plastid, chloroplast envelope {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:19682289}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:19682289}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly localized to the non-appressed regions of the thylakoid membrane. {ECO:0000269|PubMed:19682289}.
Interaction partners:
- Protein TIC 62, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic
- Protein CURVATURE THYLAKOID 1B, chloroplastic
- Photosystem II 22 kDa protein, chloroplastic
- Light-regulated protein 1, chloroplastic
- ATP synthase gamma chain 1, chloroplastic
- Protein PROTON GRADIENT REGULATION 5
- PsbP-like protein 1, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
Sequence:
MEALKTATFSPMSVLSEKRSEPRKPFSLPNLFPPKSQRPISQESFLKRFNGGLALLTSVLSSATAPAKSLTYEEALQQSMTTSSSFDSDGLIEGISNFVTDNPLVIAGGVAALAVPFVLSQVLNKKPKSWGVESAKNAYTKLGTDDNAQLLDIRATADFRQVGSPNIKGLGKKAVSTVYNGEDKPGFLKKLSLKFKDPENTTLYILDKFDGNSELVAELVALNGFKSAYAIKDGAEGPRGWLNSSLPWIEPKKTLSLDLSSLTDSISGVFGESSDGVSVALGVAAAAGLSVFAFTEIETILQLLGSAALVQLAGKKLLFAEDRKQTLKQVDEFLNTKVAPKELVDELKEIGKALLPQSTSNKALPAPATVTAEAESATATTTTVDKPVPEPETVAATTTTVDKPVPEPEPVPEPVPVPAIEAAVAAQVITEPTETEAKPKPHSRPLSPYASYPDLKPPSSPMPSQP
Protein: Zinc finger protein 64 (Zfp-64) (Zinc finger protein 338) (Q9NTW7)
Organism: Homo sapiens (Human)
Function: May be involved in the regulation of mesenchymal cell differentiation through transactivation of NOTCH1 target genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:27353377}.
Interaction partners:
Sequence:
MNASSEGESFAGSVQIPGGTTVLVELTPDIHICGICKQQFNNLDAFVAHKQSGCQLTGTSAAAPSTVQFVSEETVPATQTQTTTRTITSETQTITVSAPEFVFEHGYQTYLPTESNENQTATVISLPAKSRTKKPTTPPAQKRLNCCYPGCQFKTAYGMKDMERHLKIHTGDKPHKCEVCGKCFSRKDKLKTHMRCHTGVKPYKCKTCDYAAADSSSLNKHLRIHSDERPFKCQICPYASRNSSQLTVHLRSHTASELDDDVPKANCLSTESTDTPKAPVITLPSEAREQMATLGERTFNCCYPGCHFKTVHGMKDLDRHLRIHTGDKPHKCEFCDKCFSRKDNLTMHMRCHTSVKPHKCHLCDYAAVDSSSLKKHLRIHSDERPYKCQLCPYASRNSSQLTVHLRSHTGDTPFQCWLCSAKFKISSDLKRHMIVHSGEKPFKCEFCDVRCTMKANLKSHIRIKHTFKCLHCAFQGRDRADLLEHSRLHQADHPEKCPECSYSCSSAAALRVHSRVHCKDRPFKCDFCSFDTKRPSSLAKHVDKVHRDEAKTENRAPLGKEGLREGSSQHVAKIVTQRAFRCETCGASFVRDDSLRCHKKQHSDQSENKNSDLVTFPPESGASGQLSTLVSVGQLEAPLEPSQDL