wanglab/gogpt-training-data huggingface dataset:
Protein: Homeobox protein DLX-2 (Q07687)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator. Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina. Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Achaete-scute homolog 1
- Homeobox protein DLX-1
- Homeobox protein Meis2
- Paired box protein Pax-6
- LIM/homeobox protein Lhx6
- Myelin transcription factor 1-like protein
- T-box brain protein 1
- Bone morphogenetic protein 4
- Neurogenin-2
- LIM/homeobox protein Lhx8
Sequence:
MTGVFDSLVADMHSTQIAASSTYHQHQQPPSGGGAGPGGNSSSSSSLHKPQESPTLPVSTATDSSYYTNQQHPAGGGGGGGSPYAHMGSYQYQASGLNNVPYSAKSSYDLGYTAAYTSYAPYGTSSSPANNEPEKEDLEPEIRIVNGKPKKVRKPRTIYSSFQLAALQRRFQKTQYLALPERAELAASLGLTQTQVKIWFQNRRSKFKKMWKSGEIPSEQHPGASASPPCASPPVSAPASWDFGVPQRMAGGGGPGSGGSGAGSSGSSPSSAASAFLGNYPWYHQTSGSASHLQATAPLLHPTQTPQPHHHHHHHGGGGAPVSAGTIF
Protein: Mucin (O35888)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAHTTFVGKTSTISGPGTSTTSIPTSTTGSSSHFEVTRSPVTAHCQPQCNWTKWLDTDFPVPGPHGGDLETYGNIKKSRERLCPWPEEITRLECRAKDYPERAMEDLGQVVQCDPRVGLVCKNSDQGPTFGMCLNYEVRLLCCHVPEDCLRTDRTPVTSHKTSFPVVSSSSVSTSSSTSPRVHSTTRCFCTMSGQLYPLGTIIYNQTDLDGHCYYAMCSHDCQVVKGVSQDCPSTMPPRTPTLSTSTAPPVTERDWCNVFPPKLKGETWPMPNCSQATCEGNNVVSLSPRQCPEVKEPSCANGYPPLKVDDQDGCCQHYQCQCVCSGWGDPHYITFDGTYYTFLDNCTYVLVQQIVPVFGDFRVLIDNYYCDLGDSVSCPQSIIVEYHQDRVVLTRRPVHGVMTNQIIFNNKVVSPGFQQNGIIISRVGIKMYVTIQEIGVQVMFSGLIFSVEVPFNLFANNTEGQCGTCTNDKKDECRLPGGSIASSCSEMSLHWKVPNQPSCQGPPPTPTSMVPRSTPTPCSPSPLCQLILSDVFKLCHDIIPPLQFYEGCLFDYCHMLDLEVVCSGLELYASLCAAQGVCIPWRSHTNNTCPFTCPENQVYQPCGPSNPHYCYRNDDISLSLAIQKAGPKSEGCFCPDDMTLFSSNDSICVPSCQWCLGPHGEPVEPGHTISINCQDCICKEGTLTCQEKLCPQPTCPEPGFVPVSIALEAGQCCSQFSCVCNSSHCPPPLHCPESSSLIVTYEEGTCCPSQNCSSQKGCDVNGTLYQPGDVVSSSLCERCLCEVSSNAFSDVFVVNCETELCNTQCPKGFEYQTTPGHCCGQCVPKTCPFKNSNNSTSLYKPGEFWPEPGNPCVTHKCEKFQDVLTVVTVKIECPKINCPQDWAQLREDGCCYDCLVPQQKCTVHQRQQIIRQQNCSSEGPVSLSYCQGNCGDSTSMYSLEANTVEHTCECCQELQTSQRSVTLHCDDGSSRTFSYTQVEKCGCLGQRCHAPGDTSHSESSEQEFKSKESEEPGQQSASRVSEDTLGPFQ
Protein: NLR family, apoptosis inhibitory protein 6 (M0R915)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- NLR family CARD domain-containing protein 4
- NLR family, pyrin domain-containing 1A.
- Pyrin
- Absent in melanoma 2
- Apoptosis-associated speck-like protein containing a CARD
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 6
- NLR family, pyrin domain containing 1B
- NACHT, LRR and PYD domains-containing protein 3
- Gasdermin D
Sequence:
MAAQGEAFEERICEFDDDLVSEFSTLLRVDALQVLKRQQEEDHKTRMKMKKGFNAQMRSEAKRLKTFVTYDTFRSWTPQEMAAAGFYYTGVRHGVQCFCCSLILFATRLRKVPIEVHRKLQPECEFLSGKDVGNIGKYDIRVKSPETLPRGGRARYHEEEARLESFEDWPFYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQSKKSAEEIAKYIQTYEGFLHVTGEHFVNSWVRRELPVVSAYSNDSVFANEGLRMDTFKDWPHESPMAVEALVKAGLFYTGKKDIVQCFSCGGCMENWKEGDDPIEDHTKFFPNCVFLQTLKSSAEVIPALQSHCARPEAMETTSESNHEDGVAVHSSVAGIPTCTSLPSADLGQSEAQWCQEARSLSEQLRGTYTKASFRHMNLPEAYSSLGTDHLLGCEVFLISKHVSRPVQVALTIPEVFANLSSVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLNRFQLVFYLSLRSIRADQGLADIICAQLLEAGGCISEVSLSSGIQHLQHQVLFLLDDYSGMDSLPQALDTLITKNYLSRTCLLMAVHTNRVRDIRPYLETVLQIKEFPFYNTVYILKKIFSHDIIRVRRFINYFGFHEYLQGIHKTPLFVAGVCADWLQNPSDQPFQDVTIFKSYMQYLFLKHKATAGPLQATVSSCGHLALTGLFSSSFEFSSDDLIEAGVDEDEELSTCLMSKFTAQRLRPVYRFLSPLFQEFLAAMRLSELLGSDSQEDQDLGLYYLRQINSPLKAMSIYHTFLRYVSNHPSSKAGPKVISHLLQLVDEKESPENTSENEDYMKLHPETLLWSQCLRGLLQLSPESFSLFISERLLNIALNFAYQSNTVAACSPVILQFLQGRTLDLKVLNLQYFWDHPETLLLLKSIQVLFNGNNRVQRIDFSLMDKSFEKIQPPTIDQDYAFAFQPMSECQRNLAEKENIIKNYDDMKYQDPLNISSGYWKLSPKPYKIPRLEVGVNNMGPADQALLHVLMEVFSASQSIEFHLFNSSGFLESIRPALELNKTSVTKCSMSRLELSRAEQELLLTLPALQSLEVSGTSQIPDQLFHNLDKFLGLKELSVRLDGTQDMLSVLPGEFPNLHHMEKLSIHTSTESDLSKLVKLIQNSPNLHDFHLKCDFLSNCESLMAALASCKKLREIEFSGRCFEAVPFVNILSNFASLKILNLRNQQFPDKETSEKFAQALGSLRNLEELHLPTGDGIHQVAKPIVRRCLQLPCLRVLVFAETLDDDSVLEIAKGATSGGFQNLENLDLTLNHKITEEGYRNFFQALDNLPNLQNLDISRHIPECIQVQASTVKALGQCVSRLPSLTRLGMLSWLLDEEDMKVINDVKERHPQSKRLTVHWRWVVPFSPVIQK
Protein: Cytosine permease (P0AA82)
Organism: Escherichia coli (strain K12)
Function: Required for cytosine transport into the cell.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Cytosine deaminase
- Uracil permease
- Aspartate carbamoyltransferase regulatory chain
- Aspartate carbamoyltransferase catalytic subunit
- Dihydroorotase
- Carbamoyl phosphate synthase large chain
- Uracil phosphoribosyltransferase
- Dihydroorotate dehydrogenase
- Carbamoyl phosphate synthase small chain
Sequence:
MSQDNNFSQGPVPQSARKGVLALTFVMLGLTFFSASMWTGGTLGTGLSYHDFFLAVLIGNLLLGIYTSFLGYIGAKTGLTTHLLARFSFGVKGSWLPSLLLGGTQVGWFGVGVAMFAIPVGKATGLDINLLIAVSGLLMTVTVFFGISALTVLSVIAVPAIACLGGYSVWLAVNGMGGLDALKAVVPAQPLDFNVALALVVGSFISAGTLTADFVRFGRNAKLAVLVAMVAFFLGNSLMFIFGAAGAAALGMADISDVMIAQGLLLPAIVVLGLNIWTTNDNALYASGLGFANITGMSSKTLSVINGIIGTVCALWLYNNFVGWLTFLSAAIPPVGGVIIADYLMNRRRYEHFATTRMMSVNWVAILAVALGIAAGHWLPGIVPVNAVLGGALSYLILNPILNRKTTAAMTHVEANSVE
Protein: SCY1-like protein 2 (Coated vesicle-associated kinase of 104 kDa) (Q8CFE4)
Organism: Mus musculus (Mouse)
Function: Component of the AP2-containing clathrin coat that may regulate clathrin-dependent trafficking at plasma membrane, TGN and endosomal system. A possible serine/threonine-protein kinase toward the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L-lysine has not been confirmed (By similarity). By regulating the expression of excitatory receptors at synapses, plays an essential role in neuronal function and signaling and in brain development.
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q6P3W7}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q6P3W7}. Endosome membrane {ECO:0000250|UniProtKB:Q6P3W7}. Note=Colocalizes to the trans-Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes. {ECO:0000250|UniProtKB:Q6P3W7}.
Interaction partners:
Sequence:
MESMLNKLKSTVTKVTADVTSAVMGNPVTREFDVGRHIASGGNGLAWKIFNGTKKSTKQEVAVFVFDKKLIDKYQKFEKDQIIDSLKRGVQQLTRLRHPRLLTVQHPLEESRDCLAFCTEPVFASLANVLGNWENLPSSISPDIKDYKLYDVETKYGLLQVSEGLSFLHSSVKMVHGNVTPENVILNKSGAWKIMGFDFCVSSSNPSEQEPKFPCKEWDPNLPSLCLPNPEYLAPEYILSVSCETASDMYSLGAVMYAVFNQGRPIFEVNKQDIYKSFSRQLDQLSRLGSSSLTSIPEEVREHVKLLLNVTPTVRPDADQMTKIPFFDDVGAVTLQYFDTLFQRDNLQKSQFFKGLPKVLPKLPKRVIVQRILPCLTSEFVNPDMVPFVLPNVLLIAEECTKEEYIKLILPELGPVFKQQEPIQILLIFLQKMDLLLTKTPPDEIKNSVLPMVYRALEAPSIQIQELCLNIIPTFANLIDYPSMKNALIPRIKNACLQTSSLAVRVNSLVCLGKILEYLDKWFVLDDILPFLQQIPSKEPAVLMGILGIYKCTFTHKKLGITKEQLAGKVLPHLIPLSIENNLNLNQFSSFIAVIKEMLSRLESEHRTKLEQLHVMQEQQRSLDIGNQMSTSEETKVAHSGSQQIDKVFNNIGADLLSGSESENREDGMQGKQKRGSLTLEEKQKLAKEQEQAQKLKSQQPLKPQVHTPIAPIKQTKDLTDTLMENMSSLTSLSVSTPKISASSTFTPVPSTGLGMMFSTPIDNTKRNLTNGLNANMGFQTSGFSMPVNPNQNFFSGTGTAGVTTMSLGAPPTMSNFSPLTIPPASVKQPQQRPTDMSALNNLFGPQKPKVSMNQLSQQKPNQWLNQFAPPQGSPVMGSAAMGTQGNVMGQAAFGMQGNPFFNPQNFAQPPPTTMTSSSSASNDLKDLFG
Protein: E3 ubiquitin-protein ligase pub3 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase pub3) (O14326)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Interaction partners:
- E3 ubiquitin-protein ligase pub2
- Pheromone P-factor receptor
- E3 ubiquitin-protein ligase pub1
- Pheromone M-factor receptor
- Polyadenylate-binding protein 2
- Arrestin domain-containing protein C584.15c
- Polyubiquitin
Sequence:
MEQGAKRVRFYIVAADGLSKRDLFRQPDPFAILTVDGEQTHTTKVIKKSVNPYWNEGFEVTVKPSSVISIRLFDQKKFKKKDQGFLGLVSFRMREVGSFRSNREVSLTRPLKKSSTTNLSVLGNLVLKVAPSKIRAPAGNHSSTTANRTTSTPTTTTARTTRTTPRPTATTNTSNQSTSNSTRNGTSAATSNGTGTGAGTGASHRSSPVTNRQTNNTSALSNSNAHIMSSFEDQYGRLPPGWERRADSLGRTYYVDHNTRTTTWTRPASSTNPVHNTSSDSQRLNHQNRHLPDDSNPSLMQSDSGNDLPFGWEMRYTDTGRPYFVDHNTRTTTWVDPRNPLVRPNGGSSTVGSLMQPQSLSHLGPLPSGWEMRLTNSARVYFVDHNTKTTTWDDPRLPSALDQDVPQYKCDFRRKLIYFRSQPGMRPLPGQCNVKVRRDHIFEDSYAEIMRYSAHDLKKRLMIRFDGEDGLDYGGLSREFFFLLSHKMFDPIYCLFEYSAVDNYTLQINPHSSINPEHLNYFRFIGRVIGLAIFHRRFLDAFFVVSLYKKLLRKKVSLADMESIDAEFYRSLKWVLENDITGILDLTFSVEEDHFGEVRTVELITNGENIEVTEENKKKYVDLVTEWRVSKRVEQQFNAFYSGFVELVSPDLVNVFDERELELLIGGISDVDVEDWKSHTEYRTYIATDPVIKWFWEIIAGWKNEDRSKLLQFATGTSRIPVNGFRDLQGSDGPRKFTIEKAGTPDQLPVAHTCFNRLDLPDYPSKDTLHEKLSLAVENTVGFGNE
Protein: Lysophosphatidic acid receptor 6 (X1WDA3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Metadherin a
- Guanine nucleotide-binding protein
- Immunoglobulin heavy constant delta.
- Epithelial membrane protein 2
- G-protein alpha 13a, alpha 13a)
Sequence:
MMTERSNCTNDSFKYVLYSSVFSIVFILGLLFNMVAMYIFVCRLKMRNETTTYMMNLVVSDSLFVVSLPFRTFYFINRQWPFGDALCKISVTLFYTNMYGSILFLTCISVDRFLAIVYPFASRTLRTKRNAKIACGVIWVVLLSGGLTAGFVMDITSHKNETYCFENYSKSQWKSQVSKVVVFMETVGFLIPLMINFICSVKVLQTLRHPETISRGGQLNKAKILRMIVVHLLIFCFCFIPFNVNLVFYTLVRSEVIQNCTVETVVRTIYPIAFCIAVTNCCFDPVIYYFTSETIQNSMKRKSYGVHKNTLNNTIDNSDYNGRGTIDKITSLTAKFMIEESTI
Protein: Developmental regulatory protein wetA (P22022)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation. They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes. Responsible for activating a set of genes whose products make up the final two conidial wall layers or direct their assembly and, through this activity, is responsible for acquisition of spore dormancy.
Interaction partners:
- Conidiophore development regulator abaA
- C2H2 type master regulator of conidiophore development brlA
- Spore development regulator vosA
- C2H2-type domain-containing protein
- Cell pattern formation-associated protein stuA
- Velvet complex subunit B
- Protein fluG
- Developmental regulator flbA
- MYB family conidiophore development protein FlbD
- Sexual development regulator velC
Sequence:
MFAHPFDHSFNDLFNQYVNMDTSSTDANKDVSFPSEFDQLFPLDSFSTDCGDQSPVISTVQHNSQPAQDWGKDLWSLSQNTGCSTNQDSFSFQDSTQPSTALDLSIGLEADATGHSQASVPRSTPSTPPATPGPKVKGGLFTPKTIRHHRESNDRRGLLRKQSFSPGLMRSSQLQKGSCRMAYPEAWAQRLQNFTIRSSDECLPLSPPPSDILVQQENVKHTPVQMRNAAEGFQGSTELPQQIDSGYITQSPAIPMPSPSANALAGQQQRYLSQTGTSALTPSPPSARDVFSSPHSSDPQSMPSWHSESLNTPAFQYTPELSDHQTWWSPMPSEVAQRHASYQQMIASPAPQRPVQAAANHGDFLQGGLMIQLDPTQFDISSSFPSSTIPTTANNHDNLAYNVEAHAPQKYVDASSFNTQAVPHPSRSPSISPKADTSPRHGSANRDGMAMKNAPRRPHGRKLSGQSTSTPKPVKTPNSLSTSPRGGKSVTVSFVNFTANDRQKILTGVAPSGSSKTKARREQEARDRRRKLSEAALQAVRKAGGDVEALEAVLC
Protein: Neutral amino acid transporter B(0) (ATB(0)) (Baboon M7 virus receptor) (RD114/simian type D retrovirus receptor) (Sodium-dependent neutral amino acid transporter type 2) (Solute carrier family 1 member 5) (Q15758)
Organism: Homo sapiens (Human)
Function: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24953180, ECO:0000269|PubMed:8702519, ECO:0000305|PubMed:29872227}; Multi-pass membrane protein {ECO:0000269|PubMed:29872227}. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Interaction partners:
- Syncytin-1
- Sodium- and chloride-dependent neutral and basic amino acid transporter B
- Amino acid transporter heavy chain SLC3A2
- Large neutral amino acids transporter small subunit 1
- Sodium- and chloride-dependent glycine transporter 2
- Glutaminase liver isoform, mitochondrial
- Syncytin-2
- Glutaminase kidney isoform, mitochondrial
- Sodium-coupled neutral amino acid symporter 2
- Solute carrier family 2, facilitated glucose transporter member 1
Sequence:
MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGSRDQVRRCLRANLLVLLTVVAVVAGVALGLGVSGAGGALALGPERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLDPGALGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINASVGAAGSAENAPSKEVLDSFLDLARNIFPSNLVSAAFRSYSTTYEERNITGTRVKVPVGQEVEGMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNEATMVLVSWIMWYAPVGIMFLVAGKIVEMEDVGLLFARLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLMMKCVEENNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLSQQSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAVNLPVDHISLILAVDWLVDRSCTVLNVEGDALGAGLLQNYVDRTESRSTEPELIQVKSELPLDPLPVPTEEGNPLLKHYRGPAGDATVASEKESVM
Protein: Transmembrane protein 47 (Brain cell membrane protein 1) (Transmembrane 4 superfamily member 10) (Q9BQJ4)
Organism: Homo sapiens (Human)
Function: Regulates cell junction organization in epithelial cells. May play a role in the transition from adherens junction to tight junction assembly. May regulate F-actin polymerization required for tight junctional localization dynamics and affect the junctional localization of PARD6B. During podocyte differentiation may negatively regulate activity of FYN and subsequently the abundance of nephrin (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9XSV3}. Note=Colocalizes with FYB1 at cell-cell contacts in podocytes. {ECO:0000250|UniProtKB:Q9JJG6}.
Interaction partners:
- Apical junction component 1 homolog
Sequence:
MASAGSGMEEVRVSVLTPLKLVGLVCIFLALCLDLGAVLSPAWVTADHQYYLSLWESCRKPASLDIWHCESTLSSDWQIATLALLLGGAAIILIAFLVGLISICVGSRRRFYRPVAVMLFAAVVLQVCSLVLYPIKFIETVSLKIYHEFNWGYGLAWGATIFSFGGAILYCLNPKNYEDYY
Protein: Deoxyribonuclease-1 (EC 3.1.21.1) (Deoxyribonuclease I) (DNase I) (P00639)
Organism: Bos taurus (Bovine)
Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs. Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization. Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:4734471}. Zymogen granule {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
Interaction partners:
- Phospholipase A2
- Pancreatic polypeptide prohormone
Sequence:
MRGTRLMGLLLALAGLLQLGLSLKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT
Protein: Lamin tail domain-containing protein 1 (Intermediate filament tail domain-containing protein 1) (Lamin-A-related sequence 1 protein) (Q9D4C1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MMKEASEPLASVTSINKQDSKVQDGEIRKEKIGTITPSKQHSSVHFFPKIMDSDSTTLIPLSRSFSQEMPIGFYQITSTQNSSTLSSRGQLASKSTILSCSHKDSSLGKQSTSSMVPRRQPQSSSDVDTYTFGNGEDYFLSLFGESKKLTAHTPQAENVSEHLSVILEEVGQFTSSSLGEIKIAEVNIKGLFVRLVNSSNEKEVEIGNHILQQNVNGHAVSLYQFPDNITLQANSTVTVWAAASEAKPQPPTDFVWEEQSKFRSSPDCTTILCKPNGEAIAWYTPIHWKQAWEKLETDIEFERCSVVVPSMRNHMFGWITASVSSTNEEKEEPIQKTPSQVYPVLYREKEIPPTVLPNKSPWCRNPNTSPHPYSSLIDSHDSDISESSLDTQLKPQPTKPKPDPGTKKKKAKS
Protein: Embryo sac development arrest 6 (Q9LW53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNQNHHAHEGASRKRKDTESDLREAATPNWLLAGYMAHEYLTCGTMLGRKLYSGWAEVGPLVSPSPLQSREVKKARQSYSEVASVFKTDGNHVPGVVNPTQLAKWIQM
Protein: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (InsP6 and PP-IP5 kinase) (Q06685)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity). Required for maintaining cellular integrity, normal growth and interactions with the ARP complex. Acts as a regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating signaling of phosphate availability. Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth. Regulates polarized growth and modulates interphase microtubule cytoskeleton. Regulates microtubule dynamics without the requirement of microtubule plus-end tracking protein Mal3. Required for growth zone selection (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Inositol hexakisphosphate kinase 1
- Inositol-pentakisphosphate 2-kinase
- Inositol polyphosphate multikinase
- Phosphate system positive regulatory protein PHO81
- PHO85 cyclin PHO80
- FACT complex subunit POB3
- Nucleosome assembly protein
- Nuclear localization sequence-binding protein
- H/ACA ribonucleoprotein complex subunit CBF5
Sequence:
MSGIKKEPIESDEVPQQETKNNLPSAPSEMSPLFLNKNTQKAMQSIAPILEGFSPKTSASENMSLKLPPPGIQDDHSEENLTVHDTLQRTISTALGNGNNTNTVTTSGLKKADSESKSEADPEGLSNSNIVNDADNINSISKTGSPHLPQGTMDAEQTNMGTNSVPTSSASSRKSSTSHPKPRLPKVGKIGVCAMDAKVLSKPMRHILNRLIEHGEFETVIFGDKVILDERIENWPTCDFLISFFSSGFPLDKAIKYVKLRKPFIINDLIMQKILWDRRLCLQVLEAYNVPTPPRLEISRDGGPRANEELRAKLREHGVEVKPVEEPEWKMVDDDTLEVDGKTMTKPFVEKPVDGEDHNIYIYYHSKNGGGGRRLFRKVGNKSSEFDPTLVHPRTEGSYIYEQFMDTDNFEDVKAYTIGENFCHAETRKSPVVDGIVRRNTHGKEVRYITELSDEEKTIAGKVSKAFSQMICGFDLLRVSGKSYVIDVNGFSFVKDNKAYYDSCANILRSTFIEAKKKMDMEKKNLPIIREEKEQKWVFKGLAIIIRHADRTPKQKFKHSFTSPIFISLLKGHKEEVVIRNVNDLKIVLQALRIALDEKAGNPAKIKVLANALEKKLNFPGTKIQLKPVLNKENEVEKVQFILKWGGEPTHSAKYQATELGEQMRQDFDLLNKSILQNIKIFSSSERRVLHTAQYWTRALFGADELGSDEISIRKDLLDDSNAAKDLMDKVKKKLKPLLREGKEAPPQFAWPSKMPEPYLVIKRVVELMNYHKKIMDNNFAKKDVNSMQTRWCTSEDPSLFKERWDKLFKEFNNAEKVDPSKISELYDTMKYDALHNRQFLENIFDPGLPNEAIADELGSHSLVDRYPINVLAKNNFKIIDSHSMNNSGKNSSNSVGSLGWVLESGKTSTARNPKSSSQFDEPRFMQLRELYKLAKVLFDFICPKEYGISDAEKLDIGLLTSLPLAKQILNDIGDMKNRETPACVAYFTKESHIYTLLNIIYESGIPMRIARNALPELDYLSQITFELYESTDASGQKSHSIRLKMSPGCHTQDPLDVQLDDRHYISCIPKISLTKHLDMDYVQQKLRNKFTRVIMPPKFTPVNITSPNLSFQKRKTRRKSVSVEKLKRPASSGSSSSTSVNKTLD
Protein: Protein serine kinase H1 (A0A087WZT9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGCGTSKVLPEPPKDVQLDLVKKVEPFSGTKSDVYKHFITEVDSVGPVKAGFPAASQYAHPCPGPPTAGHTEPPSEPPRRARVAKYRAKFDPRVTAKYDIKALIGRGSFSRVVRVEHRATRQPYAIKMIETKYREGREVCESELRVLRRVRHANIIQLVEVFETQERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVRYLHALGITHRDLKPENLLYYHPGTDSKIIITDFGLASARKKGDDCLMKTTCGTPEYIAPEVLVRKPYTNSVDMWALGVIAYILLSGTMPFEDDNRTRLYRQILRGKYSYSGEVSLSCPCPGCWGGTCGGRYILQLSVRGMSSGPCS
Protein: K-box region and MADS-box transcription factor family protein (A8MQL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLFPHERKKEKERSQGFYLVTRLRIRMGRGKIEIKRIENSTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSTRGRLYEYANNNIRSTIERYKKACSDSTNTSTVQEINAAYYQQESAKLRQQIQTIQNSNRNLMGDSLSSLSVKELKQVENRLEKAISRIRSKKHELLLVEIENAQKREIELDNENIYLRTKVAEVERYQQHHHQMVSGSEINAIEALASRNYFAHSIMTAGSGSGNGGSYSDPDKKILHLG
Protein: CNMamide, isoform B (CNMamide, isoform C) (MIP09392p) (Q9W076)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CNMamide receptor
- Allatostatin C, isoform A
Sequence:
MSALSAPTTCGCSPVHWAIVIVLLSVAIGPGDAMARPARNTQLLFSELLGGGNDDNNYYGDQLKYQQQQQQQQEQKQQRVPAFARKWPSLRDLLLTVDYDDFGVTQESEEQVAPSSRLLARLHRLGDNGGGEELRYNVVNELTNMPSKKVMPGHPLKDHNTKKNVQFRKQYMSPCHFKICNMGRKRNAGFNSY
Protein: Antitoxin RelB3 (Q9A4F5)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the effect of cognate toxin RelE3, but no other RelE or ParE toxin.
Interaction partners:
- Uncharacterized protein
- Toxin RelE3
- Orphan antitoxin ParD2
Sequence:
MSGVIAPDRVDDKRRMEHSQNMALTITIPAELASRLRASAEAEGKDVDAYAIDALHVMSDEDWGYTDDDAYWRELRAHSDEVRRDGGIPLEDVKRWVASWDTENELPPPEPRIKARG
Protein: GTP-binding nuclear protein Ran (EC 3.6.5.-) (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein) (P62827)
Organism: Mus musculus (Mouse)
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation.
Subcellular location: Nucleus {ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:25946333}. Nucleus envelope {ECO:0000269|PubMed:25946333}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000269|PubMed:18347012}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}.
Interaction partners:
- Exportin-1
- Exportin-5
- Ran-specific GTPase-activating protein
- Regulator of chromosome condensation
- E3 SUMO-protein ligase RanBP2
- Exportin-T
- Ran GTPase-activating protein 1
- Importin subunit beta-1
- Snurportin-1
- Eukaryotic translation initiation factor 5A-1
Sequence:
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL