wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear polyadenylated RNA-binding protein NAB2 (P32505)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential protein that binds to polyadenylated RNA and single-stranded DNA. It may be involved not only in RNA processing but also in transcription regulation. Associates directly with nascent RNA polymerase II transcripts and remain associated during subsequent nuclear RNA processing reactions (Probable). Involved in mRNA poly(A) tail length control and nuclear export. Functions in surveillance and the packaging leading to generation of export-competent mRNPs. Controls both mRNP compaction that facilitates movement through nuclear pore complexes and the length of transcript poly(A) tails.
Subcellular location: Nucleus {ECO:0000269|PubMed:11779864, ECO:0000269|PubMed:23222640, ECO:0000269|PubMed:8474438}. Cytoplasm {ECO:0000269|PubMed:11779864}. Note=Localizes to the nucleus at steady-state, it shuttles between nucleus and cytoplasm. {ECO:0000269|PubMed:11779864}.
Interaction partners:
- Nuclear polyadenylated RNA-binding protein 4
- Nuclear cap-binding protein subunit 2
- mRNA transport factor GFD1
- Importin subunit beta-2
- mRNA export factor MEX67
- RNA annealing protein YRA1
- Serine/arginine
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Protein MLP1
- mRNA export factor GLE2
Sequence:
MSQEQYTENLKVIVAEKLAGIPNFNEDIKYVAEYIVLLIVNGGTVESVVDELASLFDSVSRDTLANVVQTAFFALEALQQGESAENIVSKIRMMNAQSLGQSDIAQQQQQQQQQQQPDIAQQQPQQQPQQQPQQQPQQQPQQQPQQQPQQQPQQQPQLQPLQPQLGTQNAMQTDAPATPSPISAFSGVVNAAAPPQFAPVDNSQRFTQRGGGAVGKNRRGGRGGNRGGRNNNSTRFNPLAKALGMAGESNMNFTPTKKEGRCRLFPHCPLGRSCPHAHPTKVCNEYPNCPKPPGTCEFLHPNEDEELMKEMERTREEFQKRKADLLAAKRKPVQTGIVLCKFGALCSNPSCPFGHPTPANEDAKVIDLMWCDKNLTCDNPECRKAHSSLSKIKEVKPISQKKAAPPPVEKSLEQCKFGTHCTNKRCKYRHARSHIMCREGANCTRIDCLFGHPINEDCRFGVNCKNIYCLFRHPPGRVLPEKKGAAPNSNVPTNERPFALPENAIIENAPPQTSFTHQEQDTEMN
Protein: Histone H2B (P23754)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2A
- Histone H2A.Z
- Histone H3
- Histone H3
- Histone H4.1
- Histone H4.2
- RNA polymerase II transcription elongation factor
- FACT complex subunit spt16
- Pol II transcription elongation factor subunit Cdc73, putative
- RNA polymerase II transcription elongation factor Rtf1p, putative
Sequence:
MPPKAAEKKPSTGGKAPAGKAPAEKKEAGKKTAAAASGEKKKRGKTRKETYSSYIYKVLKQVHPDTGISTRAMSILNSFVNDIFERVATEASKLAAYNKKSTISSREIQTSVRLILPGELAKHAVSEGTKAVTKYSSSAK
Protein: Uncharacterized protein (Q4GZG2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDEIKWPLRLLQILRNHLEQVDHPHEPRTLPIAAKCGQGGVLAFLTDVDDDVRRRTGASECITACCRGLVLDMIEQCCTLLFLSSKERRVINMAAVQREKRVVARGVGKRRRGDQGETTEETAIGETDNSQRKCAAVLPLEYLLRLFVALPSLLAHYDKLGGSTMPAAFKQPLWNYVNAVLDIMKDMTFLDPSEYIPLR
Protein: Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (p60 katanin) (Q9VN89)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186, ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03023}. Note=Predominantly cytoplasmic. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1. {ECO:0000256|HAMAP-Rule:MF_03023}.
Interaction partners:
Sequence:
MSITLLRGGKQKTTTCVGMTVMAKTTFEEICENAKLARDMALTGNYDSACIYYEGLQGLLARQLKATADPLRKGKWSMINQQISQEHAKIKAIQRTLQDISLDLQSTKFAHKLRHQLSEESTTSKDPSAWFKPDPDIWTPPPKDPDVWGPPKPPPTTQAVGRRAAPNNRRTTPATQNSRPSSTIPQSTARNGPASTRNSRNSTSATAPSGGARTTNGRAGGRKLSTSNTNEARDDDSTAAGNNGGAAGDGENGDPQAAQEEERKFQPNNHIEAELVDILERDILQKDPKVRWSDIADLHDAKRLLEEAVVLPMLMPDYFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSATLTSKYRGESEKMVRLLFEMARFYAPSTIFIDEIDSLCSRRGSESEHEASRRVKSELLVQMDGVGGGEEQAKVVMVLAATNFPWDIDEALRRRLEKRIYIPLPSDEGREALLKINLREVKVDDSVDLTYVANELKGYSGADITNVCREASMMSMRRKIAGLTPEQIRQLATEEVDLPVSNKDFNEAMSRCNKSVSRADLDKYEKWMREFGSS
Protein: T-box protein 12 (Protein male abnormal 9) (P90971)
Organism: Caenorhabditis elegans
Function: Transcription factor. Involved in cell fate determination; required to pattern the posterior hindgut. Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factor unc-3 in a subset of motor neurons. Required throughout development to repress transcription by unc-3, probably acting by binding to specific promoter elements. Represses expression of VA and VB motor neuron-specific effector genes, such as DEG/ENaC channel del-1 and the innexin inx-12, in DA and DB motor neurons. Represses expression of transcription factor bnc-1, perhaps acting directly, in DA and DB motor neurons.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201, ECO:0000269|PubMed:10716947}.
Interaction partners:
- Transcription factor unc-37
- Homeobox domain-containing protein
- Paired box protein 5 homolog
- Nuclear hormone receptor unc-55
- Putative T-box protein 34
- Basonuclin zinc finger protein homolog
- Homeobox protein unc-4
Sequence:
MSKRCASDRDDKDSEPVKKPRFSIANILDEVEDEEDVEVDVEDVDDVDLSSIPSKSPERSRGRPKIGLKMKEGNLPIECKLEGSELWAKFFDLGTEMIITKSGRRMFPTVKVSFTNVILDALYYIFLDVVPVDSKRYRYIYNKSAWLTAGKAEPVPKNRYYLHPDSPFTGDQLLKHVISFEKTKLTNNEVDKTGHLILNSMHKYQPRIHIVQRQKANPLDPNKVVMSEEKHCTYTFPETQFMAVTAYQNQLITKLKIEKNPFAKGFRDPTGRSPDEMERSPGDMMLSNFYHSSALQQAMFQQCLSKTLQLNPSIMMLYQNVFPTGNSLPAAPTVPGNPAEISIKSE
Protein: At1g76120/T23E18_5 (Pseudouridine synthase family protein) (T23E18.5) (Q9SGS1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- tRNA
Sequence:
MLTTTTDEEIDLSCDGGVTEPQKVAIIFAFCGVGYQGMQKNPGAKTIEGELEEALFHAGAVPESIRGKPKLYDFARSARTDKGVSAVGQVVSGRFIVDPLGFVNRLNSNLPNQIRIFGYKHVTPSFSSKKFCDRRRYVYLLPVFALDPISHRDRETVMASLGPGEEYVKCFECSERGRKIPPGLVGKWKGTNFGTKSLDFQSDISSNNSSALRSDIKIEALSSNLAGLCSVDVEVGRIQEDSCKLNTNSSETKVKSKFCYGEKEKERFSRILSCYVGSYNFHNFTTRTKADDPTANRQIISFTANTVINLDGIDFIKCEVLGKSFMLHQIRKMMGLAVAIMRNCASESLIQSAFSKDVNITVPMAPEVGLYLDECFFTSYNRNFEDSHEEVSMEAYKEEAEAFKLKHIYSHIGATERKYGNMALWLHSLNYRNYPDLNFGSCGQNTDQVLVHKKIDERASHSL
Protein: long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Q8T3L1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFIEDDAQMDSFWVQSAIGAIKAIAFVYDIITLPVYLVLQKPWKRRQDSRRVKAKIVRNDDNELTYRTTDPPRDVHVKMLQENIDTLEKVFNYVAKTYTSKRCLGTRQILSEEDEVQQNGRVFKKYNLGDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPKFKTLLDKCPLVKTIIYIEDQLQKTETTGFKEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLIDTSSKIKRGCKGDATVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFLYQYKVKWVQRGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPNQNHLEELAQKHGLGDKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQHDINRMYAS
Protein: Polyadenylate-binding protein 1 (PABP-1) (Poly(A)-binding protein 1) (P29341)
Organism: Mus musculus (Mouse)
Function: Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11940}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P11940}. Nucleus {ECO:0000250|UniProtKB:P11940}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P11940}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). Shuttles between the cytoplasm and the nucleus (By similarity). During stress and in the absence of DDX3X, localizes to the nucleus (By similarity). At the leading edge of migrating fibroblasts, colocalizes with DDX3X (By similarity). Relocalizes to cytoplasmic stress granules upon cellular stress where it colocalizes with ENDOV (By similarity). {ECO:0000250|UniProtKB:P11940}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Polyadenylate-binding protein-interacting protein 1
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 4B
- Eukaryotic translation initiation factor 4 gamma 1
- Regulator of nonsense transcripts 1
- Y-box-binding protein 1
- Ras GTPase-activating protein-binding protein 1
- Ataxin-2
- Heat shock cognate 71 kDa protein
Sequence:
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKELFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPSLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV
Protein: Vacuolar protein sorting-associated protein 72 (SWR complex protein 2) (Q03388)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in the catalytic exchange of histone H2A for the H2A variant HTZ1, an euchromatin-specific factor, leading to chromatin remodeling and changes in transcription of targeted genes. Indirectly involved in vacuolar protein sorting.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- RuvB-like protein 2
- SWR1-complex protein 4
- SWR1-complex protein 5
- Actin-like protein ARP6
- Protein AF-9 homolog
- RuvB-like protein 1
- Histone H2A.Z
- Vacuolar protein sorting-associated protein 71
- Helicase SWR1
- SWR1-complex protein 7
Sequence:
MSDEGADKSLDTNTEFIIQTRSRRSNAGNKLQKLLEQELRDIESTKRQISSYKNGNDDEEDEIGLLFQEDEDDEDFEMMAKDDDDEGEEKEDETQSIRKEPSQASSEQAADDLMFSSSESEDSSNENDEDAEEKEIRRQELLSRKKRNKRLQKGPVVIKKQKPKPKSGEAIPRSHHTHEQLNAETLLLNTRRTSKRSSVMENTMKVYEKLSKAEKKRKIIQERIRKHKEQESQHMLTQEERLRIAKETEKLNILSLDKFKEQEVWKKENRLALQKRQKQKFQPNETILQFLSTAWLMTPAMELEDRKYWQEQLNKRDKKKKKYPRKPKKNLNLGKQDASDDKKRESEESIKNDGDVNSLGENSSSVHNQKRIEETSTNDTVEGESSPDAAVSRVNSDELKPTALPDVTLDAIANKQSTVDEAPNSQPQKNIITNEQKITNVGEPIQNLHNEEIKDEMVSALESRENTFENSSPAAQVVSQRDNSATPTPSNSTGTEDTILISPDTDIKGEPEPCLKTEGIENLSHNVPQETKSNTDVSFLKQVTFTDHPQVAIIDTEESPSKKDTANVDESSAENSLSTQTYEGPEQLTSRNFVTLYDFPNAPPNLKDFNTNLFGDRWSYTNGLSATQRPQDMKTVFHSILPSPPQSSVPSPTVDISLDLSALANFPSFGEYDKKIVHQINTEINKDLEIKIKTQPPTGVFLANGIRKKCLITNKECQYFDPRTGVPYSDVEAYKIIQRIQDPISKEEGRSDIKRDETTNEDSDDQVRFKWFGFKNGGIYLDLSQRPAKGVPEGF
Protein: Debris buster, isoform F (R9PY22)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MPWLDYFILKNLRLWNDTLSYHYWQRPGVIRLTKLYIYNVTNPDGFLRGEKPHLQEVGPFVYREDMQKVNVKFHENNYTVSYQHKKILQFVPELSIDKDTPITTPNIPLLTLTSLSPKLGYLLSKTISVVVTAAQFKPFINVTAEQLAFGYDDALVSLAHRFYPKHMRPMERMGLLLGRNGTLTEVSSVKTGMDSMDQFGYIDQLNGLDHLPHWSEPPCTSIAGSEGSFFPPRELTKSEVVHIYDKDLCRIIPLKYVESLEKDGIAADLFRLPNNSYGDSAHNPENKCYDTSEYEPIQGLQNISPCQYGAPVYISNPHFFESHPDLLNSVEGLKPEREKHETYFKIQPKLGVPLEGKVRIQLNLKVTRAKDVYPVRDFRDFVFPVMWLEEGISELTPAIKRWIYLGTVIAPSAVPIGSYLMILGGAFAIIFSFVRAYQNFMFAQDPTLEILEMGRRSLRRGSSFIAHQQHRLLVHHRDSYSLLRHGPMATCLGEGNREEDAQPIIDVSLSGGISQES
Protein: Protein EVI2B (Ecotropic viral integration site 2B protein) (EVI-2B) (CD antigen CD361) (Q8VD58)
Organism: Mus musculus (Mouse)
Function: Required for granulocyte differentiation and functionality of hematopoietic progenitor cells through the control of cell cycle progression and survival of hematopoietic progenitor cells.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protein EVI2A
Sequence:
MEFKYLVFIVLCQYLDNTFFSETEAITTEQQSLSTLITPSLYVTTDSQNTAGNALSQTTRFKNISSGQQASPAQITPEQATPAVYVSSSPLTYNITRQAESAVNNSLPQTSPSGFTLTNQPSPSTYNSTGQPPKHLVYTSTQQPPSPAPTSSGKPEVESTHNQPTKSTPTIYLQRDTPPPPPPPLTSEPPSGKGTAHKNNHNAIAAILIGTIIISMLVAILMIILWKYLRKPVLNDQNWAGRSPFADGETPEMCMDNIRESEASTKRASVVSLMTWKPSKSTLLADDLEVKLFESSEHINDTSNLKTDNVEVQINGLSEDSADGSTVGTAVSSDDADLALPPPLLDLDENLPNKPTVTVVSPLPNDSINPQPSPDGLNQVCEEQHSKIQEPFPPPPDSFNVPLSAGDFINNQESAHEAQCQEFSTPDLHPDLTDSLPPPPTELL
Protein: HLA class I histocompatibility antigen C alpha chain (MHC class I antigen) (Major histocompatibility complex, class I, C) (Q5RIP0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRVMAPRTLILLLSGALALTETWACSHSMRYFYTAVSRPGRGEPRFIAVGYVDDTQFVQFDSDAASPRGEPRAPWVEQEGPEYWDRETQKYKRQAQTDRVNLRKLRGYYNQSEAGSHTLQRMYGCDLGPDGRLLRGYNQFAYDGKDYIALNEDLRSWTAADKAAQITQRKWEAAREAEQRRAYLEGTCVEWLRRYLENGKKTLQRAEHPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWGPSSQPTIPIVGIVAGLAVLAVLAVLGAVMAVVMCRRKSSGGKGGSCSQAASSNSAQGSDESLIACKA
Protein: Cag alpha (Cag pathogenicity island protein) (Cag pathogenicity island type IV secretion system ATPase) (Cag-alfa) (CagAlpha protein) (P-type DNA transfer ATPase VirB11) (VirB11-like protein) (Q7BK04)
Organism: Helicobacter pylori (Campylobacter pylori)
Interaction partners:
Sequence:
MTEDRLSAEDKKFLEVERALKEAALNPLRHATEELFGDFLKMENITEICYNGNKVVWVLKNNGEWQPFDVRDRKAFSLSRLMHFARCCASFKKKTIDNYENPILSSNLANGERVQIVLSPVTVNDETISISIRIPSKTTYPHSFFEEQGFYNLLDNKEQAISAIKDGIAIGKNVIVCGGTGSGKTTYIKSIMEFIPKEERIISIEDTEEIVFKHHKNYTQLFFGGNITSADCLKSCLRMRPDRIILGELRSSEAYDFYNVLCSGHKGTLTTLHAGSSEEAFIRLANMSSSNSAARNIKFESLIEGFKDLIDMIVHINHHKQCDEFYIKHR
Protein: Probable hemin degrading factor (Q9HV89)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Heme-transport protein, PhuT
- Hemin import ATP-binding protein HmuV
- Probable permease of ABC transporter
- Heme/hemoglobin uptake outer membrane receptor PhuR
- Haem-binding uptake Tiki superfamily ChaN domain-containing protein
- FAD-binding FR-type domain-containing protein
- PvdO
- Regulatory protein PchR
- Probable histidine/phenylalanine ammonia-lyase
Sequence:
MSSTPSLSHSPAELYRAWQDLRAERPQLRARDAAALLQVSEGELVASRVGIDAVRLRPDWAALLPALGELGPIMALTRNEHCVHERKGPYREVTVSANGQMGLVVSPDIDLRLFLGGWNAVFAIAEETARGTQRSIQVFDQQGVAVHKVFLAEASDVRAWEPLVERLRAAEQDAVLALHEPRAPAAALVDAQIDAAALREGWAALKDTHHFHALLKKHGAQRTQALRLAGGEWAERLDNGDLAKLFEAAAESGLPIMVFVGNAHCIQIHTGPVCNLKWLDDWFNVLDPEFNLHLKTTGIAELWRVRKPSTDGIVTSWEAFDADGELIVQLFGARKPGEPERDDWRELAESFKAL
Protein: Alpha-actinin-4 (Non-muscle alpha-actinin 4) (Q9QXQ0)
Organism: Rattus norvegicus (Rat)
Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000250|UniProtKB:P57780}.
Interaction partners:
- Alpha-actinin-1
- Vinculin
- Nephrin
- Zyxin
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Synaptopodin
- Catenin alpha-1
- LIM domain 7
Sequence:
MVDYHAANQAYQYGPSSGGNGTGGGGGMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTSVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHLRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAAPGALDYKSFSTALYGESDL
Protein: Very-long-chain 3-oxooacyl-coA reductase let-767 (LET-767) (EC 1.1.1.330) (Lethal protein 767) (Short-chain dehydrogenase 10) (Steroid dehydrogenase let-767) (EC 1.1.1.-) (Steroid-dehydrogenase/3-ketoacyl-CoA-reductase) (Q09517)
Organism: Caenorhabditis elegans
Function: Required for branched-chain fatty acid synthesis (such as (omega-1)-methyl-fatty acids). Catalyzes the reduction of the 3-keto-fatty acyl-CoA intermediate that is formed in each cycle of fatty acid elongation. Very long-chain fatty acids (VLCFAs) serve as precursors for ceramide and sphingolipids. Involved in hormone production as it metabolizes 4-androstendione (androst-4-ene-3,17-dione) into testosterone and estrone into estradiol (17beta-estradiol) in vitro, but the physiological steroid substrate is unknown.
Interaction partners:
- Very-long-chain
- Probable very-long-chain enoyl-CoA reductase art-1
- Long chain fatty acid elongase 1
- Long chain fatty acid elongase 5
- Putative fatty acid elongase 3
- Putative steroid dehydrogenase 4
- Putative steroid dehydrogenase 1
- Putative steroid dehydrogenase 2
- Putative steroid dehydrogenase 3
- Long chain fatty acid elongase 6
Sequence:
MACQCFLVGAGYVALAAVAYRLLTIFSNILGPYVLLSPIDLKKRAGASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIGVLINNVGMSYEYPDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVGNTSDTTGYITHQLQLELMDLIPTFIRDKILTNMSVGTRAAALRKKEREAKSQ
Protein: Phosphoserine phosphatase (PSP) (EC 3.1.3.3) (P94512)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. To a lesser extent, is also able to dephosphorylate phosphothreonine, phosphoethanolamine, and histidinol phosphate in vitro.
Interaction partners:
- 5'-nucleotidase YutF
- Putative methyltransferase YqeM
- 5-amino-6-
Sequence:
MKAVFFDLDDTLLWDEKSVRTTFAETCLQAEKKYGLAPEEFEAAVREAARELYMSYETYPYTVMIGINPFEGLWSNFSEPISEGFQKLNKIVPEYRRNAWTNGLKALGIDDPAYGEYLGEFFAAERRKRPFVYDETFAVLDQLKGKYELLLLTNGDPSLQKEKLAGVPELAPYFNEIVISGAFGKGKPDVSIFEHCLKLMNIEKDDAIMVGDNLNTDILGASRAGIKTVWINRTDKKNETDVKPDYIISSLHDLFPILEK
Protein: Junctophilin-1 (JP-1) (Junctophilin type 1) (Q9ET80)
Organism: Mus musculus (Mouse)
Function: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
Subcellular location: Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Sarcoplasmic reticulum membrane; Single-pass type IV membrane protein. Note=Predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic/sarcoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane. In skeletal muscle cells, it is predominantly localized at the junction of the A and I bands.
Interaction partners:
- Ryanodine receptor 1
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Triadin
- Ryanodine receptor 3
- Calsequestrin-2
- Junctophilin-3
- Aspartyl/asparaginyl beta-hydroxylase
- Synaptophysin-like protein 2
- Junctophilin-2
- Voltage-dependent L-type calcium channel subunit alpha-1D
Sequence:
MTGGRFDFDDGGTYCGGWEEGKAHGHGICTGPKGQGEYSGSWSHGFEVVGVYTWPSGNTYQGYWAQGKRHGLGVETKGKWMYRGEWSHGFKGRYGVRQSLCTPARYEGTWSNGLQDGYGVETYGDGGTYQGQWAGGMRHGYGVRQSVPYGMATVIRSPLRTSLASLRSEQSNGSVLHEAAAAAADSPAGTRGGFVLNFHADTELGKKKGGLFRRGSLLGSMKLRKSESKSSISSKRSSVRSDAAMSRISSSDANSTISFGDVDCDFCPVEDHVDATTTETYMGEWKNDKRNGFGISERSNGMKYEGEWANNKRHGYGCTVFPDGSKEEGKYKNNILVRGIRKQLIPIRNTKTREKVDRAIEGAQRAAAMARTKVEIANSRTAHARAKADAADQAALAARQECDIARAVARELSPDFYQPGPDYIKQRCQEGGDIKENPEEKVLEKPPSPKESPHFYRKGTTPPRSPESSPKQSHSPQPSSPEPSKKQNPSPGARLSQDKQSLAEEQVTAFVNKPSMSKAPAKELGASVSKYSGRHHVPNPSNGELHSQYHGYYVKLNTPQHPPEDREDDRGVSQSSSALVPRPSPNKWGPPKSVTKPVAKESKTEPKAKKSELAIPKNPASNDTCPSLEKEANSGPNSIMIVLVMLLNIGLAILFVHFLT
Protein: Alba DNA/RNA-binding protein (At1g20220) (Q944A2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein GAMETOPHYTE DEFECTIVE 1
- Uncharacterized protein At2g34160
- Ribonuclease MRP protein subunit POP4
- Alba DNA/RNA-binding protein
- Ribonucleases P/MRP protein subunit POP1
- Small ribosomal subunit protein mS77
- DEAD-box ATP-dependent RNA helicase 32
- Alba DNA/RNA-binding protein
- UBP1-associated proteins 1B
- Pentatricopeptide repeat-containing protein At4g02820
Sequence:
MDKYQRVEKPKADTPIAENEIRITSMGRARNYITYAMALLQENKSNEVIFKAMGRAINKSVTIVELIKRRIPGLHQITSIGSTDITDTWEPTEEGLQTIETTRHVSMITITLSKEQLNTSSVGYQCPIPIEMVKPLAEIDYEGQDGSPRGRGGRRGRGGRGRGRGRGGRGNGPANVEYDDGGRGRGGRGNGYVNNEYDDGGRGRGGRGSGYVNNEYNDGGMEQDRSYGRGRGRGRGGGRGGRGRGGYNGPPPPYYEAQQDGGDYGYNNVAPPADHGYDGPPPQGRGRGRGRGGRGRGGGRGGFNRSNGAPIQAAA