wanglab/gogpt-training-data huggingface dataset:
Protein: Spn43Ac (Q6V6U4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FSSELFKEIIKSQSQQNVVFSPFSVHALLALIYGASDGKTFRELQKAGEFSKNAMAVAQDFESVIKYKKHLEGADLTLATKVYYNRELGGVNHSYDEYAKFYFSAGTEAVDMQNAKDTAAKINAWVMDTTRNKIRDLVTPTDVDPQTQALLVNAVYFQGRWEHEFATMDTSPYDFQHTNGRISKVAMMFNDXVYGLAELPELGATALELAYKDSATSMLILLPNETTGLGKMLQQLSRPEFDLNRVAHRLRRQSVAVRLPKFQFEFEQDMTEPLKNLGVHQMFTPNSQVTKLMDQPVRVSKILQKAYINVGEAGTEASAASYAKFVPLSLPPKPTEFVANRPFVFAVRTPASVLLI
Protein: Uncharacterized protein, isoform B (Q8IQU2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRDQYCRELKRAKACSKAVKWKYFKELDFLRPYALARNYRGRSGQTSNGAVGTVTPLSLPMTTSFSSNSSSQNLNLSGSIKIEDASASTLLDSCSFSSPSSTDKKPAATFLASHIGAVLQQQQQQQQHQQQMHSQPEANWNYLTDAGGGATPSIIVQCGTANTTTVVDTLYNEIVDCVNAANQSSSAATITSNVSTTSAAHNQSTNAEEEDDDPIHTFLNMESYFEKELITLIQQEDMIYNYGNENYRNAKLKMEVWEEIARKLKKSVKQCRLKWKALRDQYAREHKRLRTLMHIDATSRWKHYNSLSFLQKYIQQKTLESDSQLSMLLPKNDPVRELEDHMTQSHSPPTQQITLESSSSNSQLNLPTLPHLTGPHKAEQQQQQQQQEEQHQQQQQHQQQQQQQQASELCVATYDDMDIENYINGDVHHNDDDVEDDEDEEMETTTAAEQPPQQQDQHVMTYDHEDGPVYMAVPSVGSAMSKQEQLSDGATSLENQQLQSTAEFQKIEIQTPTTPRYQNAATTPSSTSTSRYHSAPITPSKPTHMEYPSSNGHNSGEDDEIGAFFKAVSMKIRNAQLEPVAFTELQIDILRVINEALRNH
Protein: Translocon-associated protein subunit beta (TRAP-beta) (Signal sequence receptor subunit beta) (SSR-beta) (P43308)
Organism: Homo sapiens (Human)
Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- Translocon-associated protein subunit gamma
- Translocon-associated protein subunit delta
- Translocon-associated protein subunit alpha
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit alpha isoform 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Translocating chain-associated membrane protein 1
- Inactive rhomboid protein 2
- Protein transport protein Sec61 subunit gamma
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
Sequence:
MRLLSFVVLALFAVTQAEEGARLLASKSLLNRYAVEGRDLTLQYNIYNVGSSAALDVELSDDSFPPEDFGIVSGMLNVKWDRIAPASNVSHTVVLRPLKAGYFNFTSATITYLAQEDGPVVIGSTSAPGQGGILAQREFDRRFSPHFLDWAAFGVMTLPSIGIPLLLWYSSKRKYDTPKTKKN
Protein: Zinc finger protein 830 (Coiled-coil domain-containing protein 16) (Ovus mutant candidate gene 1 protein) (Q8R1N0)
Organism: Mus musculus (Mouse)
Function: May play a role in pre-mRNA splicing as component of the spliceosome (By similarity). Acts as an important regulator of the cell cycle that participates in the maintenance of genome integrity. During cell cycle progression in embryonic fibroblast, prevents replication fork collapse, double-strand break formation and cell cycle checkpoint activation. Controls mitotic cell cycle progression and cell survival in rapidly proliferating intestinal epithelium and embryonic stem cells. During the embryo preimplantation, controls different aspects of M phase. During early oocyte growth, plays a role in oocyte survival by preventing chromosomal breaks formation, activation of TP63 and reduction of transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:15988037}. Chromosome {ECO:0000269|PubMed:15988037}. Nucleus speckle {ECO:0000269|PubMed:21191184}. Note=Excluded from nucleolus. In metaphase II oocytes and in mitotic blastomeres, it is detected in cytoplasm, suggesting that it is not associated with chromosomes during mitosis. {ECO:0000269|PubMed:15988037}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase E
- Crooked neck-like protein 1
- RNA helicase aquarius
- Papillary Renal Cell carcinoma
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-splicing factor SYF1
- Poly
- Splicing factor 3B subunit 2
- Pre-mRNA-processing factor 19
- SNW domain-containing protein 1
Sequence:
MASSTSTRTPAGKRVVNQEELRRLMREKQRLSTNRKRIESPFAKYNRLGQLSCALCNTPVKSELLWQTHVLGKQHRERVAELKGAKGATQGPSTGTVPQATKRRATDVESQDAKKAKASAGPQVQPSTSASSANLDAARAAPSKPGLGLLPDYDDEEEEEEEGGGEERRDSSKHLPDAQGKEHSLASPRETTSNVLPNDPFNTNPPKAPLVPHSGSIEKAEIHEKVVERRENTAEALPEGFFDDPEVDAKVRKVDAPKDQMDKEWDEFQKAMRQVNTISEAIVAEEDEEGRLDRQIGEIDEQIECYRRVEKLRNRQDEIKNKLKEVLTIKELQKKEEENVDSDDEGELQDLLSQDWRVKGALL
Protein: Trade embargo (Q9VDQ4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Meiotic recombination protein P22
- Meiotic recombination protein W68
Sequence:
MKTESNEKWVVCRVCLNNPSEGEELLHDIFSETASTRLDQMLHICAGIPVSLDDNFPDKMCSKCVRCLRLCYKFRLTCQRSHQHIMDMLDREASNANAAGEGDLLSIAEDLSVESVLKSWEDYASQLDGGMKVEGEEDQQHQVITYVVEDGDTDDTNMFDVHDPTQPVPNEIEEAETYAEYEEYELLTNENSPEIAQEKGSTGTDVATEEPPEEEIAEDILDSDEDYDPTHAKPEKCDRSGRKPVAYHKNSPKVETFKKKVGRKPRNKLSTYICDVCGNIYPTQARLTEHMKFHSGVKPHECEICGRGFVQNQQLVRHMNTHTGNRPYKCNYCPAAFADRSTKTKHHRIHTKERPYVCDVCSRTFTYSDNLKFHKMIHTGEKPHVCDLCGKGFVKAYKLRLHRETHNRRITWRNDAEESTKAEDVKGETPEFLNELPKE
Protein: Isochorismate synthase 1, chloroplastic (AtIcs1) (IcsI) (EC 5.4.4.2) (Enhanced disease susceptibility 16) (Eds16) (Isochorismate mutase 1) (Salicylic acid induction deficient 2) (Sid2) (menF-like protein 1) (Q9S7H8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Isochorismate synthase involved in the synthesis of salicylic acid (SA) required for both local and systemic acquired resistance (LAR and SAR) while SA synthesized through the phenylalanine ammonium lyase (PAL) pathway seems to potentiate plant cell death. Also involved in phylloquinone (vitamin K1) synthesis. Has no isochorismate pyruvate lyase (IPL) activity.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17190832, ECO:0000269|PubMed:18451262}.
Interaction partners:
- anthranilate synthase
- Anthranilate synthase beta subunit 2, chloroplastic
- Anthranilate synthase beta subunit 1, chloroplastic
- anthranilate synthase
- Lipase-like PAD4
- Indole-3-glycerol phosphate synthase, chloroplastic
- indole-3-glycerol-phosphate synthase
- Anthranilate phosphoribosyltransferase, chloroplastic
- Regulatory protein NPR1
- Chorismate synthase, chloroplastic
Sequence:
MASLQFSSQFLGSNTKTHSSIISISRSYSPTPFTRFSRKKYESCSMSMNGCDGDFKTPLGTVETRTMTAVLSPAAATERLISAVSELKSQPPSFSSGVVRLQVPIDQQIGAIDWLQAQNEIQPRCFFSRRSDVGRPDLLLDLANENGNGNGNGTVSSDRNLVSVAGIGSAVFFRDLDPFSHDDWRSIRRFLSSTSPLIRAYGGMRFDPNGKIAVEWEPFGAFYFSVPQVEFNEFGGSSMLAATIAWDDELSWTLENAIEALQETMLQVSSVVMKLRNRSLGVSVLSKNHVPTKGAYFPAVEKALEMINQKSSPLNKVVLARNSRIITDTDIDPIAWLAQLQREGHDAYQFCLQPPGAPAFIGNTPERLFQRTQLGVCSEALAATRPRAASSARDMEIERDLLTSPKDDLEFSIVRENIREKLNGICDRVVVKPQKTVRKLARVQHLYSQLAGRLTKEDDEYKILAALHPTPAVCGLPAEEARLLIKEIESFDRGMYAGPIGFFGGEESEFAVGIRSALVEKGLGALIYAGTGIVAGSDPSSEWNELDLKISQFTKSIEYEATTSLQAIN
Protein: MLO-like protein 8 (AtMlo8) (O22757)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Tetraspanin-2
- Tetraspanin-6
- At5g10750)
- Toll-Interleukin-Resistance
- Tetraspanin-15
- Tetraspanin-10
- Tetraspanin-5
- Disease resistance protein
- Protein HIGH ARSENIC CONTENT 1, mitochondrial
Sequence:
MGIIDGSLLRRLICLCLWCLLGGGVTVVTAEDEKKVVHKQLNQTPTWAVAAVCTFFIVVSVLLEKLLHKVGKVLWDRHKTALLDALEKIKAELMVLGFISLLLTFGQTYILDICIPSHVARTMLPCPAPNLKKEDDDNGESHRRLLSFEHRFLSGGEASPTKCTKEGYVELISAEALHQLHILIFFLAIFHVLYSFLTMMLGRLKIRGWKHWENETSSHNYEFSTDTSRFRLTHETSFVRAHTSFWTRIPFFFYVGCFFRQFFRSVGRTDYLTLRNGFIAVHLAPGSQFNFQKYIKRSLEDDFKVVVGVSPVLWGSFVLFLLLNIDGFKMMFIGTAIPVIIILAVGTKLQAIMTRMALGITDRHAVVQGMPLVQGNDEYFWFGRPHLILHLMHFALFQNAFQITYFFWIWYSFGSDSCYHPNFKIALVKVAIALGVLCLCSYITLPLYALVTQMGSRMKKSVFDEQTSKALKKWRMAVKKKKGVKATTKRLGGDGSASPTASTVRSTSSVRSLQRYKTTPHSMRYEGLDPETSDLDTDNEALTPPKSPPSFELVVKVEPNKTNTGETSRDTETDSKEFSFVKPAPSNESSQDR
Protein: POU domain, class 5, transcription factor 2 (Sperm 1 POU domain transcription factor) (SPRM-1) (Q8N7G0)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds preferentially to the octamer motif (5'-ATGTTAAT-3'). May exert a regulatory function in meiotic events that are required for terminal differentiation of male germ cell (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530}.
Interaction partners:
Sequence:
MAGHRPSNHFCPLPGSGGGGPRGPMPLRVDTLTWLSTQAAPGRVMVWPAVRPGICPGPDVWRIPLGPLPHEFRGWIAPCRPRLGASEAGDWLRRPSEGALPGPYIALRSIPKLPPPEDISGILKELQQLAKELRQKRLSLGYSQADVGIAVGALFGKVLSQTTICRFEAQQLSVANMWKLRPLLKKWLKEVEAENLLGLCKMEMILQQSGKWRRASRERRIGNSLEKFFQRCPKPTPQQISHIAGCLQLQKDVVRVWFYNRSKMGSRPTNDASPREIVGTAGPPCPGAPVCFHLGLGLPVDIPHYTRLYSAGVAHSSAPATTLGLLRF
Protein: Proline-rich protein 5-like (Protein observed with Rictor-2) (Protor-2) (Q6MZQ0)
Organism: Homo sapiens (Human)
Function: Associates with the mTORC2 complex that regulates cellular processes including survival and organization of the cytoskeleton. Regulates the activity of the mTORC2 complex in a substrate-specific manner preventing for instance the specific phosphorylation of PKCs and thereby controlling cell migration. Plays a role in the stimulation of ZFP36-mediated mRNA decay of several ZFP36-associated mRNAs, such as TNF-alpha and GM-CSF, in response to stress. Required for ZFP36 localization to cytoplasmic stress granule (SG) and P-body (PB) in response to stress.
Interaction partners:
- Target of rapamycin complex 2 subunit MAPKAP1
- Rapamycin-insensitive companion of mTOR
- Target of rapamycin complex subunit LST8
- Serine/threonine-protein kinase mTOR
- Proline-rich protein 5
- DEP domain-containing mTOR-interacting protein
- Regulatory-associated protein of mTOR
- Telomere length regulation protein TEL2 homolog
- TELO2-interacting protein 1 homolog
Sequence:
MTRGFAPILPVEFHKMGSFRRPRPRFMSSPVLSDLPRFQAARQALQLSSSSAWNSVQTAVINVFKGGGLQSNELYALNENIRRLLKSELGSFITDYFQNQLLAKGLFFVEEKIKLCEGENRIEVLAEVWDHFFTETLPTLQAIFYPVQGQELTIRQISLLGFRDLVLLKVKLGDLLLLAQSKLPSSIVQMLLILQSVHEPTGPSESYLQLEELVKQVVSPFLGISGDRSFSGPTYTLARRHSRVRPKVTVLNYASPITAVSRPLNEMVLTPLTEQEGEAYLEKCGSVRRHTVANAHSDIQLLAMATMMHSGLGEEASSENKCLLLPPSFPPPHRQCSSEPNITDNPDGLEEGARGSQEGSELNCASLS
Protein: Elongation of fatty acids protein (EC 2.3.1.-) (A0A1D8PGU2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Acyl-CoA desaturase
- Acyl-CoA desaturase
- very-long-chain enoyl-CoA reductase
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain
- Elongation of fatty acids protein
- Very-long-chain
- Fad2p
- 3-oxoacyl-[acyl-carrier-protein] synthase
Sequence:
MSLPIPTWETPFGIQLWPIFDFVASKLSQGKFVPSEFLFINGITPLSTFPEAAVIIVIYYIVIFGGRFVISTLNLPVIKLNGLFQIHNLFLTSLSLTLLVLILEQIIPIFHSGGSYHSICSPNAYTSKLVVLYYLNYITKFIELIDTVFLVLRQKKLTFLHTYHHGATAWLCYTQLTGYTSVQWVPITLNLAVHVVMYWYYFLAARGIRVWWKEWVTRFQIIQFIIDLGVVYYSTFTHFVYKYSGKMRDCSGTETAAVVGCSILTSYLILFISFYITVYKKSGNASKKVKKA
Protein: Thyroid hormone receptor beta (A0A0C4DG57)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQTTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCI
Protein: Transcription factor PRE1 (Basic helix-loop-helix protein 136) (AtbHLH136) (bHLH 136) (Protein BANQUO 1) (Protein PACLOBUTRAZOL RESISTANCE 1) (bHLH transcription factor bHLH136) (Q9FLE9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Atypical and probable non DNA-binding bHLH transcription factor that integrates multiple signaling pathways to regulate cell elongation and plant development. Binds IBH1, forming a pair of antagonistic bHLH transcription factors that function downstream of BZR1 to mediate brassinosteroid regulation of cell elongation. Regulates light responses by binding and inhibiting the activity of the bHLH transcription factor HFR1, a critical regulator of light signaling and shade avoidance. May have a regulatory role in various aspects of gibberellin-dependent growth and development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor IBH1
- Transcription factor PAR1
- Transcription factor HBI1
- Transcription factor PIF4
- Transcription factor HFR1
- Expansin-A8
- Transcription factor BEE 2
- Transcription factor bHLH150
- Auxin-responsive protein IAA19
- Protein BRASSINAZOLE-RESISTANT 1
Sequence:
MSNRRSRQSSSAPRISDNQMIDLVSKLRQILPEIGQRRRSDKASASKVLQETCNYIRNLNREVDNLSERLSQLLESVDEDSPEAAVIRSLLM
Protein: RNA polymerase I-specific transcription initiation factor RRN3 (P36070)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for efficient transcription initiation by RNA polymerase I. Interacts with Pol I in the absence of template DNA and stimulates recruitment of Pol I, but does not remain as part of stable preinitiation complex.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerase I subunit RPA135
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase I subunit RPA190
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase I subunit RPA34
- RNA polymerase I-specific transcription initiation factor RRN7
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MMAFENTSKRPPQDFVAPIDQKKRKVQFSDSTGLVTLQPEEIKDEVFSAAMYSRFVKSALDDLDKNDSTQIGIIANQVALPSKNPERINDKNLNILLDILSSNINRIESSRGTFLIQSIINFEKWWELPPHTLSKYIYFIKILCSSIPKWWQDVSMILVSCFILPIKQTVCHHDMLKYFLRMIPSSMGFIDTYLAKFFPNKNDTRRKLVNYTSNLLKLRGYCSELGFQIWSLLIEKIISIDVELQNELDELDDDVDDDDLEEVDLEDDDDLDDDSGDDDDENCGNSNEELRSGAADGSQSDSEDMDIIEGMDGTEEYNVELTQGIKELSTKLDSILTLVSTHVEEQVTPESLESGEGVGVFNTLTTLFKTHVLPTYYTRSIQYIMFHVSQQQLELMDSFLVTLIDISFAVNEAAEKKIKSLQYLGSYIARAKKLSRTQIIFVASYLTSWLNRYVIEREEEVDQRGGMERFKHFYAAFQALCYIFCFRHNIFRDTDGNWECELDKFFQRMVISKFNPLKFCNENVMLMFARIAQQESVAYCFSIIENNNNERLRGIIGKADSDKKENSAQANTTSSSWSLATRQQFIDLQSYFPYDPLFLKNYKILMKEYYIEWSEASGEYESDGSDD
Protein: Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 (EC 1.14.11.4) (Lysyl hydroxylase 1) (LH1) (Q9R0E2)
Organism: Mus musculus (Mouse)
Function: Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (By similarity). These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Subcellular location: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
Interaction partners:
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
- Procollagen galactosyltransferase 1
- Procollagen galactosyltransferase 2
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Calmodulin-lysine N-methyltransferase
- Collagen alpha-2
- Prolyl 4-hydroxylase subunit alpha-2
- Prolyl 4-hydroxylase subunit alpha-1
- Collagen alpha-1
- von Willebrand factor A domain-containing protein 1
Sequence:
MRSLLLLAPLAWLLLVQAKDDAKLEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQSLGLGEDWSVDGGPAAAGGGQKVRLLKKALEKHADKEDLVILFVDSYDVVFASGPRELLKKFQQAKSQVVFSAEEHIYPDRRLEAKYPTVPDGKRFLGSGGFIGYAPSLSKLVAEWEGQDSDSDQLFYTKIFLNPEKREQINISLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVVVHGNGPTKLQLNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPFLSLFFLRLLRLRYPQKQMRLFIHNQERHHKLQVEQFLAEHGSEYQSVKLVGPEVRMANADARNMGADLCRQDQTCTYYFSVDADVALTEPNSLRLLIEQNKNVIAPLMTRHGRLWSNFWGGLSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRAELQNVDLFHYSKLDSDMSFCANVRQQEVFMFLTNRHTFGHLLSLDNYQTTHLHNDLWEVFSNPEDWKEKYIHENYTKALAGKLVETPCPDVYWFPIFTEAACDELVEEMEHYGQWSLGDNKDNRIQGGYENVPTIDIHMNQITFEREWHKFLVEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDASTFTVNIALNRVGEDYEGGGCRFLRYNCSVRAPRKGWALLHPGRLTHYHEGLPTTKGTRYIAVSFVDP
Protein: KH domain-containing, RNA-binding, signal transduction-associated protein 3 (RNA-binding protein T-Star) (Sam68-like mammalian protein 2) (SLM-2) (Sam68-like phosphotyrosine protein) (O75525)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. Binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). RNA-binding abilities are down-regulated by tyrosine kinase PTK6. Involved in splice site selection of vascular endothelial growth factor. In vitro regulates CD44 alternative splicing by direct binding to purine-rich exonic enhancer (By similarity). Can regulate alternative splicing of neurexins NRXN1-3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners such as neuroligins and LRRTM family members. Targeted, cell-type specific splicing regulation of NRXN1 at AS4 is involved in neuronal glutamatergic synapse function and plasticity (By similarity). May regulate expression of KHDRBS2/SLIM-1 in defined brain neuron populations by modifying its alternative splicing (By similarity). Can bind FABP9 mRNA (By similarity). May play a role as a negative regulator of cell growth. Inhibits cell proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:15901763}. Note=Localized in a compartment adjacent to the nucleolus, but distinct from the peri-nucleolar one.
Interaction partners:
- Protein-tyrosine kinase 6
- KH domain-containing, RNA-binding, signal transduction-associated protein 1
- KH domain-containing, RNA-binding, signal transduction-associated protein 2
- E3 ubiquitin-protein ligase SIAH1
- Heterogeneous nuclear ribonucleoprotein K
- Polypyrimidine tract-binding protein 2
- RNA-binding motif protein, X chromosome
- Protein arginine N-methyltransferase 1
Sequence:
MEEKYLPELMAEKDSLDPSFTHALRLVNQEIEKFQKGEGKDEEKYIDVVINKNMKLGQKVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKSGEAKYFHLNDDLHVLIEVFAPPAEAYARMGHALEEIKKFLIPDYNDEIRQAQLQELTYLNGGSENADVPVVRGKPTLRTRGVPAPAITRGRGGVTARPVGVVVPRGTPTPRGVLSTRGPVSRGRGLLTPRARGVPPTGYRPPPPPPTQETYGEYDYDDGYGTAYDEQSYDSYDNSYSTPAQSGADYYDYGHGLSEETYDSYGQEEWTNSRHKAPSARTAKGVYRDQPYGRY
Protein: Troponin I, slow skeletal muscle (Troponin I, slow-twitch isoform) (P19237)
Organism: Homo sapiens (Human)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin T, slow skeletal muscle
- Troponin T, cardiac muscle
- Troponin C, slow skeletal and cardiac muscles
- Troponin T, fast skeletal muscle
- Myosin-7
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin C, skeletal muscle
- Myosin-6
- Myosin-3
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
Sequence:
MPEVERKPKITASRKLLLKSLMLAKAKECWEQEHEEREAEKVRYLAERIPTLQTRGLSLSALQDLCRELHAKVEVVDEERYDIEAKCLHNTREIKDLKLKVMDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVKKEDTEKERPVEVGDWRKNVEAMSGMEGRKKMFDAAKSPTSQ
Protein: Human immunodeficiency virus type I enhancer binding protein 1 (F8VPM9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPRTKQIHPRNLRDKIEEAQKELNGAEVSKKEVLEAGVKGTSESLKGVKRKKIVAENHLKKIPKSPLRNPLQTKHKQNTEEPPFSVLPSASESHKKHNCVPAKQGRQFTKQNGETPGMTAESSESGDLVSPKKTSSPHQRSELRRWRSEGSDPTRLSGLDGQRDSSSSSSKARTDNSECSSPCCSTTPPSYTSTAFDVLLKAMEPELSTLSQKGSSCAIKTEKLRPNKTVRSPSKLKNSSLDAPNATSPDLVVESPCPPCTSYPVHVASTQKSEQVAAQCVSHLYSSQDHLVPKLSQQNQQLPGHLGFTGSLTNLHTLESTKLEPIYNTAVTSTVGLTSPSTRTQVTPPHQQMDSVSPLSVSPASSTQSPPGPIYSSAHVASVVSQSVEQMCSLLLRDQKPKKQGKYICEYCNRACAKPSVLLKHIRSHTGERPYPCVTCGFSFKTKSNLYKHKKSHAHTIKLGLVLQPEAGGLFLSQECPKALSVHSDIEDSGESDEEGLADGRQNNPCVKDLQPVQTMKTVSNPESLPKLIPSNSDHVVRGFSSQDRPSDSQAPTELPKVVVHPVSMPPLKTDCLQVANPNPELPSPQSPRDLHVASILSHSASVSSLEMDESCHQKGDVIQSEGKPDSHSGTAHAQLQRQQATEDPQEQQGKLLLSPRSLGSTDSGYFSRSESADQAVSPPTPFARTFPTMDPDPAKNGGAPGPRISAPAPSALATGEKSSVVTGQMRPPLATKTLEERISKLISDNEALVDDKQLDSVKPRRTSLSRRGSIDSPKSYIFKDSFQFDLKPMGRRTSSSSDIPKSPFTPTEKSKQVFLLSVPSLDCLPITRSNSMPTTGYSAIPANIIPPPPSLRGSQSFDDKIGTLYDDVFVSGPNPSMPPSGHHRPLVRQAAVEDSTASESHVPGSGQSVDESCQGCPSSSEAGPVQSKAAQTPHLEKKKSHQGRGTMFECETCRNRYRKLENFENHKKFYCSELHGPKTKAAVREAEHGPAPGGAQPQVLHYRVAAPTAVWEQTPQIRKRRKMKSVGDEEDLQPHESGRSPESADALQLQPVPGAAPSPSKHTSATAADQAHRGVQLVARGPERALPLKQCPMVEQQLNAAAQDKMEVKRQGGGISVIQHTNSLSRPNSFDKPEPLEGGITFSLQELGRTGMPGALKVIGMAPEEGHPPQDAMHQTALSHNLRGEPRESARKIPSERYVLGQPLRLVRQHNIQVPEILVTEEPDRDLEAQSHDEEKSEKFTWPQRSETLSKLPTEKLPPKKKRLRLAEIEHSSTESSFESTLSRSLSRESSLSHASSFSASLDLEDISKVELAPKIDFPSKAEFLLIPLGSNTLSVPGSHREMRRAASEQISCVPTLMEVSDFRSKSFDCGSIAPSHVVPALVESQPSYSPSAVGGTAHVPLLERRRGPLIRQISLNIASDSHLSPGSAAALQTIVLPSVNTVPFQAPRLPDMASADCPAHTVHPQALAKDLQAEISSSSSTDTFPPQQLFGAHLLNKTNTSLSHQNTPLPLPVSAQGGKPDAAPTACVSSTGEGSFAPKYQLQCQAFTSDQGCSAPLRSSPNQVLPGQAGADPCPASEAPPAKAADPMAKPCPLPPLELGLPRDEVLQKQLPSFVLPVPQKRNVTVDCFTPVTSLPQILVTQDLPNMPICQTNQSLVPVSEEQNSMPKSQNYLQNASPTPEKELACKTVLPEVGQSVPVSESSPTVQKVSVGRLSPQQESSASSKRMLSPANSLDIAMEKHQKRAKDENGAVCSTNIRALELPSSRANESHKQKKPVLVRQLCTTEPLEGAALEQGACSASGRSSNKAANLTQVLPTDSLSSRPSTFAVTDHVNELQEFKNTKVSTSLTPTVGSFPAPSESACVLPLKSIDNNQEKGSPGVRHEENKVIQGQRPPLVSGLSLVSSSDTQQPSFPSLKTATSFTWCYLLRQKALPLAQNDQKTSAYTGWTVSSSNPNPLGLPTKVALSLLNSKQKTGKSLYCQAITTHSKSDLVVYSSKWKNNLSKRALGNQKATVVEFSNKDDSEINSEQDKENSLIKSEPRRIKIFDGGYKSNEDYVYVRGRGRGKYICEECGIRCKKPSMLKKHIRTHTDVRPYHCSYCNFSFKTKGNLTKHMKSKAHSKKCVDLGVSVGLIDEQDTEESDEKQRFGCERSGYDLEESDGPDEDDNDNEEDDDDSQAESGLSAAPSVTASPQHLPSRSGLQDPGSVEEELRVSSCFSGVHTDPMDILPRALLTKMTVLSTVQSSPNRTDLPAKARQSTEKDEHEQAPPADTPRSPGHQLSVHSSESDVLRSPAAGNPAAGSPGAAVQDSSVGLPPAVAQLNPQPAARISSSVSPHPDSQDQKQQIILQPPPGLPSPQTHLFSHLPLHSQQQSRTPYNMVPVGGIHVVTAGLTYSTFVPIQAGPMQLTIPAVSVIHRTVGTSGDTITEASGAPNRPTGVAELSSVVPCIPIGQIHVPGLQNLSPPALQSLTSLGMETVNLVGLANATVGPQGHPPGLALNAVGLQVLANAPAQSSPAPPAHIQGLQILNIALPTLIPSVGPVAVGTTGTPETTAPNSKAMELQMPAGQGHSAEPPQGSPEGPQETPQTVSGPSADHARPEDSTKMDTKKGPSAGHVLPGRSPAQAQPAPTPEALQKVATSAPPSLPTDRAAPRPPVPHRQPIVHFSDVSSDDDEDRLVIAT
Protein: Claudin-1 (P56745)
Organism: Rattus norvegicus (Rat)
Function: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:11159859}. Cell membrane {ECO:0000269|PubMed:11159859}; Multi-pass membrane protein {ECO:0000269|PubMed:11159859}. Basolateral cell membrane {ECO:0000250|UniProtKB:O95832}. Note=Associates with CD81 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000250|UniProtKB:O95832}.
Interaction partners:
- Tight junction protein ZO-1
- Occludin
- Tight junction protein 2
- CD81 antigen
- Junctional adhesion molecule A
- Tight junction protein 3
- Claudin
- InaD-like protein
- Claudin-12
- Cadherin-1
Sequence:
MANAGLQLLGFILASLGWIGSIVSTALPQWKIYSYAGDNIVTAQAIYEGLWMSCVSQSTGQIQCKVFDSLLNLNSTLQATRALMVIGILLGLIAIFVSTIGMKCMRCLEDDEVQKMWMAVIGGIIFVISGLATLVATAWYGNRIVQEFYDPMTPVNARYEFGQALFTGWAAASLCLLGGALLSCSCPRKTTSYPTPRPYPKPTPSSGKDYV