wanglab/gogpt-training-data huggingface dataset:
Protein: Protein transport protein TIP20 (P33891)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for protein transport between the Golgi and the endoplasmic reticulum. May contribute to tethering of coatomer-coated retrograde transport vesicles to the ER membrane through interaction with and stabilization of the SNARE complex.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8334998}; Peripheral membrane protein {ECO:0000269|PubMed:8334998}.
Interaction partners:
- Syntaxin UFE1
- Protein transport protein SEC39
- Protein transport protein DSL1
- Protein transport protein SEC20
- Protein transport protein USE1
- Protein transport protein SEC22
- Pleckstrin homology domain protein OPY1
- Coatomer subunit delta
- Protein SLY1
- FKBP12-associated protein 1
Sequence:
MNGIDDLLNINDRIKQVQNERNELASKLQNLKQSLASNDTEVALSEVIAQDIIEVGASVEGLEQLRAKYGDLQILNKLEKVAVQQTQMQAGVDKLDSFERQLDELAEQPPDQFTLDDVKALHSKLTSVFATVPQINNIDSQYAAYNKLKSKVTGKYNDVIIQRLATNWSNTFDQKLLEAQWDTQKFASTSVGLVKCLRENSTKLYQLSLLYLPLEEETQNGDSERPLSRSNNNQEPVLWNFKSLANNFNVRFTYHFHATSSSSKIETYFQFLNDYLAENLYKCINIFHDDCNGLTKPVIHEQFINYVLQPIRDKVRSTLFQNDLKTLIVLISQILATDKNLLNSFHYHGLGLVSLISDEVWEKWINYEVEMANRQFINITKNPEDFPKSSQNFVKLINKIYDYLEPFYDLDFDLLVRYKLMTCSLIFMNLTSSYLDYILTVDSLNETRTKEQELYQTMAKLQHVNFVYRKIKSLSSNFIFIQLTDIVNSTESKKYNSLFQNVENDYEKAMSTDMQNSIVHRIQKLLKETLRNYFKISTWSTLEMSVDENIGPSSVPSAELVNSINVLRRLINKLDSMDIPLAISLKVKNELLNVIVNYFTESILKLNKFNQNGLNQFLHDFKSLSSILSLPSHATNYKCMSLHELVKILKLKYDPNNQQFLNPEYIKTGNFTSLKEAYSIKYLKDTKIQDALYRIIYGNIL
Protein: Kinesin-like protein KIN-14P (Q0WN69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g20110
- Cell division cycle protein 27 homolog A
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Protein ENHANCED DISEASE RESISTANCE 2
- Cell division cycle protein 27 homolog B
- Origin of replication complex subunit 3
Sequence:
MNPMRDQPGSPYGDSTPRSPFSPFSPLSVDDRHRNHADTKTPRSPFSPFSPLSGDERHKSLAESKFQQALASSGQLDPLSPGSMHHGGHKFHEVFQMKQGRYDLQASKISEMMKSSSLDNAPTQSLLSVLNGILDESIERKNGEIPQRVACLLRKVVQEIERRISTQAEHLRTQNNIFKTREEKYQSRINVLEALASGTGVEHEIATQQLRQIETEKSMWEEKKKHEEEDMVKLMKQNDQHNLEISALKQELETTKRKYEQQYSQIESQTKTEKSKWEEQKKNEEEDMDKLLKENDQFNLQISALRQELETTRKAYEQQCSQMESQTMVATTGLESRLKELEQEGKVVNTAKNALEERVKELEQMGKEAHSAKNALEEKIKQLQQMEKETKTANTSLEGKIQELEQNLVMWKTKVREMEKKSESNHQRWSQKELSYKSFIDNQSQALLELRSYSRSIKQEILKVQENYTDQFSQLGKKLIELSNAAENYHAVLTENRKLFNELQELKGNIRVFCRVRPFLPAQGAANTVVEYVGEDGELVVTNPTRPGKDGLRQFKFNKVYSPTASQADVFSDIRPLVRSVLDGYNVCIFAYGQTGSGKTYTMTGPDGSSEEDWGVNYRALNDLFKISQSRKGNISYEVGVQMVEIYNEQVLDLLSDDNSQKKTLGILSTTQQNGLAVPDASMYPVTSTSDVITLMDIGLQNRAVGSTALNERSSRSHSIVTVHVRGKDLKTGSVLYGNLHLVDLAGSERVDRSEVTGDRLREAQHINKSLSSLGDVIFSLASKSSHVPYRNSKLTQLLQTSLGGRAKTLMFVQLNPDATSYSESMSTLKFAERVSGVELGAAKTSKEGKDVRDLMEQLASLKDTIARKDEEIERLQHQPQRLQKSMMRRKSIGHTDDINSDTGEYSSQSRYSVTDGESLASSAEAEYDERLSEITSDAASMGTQGSIDVTKRPPRISDRAKSVTAKSSTSVTRPLDKLRKVATRTTSTVAKVTGLTSSSKGLASSSIKKTGSTSSLAKSSKRWA
Protein: Triacylglycerol lipase 1 (EC 3.1.1.3) (Q71DJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Triacylglycerol (TAG) lipase active on triolein, trioctanoin, tributyrin and 1,3-Diolein, but not on phospho- and galactolipids. Involved but dispensable for TAG storage breakdown during seed germination.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Triacylglycerol lipase SDP1
- Triacylglycerol lipase SDP1L
- 7-dehydrocholesterol reductase
- Delta
- Phospholipase A1 PLIP1, chloroplastic
- GDSL esterase/lipase 1
- Receptor-like kinase LIP1
- GDSL esterase/lipase 2
- Triacylglycerol lipase OBL1
- Phospholipase A1 PLIP2, chloroplastic
Sequence:
MKWLLVAVLTSLTIFSALTQSHLLHGSPVNSLCADLIHPANYSCTEHSIQTKDGYILALQRVASLGPRLQSGPPVLLQHGLFMAGDVWFLNSPKESLGFILADHGFDVWVGNVRGTRYSYGHVTLSDTDKEFWDWSWQDLAMYDLAEMIQYLYSISNSKIFLVGHSQGTIMSFAALTQPHVAEMVEAAALLCPISYLDHVTAPLVERMVFMHLDQMVVALGLHQINFRSDMLVKLVDSLCEGHMDCTDFLTSITGTNCCFNASKIEYYLDYEPHPSSVKNIRHLFQMIRKGTFAQYDYGYFKNLRTYGLSKPPEFILSHIPASLPMWMGYGGTDGLADVTDVEHTLAELPSSPELLYLEDYGHIDFVLGSSAKEDVYKHMIQFFRAKVKSSSW
Protein: Amyloid-beta A4 precursor protein-binding family A member 2 (Adapter protein X11beta) (Neuron-specific X11L protein) (Neuronal Munc18-1-interacting protein 2) (Mint-2) (Q99767)
Organism: Homo sapiens (Human)
Function: Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta.
Interaction partners:
- Amyloid-beta precursor protein
- Syntaxin-binding protein 1
- N-terminal EF-hand calcium-binding protein 3
- Calsyntenin-1
- Protein TAMALIN
- Amyloid beta precursor protein binding family B member 2
- Neurexin-1
- Amyloid beta precursor protein binding family B member 1
- Syntaxin-1A
- Peripheral plasma membrane protein CASK
Sequence:
MAHRKLESVGSGMLDHRVRPGPVPHSQEPESEDMELPLEGYVPEGLELAALRPESPAPEEQECHNHSPDGDSSSDYVNNTSEEEDYDEGLPEEEEGITYYIRYCPEDDSYLEGMDCNGEEYLAHSAHPVDTDECQEAVEEWTDSAGPHPHGHEAEGSQDYPDGQLPIPEDEPSVLEAHDQEEDGHYCASKEGYQDYYPEEANGNTGASPYRLRRGDGDLEDQEEDIDQIVAEIKMSLSMTSITSASEASPEHGPEPGPEDSVEACPPIKASCSPSRHEARPKSLNLLPEAKHPGDPQRGFKPKTRTPEERLKWPHEQVCNGLEQPRKQQRSDLNGPVDNNNIPETKKVASFPSFVAVPGPCEPEDLIDGIIFAANYLGSTQLLSERNPSKNIRMMQAQEAVSRVKRMQKAAKIKKKANSEGDAQTLTEVDLFISTQRIKVLNADTQETMMDHALRTISYIADIGNIVVLMARRRMPRSASQDCIETTPGAQEGKKQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDIINTQEMYNDDLIHFSNSENCKELQLEKHKGEILGVVVVESGWGSILPTVILANMMNGGPAARSGKLSIGDQIMSINGTSLVGLPLATCQGIIKGLKNQTQVKLNIVSCPPVTTVLIKRPDLKYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATAHEKIVQALSNSVGEIHMKTMPAAMFRLLTGQETPLYI
Protein: Sterol regulatory element-binding protein 2 (SREBP-2) (Sterol regulatory element-binding transcription factor 2) [Cleaved into: Processed sterol regulatory element-binding protein 2 (Transcription factor SREBF2)] (A3KNA7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 2), which is embedded in the endoplasmic reticulum membrane. Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis.
Subcellular location: [Sterol regulatory element-binding protein 2]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Note=At high sterol concentrations, the SCAP-SREBP is retained in the endoplasmic reticulum. Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed. {ECO:0000250|UniProtKB:Q12772}.; SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding protein 2]: Nucleus {ECO:0000250|UniProtKB:Q12772}.
Interaction partners:
- Sterol regulatory element-binding protein cleavage-activating protein
- Membrane-bound transcription factor peptidase, site 2.
- 3-hydroxy-3-methylglutaryl coenzyme A reductase
- Fatty acid synthase
- NPC intracellular cholesterol transporter 1 isoform X1
- Hydroxymethylglutaryl-CoA synthase
- Insulin-induced gene 1 protein
- Importin subunit beta-1
- P-type phospholipid transporter
- ATP-binding cassette, sub-family G
Sequence:
MDASEFMDTMDPSLSELGDEFTLGDIDEMLQFVSNQVDFPDIFEDQMGGGATARTLPQAVPSAILTPPHTPVQTSSQTHTQTLTQAHTQTHTQTHTQTRTPPVLQPRPQPITQVQTQTFPMQTLAVQTQAQPQTVMITPTATPSRFIQNQVICQQNNATSFQVLQPQMQSIMTSPQVQPMTIQHQRVLTPAGQTIQTLSTAPTTVHTMSQQVPVLVHQPQILKTDSLLLTTKPDGTQVLSTVQSPTGITTLTTPIQTTALQMPTLMSSNILTTVPVVMGGGDKLPIKQLSSGPAHNIGGARVGVEQSPVVGPGGVVKEGERRTTHNIIEKRYRSSINDKILELRDLVLGNDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENLTLKMANQKNKSACVSDVDLELKAEVSLISPPPSDSGSSSPAQLSPYCIDSEPGSPLLEHEQLKSEPDSPSCVGVMDRSRLLLCALSFLCLSLNPLPSLLGAEAPAGSPEVAGHGPTRTLFSLPAQTQSFGAWLWCVLPFLLVWVVSGVGVVWGCVRVLYLWEPVTPLHSPTSVRFWRHRKQADLQLYRGDYAGAVLSLQTCLSVLSRVLPVTTLDIMCSLSWNLIRYCLRRPAPLGWLVRLVGGRHEGEESQTSSRDAALVYHKLSQLQLTGQMERRPLWGVCVSLSAVNLCESAEGKLTATQQVQVYVTAAISVRAALGKHLTCLPAYLLSCAEALTCQSDSKPLPDCLRWIFTPLGRQFFLSCDWSVRSESDGQIFTSARDKADPIAQLHRCFCQKLLERATHTLIEPQSREDAGEFTGVLEFLQLLNSCTEDSAPSTAPFPALANQSSTSVRDPVCRWWASVLTAAVHWLQGDDASVRSLLAEAERMPRALHTLDHPLPKAVLALCKAVQMSVCPQKGEGVVSCLSHCQRASAQLHISVCQSHNNTWLHKGVELLVCDLLLTLRTSLWQRGGGSNGEPGPAPGSQLSGFQRDLSSLRRLGQAHRQAQHKLFLHETTVRLMAGASPTRTHQLLRHRTHNYTTTDGECVLGERERAHAILLACRHLPLPLLTPPGHRARLLAEAKRTLERVGDRRSLQDCQHILLRLSGGTTIAAS
Protein: Diglucosylglycerate octanoyltransferase (DGG octanoyltransferase) (EC 2.3.1.273) (P71725)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sugar octanoyltransferase likely involved in the biosynthesis of mycobacterial methylglucose lipopolysaccharide (MGLP). Catalyzes the transfer of an octanoyl group from octanoyl-CoA to the C6 OH of the second glucose in diglucosylglycerate (DGG). DGG is the preferred acceptor, but to a lesser extent, GG (glucosylglycerate) can also be used as substrate. DGG and GG are the two earliest intermediates in MGLP biosynthesis.
Interaction partners:
- Glucosyl-3-phosphoglycerate phosphatase
- DegV domain-containing protein Rv2417c
- Probable acetyltransferase Rv3034c
- Probable S-adenosylmethionine-dependent methyltransferase Rv3030
- Probable 1,4-alpha-glucan branching enzyme Rv3031
- Ribosomal silencing factor RsfS
- Probable nicotinate-nucleotide adenylyltransferase
- Glycogen synthase
- Octanoyltransferase
- Monoacylglycerol lipase
Sequence:
MSSRRGRRPALLVFADSLAYYGPTGGLPADDPRIWPNIVASQLDWDLELIGRIGWTCRDVWWAATQDPRAWAALPRAGAVIFATGGMDSLPSVLPTALRELIRYVRPSWLRRWVRDGYAWVQPRLSPVARAALPPHLTAEYLEKTRGAIDFNRPGIPIIASLPSVHIAETYGKAHHGRAGTVAAITEWAQHHDIPLVDLKAAVAEQILSGYGNRDGIHWNFEAHQAVAELMLKALAEAGVPNEKSRG
Protein: Histidine-containing phosphotransfer protein (Q9SLX1)
Organism: Zea mays (Maize)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU369004}. Nucleus {ECO:0000256|RuleBase:RU369004}.
Interaction partners:
- histidine kinase
- Two-component response regulator
- Two-component response regulator
- Two-component response regulator
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- Response regulator 8
- ARR-B transcription factor
Sequence:
MAAAALREQLNALLSSMFASGLVDEQFQQLQMLQEDGGTPGFVAEVVTLFCDDADRIISELAALLDQPIVDFDKVDAYVHQLKGSSASVGAQKVKFTCMQFRQLCQDKNRDGCIMALAVVRNEFYDLRNKFQTMLQLEQQIQAQQ
Protein: Phenylalanine ammonia-lyase 2 (EC 4.3.1.24) (P45724)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Trans-cinnamate 4-monooxygenase
- 4-coumarate--CoA ligase 1
- 4-coumarate--CoA ligase 3
- 4-coumarate--CoA ligase-like 9
- 4-coumarate--CoA ligase-like 7
- 4-coumarate--CoA ligase 2
- 4-coumarate--CoA ligase-like 1
- 4-coumarate--CoA ligase-like 6
- 4-coumarate--CoA ligase 4
- Chalcone synthase
Sequence:
MDQIEAMLCGGGEKTKVAVTTKTLADPLNWGLAADQMKGSHLDEVKKMVEEYRRPVVNLGGETLTIGQVAAISTVGGSVKVELAETSRAGVKASSDWVMESMNKGTDSYGVTTGFGATSHRRTKNGTALQTELIRFLNAGIFGNTKETCHTLPQSATRAAMLVRVNTLLQGYSGIRFEILEAITSLLNHNISPSLPLRGTITASGDLVPLSYIAGLLTGRPNSKATGPDGESLTAKEAFEKAGISTGFFDLQPKEGLALVNGTAVGSGMASMVLFEANVQAVLAEVLSAIFAEVMSGKPEFTDHLTHRLKHHPGQIEAAAIMEHILDGSSYMKLAQKVHEMDPLQKPKQDRYALRTSPQWLGPQIEVIRQATKSIEREINSVNDNPLIDVSRNKAIHGGNFQGTPIGVSMDNTRLAIAAIGKLMFAQFSELVNDFYNNGLPSNLTASSNPSLDYGFKGAEIAMASYCSELQYLANPVTSHVQSAEQHNQDVNSLGLISSRKTSEAVDILKLMSTTFLVGICQAVDLRHLEENLRQTVKNTVSQVAKKVLTTGINGELHPSRFCEKDLLKVVDREQVFTYVDDPCSATYPLMQRLRQVIVDHALSNGETEKNAVTSIFQKIGAFEEELKAVLPKEVEAARAAYGNGTAPIPNRIKECRSYPLYRFVREELGTKLLTGEKVVSPGEEFDKVFTAMCEGKLIDPLMDCLKEWNGAPIPIC
Protein: Protease 2 (EC 3.4.21.83) (Oligopeptidase B) (Protease II) (P24555)
Organism: Escherichia coli (strain K12)
Function: Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues.
Interaction partners:
- Thioesterase 1/protease 1/lysophospholipase L1
- Protease ElaD
- Protease 3
Sequence:
MLPKAARIPHAMTLHGDTRIDNYYWLRDDTRSQPEVLDYLQQENSYGHRVMASQQALQDRILKEIIDRIPQREVSAPYIKNGYRYRHIYEPGCEYAIYQRQSAFSEEWDEWETLLDANKRAAHSEFYSMGGMAITPDNTIMALAEDFLSRRQYGIRFRNLETGNWYPELLDNVEPSFVWANDSWIFYYVRKHPVTLLPYQVWRHAIGTPASQDKLIYEEKDDTYYVSLHKTTSKHYVVIHLASATTSEVRLLDAEMADAEPFVFLPRRKDHEYSLDHYQHRFYLRSNRHGKNFGLYRTRMRDEQQWEELIPPRENIMLEGFTLFTDWLVVEERQRGLTSLRQINRKTREVIGIAFDDPAYVTWIAYNPEPETARLRYGYSSMTTPDTLFELDMDTGERRVLKQTEVPGFYAANYRSEHLWIVARDGVEVPVSLVYHRKHFRKGHNPLLVYGYGSYGASIDADFSFSRLSLLDRGFVYAIVHVRGGGELGQQWYEDGKFLKKKNTFNDYLDACDALLKLGYGSPSLCYAMGGSAGGMLMGVAINQRPELFHGVIAQVPFVDVVTTMLDESIPLTTGEFEEWGNPQDPQYYEYMKSYSPYDNVTAQAYPHLLVTTGLHDSQVQYWEPAKWVAKLRELKTDDHLLLLCTDMDSGHGGKSGRFKSYEGVAMEYAFLVALAQGTLPATPAD
Protein: Ribonuclease T2-like (RNase T2-like) (EC 4.6.1.19) (Q02933)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high salt concentration.
Subcellular location: Vacuole lumen. Cytoplasm. Note=Is released from the vacuole to the cytoplasm during stress conditions like oxidative stress or stationary phase stress.
Interaction partners:
Sequence:
MLLKNLHSLLQLPIFSNGADKGIEPNCPINIPLSCSNKTDIDNSCCFEYPGGIFLQTQFWNYFPSKNDLNETELVKELGPLDSFTIHGLWPDNCHGGYQQFCNRSLQIDDVYYLLHDKKFNNNDTSLQISGEKLLEYLDLYWKSNNGNHESLWIHEFNKHGTCISTIRPECYTEWGANSVDRKRAVYDYFRITYNLFKKLDTFSTLEKNNIVPSVDNSYSLEQIEAALSKEFEGKKVFIGCDRHNSLNEVWYYNHLKGSLLSEMFVPMDSLAIRTNCKKDGIKFFPKGYVPTFRRRPNKGARYRGVVRLSNINNGDQMQGFLIKNGHWMSQGTPANYELIKSPYGNYYLRTNQGFCDIISSSSNELVCKFRNIKDAGQFDFDPTKGGDGYIGYSGNYNWGGDTYPRRRNQSPIFSVDDEQNSKKYKFKLKFIKN
Protein: Survival motor neuron protein (P97801)
Organism: Mus musculus (Mouse)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits (By similarity). Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs) (By similarity).
Subcellular location: Nucleus, gem {ECO:0000250|UniProtKB:Q16637}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q16637}. Cytoplasm {ECO:0000269|PubMed:21389246}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q16637}. Perikaryon {ECO:0000250|UniProtKB:Q16637}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q16637}. Cell projection, axon {ECO:0000269|PubMed:21389246}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:17353360}. Note=Colocalizes with actin and at the Z-line of skeletal muscle (PubMed:17353360). Under stress conditions colocalizes with RPP20/POP7 in punctuated cytoplasmic granules. Colocalized and redistributed with ZPR1 from the cytoplasm to nuclear gems (Gemini of coiled bodies) and Cajal bodies. Colocalizes with FMR1 in cytoplasmic granules in the soma and neurite cell processes (By similarity). {ECO:0000250|UniProtKB:Q16637, ECO:0000269|PubMed:17353360}.
Interaction partners:
- Probable ATP-dependent RNA helicase DDX20
- Gem-associated protein 2
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- Serine-threonine kinase receptor-associated protein
- Small nuclear ribonucleoprotein E
- Gem-associated protein 5
- Gem
- Gem-associated protein 8
- Small nuclear ribonucleoprotein G
Sequence:
MAMGSGGAGSEQEDTVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETPDKPKGTARRKPAKKNKSQKKNATTPLKQWKVGDKCSAVWSEDGCIYPATITSIDFKRETCVVVYTGYGNREEQNLSDLLSPTCEVANSTEQNTQENESQVSTDDSEHSSRSLRSKAHSKSKAAPWTSFLPPPPPMPGSGLGPGKPGLKFNGPPPPPPLPPPPFLPCWMPPFPSGPPIIPPPPPISPDCLDDTDALGSMLISWYMSGYHTGYYMGFRQNKKEGKCSHTN
Protein: ATP-dependent DNA helicase hus2/rqh1 (EC 5.6.2.4) (DNA 3'-5' helicase Rqh1) (Q09811)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the repair of UV-induced DNA damage in G2 via recombination-mediated repair. Also has a role in the repair of infrared-induced double DNA strand breaks. Exhibits an ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.
Subcellular location: Nucleus {ECO:0000269|PubMed:12724426}.
Interaction partners:
- DNA topoisomerase 3
- RecQ-mediated genome instability protein 1
- DNA repair protein rhp51
- ATP-dependent DNA helicase srs2
- Exodeoxyribonuclease 1
- Crossover junction endonuclease mus81
- Replication factor A protein 1
- DNA repair and recombination protein rad22
- DNA repair protein rhp57
- Protein kinase rad3
Sequence:
MTVTKTNLNRHLDWFFRESPQKIENVTSPIKTLDFVKVKVSSSDIVVKDSIPHKSKNVFDDFDDGYAIDLTEEHQSSSLNNLKWKDVEGPNILKPIKKIAVPASESEEDFDDVDEEMLRAAEMEVFQSCQPLAVNTADTTVSHSTSSSNVPRSLNKIHDPSRFIKDNDVENRIHVSSASKVASISNTSKPNPIVSENPISATSVSIEIPIKPKELSNNLPFPRLNNNNTNNNNDNNAIEKRDSASPTPSSVSSQISIDFSTWPHQNLLQYLDILRDEKSEISDRIIEVMERYPFSSRFKEWIPKRDILSQKISSVLEVLSNNNNSNNNNGNNGTVPNAKTFFTPPSSITQQVPFPSTIIPESTVKENSTRPYVNSHLVANDKITATPFHSEAVVSPLQSNIRNSDIAEFDEFDIDDADFTFNTTDPINDESGASSDVVVIDDEEDDIENRPLNQALKASKAAVSNASLLQSSSLDRPLLGEMKDKNHKVLMPSLDDPMLSYPWSKEVLGCLKHKFHLKGFRKNQLEAINGTLSGKDVFILMPTGGGKSLCYQLPAVIEGGASRGVTLVISPLLSLMQDQLDHLRKLNIPSLPLSGEQPADERRQVISFLMAKNVLVKLLYVTPEGLASNGAITRVLKSLYERKLLARIVIDEAHCVSHWGHDFRPDYKQLGLLRDRYQGIPFMALTATANEIVKKDIINTLRMENCLELKSSFNRPNLFYEIKPKKDLYTELYRFISNGHLHESGIIYCLSRTSCEQVAAKLRNDYGLKAWHYHAGLEKVERQRIQNEWQSGSYKIIVATIAFGMGVDKGDVRFVIHHSFPKSLEGYYQETGRAGRDGKPAHCIMFYSYKDHVTFQKLIMSGDGDAETKERQRQMLRQVIQFCENKTDCRRKQVLAYFGENFDKVHCRKGCDICCEEATYIKQDMTEFSLQAIKLLKSISGKATLLQLMDIFRGSKSAKIVENGWDRLEGAGVGKLLNRGDSERLFHHLVSEGVFVEKVEANRRGFVSAYVVPGRQTIINSVLAGKRRIILDVKESSSKPDTSSRSLSRSKTLPALREYQLKSTTASVDCSIGTREVDEIYDSQMPPVKPSLIHSRNKIDLEELSGQKFMSEYEIDVMTRCLKDLKLLRSNLMAIDDSRVSSYFTDSVLLSMAKKLPRNVKELKEIHGVSNEKAVNLGPKFLQVIQKFIDEKEQNLEGTELDPSLQSLDTDYPIDTNALSLDHEQGFSDDSDSVYEPSSPIEEGDEEVDGQRKDILNFMNSQSLTQTGSVPKRKSTSYTRPSKSYRHKRGSTSYSRKRKYSTSQKDSRKTSKSANTSFIHPMVKQNYR
Protein: Cathepsin D (EC 3.4.23.5) [Cleaved into: Cathepsin D light chain; Cathepsin D heavy chain] (P00795)
Organism: Sus scrofa (Pig)
Function: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation.
Subcellular location: Lysosome. Melanosome {ECO:0000250}. Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Cathepsin B
- Lysosome-associated membrane glycoprotein 1
- BH3-interacting domain death agonist
- Bcl-2-like protein 1
- Lysosome-associated membrane glycoprotein 2
- Angiotensinogen
- Cathepsin S
- Bis
- Transcription factor EB
- Insulin
Sequence:
GPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSGKSSTYVKNGTTFAIHYGSGSLSGYLSSQDTVSVPCNSALSGVGGIKVERQTFGEATKQPGLTFIAAKFDGILGMAYPRISVNNVVPVFDNLMQQKLVDKDIFSFYLNRDPGAQPGGELMLGGIDSKYYKGSLDYHNVTRKAYWQIHMNQVAVGSSLTLCKGGCEAIVDTGTSLIVGQPEEVRELGKAIGAVPLIQGEYMIPCEKVPSLPDVTVTLGGKKYKLSSENYTLKVSQAGQTICLSGFMGMDIPPPGGPLWILGDVFIGRYYTVFDRDLNRVGLAEAA
Protein: Insulin-like growth factor I (Insulin-like growth factor I precursor) (A4GUE7)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
MSSGHFFQWHVCDVFKSAMCCISCTHTLSLLLCVLTLTSAATGAGPETLCGAELVDTLQFVCGERGFYFSKPTGYGPSSRRSHNRGIVDECCFQSCELRRLEMYCAPVKSGKAARSVRAQRHTDMPRTPKVSTAVQNVDRGTERRTAQHPDKTKTKKEVHQKNSSRGNTGGRNYRM
Protein: Small ribosomal subunit protein uS7cz/uS7cy (30S ribosomal protein S7, chloroplastic) (P0C489)
Organism: Oryza sativa (Rice)
Function: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MSRRGTAEKRTAKSDPIFRNRLVNMVVNRIMKDGKKSLAYQILYRAVKKIQQKTETNPLLVLRQAIRRVTPNIGVKTRRNKKGSTRKVPIEIGSKQGRALAIRWLLEASQKRPGRNMAFKLSSELVDAAKGGGGAIRKKEATHRMAEANRALAHFR
Protein: NFAT nuclear factor, isoform G (M9PH25)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLLKFTKTSGAGPSAVPLLTTAPATVTSSASMQATTTSYAARGTGMRMTMSTNSTMSARIHRKGFRIPSKRQPGKGLPGKLHTITRTGPGKMVPGKRIPQRPHPPPCDNSNDSGLGFDQHTELRSSAGAGGVTDPAANGGSGSNSGQRSSLLVNSALTNTVAAAAAAAAAAVASNTLQQHQQHHQQQQQQQQQQQQQQQQQQQQQQQQQHSPQQHLIRAIPVSRFISARNVTRVANKRQPTTPLNSVASSNDGQVQLEILSQPEQQHRARYQTEGSRGAVKDRSGNGFPIVRLTGYDKVAVLQVFIGTDIGRVAPHMFYQACKVAGKNSTQCNEKKVDGTMVIEIDFKPETDMTITCDCVGILKERNVDVEHRFPEHLAQKNKKKSTRCRMVFRTQLTRDDGTTETLQVCSNPIICTQPPGVPEICKKSLNSCPVDGGLELFIIGKNFLKDTHVVFQETYDSVNGDDPATEIAVRQQLIGGTAALWEQSVLPDKEYLHQTHLICTVPPYLHQNILKPVQVQVSIVSSGKKSEPHTFTYTAKGQYTTLAAASTLSNTIHAQAI
Protein: Hemiasterlin resistant protein 1 (Q09254)
Organism: Caenorhabditis elegans
Interaction partners:
- RING-type domain-containing protein
Sequence:
MVRRRTASPSPSAPVRSAPRPAAQSSFAAPPPRPAAAAPAYHPPAAPTPMGAPMGAPSQGPGLMKQMAATAGGVAIGSAVGHAVGGMFTGGGSSHAEQAPAAAAAPAGAPQASGYSQPCEFEWRQFVDCAQNQSDVSLCNGFNDIFKQCKARYA
Protein: Expansin-A15 (AtEXPA15) (Alpha-expansin-15) (At-EXP15) (AtEx15) (Ath-ExpAlpha-1.3) (O80622)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Subcellular location: Secreted, cell wall. Membrane; Peripheral membrane protein.
Interaction partners:
- At1g30260/F12P21_9
- Endo-1,4-beta-xylanase 4
- Probable xyloglucan endotransglucosylase/hydrolase protein 16
Sequence:
MFMGKMGLLGIALFCFAAMVCSVHGYDAGWVNAHATFYGGSDASGTMGGACGYGNLYSQGYGTNTAALSTALFNNGLSCGACFEIKCQSDGAWCLPGAIIVTATNFCPPNNALPNNAGGWCNPPLHHFDLSQPVFQRIAQYKAGVVPVSYRRVPCMRRGGIRFTINGHSYFNLVLVTNVGGAGDVHSVAVKGSRTRWQQMSRNWGQNWQSNNLLNGQALSFKVTASDGRTVVSNNIAPASWSFGQTFTGRQFR