wanglab/gogpt-training-data huggingface dataset:
Protein: Neurotrophic factor BDNF precursor form (proBDNF) (Abrineurin) (Brain-derived neurotrophic factor) [Cleaved into: Neurotrophic factor BDNF] (P23560)
Organism: Homo sapiens (Human)
Function: Important signaling molecule that activates signaling cascades downstream of NTRK2. During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
Subcellular location: Secreted {ECO:0000269|PubMed:11152678, ECO:0000269|PubMed:19467646, ECO:0000269|PubMed:8527932}.; SUBCELLULAR LOCATION: [Neurotrophic factor BDNF precursor form]: Secreted {ECO:0000269|PubMed:11152678, ECO:0000269|PubMed:19467646}. Note=A proportion of BDNF is secreted as immature precursor (proBDNF). {ECO:0000269|PubMed:11152678, ECO:0000269|PubMed:19467646}.
Interaction partners:
- BDNF/NT-3 growth factors receptor
- Tumor necrosis factor receptor superfamily member 16
- High affinity nerve growth factor receptor
- NT-3 growth factor receptor
- Sortilin
- Neurotrophin-3
- Neurotrophin-4
- Methyl-CpG-binding protein 2
- Glial cell line-derived neurotrophic factor
- Cyclic AMP-responsive element-binding protein 1
Sequence:
MTILFLTMVISYFGCMKAAPMKEANIRGQGGLAYPGVRTHGTLESVNGPKAGSRGLTSLADTFEHVIEELLDEDQKVRPNEENNKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR
Protein: Protein phosphatase 1 regulatory subunit 3B (Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL) (Protein phosphatase 1 regulatory subunit 4) (PP1 subunit R4) (Protein phosphatase 1 subunit GL) (PTG) (Q86XI6)
Organism: Homo sapiens (Human)
Function: Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes (By similarity).
Interaction partners:
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Glycogen [starch] synthase, liver
- Glycogen [starch] synthase, muscle
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit 3D
- Protein phosphatase 1 regulatory subunit 3A
- Protein phosphatase 1 regulatory subunit 3E
- Protein phosphatase 1 regulatory subunit 3F
- Malignant fibrous histiocytoma-amplified sequence 1
Sequence:
MMAVDIEYRYNCMAPSLRQERFAFKISPKPSKPLRPCIQLSSKNEASGMVAPAVQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDMPFNITELLDNIVSLTTAESESFVLDFSQPSADYLDFRNRLQADHVCLENCVLKDKAIAGTVKVQNLAFEKTVKIRMTFDTWKSYTDFPCQYVKDTYAGSDRDTFSFDISLPEKIQSYERMEFAVYYECNGQTYWDSNRGKNYRIIRAELKSTQGMTKPHSGPDLGISFDQFGSPRCSYGLFPEWPSYLGYEKLGPYY
Protein: T. brucei spp.-specific protein (Q581D4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCPVRMVPKVVMITEELFRSFVEQAWGGATGVRTENNEAGPQHTQQQHPNHGSVPTSAISHLITTPFTARACSPLDYPNLLMAYHRASKNALLRYHYDAPILQPRMIYSHPKRPTPASLEHAHSSRPTQSQHQHSQYYHPRHAQRQHRAIPRHAHEAAGARPRPSPHTRAHREAEASLSSASILLPATASDTLPRTSGYTDLRITPVMLSRASTSWPHEGVEDYMLEKPTVVAEEGVRPSWSPQQVRYRPPTSSTSSNNAHQRISSGMSMEVLNYGGFADEHDEEYDNSNNEGQYNPLDYGQKDVEEPEGRSTVWLDARDATDGFRSSQRYRYSTNARNSHHPHRTETEDFSRTSGALEQSAHWHVHSHRQTVELDSNYEEASRRTYAWRASDGGEIFLATHSTRRSTLLDDRHV
Protein: Uncharacterized protein orf153 (Q2F975)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MSRASSYAAGSSFVVSREAPVKRIVGLAFQYWKLELQIGITTLGFKTTTSASFFAHRGSFVNSPEDHWNRNQYPWPHNSNLPNYSTYIPNHYPPPQNESNPGQGPCNCTSMPNPMWVANYTVQILVSKPMIQGPCHKINSKNIIIRTRFLLIS
Protein: Bcl-2/adenovirus E1B 19 kDa-interacting protein 2-like protein (Q7Z465)
Organism: Homo sapiens (Human)
Function: May be a bridge molecule between BCL2 and ARHGAP1/CDC42 in promoting cell death.
Interaction partners:
- Apoptosis regulator Bcl-2
- FAD-linked sulfhydryl oxidase ALR
- Annexin A5
Sequence:
MGTIQEAGKKTDVGVREIAEAPELGAALRHGELELKEEWQDEEFPRLLPEEAGTSEDPEDPKGDSQAAAGTPSTLALCGQRPMRKRLSAPELRLSLTKGPGNDGASPTQSAPSSPDGSSDLEIDELETPSDSEQLDSGHEFEWEDELPRAEGLGTSETAERLGRGCMWDVTGEDGHHWRVFRMGPREQRVDMTVIEPYKKVLSHGGYHGDGLNAVILFASCYLPRSSIPNYTYVMEHLFRYMVGTLELLVAENYLLVHLSGGTSRAQVPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALLRPFISSKFTRKIRFLDSLGELAQLISLDQVHIPEAVRQLDRDLHGSGGT
Protein: Uncharacterized protein C15D4.13c (A6X982)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS17m
- Putative thiosulfate sulfurtransferase, mitochondrial
- Small ribosomal subunit protein mS29
- RQC trigger complex subunit RQT4 homolog
- RQC trigger complex helicase rqt2
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL29m
Sequence:
MRYPNLLFLALPISEHYIEESLKYFKLTSNDPMILSGFRGPRVSHLTIGMIPVKNDEDVLKCMDFLYNKEDEIRKSYGEKKITIDLKGTSFFGKSPQEAKVLYATPVDKHNEWLKVIFTEHNLFTKDARPLTLHCTLLNSRYIKYQGRRIRFFNSEPFMEKYGQFLWAHNIELDKLSIMKTGAVGEPGNMYYEELASIPLLVND
Protein: A-kinase anchoring protein beta (Q2VEB3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
MTTSQAKTKSFDSWSYSEMEKEFPELIRSVGLLTVATEPVPSSCGAANEDSSQVILSEDHRGGHEEDGALEPGEQLGSTLETSSLGDTLTNAAEHPPETANQDSTSSPQLGAKKSQPGPCEMMTPKRSIRDCFNYNEDSPTQPTLPKRGLFLKETLKNERRGSDGKGRVVDLKPELSRSTPSLVEPPDRSKLCLVLQSSYPSSPSAASQSYECLHKVGIGNLENIVRSHIKEISSSLGRLTDCHKEKPRLKKPHKTLAEVSLCKIPKRGTGSGKQSENTRSSVVPTMVSPGAPKATARPATDSASTTSGDTCHQRNRGGKLPAQSKASSSSPCSHSSESSLGSDNIKSPLPLLSKSQKGSPPAPCHATQNGQVVEAWYGSDEYLALPSHLKQTEVLALKLENLTKLLPQKPRGETIQDIDDWELSEMNSDSEIYPTYHIKKKHTRLGTVSPSSSSDIASSLGESIESGPLSDILSDEDLCMPLSGMKKFTDEKSERPSSSEKNESHSATKSALIQKLMKDIQHQDNYEAIWERIEVGFVNKLDEFIQWLNEAMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLKMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEAQLCYLEAQRDAVEQMSLKLYSEQYTSGSKRKEEFADMSKAHSVGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEKVDSINEKWELLGKTLREKIQDTMAGHSGSGPRDLLSPESGSLVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEGTSAEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLRKKMGKESETLNVIDPGLMDLNGMSEDALEWDETDISNKLISVHEESNDLDQDLEPMVPTVKLEETHHKDSGYEEEAGDCGGSQYTSNITAPSSPHIYQVYSLHNVEFHEDSHTQFLKSSPKFTGTVQPTVLTKSLSKDSSFSSTKSLPDLLGGSSLVRPYSCQSGDLSQNSGSESGIVSEGDNEMPTNSDMSLFSMVDGSPSNPETQHLDPQMGDAANVLEQKFKDEGECIKLSSVSQASVSPVGCVNGKAGDLNSITKHTTDCLGDELQGKHEVFTFYDYSYLQGSKLKFPMIMKQPQSEKAHLEDPLLRGFYFDKKSCKPKHQTSESQPDAPLHEKILASAPHEMGRSSYKSSDIEKALTGIQNARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFSGQMSLDVASSINEDSPASLTELSSSDELSLCSEDIVLHKNKVPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLSREKKRPSVTDEIKVNKDGGSTERANPSDTLDIEALLNCSIKRLSENNGNGKNPPRTHDLGTKGENKKNTYDVTKDPHVADMENGNVESTPEREKEKPEIPEASANLASNVKKISESKHDEYEALMDGSDDSSVTGKEFGPPNDRHPPQIGADPQHPERGDCTSVQNSCSGLLLETGGGSRQDSDGLKSLSNDAPSVARNAAGCCLLEQNETEESASISSSTSCCNCKPDVFHQKDDEDCSVHDFVKEIIDMASTALKSKSQPESEVAAPTSLTQIKEKVLEHSHRPIHLRKGDFYSYLSLSSHDSDCGEVTNYIDEKSNTPLPPDTVDSGLDDKEDVDCFFEACVEDEPADEEARLSSALPNESEVQDEAAKPEQMTASSSVFRDETDTVPLSGLSPQKGADDAKEGDGASHTSQGCVESAEPTTPPGKAKREGSSRKQSVSGTPEENAASAKPKIQAFSLNAKQPKGKAALYPSPQTLTCKEKLVSFHEDRHSNMHR
Protein: Citron rho-interacting kinase (CRIK) (EC 2.7.11.1) (Rho-interacting, serine/threonine-protein kinase 21) (E9PSL7)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in cytokinesis (By similarity). Required for KIF14 localization to the central spindle and midbody (By similarity). Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1 (By similarity). It probably binds p21 with a tighter specificity in vivo (By similarity). Displays serine/threonine protein kinase activity (By similarity). Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P49025}.
Interaction partners:
- Transforming protein RhoA
- Kinesin-like protein KIF14
- Assembly factor for spindle microtubules
- Anillin
- Protein regulator of cytokinesis 1
- Anillin
- Rhophilin, Rho GTPase-binding protein 1.
- Kinesin-like protein
Sequence:
MLKFKYGVRNPSEASAPEPIASRASRLNLFFQGKPPLMTQQQMSALSREGVLDALFVLLEECSQPALMKIKHVSSFVRKYSDTIAELRELQPSVRDFEVRSLVGCGHFAEVQVVREKATGDVYAMKIMKKAALRAQEQVSFFEEERNILSQSTSPWIPQLQYAFQDKNNLYLVMEYQPGGDLLSLLNRYEDQLDENMIQFYLAELILAVHSVHQMGYVHRDIKPENILIDRTGHIKLVDFGSAAKMNSNKVDAKLPIGTPDYMAPEVLTVMNEDRRGTYGLDCDWWSVGVVAYEMLYGKTPFTEGTSARTFNNIMNFQRFLKFPDDPKVSSELLDLIQSLLCVQKERLKFEGLCCHPFFARTDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFSYSKALGYLGRSESVVSGLDSPAKISSMEKKLLIKSKELQDSQDKCHKMEQEMARLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKAKDLGKPEVGECSRLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLETMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKEASTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKVSSPGLQSKEPSSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHIPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDVSPNIFEAVKGCHLFAAGKIENSLCICAAMPSKVVILRYNDNLSKFCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFASSTNSFPVSIVQANSTGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSLGTPARAYLEIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEQHRVPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYRDREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV
Protein: Magnesium-protoporphyrin O-methyltransferase (EC 2.1.1.11) (Magnesium-protoporphyrin IX methyltransferase) (P26236)
Organism: Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Function: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX methylester using S-adenosyl-L-methionine as a cofactor.
Interaction partners:
Sequence:
MPSDYAEIRNRVEHYFDRTATRAWARLTTADEKVSKVRQTVREGRDTMRAVMLSRLPDDLTGCRVMDAGCGTGLTTVELARRGADVVAVDISPQLIDIAKDRLPPELRGKVSFHVGDMADPALGQFDYVVAMDSLIYYRAPDIGRVLTELGKRTHSAIVFTVAPKTAFLMAFWWLGKLFPRSNRSPVMIPHALDKLQRHAGDSLIKIDRVARGFYISECLEYRP
Protein: Mastermind-like domain-containing protein 1 (F18) (Protein CG1) (Q13495)
Organism: Homo sapiens (Human)
Function: Transactivates the HES3 promoter independently of NOTCH proteins. HES3 is a non-canonical NOTCH target gene which lacks binding sites for RBPJ.
Subcellular location: Nucleus {ECO:0000269|PubMed:18162467}. Note=Punctate nuclear localization.
Interaction partners:
- Myotubularin
- Phosphatidylinositol-3-phosphate phosphatase MTMR1
- Protein FAM118B
- Androgen receptor
- Zinc finger translocation-associated protein
- Mastermind-like protein 3
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
Sequence:
MDDWKSRLVIKSMLPHFAMVGNRQEPRKLQESGKKPSWMEEEDLSFLYKSSPGRKHQGTVKRRQEEDHFQFPDMADGGYPNKIKRPCLEDVTLAMGPGAHPSTACAELQVPPLTINPSPAAMGVAGQSLLLENNPMNGNIMGSPFVVPQTTEVGLKGPTVPYYEKINSVPAVDQELQELLEELTKIQDPSPNELDLEKILGTKPEEPLVLDHPQATLSTTPKPSVQMSHLESLASSKEFASSCSQVTGMSLQIPSSSTGISYSIPSTSKQIVSPSSSMAQSKSQVQAMLPVALPPLPVPQWHHAHQLKALAASKQGSATKQQGPTPSWSGLPPPGLSPPYRPVPSPHPPPLPLPPPPPPFSPQSLMVSCMSSNTLSGSTLRGSPNALLSSMTSSSNAALGPAMPYAPEKLPSPALTQQPQFGPQSSILANLMSSTIKTPQGHLMSALPASNPGPSPPYRPEKLSSPGLPQQSFTPQCSLIRSLTPTSNLLSQQQQQQQQQQQANVIFKPISSNSSKTLSMIMQQGMASSSPGATEPFTFGNTKPLSHFVSEPGPQKMPSMPTTSRQPSLLHYLQQPTPTQASSATASSTATATLQLQQQQQQQQQQPDHSSFLLQQMMQQPQRFQRSVASDSMPALPRQGCCHLFAWTSAASSVKPQHQHGNSFTSRQDPQPGDVSPSNITHVDKACKLGEARHPQVSLGRQPPSCQALGSESFLPGSSFAHELARVTSSYSTSEAAPWGSWDPKAWRQVPAPLLPSCDATARGTEIRSYGNDP
Protein: Probable transport protein MmpL6 (P9WJU9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable membrane protein
- F420H
- Probable transcriptional regulatory protein
- Probable oxidoreductase
- Small ribosomal subunit protein uS9
- Probable conserved transmembrane transport protein MmpL13a
Sequence:
MQGISVTGLVKRGWMVRSVFDTIDGIDQLGEQLASVTVTLDKLAAIQPQLVALLPDEIASQQINRELALANYATMSGIYAQTAALIENAAAMGQAFDAAKNDDSFYLPPEAFDNPDFQRGLKLFLSADGKAARMIISHEGDPATPEGISHIDAIKQAAHEAVKGTPMAGAGIYLAGTAATFKDIQDGATYDLLIAGIAALSLILLIMMIITRSLVAALVIVGTVALSLGASFGLSVLVWQHLLGIQLYWIVLALAVILLLAVGSDYNLLLISRFKEEIGAGLNTGIIRAMAGTGGVVTAAGLVFAATMSSFVFSDLRVLGQIGTTIGLGLLFDTLVVRAFMTPSIAVLLGRWFWWPQRVRPRPASRMLRPYGPRPVVRELLLREGNDDPRTQVATHR
Protein: Guanylate binding protein 1 (B2XWS1)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MASKVHMPEPQCLIENINGRLVVNPKALKLLSAIKQPLVVVAIVGLYRTGKSYLMNKLAGKNKGFSLGSTVQSHTKGIWMWCVPHPKKREHTLALLDTEGLGDVEKGDNQNDSWIFALAILLSSTFVYNSMGTINQQAMDQLHYVTELTERIRAKSEPDEGIEDSADFVSFFPDFVWTLRDFSLDLETDGESITADEYLENSLKLKKGTSQKDKNFNLPRLCIRKFFPKKKCFIFDRPTQRKKLGQLEDLGDDELDSEFVQQAAEFCSYIFLNSKTKTLSGGIKVTGPRLETLVLTFVNTISSGDLPCVENAVLALAEIENSAAVQKAIAHYEQQMAEKLQLPTETLQELLDLHRDVEKEAIDIFMKNSFKDEENVFQKELATKLDKKRDEFCDQNVKASSERCSALIKEIFSPLEEGVKQGLYSKSGGYRLYVEKKEELKIKYLETPRKGLQAEEILQEYLKSKESVGEAILQTDQTLSEKEKQIEVERVRAEAAQAAAKMLEEMQIRNQQIMEQKEKSYQEHVRQLAEKMEKDRAQMLEEQERTMALKLQEQARLIQEGFQEENRRLHNEIQNLQKKMKKSKKECFLS
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (Q0KI98)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tyrosine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, mitochondrial
- serine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- serine--tRNA ligase
- Lysine--tRNA ligase
- Tyrosine--tRNA ligase, mitochondrial
- leucine--tRNA ligase
- histidine--tRNA ligase
Sequence:
MADTKETVVEGVEALTLNGKPDAEPVETGTDAQAQEGATAPTEDVVDPWNVASSNDAGVDYDKLIKRFGSSKIDEELIARFEKITGKPAHHFIRRGMFFSHRDLHTILTLREQGKPFYLYTGRGPSSGSLHVGHLVPFIMTKWLQETFDVPLVIQLTDDEKTLWKDLKVEDAIKLGRENAKDIVAIGFDVNKTFIFNNLEFVGKCPAMYQNIIRIQKCVTFNQVKGIFGFGDSDIIGKIGFPAAQAAPAISSTFPFIFGNRKVHCLIPCAIDQDPYFRMTRDVAPRLGFPKCALIHSTFFPALQGAKTKMSASDQNSAVYLTDTPKQIKNKINKYAFSGGRVSVEEHRKLGGVPEVDVSYQLLKFFLEDDAKLEEVRVAYSKGEMLTGEIKKLAVETLTPIVEQHQAARKLITDEVLDKYFELRPLKFGS
Protein: DNA ligase 4 (EC 6.5.1.1) (DNA ligase IV) (Polydeoxyribonucleotide synthase [ATP] 4) (Q8BTF7)
Organism: Mus musculus (Mouse)
Function: DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination. Catalyzes the NHEJ ligation step of the broken DNA during DSB repair by resealing the DNA breaks after the gap filling is completed. Joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. LIG4 is mechanistically flexible: it can ligate nicks as well as compatible DNA overhangs alone, while in the presence of XRCC4, it can ligate ends with 2-nucleotides (nt) microhomology and 1-nt gaps. Forms a subcomplex with XRCC4; the LIG4-XRCC4 subcomplex is responsible for the NHEJ ligation step and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. LIG4 regulates nuclear localization of XRCC4.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P49917}.
Interaction partners:
- Non-homologous end-joining factor 1
- DNA repair protein XRCC4
- X-ray repair cross-complementing protein 5
- X-ray repair cross-complementing protein 6
- DNA-dependent protein kinase catalytic subunit
- TP53-binding protein 1
- DNA repair protein XRCC1
- DNA mismatch repair protein Msh6
- Protein artemis
- Serine-protein kinase ATM
Sequence:
MASSQTSQTVAAHVPFADLCSTLERIQKGKDRAEKIRHFKEFLDSWRKFHDALHKNRKDVTDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPREGKDAQKLLNYRTPSGARTDAGDFAMIAYFVLKPRCLQKGSLTIQQVNELLDLVASNNSGKKKDLVKKSLLQLITQSSALEQKWLIRMIIKDLKLGISQQTIFSIFHNDAVELHNVTTDLEKVCRQLHDPSVGLSDISITLFSAFKPMLAAVADVERVEKDMKQQSFYIETKLDGERMQMHKDGALYRYFSRNGYNYTDQFGESPQEGSLTPFIHNAFGTDVQACILDGEMMAYNPTTQTFMQKGVKFDIKRMVEDSGLQTCYSVFDVLMVNKKKLGRETLRKRYEILSSTFTPIQGRIEIVQKTQAHTKKEVVDALNDAIDKREEGIMVKHPLSIYKPDKRGEGWLKIKPEYVSGLMDELDVLIVGGYWGKGSRGGMMSHFLCAVAETPPPGDRPSVFHTLCRVGSGYTMKELYDLGLKLAKYWKPFHKKSPPSSILCGTEKPEVYIEPQNSVIVQIKAAEIVPSDMYKTGSTLRFPRIEKIRDDKEWHECMTLGDLEQLRGKASGKLATKHLHVGDDDEPREKRRKPISKTKKAIRIIEHLKAPNLSNVNKVSNVFEDVEFCVMSGLDGYPKADLENRIAEFGGYIVQNPGPDTYCVIAGSENVRVKNIISSDKNDVVKPEWLLECFKTKTCVPWQPRFMIHMCPSTKQHFAREYDCYGDSYFVDTDLDQLKEVFLGIKPSEQQTPEEMAPVIADLECRYSWDHSPLSMFRHYTIYLDLYAVINDLSSRIEATRLGITALELRFHGAKVVSCLSEGVSHVIIGEDQRRVTDFKIFRRMLKKKFKILQESWVSDSVDKGELQEENQYLL
Protein: Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Fatty acid activator 1) (Long-chain acyl-CoA synthetase 1) (O60135)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. It may supplement intracellular myristoyl-CoA pools from exogenous myristate. Preferentially acts on C12:0-C16:0 fatty acids with myristic and pentadecanic acid (C15:0) having the highest activities (By similarity). Appears to play a role in the maintenance of cell viability during stationary phase.
Interaction partners:
- Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1
- Long-chain-fatty-acid--CoA ligase 2
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Fatty acid synthase subunit alpha
- Triacylglycerol lipase ptl1
- Putative monoglyceride lipase
- Triacylglycerol lipase ptl3
- Putative lipase atg15
- Secretory component protein psh3
- Vacuolar ATPase assembly integral membrane protein vph2
Sequence:
MKVQSKAISKPKEHESAIYRNANFPDHLVETYSDDVHTLFDVFRHSVKQFGNKKAMGYRNLVKEHVETKMVTKVVDGEKKEVPKSWSYFELSDYNYLSFNDIYDKALRYAGALRKLGLNKGDKFELYAPTSAFWLLTAEACLSQSMTIVTAYDTLGEEGLLHSLRESGVRGMYTEGHLLKTLVNPLKEIESLEVIIYRNDAKEEDIKTIQEIRPNLKLIKFADFEKMSPPVEPDPPSPEEICCIMYTSGSTGLPKGVILSHKNMVAIVTAIVKHVPEVTSKDYLLAYLPLAHILEFAFENICLAWGGTIGYANVRTLVDTNCRNCKGDINTFRPTIMVGVPAVWEMVRKGIMSKLNAASAVKRSVFWTAYYTKAKLMRHNLPGSCVLDTAVFNKIRSMGTGGRLRYTLSGGSALSPDTKRFLSIVLCPMLIGYGLTEISAAAMVQNPACFNLDDSAGSLLPCTEMKLVDCEEGNYNSHGHPPRGEIWLRGPSLTRGYLNRDKENKESFTPDGWFRTGDVGELTPEGLLRIIDRKKNLVKTQNGEYIALEKLESRYRTSSLVSNICVYADQTKVKPLAIIVPNEPVVRKLATEQAGLSPDASWEEVCHNKKVRQLVYDDLIRIGRSHHFANIELIQNVVLVPIEFTPENGLVTAAQKLQRRKILDRFKKEIDAAYAE
Protein: Low-temperature-induced 65 kDa protein (Desiccation-responsive protein 29B) (Q04980)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- BURP domain protein RD22
- Protein COLD-REGULATED 15A, chloroplastic
- Probable peroxygenase 3
- Dehydration-responsive element-binding protein 2A
- Dehydrin COR47
- Protein phosphatase 2C 56
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
- ABSCISIC ACID-INSENSITIVE 5-like protein 5
- ABSCISIC ACID-INSENSITIVE 5-like protein 6
- Delta-1-pyrroline-5-carboxylate synthase A
Sequence:
MESQLTRPYGHEQAEEPIRIHHPEEEEHHEKGASKVLKKVKEKAKKIKNSLTKHGNGHDHDVEDDDDEYDEQDPEVHGAPVYESSAVRGGVTGKPKSLSHAGETNVPASEEIVPPGTKVFPVVSSDHTKPIEPVSLQDTSYGHEALADPVRTTETSDWEAKREAPTHYPLGVSEFSDRGESREAHQEPLNTPVSLLSATEDVTRTFAPGGEDDYLGGQRKVNVETPKRLEEDPAAPGGGSDYLSGVSNYQSKVTDPTHKGGEAGVPEIAESLGRMKVTDESPDQKSRQGREEDFPTRSHEFDLKKESDINKNSPARFGGESKAGMEEDFPTRGDVKVESGLGRDLPTGTHDQFSPELSRPKERDDSEETKDESTHETKPSTYTEQLASATSAITNKAIAAKNVVASKLGYTGENGGGQSESPVKDETPRSVTAYGQKVAGTVAEKLTPVYEKVKETGSTVMTKLPLSGGGSGVKETQQGEEKGVTAKNYISEKLKPGEEDKALSEMIAEKLHFGGGGEKKTTATKEVEVTVEKIPSDQIAEGKGHGEAVAEEGKGGEGMVGKVKGAVTSWLGGKPKSPRSVEESPQSLGTTVGTMGFSDSGGSELGGSGGGKGVQDSGN
Protein: Calcium-transporting ATPase 2 (EC 7.2.2.10) (Vacuolar Ca(2+)-ATPase) (P38929)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports the calcium to the vacuole and participates in the control of the cytosolic free calcium.
Subcellular location: Vacuole membrane; Multi-pass membrane protein.
Interaction partners:
- Vacuolar calcium ion transporter
- Calcium-transporting ATPase 1
- Transcriptional regulator CRZ1
- Calcium-channel protein CCH1
- Vacuolar v-SNARE NYV1
- Calcium channel YVC1
- Calcineurin subunit B
- Stretch-activated cation channel MID1
- Calmodulin
- NADPH--cytochrome P450 reductase
Sequence:
MSRQDENSALLANNENNKPSYTGNENGVYDNFKLSKSQLSDLHNPKSIRSFVRLFGYESNSLFKYLKTDKNAGISLPEISNYRKTNRYKNYGDNSLPERIPKSFLQLVWAAFNDKTMQLLTVAAVVSFVLGLYELWMQPPQYDPEGNKIKQVDWIEGVAIMIAVFVVVLVSAANDYQKELQFAKLNKKKENRKIIVIRNDQEILISIHHVLVGDVISLQTGDVVPADCVMISGKCEADESSITGESNTIQKFPVDNSLRDFKKFNSIDSHNHSKPLDIGDVNEDGNKIADCMLISGSRILSGLGRGVITSVGINSVYGQTMTSLNAEPESTPLQLHLSQLADNISVYGCVSAIILFLVLFTRYLFYIIPEDGRFHDLDPAQKGSKFMNIFITSITVIVVAVPEGLPLAVTLALAFATTRMTKDGNLVRVLRSCETMGSATAVCSDKTGTLTENVMTVVRGFPGNSKFDDSKSLPVSEQRKLNSKKVFEENCSSSLRNDLLANIVLNSTAFENRDYKKNDKNTNGSKNMSKNLSFLDKCKSRLSFFKKGNREDDEDQLFKNVNKGRQEPFIGSKTETALLSLARLSLGLQPGELQYLRDQPMEKFNIEKVVQTIPFESSRKWAGLVVKYKEGKNKKPFYRFFIKGAAEIVSKNCSYKRNSDDTLEEINEDNKKETDDEIKNLASDALRAISVAHKDFCECDSWPPEQLRDKDSPNIAALDLLFNSQKGLILDGLLGIQDPLRAGVRESVQQCQRAGVTVRMVTGDNILTAKAIARNCAILSTDISSEAYSAMEGTEFRKLTKNERIRILPNLRVLARSSPEDKRLLVETLKGMGDVVAVTGDGTNDAPALKLADVGFSMGISGTEVAREASDIILMTDDFSAIVNAIKWGRCVSVSIKKFIQFQLIVNITAVILTFVSSVASSDETSVLTAVQLLWINLIMDTLAALALATDKPDPNIMDRKPRGRSTSLISVSTWKMILSQATLQLIVTFILHFYGPELFFKKHEDEITSHQQQQLNAMTFNTFVWLQFFTMLVSRKLDEGDGISNWRGRISAANLNFFQDLGRNYYFLTIMAIIGSCQVLIMFFGGAPFSIARQTKSMWITAVLCGMLSLIMGVLVRICPDEVAVKVFPAAFVQRFKYVFGLEFLRKNHTGKHDDEEALLEESDSPESTAFY
Protein: Small nuclear ribonucleoprotein Sm D2 (Sm-D2) (snRNP core protein D2) (F7FB70)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU365051}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365051}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000256|RuleBase:RU365051}.
Interaction partners:
Sequence:
MSWSSLLNKPKSEMTPEELQKREEEEFNTGPLSVLTQSVKNNTQVLINCRNNKKLLGRVKAFDRHCNMVLENVKEMWTEVPKSGKGKKKSKPVNKDRYISKMFLRGDSVIVVLRNPLIAGK