wanglab/gogpt-training-data huggingface dataset:
Protein: Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I) (P07756)
Organism: Rattus norvegicus (Rat)
Function: Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.
Subcellular location: Mitochondrion. Nucleus, nucleolus {ECO:0000250|UniProtKB:P31327}. Cell membrane {ECO:0000250|UniProtKB:Q8C196}; Peripheral membrane protein {ECO:0000305}; Extracellular side {ECO:0000250|UniProtKB:Q8C196}. Note=Localizes to the cell surface of hepatocytes. {ECO:0000250|UniProtKB:Q8C196}.
Interaction partners:
- Ornithine transcarbamylase, mitochondrial
- Argininosuccinate synthase
- Glutamate dehydrogenase 1, mitochondrial
- Glutamine synthetase
- N-acetylglutamate synthase, mitochondrial
- Argininosuccinate lyase
- Glutaminase liver isoform, mitochondrial
- Glutaminase kidney isoform, mitochondrial
- Multifunctional protein CAD
- Dihydroorotate dehydrogenase
Sequence:
MTRILTACKVVKTLKSGFGLANVTSKRQWDFSRPGIRLLSVKAQTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYSEALTDPAYKGQILTMANPIIGNGGAPDTTARDELGLNKYMESDGIKVAGLLVLNYSHDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVDFVDPNKQNLIAEVSTKDVKVFGKGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTQMDYDGLLIAGGPGNPALAQPLIQNVKKILESDRKEPLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALDNTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLIKKGKGTTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQADAVYFLPITPQFVTEVIKAERPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLMDLGTKAFAMTNQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSVDGFTPRLPMNKEWPANLDLRKELSEPSSTRIYAIAKALENNMSLDEIVKLTSIDKWFLYKMRDILNMDKTLKGLNSESVTEETLRQAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDIKFDEHGIMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACNGCIISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEATRVSQEHPVVLTKFIEGAREVEMDAVGKEGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESVDEKHLPTLEQPIIPSDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIALLTNFQVTKLFAEAVQKARTVDSKSLFHYRQYSAGKAA
Protein: AP complex subunit sigma (Q9VDC3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004277}.
Interaction partners:
- AP-2 complex subunit alpha
- Adaptor protein complex 2, mu subunit, isoform A
- AP complex subunit beta
- Clathrin heavy chain
- AP-1 complex subunit gamma
- AT02057p
- Adaptor protein complex 1, mu subunit
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- AP-3 complex subunit delta
- Clathrin light chain
Sequence:
MIRFILIQNRAGKTRLAKWYMNFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIVYRRYAGLYFCICVDVNDNNLCYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYSVVDEMFLAGEIRETSQTKVLKQLLTLNSLE
Protein: Rod outer segment membrane protein 1 (ROSP1) (Tetraspanin-23) (Tspan-23) (Q03395)
Organism: Homo sapiens (Human)
Function: Plays a role in rod outer segment (ROS) morphogenesis (By similarity). May play a role with PRPH2 in the maintenance of the structure of ROS curved disks (By similarity). Plays a role in the organization of the ROS and maintenance of ROS disk diameter (By similarity). Involved in the maintenance of the retina outer nuclear layer (By similarity).
Subcellular location: Photoreceptor inner segment membrane {ECO:0000250|UniProtKB:P32958, ECO:0000305|PubMed:1610568}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor outer segment membrane {ECO:0000269|PubMed:1610568}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peripherin-2
- Rhodopsin
- Cyclic nucleotide-gated channel beta-1
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Fascin-2
- Glycogen phosphorylase, muscle form
- Cyclic nucleotide-gated channel alpha-1
- Ferritin heavy chain
- Muscarinic acetylcholine receptor M1
- Uteroglobin
Sequence:
MAPVLPLVLPLQPRIRLAQGLWLLSWLLALAGGVILLCSGHLLVQLRHLGTFLAPSCQFPVLPQAALAAGAVALGTGLVGVGASRASLNAALYPPWRGVLGPLLVAGTAGGGGLLVVGLGLALALPGSLDEALEEGLVTALAHYKDTEVPGHCQAKRLVDELQLRYHCCGRHGYKDWFGVQWVSSRYLDPGDRDVADRIQSNVEGLYLTDGVPFSCCNPHSPRPCLQNRLSDSYAHPLFDPRQPNQNLWAQGCHEVLLEHLQDLAGTLGSMLAVTFLLQALVLLGLRYLQTALEGLGGVIDAGGETQGYLFPSGLKDMLKTAWLQGGVACRPAPEEAPPGEAPPKEDLSEA
Protein: Heme-responsive zinc finger transcription factor HAP1 (CYP1 activatory protein) (Heme activator protein 1) (P0CS82)
Organism: Saccharomyces cerevisiae (Baker's yeast)
Function: Regulation of oxygen dependent gene expression. It modulates the expression of Iso-1 (CYP1) and Iso-2 (CYP3) cytochrome c. In response to heme, promotes transcription of genes encoding functions required for respiration, controlling oxidative damage and repression of anaerobic genes. Binds to the sequence 5'-CGGNNNTNNCGG-3'. Is non-functional in terms of iso-1 cytochrome c expression in strain S288c and its derivatives.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:8182072}.
Interaction partners:
Sequence:
MSNTPYNSSVPSIASMTQSSVSRSPNMHTATTPGANTSSNSPPLHMSSDSSKIKRKRNRIPLSCTICRKRKVKCDKLRPHCQQCTKTGVAHLCHYMEQTWAEEAEKELLKDNELKKLRERVKSLEKTLSKVHSSPSSNSLKSYNTPESSNLFMGSDEHTTLVNANTGSASSASHMHQQQQQQQQQEQQQDFSRSANANANSSSLSISNKYDNDELDLTKDFDLLHIKSNGTIHLGATHWLSIMKGDPYLKLLWGHIFAMREKLNEWYYQKNSYSKLKSSKCPINHAQAPPSAAAAATRKCPVDHSAFSSGMVAPKEETPLPRKCPVDHTMFSSGMIPPREDTSSQKRCPVDHTMYSAGMMPPKDETPSPFSTKAMIDHNKHTMNPPQSKCPVDHRNYMKDYPSDMANSSSNPASRCPIDHSSMKNTAALPASTHNTIPHHQPQSGSHARSHPAQSRKHDSYMTESEVLATLCEMLPPKRVIALFIEKFFKHLYPAIPILDEQNFKNHVNQMLSLSSMNPTVNNFGMSMPSSSTLENQPITQINLPKLSDSCNLGILIIILRLTWLSIPSNSCEVDLGEESGSFLVPNESSNMSASALTSMAKEESLLLKHETPVEALELCQKYLIKFDELSSISNNNVNLTTVQFAIFYNFYMKSASNDLTTLTNTNNTGMANPGHDSESHQILLSNITQMAFSCGLHRDPDNFPQLNATIPATSQDVSNNGSKKANPSTNPTLNNNMSAATTNSSSRSGSADSRSGSNPVNKKENQVSIERFKHTWRKIWYYIVSMDVNQSLSLGSPRLLRNLRDFSDTKLPSASRIDYVRDIKELIIVKNFTLFFQIDLCIIAVLNHILNVSLARSVRKFELDSLINLLKNLTYGTENVNDVVSSLINKGLLPTSEGGSVDSNNDEIYGLPKLPDILNHGQHNQNLYADGRNTSSSDIDKKLDLPHESTTRALFFSKHMTIRMLLYLLNYILFTHYEPMGSEDPGTNILAKEYAQEALNFAMDGYRNCMIFFNNIRNTNSLFDYMNVILSYPCLDIGHRSLQFIVCLILRAKCGPLTGMRESSIITNGTSSGFNSSVEDEDVKVKQESSDELKKDDFMKDVNLDSGDSLAEILMSRMLLFQKLTKQLSKKYNYAIRMNKSTGFFVSLLDTPSKKSDSKSGGSSFMLGNWKHPKVSNMSGFLAGDKDQLQKCPVYQDALGFVSPTGANEGSAPMQGMSLQGSTARMGGTQLPPIRSYKPITYTSSNLRRMNETGEAEAKRRRFNDGYIDNNSNNDIPRGISPKPSNGLSSVQPLLSSFSMNQLNGGTIPTVPSLTNITSQMGALPSLDRITTNQINLPDPSRDEAFDNSIKQMTPMTSAFMNANTTIPSSTLNGNMNMNGAGTANTDTSANGSALSTLTSPQGSDLASNSATQYKPDLEDFLMQNSNFNGLMINPSSLVEVVGGYNDPNNLGRNDAVDFLPVDNVEIDGLVDFYRADFPIWE
Protein: DNA-binding dual master transcriptional regulator RpaA (Regulator of phycobilisome-associated protein A) (RpaA) (Q31S42)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Response regulator of 2 two-component regulatory systems SasA/RpaA and CikA/RpaA involved in genome-wide circadian gene expression. The histidine kinases have opposing effects modulated by the clock oscillator proteins; SasA phosphorylates RpaA (stimulated by fully phosphorylated KaiC) while CikA dephosphorylates phospho-RpaA (stimulated by the phospho-Ser-431-KaiC-KaiB complex). A very robust clock is reconstituted with KaiA, KaiB, KaiC, SasA, CikA and RpaA; output is measured by transcription from an appropriate reporter. Phosphorylation by SasA is maximal when KaiC phosphorylation is active during the circadian cycle. Functions downstream of LabA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q55890}.
Interaction partners:
- Adaptive-response sensory kinase SasA
- histidine kinase
- histidine kinase
- Diguanylate cyclase with GAF sensor
- Circadian input-output histidine kinase CikA
- histidine kinase
- Diguanylate cyclase with GAF sensor
- histidine kinase
- Sensor protein SphS
- Metal dependent phosphohydrolase
Sequence:
MKPRILVIDDDSAILELVAVNLEMSGYDVRKAEDGIKGQALAVQLVPDLIMLDLMLPRVDGFTVCQRLRRDERTAEIPVLMLTALGQTQDKVEGFNAGADDYLTKPFEVEEMLARVRALLRRTDRIPHAARHSEILSYGPLTLIPERFEAIWFNRTVKLTHLEFELLHCLLQRHGQTVAPSEILKEVWGYDPDDDIETIRVHIRHLRTKLEPDPRHPRYIKTVYGAGYCLELPAETELHQHADQFPSAS
Protein: CASP-like protein 2D1 (AtCASPL2D1) (Q9FFT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:24920445}; Multi-pass membrane protein {ECO:0000269|PubMed:24920445}.
Interaction partners:
Sequence:
MRDNNNNNTREEERSSSSKQQQPQAPMSLKIIDSCLRLSVVPLSVATIWLTVTNHESNPDYGNLEYNSIMGLKYMVGVSAISAIYALLSTVSSWVTCLVSKAWLFFIPDQVLAYVMTTSVAGATEIVYLLNKGDKIVTWSEMCSSYPHYCSKLTIALGLHVFVLFFFLFLSVISAYRAFSPFDPPCDSQTNNDA
Protein: Submandibular gland protein C (E9PTP9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKLILLYLAVVLCTVCKATSVRGRAGLGTYSRFGLGVLLSGKKTLSAKNSGGNKDDSVSAGGKENSNDALRLGLDGAASVNTNLDASATHRVGGSGSSTTPQKDERSPFDLIKAILRLQGATSGSSKLSVHSTNDPSAEPGDDPTAQGPQATASSTPKQNVDINLSSAGSATSNDGAPTPREQSSADSLLEESQNLGNESPTEASGSADKPTAHSGKENSNDALRLGLDGAASVNTNLDASATHRVGGSGSSTTPQKDERSPFDLIKAILRLQGSGKGGSSAETGSSRGRGRGSGATSGSSKLSVHSTNDPSAEPGDDPTAQGPQATASSTPKQNVDINLSSAGSATSNDGASPAREQSSADPLMEESQNLGNESPTETSGSEDSSNEENLKKVLKAFADRIPQSSTGSSDSADRPNAYSGNSFSGELERIFDSNPTKASVSGKENSNDALRLGLDGAASVNTNLDASATHHVGRSGSSTTPQKDERSLFDLIKAILRLQGSGKGGSSAETGSSRGRGRGSGNGLMLQDQPAPASGRNDKTVDTSGLSTESAISNEENLSGSGDSNKVSGPSSSAVVSTDSGDDGNLEDKQVPRFNGDERDGENNSDFFGAGSLDTGNTSDSGSHNLSSGSGSSVRSNVSIGAGPSDQNESADLGGSGRVTCAGKTVSGASSVA
Protein: Protein APA1 [Includes: Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase 1 (Ap4A phosphorylase 1) (EC 2.7.7.53) (ADP-sulfurylase) (EC 2.7.7.5) (ATP adenylyltransferase) (Diadenosine tetraphosphate alpha,beta-phosphorylase (ADP-forming))] (P16550)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates with equal efficiency. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catalyze the phosphorolytic degradation of adenosine 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange reaction between inorganic phosphate and the beta-phosphate of a nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus ATP.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Bis
- Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase 2
- Sulfate adenylyltransferase
- Adenylyl-sulfate kinase
- 3'
- Flavin adenine dinucleotide synthase
- Inorganic pyrophosphatase
- L-2-aminoadipate reductase
Sequence:
MSIPADIASLISDKYKSAFDNGNLKFIQTETTKTKDPKTSMPYLISHMPSLIEKPERGQTPEGEDPLGKPEEELTVIPEFGGADNKAYKLLLNKFPVIPEHTLLVTNEYQHQTDALTPTDLLTAYKLLCALDNEESDKRHMVFYNSGPASGSSLDHKHLQILQMPEKFVTFQDRLCNGKEHFLPTFNTEPLQDAKVSFAHFVLPMPESEETVDEDLLAMCYISILQRALTFFQDWLNENPELKKSYNLMLTKEWICVVPRSKAFSDEMKIGFNSTGYCGMILTKNDEVFSKITEKPELINDILLECGFPNTSGQKPNEYNY
Protein: Structural maintenance of chromosomes protein 4 (SMC protein 4) (SMC-4) (Chromosome-associated polypeptide C) (XCAP-C homolog) (Q8CG47)
Organism: Mus musculus (Mouse)
Function: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}.
Interaction partners:
- Non-SMC condensin I complex, subunit G
- Condensin complex subunit 1
- Structural maintenance of chromosomes protein 2
- Condensin complex subunit 2
- Condensin-2 complex subunit H2
- Condensin-2 complex subunit G2
- Condensin-2 complex subunit D3
- Kinesin-like protein KIF11
- DNA replication licensing factor MCM7
- Centromere-associated protein E
Sequence:
MRRKGTKPSTACHQEEGPPPSQDGAHSDEEMEQPAGEAESAAPAKPPGEELDNRSLEEILNSIPPPPPPAMASEAGAPRLMITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVEVHFQKIIDKEGDDYEVLPNSNFYVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKGQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDIAISSCCHALDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRLFDLVKVKNEEIRQAFYFALRDTLVANNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTKSVAVNPKQIASKGLC
Protein: Variant surface glycoprotein (VSG)-related, putative (Q57YT2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MCGIKYCVVLFALVLRTSIFGEGKIVNEDEFGALCGMINFAKGALQRVEEAQEVNKSLTKIGSRCLELAGDVKLSNTCIDNNDESCEYSKVFWDAAKLSMSEGNAGKESLDDEKLEKVKQVASAAETIYGNMTKRHWVLNGDIIKQMLNRALYGIPHQPKKMRERSATRKRVCEGDVSQPEVNQGPVSLSRDLLCLCATDRKSRRKTKLCCENCVSGENRRVWRPRNDAQKRWNFLVSQCSNVEGHKEGFAKLVEKFRRSLNHRVDGCSGTMYVLGKHKKQLFWPLEFLSGYVPGPGVHYIINTRAGMVEDIPWLGELREIATLMGDLSEDNVEGRGLKSAIEKLEGDLEELFPTGGVRRG
Protein: Protein phosphatase 1 regulatory subunit 12B (Myosin phosphatase-targeting subunit 2) (Myosin phosphatase target subunit 2) (Q8BG95)
Organism: Mus musculus (Mouse)
Function: Regulates myosin phosphatase activity. Augments Ca(2+) sensitivity of the contractile apparatus (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O60237}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O60237}. Note=Along actomyosin filaments. {ECO:0000250|UniProtKB:O60237}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Protein phosphatase 1 regulatory subunit 12C
- Rho-associated protein kinase 1
- Rho-associated protein kinase 2
- Myosin regulatory light polypeptide 9
- Protein phosphatase 1 regulatory subunit 14A
- cGMP-dependent protein kinase 1
- Myosin light polypeptide 6
Sequence:
MAELEHLGGKRAESARARRAEQLRRWRGSLTEQEPAERQGAGRQLQTRRGSPRVRFEDGAVFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQDARQWLNSGRIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGLVEHLEMLQKKQDVLRSEKETRNKLIESDLNSKFQSGLFKNKEKMLYEEEIPKSQDTEEENKESSSSSSEEEEGEDEVSESETEKEADKKPEATVNHSNSEIKSRIMEQIPAPAQNTFSASSARRLSSLFNKAEEPKDESPSSWRLGLRKTGSHNMLSEVANSREALRDRGSSIYRSSSSPRISALLDDKDKERENKSYFSMLVPRRLSSTSDIEEKENRESAVNLVRSGSHTRQLWRDEAKGSETPQTIAPSTYTSTYLKRTPYKSQADSTAEKTADSVSSSTPLCVITNRPAPSTANGVPAATVFSSAGTDPSVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRSRAERQAQEQPGEKLEDPGGLEGSTKKQEPSAAPTKGAGEGRSLEEEPIYHRLRYPTQPDKPTTPVSPSASRPSLYTGSHLLRTSRASGPDSENSETSTHATAAKEMDTSEKGEADLDDQSSNRLSVRERRRAKDRRRGTGINFWTNDEDETDVSEEVKEALHERLSRLESGGTNPTSSDSYSDRASARARREAREARLASLTSRVEEDSNRDYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEMKVLTELKSDNQRLKDENGALIRVISKLSK
Protein: Serine/threonine-protein phosphatase 2B catalytic subunit A2 (EC 3.1.3.16) (Calcineurin A2) (Calmodulin-binding protein 2) (P14747)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Interaction partners:
- Calcineurin subunit B
- Serine/threonine-protein phosphatase 2B catalytic subunit A1
- Protein phosphatase PP2A regulatory subunit A
- Calcipressin-like protein
- Calmodulin
- Protein phosphatase PP2A regulatory subunit B
- FK506-binding protein 1
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
Sequence:
MSSDAIRNTEQINAAIKIIENKTERPQSSTTPIDSKASTVAAANSTATETSRDLTQYTLDDGRVVSTNRRIMNKVPAITSHVPTDEELFQPNGIPRHEFLRDHFKREGKLSAAQAARIVTLATELFSKEPNLISVPAPITVCGDIHGQYFDLLKLFEVGGDPATTSYLFLGDYVDRGSFSFECLIYLYSLKLNFNDHFWLLRGNHECKHLTSYFTFKNEMLHKYNLDIYEKCCESFNNLPLAALMNGQYLCVHGGISPELNSLQDINNLNRFREIPSHGLMCDLLWADPIEEYDEVLDKDLTEEDIVNSKTMVPHHGKMAPSRDMFVPNSVRGCSYAFTYRAACHFLQETGLLSIIRAHEAQDAGYRMYKNTKTLGFPSLLTLFSAPNYLDTYNNKAAILKYENNVMNIRQFNMTPHPYWLPDFMDVFTWSLPFVGEKVTEMLVAILNICTEDELENDTPVIEELVGTDKKLPQAGKSEATPQPATSASPKHASILDDEHRRKALRNKILAVAKVSRMYSVLREETNKVQFLKDHNSGVLPRGALSNGVKGLDEALSTFERARKHDLINEKLPPSLDELKNENKKYYEKVWQKVHEHDAKNDSK
Protein: Asparagine--tRNA ligase, cytoplasmic 2 (EC 6.1.1.22) (Asparaginyl-tRNA synthetase 2) (AsnRS 2) (AtNS2) (Q9SW95)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277, ECO:0000305|PubMed:16297076}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Glutamyl-tRNA
- Proline--tRNA ligase, cytoplasmic
- Proline--tRNA ligase, chloroplastic/mitochondrial
- proline--tRNA ligase
- Putative glycine--tRNA ligase, cytoplasmic
- Protein SWOLLEN 1
- Histidine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MESHGKTHQKEHDNDLSPKPITLSKYSKRVELKTLLDRSDRGAGLAGKRVVIGGWVKSARAVKKNSPPPPLPVVAAPSPSSGGDQAHTTANIRCTEIIQSKMNIFKRFFDVLSGGGKTYPIFDKTELAGQKAVPPPEYVFYFLISDGSSISSLQVVVDSALSTVPATQLMALGTCIVAEGVLRLPLAASAKHVIELEAEKLLHVGTVDPEKYPLSKKQLPLHMLRDFSHFRPRTTTVGSVTRVHSALTLASHTFLQYHGFQYVQVPVITTTTGFGEMFRVTTLLGKTDDKEEKKPPVQEKDGFSIDTVKAVIKEKTRLIDHLKRSDSNRETVVAAVHDLKKTNDLASQIEMKQKSKTGTLVKPEKLDFSKDFFGRDTYLTASGRFHLESYASALGKVYTFGPRFIADKIDNARHLAEKWNVETEMAFAELDDAMDCADEYFKFLCKYVLENRDEDMKFISKRVDKTITTRLEATASSSLLRFSYTEVISLLQKATTTKFETKPEWGVALTTEHLSYLTDEIYKGPVIVHTYPKAIKQFYVRLNDDKKTVAAFDLVVPKVGVVITGSQNEERFEILDARIGESGFTREKFEWYLDLRRHGTVKHSGISLSMEQMLLYATGLPDIKDAIPFPRSWGKANN
Protein: L-glutamate/L-aspartate-binding protein (Q9I402)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Binds L-glutamate and L-aspartate.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Amino acid ABC transporter membrane protein
- Glutamate/aspartate import permease protein GltK
- Amino acid ABC transporter ATP binding protein
- Glutaminase-asparaginase
- DUF541 domain-containing protein
- Glutathione hydrolase proenzyme
- Probable permease of ABC transporter
- Sulfate-binding protein
- Probable amino acid permease
- Probable major facilitator superfamily
Sequence:
MRIAPSLLSTAIVAALLSAPVVADELTGTLKKIKETGTITLGHRDASIPFSYLGTEPGKPIGYSHDLQLKVVEAVKKELNLPELKVRYNLVTSQTRIPLVQNGTVDIECGSTTNNEERQKQVDFSVGIFEVGTRLLSKKTANIKDFDDLKGKNVVTTAGTTSERLLKAMNADKKMGMNIISAKDHGESFMMLESGRAVAFMMDDALLYGEMAKAKKPDDWVVGGTPQSFEIYGCMVRKGDAAFKKVVDKAITDTYASGEVNKIYDKWFTQPIPPKGLNLNFPMSEELKKLIASPTDKAAEQM
Protein: General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 5.6.2.3) (Basic transcription factor 2 80 kDa subunit) (BTF2 p80) (CXPD) (DNA 5'-3' helicase XPD) (DNA excision repair protein ERCC-2) (DNA repair protein complementing XP-D cells) (TFIIH basal transcription factor complex 80 kDa subunit) (TFIIH 80 kDa subunit) (TFIIH p80) (Xeroderma pigmentosum group D-complementing protein) (P18074)
Organism: Homo sapiens (Human)
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers.
Subcellular location: Nucleus {ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:23352696, ECO:0000269|PubMed:23585563}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20797633}.
Interaction partners:
- Cyclin-H
- General transcription factor IIE subunit 1
- DNA repair protein complementing XP-A cells
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Cyclin-dependent kinase 7
- General transcription factor IIH subunit 5
- General transcription factor IIH subunit 3
- Transcription initiation factor IIE subunit beta
- General transcription factor IIH subunit 4
- General transcription factor IIH subunit 2
Sequence:
MKLNVDGLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEITDLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLESEETLKRIEQIAQQL