wanglab/gogpt-training-data huggingface dataset:
Protein: Importin-9 (Imp9) (Ran-binding protein 9) (RanBP9) (Q96P70)
Organism: Homo sapiens (Human)
Function: Nuclear transport receptor that mediates nuclear import of proteins, such as histones, proteasome and actin. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates the import of pre-assembled proteasomes into the nucleus; AKIRIN2 acts as a molecular bridge between IPO9 and the proteasome complex. Mediates the nuclear import of histones H2A, H2B, H4 and H4. In addition to nuclear import, also acts as a chaperone for histones by preventing inappropriate non-nucleosomal interactions. Mediates the nuclear import of actin (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11823430}. Nucleus {ECO:0000269|PubMed:11823430}.
Interaction partners:
- Histone H2A type 1-B/E
- Histone H2B type 1-J
- Histone H2A type 1-C
- Histone H2A type 1
- Importin-7
- Transportin-1
- Importin-8
- Transportin-2
- Exportin-6
- Importin-5
Sequence:
MAAAAAAGAASGLPGPVAQGLKEALVDTLTGILSPVQEVRAAAEEQIKVLEVTEEFGVHLAELTVDPQGALAIRQLASVILKQYVETHWCAQSEKFRPPETTERAKIVIRELLPNGLRESISKVRSSVAYAVSAIAHWDWPEAWPQLFNLLMEMLVSGDLNAVHGAMRVLTEFTREVTDTQMPLVAPVILPEMYKIFTMAEVYGIRTRSRAVEIFTTCAHMICNMEELEKGAAKVLIFPVVQQFTEAFVQALQIPDGPTSDSGFKMEVLKAVTALVKNFPKHMVSSMQQILPIVWNTLTESAAFYVRTEVNYTEEVEDPVDSDGEVLGFENLVFSIFEFVHALLENSKFKSTVKKALPELIYYIILYMQITEEQIKVWTANPQQFVEDEDDDTFSYTVRIAAQDLLLAVATDFQNESAAALAAAATRHLQEAEQTKNSGTEHWWKIHEACMLALGSVKAIITDSVKNGRIHFDMHGFLTNVILADLNLSVSPFLLGRALWAASRFTVAMSPELIQQFLQATVSGLHETQPPSVRISAVRAIWGYCDQLKVSESTHVLQPFLPSILDGLIHLAAQFSSEVLNLVMETLCIVCTVDPEFTASMESKICPFTIAIFLKYSNDPVVASLAQDIFKELSQIEACQGPMQMRLIPTLVSIMQAPADKIPAGLCATAIDILTTVVRNTKPPLSQLLICQAFPAVAQCTLHTDDNATMQNGGECLRAYVSVTLEQVAQWHDEQGHNGLWYVMQVVSQLLDPRTSEFTAAFVGRLVSTLISKAGRELGENLDQILRAILSKMQQAETLSVMQSLIMVFAHLVHTQLEPLLEFLCSLPGPTGKPALEFVMAEWTSRQHLFYGQYEGKVSSVALCKLLQHGINADDKRLQDIRVKGEEIYSMDEGIRTRSKSAKNPERWTNIPLLVKILKLIINELSNVMEANAARQATPAEWSQDDSNDMWEDQEEEEEEEEDGLAGQLLSDILATSKYEEDYYEDDEEDDPDALKDPLYQIDLQAYLTDFLCQFAQQPCYIMFSGHLNDNERRVLQTIGI
Protein: Probable calcium-binding protein CML23 (Calmodulin-like protein 23) (Q9C8Y1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential calcium sensor.
Interaction partners:
- F25I16.5 protein
- Calmodulin-binding protein-like protein
- Probable calcium-binding protein CML45
Sequence:
MSKNVSRNCLGSMEDIKKVFQRFDKNNDGKISIDELKDVIGALSPNASQEETKAMMKEFDLDGNGFIDLDEFVALFQISDQSSNNSAIRDLKEAFDLYDLDRNGRISANELHSVMKNLGEKCSIQDCQRMINKVDSDGDGCVDFEEFKKMMMINGSA
Protein: Protocadherin gamma B4 (Protocadherin gamma subfamily B, 4) (Q91XX6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MREGTAERGRGQRRPMLLPFLLPLFCPTLSEQIRYKIPEEMPTGSVVGNLAKDLGFSVQELPTRKLRISSEKPYFSVSSESGELLVSSRLDREQICGKKLMCALEFEAVAENPLNFYHLSVELEDINDHTPKFAHTSFELQISESSKPGTRFILGSAHDADIGTNSLQNYQLSPNDHFSLVNKEKSDGSKYPEMILKTALDREKQKLYHLTLTALDFGHPPLNSTAQIQVLVTDANDNPPVFSQDIYRVSLPENVYPGTTVLRVVATDQDEGVNSEITFSFSEAGQVTQFNLDSNTGEITTLHTLDFEEVKEYSLVLEAKDGGGMIAQCTVEIEVLDENDNVPEVLFQSLPDLIMEDAEPGTYIALLKTRDKDSGRNGEVICKLEGGAPFKILTSSGNTYKLVTDGVLDREQNPEYNITIRATDKGDPPLSSSSSVTLHIGDVNDNAPVFTKVSYLVHVAENNPPGASIAQVSASDPDLGANGQVTYYIIASDLEPESLWSYVTINAQSGVLFAQRAFDHEQLRSFQLTLQARDHGSPTLSANVSMRLLVGDRNDNAPRVLYPTLEPDGSALFDMVPRSAEPGYLVTKVVAVDADSGHNAWLSYHVLQASDPGLFSLGLRTGEVRTARALGDRDSARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDLSDDPLPPDPQSELQFYLVVALALISVLFLLAVILAIALRLRHSSSRKAWGCFQSEVVVPPNYSEGTLPYSYNLCAAEFNSLTCNDQLKSGQDLQFADSAGALFPLCNSNESTSHQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Cytokine-like nuclear factor N-PAC (NPAC) (Glyoxylate reductase 1 homolog) (Nuclear protein NP60) (Putative oxidoreductase GLYR1) (Q922P9)
Organism: Mus musculus (Mouse)
Function: Cytokine-like nuclear factor with chromatin gene reader activity involved in chromatin modification and regulation of gene expression. Acts as a nucleosome-destabilizing factor that is recruited to genes during transcriptional activation. Recognizes and binds histone H3 without a preference for specific epigenetic markers and also binds DNA. Interacts with KDM1B and promotes its histone demethylase activity by facilitating the capture of H3 tails, they form a multifunctional enzyme complex that modifies transcribed chromatin and facilitates Pol II transcription through nucleosomes. Stimulates the acetylation of 'Lys-56' of nucleosomal histone H3 (H3K56ac) by EP300 (By similarity). With GATA4, co-binds a defined set of heart development genes and coregulates their expression during cardiomyocyte differentiation. Regulates p38 MAP kinase activity by mediating stress activation of MAPK14/p38alpha and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q49A26}. Chromosome {ECO:0000250|UniProtKB:Q49A26}. Note=Found in actively RNAPolII-transcribed gene bodies. {ECO:0000250|UniProtKB:Q49A26}.
Interaction partners:
- Lysine-specific histone demethylase 1B
- Lysine-specific histone demethylase 1A
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Integrator complex subunit 3
- Integrator complex subunit 1
Sequence:
MAAVSLRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQTSSHTSADDKNRRNSSEERSRPNSGDEKRKLSLSEGKVKKNMGEGKKRVTSGSADRGSKCLKRAQEQSPRKRGRPPKDEKDLTIPESSTVKGMMAGPMAAFKWQPTATEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAYIH
Protein: Membrane insertase YidC/Oxa/ALB C-terminal domain-containing protein (O02207)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|RuleBase:RU003945}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003945}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- Translocon Sec61/SecY plug domain-containing protein
- ER membrane protein complex subunit 3
- Cytochrome c oxidase subunit 2
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit TIM50
- Cytochrome c oxidase assembly protein COX11
- Large ribosomal subunit protein uL4m
- Ribosomal protein L13
- ER membrane protein complex subunit 1
- Cytochrome OXidase assembly protein
Sequence:
MLSVSIRTAAASFRLAPTRLRLIRPVIATCQTRNISSNDVFKITESASIPDLPPLPTPPIPGMSVDELIASGASVLEELGLWTWWKPSSYFRWALESIHVHLDIPWWVTIVAATVTLRALLIGVPVMSQKLVAKQSMYRKEMNEFRDRIDEARKENNQLLQQQILLEQRDFLRSKDIRLGRQFMVMAANGAVFATQFFAIKKMVVVNYPGLSTGGTLWFTDLTATDPYYALPFISAATMALVTKVGIEMGTSADQMPPIMRAFMTYGLPVVIFGVSSQFATGLCVYWTASNAVSLIYAAAFKVDAIRKIFGIPPVVPLPPSAVQKNAISQVLKSYKDNKAIPPSMADLRQRDASSFKKAGRGKPIT
Protein: Patatin-like phospholipase domain-containing protein 6 (Neuropathy target esterase) (EC 3.1.1.5) (Q3TRM4)
Organism: Mus musculus (Mouse)
Function: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho) (Probable). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Catalyzes the hydrolysis of several naturally occurring membrane-associated lipids. Hydrolyzes lysophospholipids and monoacylglycerols, preferring the 1-acyl to the 2-acyl isomer. Does not catalyze hydrolysis of di- or triacylglycerols or fatty acid amides (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16963094}; Single-pass type III membrane protein {ECO:0000305|PubMed:16963094}.
Interaction partners:
- Phospholipase B1, membrane-associated
- Lysosomal phospholipase A and acyltransferase
- Patatin-like phospholipase domain-containing protein 7
- Glycerophosphocholine phosphodiesterase GPCPD1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Acyl-protein thioesterase 1
- Phosphatidylcholine-sterol acyltransferase
- Acyl-protein thioesterase 2
- Phospholipase A and acyltransferase 3
- Lysophospholipid acyltransferase LPCAT4
Sequence:
MGTPSHELNTTSSGAEVIQKTLEEGLGRRICVAQPVPFVPQVLGVMIGAGVAVLVTAVLILLVVRRLRVQKTPAPEGPRYRFRKRDKVLFYGRKIMRKVSQSTSSLVDTSVSTTSRPRMKKKLKMLNIAKKILRIQKETPTLQRKEPPPSVLEADLTEGDLANSHLPSEVLYMLKNVRVLGHFEKPLFLELCRHMVFQRLGQGDYVFRPGQPDASIYVVQDGLLELCLPGPDGKECVVKEVVPGDSVNSLLSILDVITGHQHPQRTVSARAARDSTVLRLPVEAFSAVFTKYPESLVRVVQIIMVRLQRVTFLALHNYLGLTNELFSHEIQPLRLFPSPGLPTRTSPVRGSKRVVSTSGTEDTSKETSGRPLDSIGAPLPGPAGDPVKPTSLEAPPAPLLSRCISMPVDISGLQGGPRSDFDMAYERGRISVSLQEEASGGPQTASPRELREQPAGACEYSYCEDESATGGCPFGPYQGRQTSSIFEAAKRELAKLMRIEDPSLLNSRVLLHHAKAGTIIARQGDQDVSLHFVLWGCLHVYQRMIDKAEEVCLFVAQPGELVGQLAVLTGEPLIFTLRAQRDCTFLRISKSHFYEIMRAQPSVVLSAAHTVAARMSPFVRQMDFAIDWTAVEAGRALYRQGDRSDCTYIVLNGRLRSVIQRGSGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELAKLPEGTLGHIKRRYPQVVTRLIHLLSQKILGNLQQLQGPFPGSGLSVPQHSELTNPASNLSTVAILPVCAEVPMMAFTLELQHALQAIGPTLLLNSDVIRALLGASALDSIQEFRLSGWLAQQEDAHRIVLYQTDTSLTPWTVRCLRQADCILIVGLGDQEPTVGQLEQMLENTAVRALKQLVLLHREEGPGPTRTVEWLNMRSWCSGHLHLRCPRRLFSRRSPAKLHELYEKVFSRRADRHSDFSRLARVLTGNTIALVLGGGGARGCSHIGVLKALEEAGVPVDLVGGTSIGSFIGALYAEERSASRTKQRAREWAKSMTSVLEPVLDLTYPVTSMFTGSAFNRSIHRVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGHLLMDGGYINNLPADIARSMGAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWADKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYLRPSIDCFKTMDFGKFDQIYDVGYQYGKAVFGGWTRGEVIEKMLTDRRSTDLNESRRADILAFPSSGFTDLAEIVSRIEPPTSYVSDGCADGEESDCLTEYEEDAGPDCSRDEGGSPEGASPSTASEVEEEKSTLRQRRFLPQETPSSVADA
Protein: ATP synthase peripheral stalk subunit d, mitochondrial (ATPase subunit d) (ATP synthase peripheral stalk subunit d) (O75947)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
Sequence:
MAGRKLALKTIDWVAFAEIIPQNQKAIASSLKSWNETLTSRLAALPENPPAIDWAYYKANVAKAGLVDDFEKKFNALKVPVPEDKYTAQVDAEEKEDVKSCAEWVSLSKARIVEYEKEMEKMKNLIPFDQMTIEDLNEAFPETKLDKKKYPYWPHQPIENL
Protein: Importin subunit beta-1 (Karyopherin subunit beta-1) (ATKPNB1) (Q9FJD4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as negative effector of drought tolerance. Involved in the regulation of stomatal closure and in the abscisic acid (ABA)-mediated pathway that lead to drought tolerance. Does not directly mediate nuclear import of ABI1 and ABI2 which are key regulators of the ABA signaling pathway. May be involved in nuclear translocation of other type 2C protein phosphatases that mediate ABA signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23582042}. Nucleus {ECO:0000269|PubMed:23582042}.
Interaction partners:
- Snurportin-1
- Importin subunit alpha-2
- GTP-binding nuclear protein Ran-1
- Importin subunit alpha-1
- Importin beta-like SAD2
- Importin subunit alpha-5
- Importin subunit alpha-8
- Importin subunit alpha-7
- Importin subunit alpha-9
- Importin subunit alpha-4
Sequence:
MAMEVTQLLINAQSIDGTVRKHAEESLKQFQEQNLAGFLLSLAGELANDEKPVDSRKLAGLVLKNALDAKEQHRKYELVQRWLALDMSTKSQIRAFLLKTLSAPVPDVRSTASQVIAKVAGIELPQKQWPELIVSLLSNIHQLPAHVKQATLETLGYLCEEVSPDVVEQEHVNKILTAVVQGMNAAEGNTDVRLAATRALYMALGFAQANFNNDMERDYIMRVVCEATLSPEVKIRQAAFECLVSIASTYYEKLAHYMQDIFNITAKAVREDDESVALQAIEFWSSICDEEIDILEEYGGEFAGDSDVPCFYFTKQALPGLVPLLLETLLKQEEDQDLDEGAWNIAMAGGTCLGLVARAVGDDIVPHVMPFIEEKISKPDWREREAATYAFGSILEGPSADKLMAIVNAALTFMLNALTNDPSNHVKDTTAWTLGRIFEFLHGSTIETPIINQANCQQIITVLIQSMNDAPNVAEKACGALYFLAQGYEDIGPSSPLTPFFQEIIKSLLAVAHREDATESRLRTAAYEALNEVVRCSTDETSTMVLQLVPVIMMELHNTLEGEKLSLDEREKQNELQGLLCGCLQVIIQKLGSEPTKSKFMEYADQMMGLFLRVFGCRSATAHEEAMLAIGALAYAAGPNFAKYMPEFYKYLEMGLQNFEEYQVCAVTVGVVGDVCRALEDKILPYCDGIMTQLLKDLSSNQLHRSVKPPIFSCFGDIALAIGEDFDKYWRYSMPMLQSAAELSAHSAGADDEMTEYTNSLRNGILEAYSGIFQGFKNSAKTQLLIPFAPHILQFLDSIYMEKDMDEVVMKTAIGVLGDLADTLGSHVGGLIQQSVSSKEFLNECLSSEDHTIKEAAEWAKHAITRAISV
Protein: Protein FAM209 (A2APA5)
Organism: Mus musculus (Mouse)
Function: Required for sperm acrosome biogenesis.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:34471926}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- RIKEN cDNA 1700013G24 gene
- Transmembrane and coiled-coil domain-containing protein 5A
- Testis expressed protein 56
- Sperm acrosome-associated protein 9
- Ciliary microtubule inner protein 6
Sequence:
MRTLLRWCLFLSLCVSCACAFMFSSMREKTKESPGKVPCGGHFRIRQNLPENAQGWLGNKWLWLFVAIMIYVMLKFRGDGENKEQHPPGLRGCQLRSPPKKAQNISPSKDFTFNTLTQLEMELVKFVSKVRNLKVSMATNSNSRQQVPESPTNLYNNVTIYEIWGEEDSE
Protein: DX11 (Q9GQQ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSNSCSDSSNESMVNPPHIQMNFGQQAQQQQSHQHQQQQQQQERYVWEMRTRSPNVTPASTVLNSPDLNGELSYVPLQGLSPSGGGVQGSDSYGSNAGRDSGSYYYQRPQLHQIRLGRSPGSQFETRDVLPQGLASPGSPTDVGKADGQCLRDGEIVVFDDIDTNWMNKASSGQRPGSNEDVLNVTKMIGQLPIAEYEGSPRRFGSQPNTNTITMGGPRKRPPGFPQRVSPTTSVANNATAAAKASVGNLIDLVDHEEERSGTLREKTPTFDYLYEFSETRKVLEEFFKANPEDKKRYTDYTTESGDDVASSQPQEYPATPMEQAYIGQRLARIPKDELYMVHRSPTKKPPSDQNPSTAYQEHNDIELYIDSNSRSSGDLADTELEANLRRHSRNFTLSPETTDYDSNCGDLDSLSNDINCPTDFGKLYTSMPVLEDGLSSGHASDTENNVSVVCDKQQSSQSQPVHEHNGNGERLENDYNVMSASLATLTTDASQSALISDFASLPMPPAPPPSSPPQIEIADASESMTMAPDADNPLDSHYGAVYAAALGGTHTEKSAGSGLGVTPVTAGGSLPSQAASEIQEAMKEIRSALQRAKTQPEKLKFCDEVLPTDPDSPVWVPRKGTTISTAQGAAADEEPDTDLETDRLLGQQRHDEQDFFADQSLADNNANEGTDIASNGHLNGTSDNNNPNPMNNSKPQTYSTATIRQGIGTSLTPNSPDICQIVGTTDISISSPEKLQFTKSPTGSIKSLKDSANSDKKAKSRNKEGLLEPKVLIEGVLFRARYLGSTQLVCEGQPTKSTRMMQAEEAVSRIKAPEGESQPSTEVDLFISTEKIMVLNTDLKEIMMDHALRTISYIADIGDLVVLMARRRFVPNSVVDPSITSPLGDVPTPGIGEEESPPKEPLSKHNRTPKMICHVFESDEAQFIAQSIGQAFQVAYMEFLKANGIENESLAKEMDYQEVLNSQEIFGDELEIFAKKELQKEVVVPKAKGEILGVVIVESGWGSMLPTVVIANLMSSGAAARCGQLNIGDQLIAINGMSLVGLPLSTCQSYIRNAKNQTAVKFTVVPCPPVVEVKILRPKALFQLGFSVQNGVICSLLRGGIAERGGVRVGHRIIEINNQSVVAVPHDTIVKLLSSSVGEILMKTMPTSMFRLLTGQETPIYI
Protein: Formin-G (Q1ZXK2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Formins play an important role in the nucleation of actin and the formation of linear actin filaments.
Interaction partners:
- Leucine-rich repeat-containing protein
Sequence:
MILSITFQLDPISNNSTSLSNSIDNRSSINVTALQMQQGSKTYNLDQNSSYKTVFLAICQLFGIKESSAQDYCLQLESSKKYLNWPPQSDESKTKHIVKQLYESGETALVLQLNPTYRSSKWVKALNDSETNEKDIMFHLKYKLQENEFAESFIEQNGMEGILRMVTNGKGNAQTYSLASLRACLEYVSAMEIITKTPHLVKQLFSLVDSNVVGVCRGALELLFVLCDFRKEEGFKSVHLAAKGTAVAQGKKPYLNVIKLLDSGDLETKINAFTLLNVLLSNCPTDEKVGKLCKKWGELGLDDKLRSLTSIQQQEFQIQLEIYEETSGVNLRTKASRLEAICNRLKSKLTEYEAQQPLIAILKEELKLAQQLIKEASTDRVFLSSHPMQRYLGPTIQSYPADLSFLKTTAAERDKINEFEKKILAINEQLRQETKLSEELKNQVLANKKQFDSTIAELNEENQRLTQVEVKFKLQQSISPSQDSSNNQKASSSSSNTSTLNDSDIQSIQSSLKEATLEIERLKLAIEEKMPPNEAQQIFSQSLITTAAFTPTSPDISNDGQPISGGGAPPPSPSPPPPISGGGAPPPPPPPPPPPSGGGAPPPPPPPPPSGGKKAGAPGAPPTGPAAIQPNKPVINPSSKMKPLYWKRIILPPSNRNESIWDQVLEPTFDSKDFENLFCAKKKAVDSSLSTNPSSTTGKEGEKVKLVSLVDIKKSNSIAFMLAKIPTAEGLKKAIDTVDNSILGKEIIKTLITNVPTEQDYQLIKGSEIHESKLDKPERWILEIYGFPMMKERLVAWLFQLEYQEMYNNIIQILEKLQNAIKDTKSSDSLKKILGIVLVLGNYMNGGSGRGQADGFTLEILDSLATSKDVENKTSLLDYVSKISMEKYPKTMNVAQELDSLKLVQLSISDMSTDINDLEKQFNISKNNCKKVLEANIPSSSKFQSTIGSFLEKTEIDIKNLKENQKNIVDSFIQLVEFFGYPKSYATTASCQQFFNSIYSFSLLFSKQCQKIEKEREALAKASGDNGAVQNKKIAGGADPLAALANAIKLGQTGLRKRPGPENSSGGSQLNLNK
Protein: Viral IRF2-like protein (vIRF-2) (Q2HR71)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: DNA-binding transcription factor that plays a role in the modulation of host immune response. Acts by interacting with host EIF2AK2/PKR and inhibiting its activation. In turn, EIF2AK2/PKR substrates including EIF2S1 or histone H2A are not phosphorylated. Inhibits type I interferon signaling by targeting host IRF3 during viral reactivation from latency. Attenuates the transcriptional activity of host FOXO3 via activation of the AKT1 signaling pathway, inhibiting FOXO3-mediated apoptosis. Suppresses also the expression of viral early lytic genes in both newly infected and reactivated infected host cells allowing regulation of viral life cycle by harnessing the interferon pathway. Mechanistically, promotes host PML bodies formation as well as host antiviral restriction factors IFIT1-3 expression leading to inhibition of viral early lytic proteins. Regulates also host TRAF3 and TRAF6 ubiquitination by interacting with USP7 deubiquitinase thereby influencing TRAF3/6-mediated signal transduction.
Subcellular location: Host nucleus {ECO:0000269|PubMed:11160738, ECO:0000269|PubMed:26797279, ECO:0000269|PubMed:31059555}. Host cytoplasm {ECO:0000269|PubMed:26797279}.
Interaction partners:
Sequence:
MPRYTESEWLTDFIIDALDSGRFWGVGWLDEQKRIFTVPGRNRRERMPEGFDDFYEAFLEERRRHGLPEIPETETGLGCFGRLLRTANRARQERPFTIYKGKMKLNRWIMTPRPYKGCEGCLVYLTQEPAMKNMLKALFGIYPHDDKHREKALRRSLRKKAQREAARKQAAAVATPTTSSAAEVSSRSQSEDTESSDSENELWVGAQGFVGRDMHSLFFEEPEPSGFGSSGQSSSLLAPDSPRPSTSQVQGPLHVHTPTDLCLPTGGLPSPVIFPHETQGLLAPPAGQSQTPFSPEGPVPSHVSGLDDCLPMVDHIEGCLLDLLSDVGQELPDLGDLGELLCETASPQGPMQSEGGEEGSTESVSVLPATHPLESSAPGASVMGSGQELPDLGDLSELLCETASPQGPMQSEGGEEGSTESVSVLPATHPLESSAPGASVMGSSFQASDNVDDFIDCIPPLCRDDRDVEDQEKADQTFYWYGSDMRPKVLTATQSVAAYLSKKQAIYKVGDKLVPLVVEVYYFGEKVKTHFDLTGGIVICSQVPEASPEHICQTVPPYKCLLPRTAHCSVDANRTLEQTLDRFSMGVVAIGTNMGIFLKGLLEYPAYFVGNASRRRIGKCRPLSHRHEIQQAFDVERHNREPEGSRYASLFLGRRPSPEYDWDHYPVILHIYLAPFYHRD
Protein: Insulin gene enhancer protein ISL-1 (Islet-1) (P61372)
Organism: Mus musculus (Mouse)
Function: DNA-binding transcriptional activator. Recognizes and binds to the consensus octamer binding site 5'-ATAATTAA-3' in promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Cooperates with the transcription factor POU4F2 to achieve maximal levels of expression of RGC target genes and RGC fate specification in the developing retina. Involved in the specification of motor neurons in cooperation with LHX3 and LDB1. Binds to insulin gene enhancer sequences (By similarity). Essential for heart development. Marker of one progenitor cell population that give rise to the outflow tract, right ventricle, a subset of left ventricular cells, and a large number of atrial cells as well, its function is required for these progenitors to contribute to the heart. Controls the expression of FGF and BMP growth factors in this cell population and is required for proliferation and survival of cells within pharyngeal foregut endoderm and adjacent splanchnic mesoderm as well as for migration of cardiac progenitors into the heart.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:14664703}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:14664703}.
Interaction partners:
- LIM/homeobox protein Lhx3
- LIM domain-binding protein 1
- LIM/homeobox protein Lhx4
- Homeobox protein Nkx-2.5
- LIM domain-binding protein 2
- POU domain, class 4, transcription factor 2
- Motor neuron and pancreas homeobox protein 1
- Paired box protein Pax-6
- Homeobox protein Nkx-2.2
- Homeobox protein Nkx-6.1
Sequence:
MGDMGDPPKKKRLISLCVGCGNQIHDQYILRVSPDLEWHAACLKCAECNQYLDESCTCFVRDGKTYCKRDYIRLYGIKCAKCSIGFSKNDFVMRARSKVYHIECFRCVACSRQLIPGDEFALREDGLFCRADHDVVERASLGAGDPLSPLHPARPLQMAAEPISARQPALRPHVHKQPEKTTRVRTVLNEKQLHTLRTCYAANPRPDALMKEQLVEMTGLSPRVIRVWFQNKRCKDKKRSIMMKQLQQQQPNDKTNIQGMTGTPMVAASPERHDGGLQANPVEVQSYQPPWKVLSDFALQSDIDQPAFQQLVNFSEGGPGSNSTGSEVASMSSQLPDTPNSMVASPIEA
Protein: MADS box transcription enhancer factor 2, polypeptide A (Myocyte enhancer factor 2A), isoform CRA_b (Myocyte enhancer factor 2A isoform 1) (A0A0S2Z454)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGFVNSRASPNLIGATGANSLGKVMPTKSPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT
Protein: Cdc42-interacting protein 4 (Protein Felic) (Salt tolerant protein) (hSTP) (Thyroid receptor-interacting protein 10) (TR-interacting protein 10) (TRIP-10) (Q15642)
Organism: Homo sapiens (Human)
Function: Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projection, phagocytic cup. Note=Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ (By similarity). Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, perinuclear region.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Cell division control protein 42 homolog
- Actin nucleation-promoting factor WASL
- Rho-related GTP-binding protein RhoQ
- F-BAR domain only protein 2
- F-BAR domain only protein 1
- Rho GTPase-activating protein 17
- Tyrosine-protein kinase Fes/Fps
- Rho GTPase-activating protein 1
- Amphiphysin
Sequence:
MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN