wanglab/gogpt-training-data huggingface dataset:
Protein: bZIP transcription factor 28 (AtbZIP28) (Q9SG86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator involved in ER stress responses. Functions as a stress sensor and transducer in ER stress signaling pathway. After proteolysis by SBT6.1 (S1P) and S2P, the N-terminal bZIP component is translocated to the nucleus, where it activates the expression and production of ER chaperones. Following ER stress, activates proteins involved in brassinosteroid (BR) signaling, which is required for stress acclimation and growth.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:18156219, ECO:0000305|PubMed:18634751, ECO:0000305|PubMed:18849477, ECO:0000305|PubMed:20876872, ECO:0000305|PubMed:22335396, ECO:0000305|PubMed:23558471, ECO:0000305|PubMed:23624714}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000305|PubMed:20876872, ECO:0000305|PubMed:22335396, ECO:0000305|PubMed:23558471, ECO:0000305|PubMed:23624714}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:18156219, ECO:0000269|PubMed:18849477, ECO:0000269|PubMed:20876872, ECO:0000305|PubMed:18634751, ECO:0000305|PubMed:22335396, ECO:0000305|PubMed:23558471, ECO:0000305|PubMed:23624714}. Note=Translocates to the nucleus following heat shock or tunicamycin treatment (ER stress) (PubMed:18156219, PubMed:18634751, PubMed:18849477, PubMed:20876872, PubMed:22335396, PubMed:23558471, PubMed:23624714). Relocation of BZIP28 from ER to the nucleus occurs through the Golgi and is S2P-dependent (PubMed:20876872, PubMed:22335396, PubMed:23558471, PubMed:23624714). {ECO:0000269|PubMed:18156219, ECO:0000269|PubMed:18634751, ECO:0000269|PubMed:18849477, ECO:0000269|PubMed:20876872, ECO:0000269|PubMed:22335396, ECO:0000269|PubMed:23558471, ECO:0000269|PubMed:23624714}.
Interaction partners:
- Nuclear transcription factor Y subunit A-4
- Nuclear transcription factor Y subunit B-3
- Nuclear transcription factor Y subunit C-2
- Heat shock 70 kDa protein BIP3
- Serine/threonine-protein kinase/endoribonuclease IRE1a
- Serine/threonine-protein kinase/endoribonuclease IRE1b
- Subtilisin-like protease SBT6.1
- Membrane-bound transcription factor site-2 protease homolog
- Basic leucine zipper 10
- Heat shock 70 kDa protein BIP1
Sequence:
MTESTSVVAPPPEIPNLNPSMFSESDLFSIPPLDPLFLSDSDPISMDAPISDLDFLLDDENGDFADFDFSFDNSDDFFDFDLSEPAVVIPEEIGNNRSNLDSSENRSGDGGLEGRSESVHSQVSSQGSKTFVSDTVDASSSPESSNHQKSSVSKRKKENGDSSGELRSCKYQKSDDKSVATNNEGDDDDDKRKLIRQIRNRESAQLSRLRKKQQTEELERKVKSMNATIAELNGKIAYVMAENVALRQQMAVASGAPPMNPYMAAPPLPYQWMPYPPYPVRGYGSQTPLVPIPKLNPKPVSSCRPKKAESKKNEGKSKLKKVASISFIGILFFVFLFGTLVPFMNVNFGGERGSFGGLSKYDGHRYYDEHKGRVLMVGDGSDVRRNSGISEGNIHSSRISHGERDSCGGVDYNAHPKVEGRPSSLSNASDPLFASLYVPRNDGLVKIDGNLIIHSVLASEKARGLGKKNITETVKTKEPDLTIPGALSSALAVPGVRGNAAMLPHSTALSSEGKRLHQWFHEGGSGPLMDYSMCTEVFQFDIAPGAIVPSSVSSISAEHLQNVTTHGKRMKNRRILEGLPVSLVASELNITGTQPNKDAQNKTFNGNTNKPTSSSSMVVSVLLDPREVVDSETDRVVPPNPKSLSRIFVVVLLDSVKYVTYSCVLPRSGLHLVAT
Protein: U4/U5/U6 small nuclear ribonucleoprotein prp3 (Pre-mRNA-splicing factor 3) (Q09856)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Participates in pre-mRNA splicing and in nuclear mRNA export. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor prp1
- Uncharacterized WD repeat-containing protein C227.12
- Pre-mRNA-processing factor 31
- U4/U6.U5 tri-snRNP-associated protein snu66
- 13 kDa ribonucleoprotein-associated protein
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-splicing factor spp42
- Pre-mRNA-splicing factor cwf10
- U4/U6.U5 small nuclear ribonucleoprotein component snu23
- LSM complex subunit lsm3
Sequence:
MDRNKRRLESSQLRESSSPNSQNKPNAMEEIKRRRLQLEQRLAQQAQVPWEKRSENGNNAGMETIQNRISELKEKTAKRFNANIPKSEGLFRDDSNGAKGGLKVGIHPVLLDGNIQNTILTPENRKRTASFSTKGVSLSQHQLLKPPAITEQNPFLDTAPTPRLEDSPFYDPRTKESRKTRGSRNLHLNESGKFIEEANQARRQARLEDLKKRIALHSHKAGIEDELDITSKSIGRDTIPNIEWWDLPFIKDYNDYGDENNWLIDGPQSIINSAIQHPIPVLPPYAKNQPSSHSVFLTKKEQKKIRRQTRAEARKEKQDRQLLGIEPPEPPKVKLSNLMHVLGDDAIKDPTKIEAEVRKQVEERRLRHERENEERKLTPEERKEKAFRKKDEDSAAGLRCLVFRIKYLAHRPHRLKIDLNAKQWGATGVCILNANFNLVIFEAGQKAIKKLKRLMLERIDWTDTSRNSIIAQGNKLVDTEGRELNYTENTCNLVWEGEIGRRAFRYWSFRSCPSENDAKSYLEEQGGAEHFWMLAKSWSENV
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q9VDD8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- E3 ubiquitin-protein ligase NRDP1
- Jak pathway signal transduction adaptor molecule
- E3 ubiquitin-protein ligase parkin
- FI19924p1
- Ubiquitin-ribosomal protein eS31 fusion protein
- E3 ubiquitin-protein ligase NRDP1
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Ubiquitin-ribosomal protein eL40 fusion protein
- GH17761p
- Polyubiquitin
Sequence:
MAKLKKLHMSSNLDDLEKMSIIPDLRSKGMKILLNTARKLYMTAEEYRLDGDEELAYITYMKYFNMLTAIHKKSDYPSHKTTVRQMLGDTESNRRIMDTLEEIINSLRHRYAQQHQAPEPIAPDLVSNGRAGVDSPITQPTQYARLGLITCQDLYRRMQEKSVLVMDCRPSADYEASHLTYYCAFNVPEELITPGMSAGRLQARLSSSAKASWASRSVKDSVVLMDWNTKDAQPATNTAISTLLDILKNWDPDVTYRAPIQIVEGGYEYFIMMYPTHCTNPSVQAPQQNNNDIETIDDIEYPSIHDITMKEDISAKDFRPRPDFNRANKPAATRVNEQGISRPSPPAKPIAEIMRDQAEFLQRAEQNDEQLEKASKMWKRQAAEGDGLNATEDQELHFRILQLESKAQDYIVENNRLREELSRIQELHNVTQQLSQKEVEATRNIESKIRERQRLDEQHELERQERERLLAIARETKKHYKSPTPSGPPSPGRNLEDVHVVSDSLESLLQLTGDPDPTIAPNKAEIPTFDRAMKPQPRNVERTSQRVRDFSPVIGQNVGRGLTGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNKTNGQVIEEVAALIKELWNGQYKCVASRDLRYVVGQYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVPRQREMISASEKAWLEFTKAKESMILHLFYGQMKSTVKCVACHKESATYESFSNLSLELPPNSNVCQLNQCMDMYFSGERIHGWNCPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPSNSGSYMKKQNYLRFPLENLDMNPYIARAESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVVSSAAYILFYTWLPPMQVPL
Protein: Centromere protein Q (CENP-Q) (Q7L2Z9)
Organism: Homo sapiens (Human)
Function: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Plays an important role in chromosome congression and in the recruitment of CENP-O complex (which comprises CENPO, CENPP, CENPQ and CENPU), CENPE and PLK1 to the kinetochores.
Subcellular location: Nucleus {ECO:0000269|PubMed:16622420}. Chromosome, centromere {ECO:0000269|PubMed:16622420}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.
Interaction partners:
- Centromere protein U
- Centromere protein M
- Centromere protein P
- Centromere protein O
- Centromere protein K
- Centromere protein H
- Centromere protein R
- Centromere protein N
- Centromere protein L
- Centromere protein I
Sequence:
MSGKANASKKNAQQLKRNPKRKKDNEEVVLSENKVRNTVKKNKNHLKDLSSEGQTKHTNLKHGKTAASKRKTWQPLSKSTRDHLQTMMESVIMTILSNSIKEKEEIQYHLNFLKKRLLQQCETLKVPPKKMEDLTNVSSLLNMERARDKANEEGLALLQEEIDKMVETTELMTGNIQSLKNKIQILASEVEEEEERVKQMHQINSSGVLSLPELSQKTLKAPTLQKEILALIPNQNALLKDLDILHNSSQMKSMSTFIEEAYKKLDAS
Protein: Myosin light chain 2 Mlc2a (Myosin regulatory light chain 2, atrial isoform) (Myosin, light chain 7, regulatory) (Myosin, light polypeptide 7, regulatory) (Q801M3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cardiac myosin light chain-1.
- Myosin, heavy chain 6, cardiac muscle, alpha
- Troponin T type 2a
- Actin, cytoplasmic 2
- Myosin heavy chain 7
- Natriuretic peptide A
- NK2 homeobox 5.
- Fli-1 protein
- Myosin, light chain 1, alkali; skeletal, fast
- Heart- and neural crest derivatives-expressed protein 2
Sequence:
MASKKAAAKRGKTAQRGSSNVFSMFEQSQIQEFKEAFGCIDQNRDGVINKSDLKETYAQLGKLNVSDEELESMLTEGKGPINFTVFLTLFGEKLNGTDPEETILAAFKLFDPNATGVVNKDEFKRLLMTQADKFTAEEVDQAFAVAPIDVAGNIDYKSLCYIITHGDEKEES
Protein: Zinc finger protein 280A (3'OY11.1) (Suppressor of hairy wing homolog 1) (Zinc finger protein 636) (P59817)
Organism: Homo sapiens (Human)
Function: May function as a transcription factor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MGDIFLCKKVESPKKNLRESKQREEDDEDPDLIYVGVEHVHRDAEVLFVGMISNSKPVVSNILNRVTPGSNSRRKKGHFRQYPAHVSQPANHVTSMAKAIMPVSLSEGRSTDSPVTMKSSSEPGYKMSSPQVVSPSSSDSLPPGTQCLVGAMVSGGGRNESSPDSKRLSTSDINSRDSKRVKLRDGIPGVPSLAVVPSDMSSTISTNTPSQGICNSSNHVQNGVTFPWPDANGKAHFNLTDPERASESALAMTDISSLASQNKTFDPKKENPIVLLSDFYYGQHKGDGQPEQKTHTTFKCLSCVKVLKNIKFMNHMKHHLEFEKQRNDSWEDHTTCQHCHRQFPTPFQLQCHIDSVHIAMGPSAVCKICELSFETDQVLLQHMKDHHKPGEMPYVCQVCHYRSSVFADVETHFRTCHENTKNLLCLFCLKLFKTAIPYMNHCWRHSRRRVLQCSKCRLQFLTLKEEIEHKTKDHQTFKKPEQLQGLPSETKVIIQTSVQPGSSGMASVIVSNTDPQSSPVKTKKKTAMNTRDSRLPCSKDSS
Protein: Peroxidase 69 (Atperox P69) (EC 1.11.1.7) (ATP3a) (Q96511)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- En/Spm-like transposon protein-like
- rhamnogalacturonan endolyase
- Berberine bridge enzyme-like 9
- F13F21.11 protein
- Proline-tRNA ligase
- Berberine bridge enzyme-like 23
- Protein RALF-like 22
- Berberine bridge enzyme-like 27
- Glycoside hydrolase family 28 protein / polygalacturonase
- At1g04800
Sequence:
MGRGYNLLFVLVTFLVLVAAVTAQGNRGSNSGGGRRPHVGFYGNRCRNVESIVRSVVQSHVRSIPANAPGILRMHFHDCFVHGCDGSVLLAGNTSERTAVPNRSLRGFEVIEEAKARLEKACPRTVSCADILTLAARDAVVLTGGQRWEVPLGRLDGRISQASDVNLPGPSDSVAKQKQDFAAKTLNTLDLVTLVGGHTIGTAGCGLVRGRFVNFNGTGQPDPSIDPSFVPLILAQCPQNGGTRVELDEGSVDKFDTSFLRKVTSSRVVLQSDLVLWKDPETRAIIERLLGLRRPSLRFGTEFGKSMVKMSLIEVKTGSDGEIRRVCSAIN
Protein: Nuclear hormone receptor 114 (G5EEM0)
Organism: Caenorhabditis elegans
Function: Probable transcription factor which may have a role in detoxifying dietary metabolites arising from bacterial tryptophan metabolism. Required for fertility and involved in proper postembryonic germline development, especially germline stem cell (GSC) proliferation. Required for activation of the methionine/S-adenosylmethionine (Met/SAM) cycle in response to low levels of SAM.
Subcellular location: Nucleus {ECO:0000255|RuleBase:RU004334, ECO:0000269|PubMed:18629017, ECO:0000269|PubMed:23499532}.
Interaction partners:
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MTPQSSPSSSRDHVCLVCQDFASGYHYGVPSCVGCKTFFRRTIMKKQKYICQFEGNCPVDKTIRCACRYCRFEKCLSVGMDRNALQQNRDPIGYTKRTRRPKKELKTTSDCSSDEGASTPPSVSPLQLSPPPISPLLFQAAPLKPRRCILQTLAEREKCANDLRLSEYLPIRSLHEALCSKALLNDTAFLEKWGQPSERHQIFDLRFVNHDDYHYWHERDWFLLTEYAKTFDVFEALDYQDKAELVRHAAITVPVLVQVWNSPDYGPDTIVFPDGAYFDRTPEPTRPAGLNRKKYQMLDLVLKPFRDLQLDATEFAAFKAVTFLNPDADISLPARKLVNNERVRITKQLYGYMAMKDDVDTAIERFARLVLMGTSMSKMACESKEAVWIADFFENIGFSAFARQLFFGDTTSVVAHKL
Protein: Heptahelical transmembrane protein 2 (PAQR family protein HHP2) (Q84N34)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in abiotic stress response.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- F-box/kelch-repeat protein At1g57790
- AT3g59090/F17J16_140
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 6
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 8
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7
- AT5g66920/MUD21_18
- At3g09570
- Tobamovirus multiplication protein 3
Sequence:
MQKRRTVKESTKIRNGKGMDSGEKKRSEKRLMKFEELPRYLKDNEFIHNHYRCEWSIKETFLSAFSWHNETLNIWTHLCGFAIFTWMMVVSSMETTELGLAGFVSLLSGATIRWPWPSMAMSKDVYFSSDQTLHHDLNVTHTRSLLNSQGDVNYEAIPKWPWLVFLTGAMGCLICSSMSHLFACHSRRFNLFFWRLDYAGISLMIVCSFFAPIYYAFSCHTYWRLFYLSSISILGLLAIFTLLSPSLSAPRFRSFRAALFLTMGFSGVIPATHVLYLHKDHPNVLIALVYELAMAVLYATGAAFYVTRIPERWKPGAFDIAGHSHQIFHVFVVLGALAHSVASLLIMDFRRASPSCAF
Protein: Dedicator of cytokinesis protein 6 (Q96HP0)
Organism: Homo sapiens (Human)
Function: Acts as guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases. Through its activation of CDC42 and RAC1, may regulate neurite outgrowth (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17196961}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17196961}. Note=Mainly located near the cell surface.
Interaction partners:
- Dedicator of cytokinesis protein 8
- DISP complex protein LRCH3
- Cell division control protein 42 homolog
- Leucine-rich repeat and calponin homology domain-containing protein 1
- EGF domain-specific O-linked N-acetylglucosamine transferase
- Rho GTPase-activating protein 31
Sequence:
MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRCSSSLGVPLTEVVEPLDFEDVLLSRPPDAEPGPLRDLVEFPADDLELLLQPRECRTTEPGIPKDEKLDAQVRAAVEMYIEDWVIVHRRYQYLSAAYSPVTTDTQRERQKGLPRQVFEQDASGDERSGPEDSNDSRRGSGSPEDTPRSSGASSIFDLRNLAADSLLPSLLERAAPEDVDRRNETLRRQHRPPALLTLYPAPDEDEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGILALYDVREKKKISENFYFDLNSDSMKGLLRAHGTHPAISTLARSAIFSVTYPSPDIFLVIKLEKVLQQGDISECCEPYMVLKEVDTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVHLANIVSSAGQLDRDSDSEGERRPAWTDRRRRGPQDRASSGDDACSFSGFRPATLTVTNFFKQEAERLSDEDLFKFLADMRRPSSLLRRLRPVTAQLKIDISPAPENPHFCLSPELLHIKPYPDPRGRPTKEILEFPAREVYAPHTSYRNLLYVYPHSLNFSSRQGSVRNLAVRVQYMTGEDPSQALPVIFGKSSCSEFTREAFTPVVYHNKSPEFYEEFKLHLPACVTENHHLLFTFYHVSCQPRPGTALETPVGFTWIPLLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQDPYLDKFFTLVHVLEEGAFPFRLKDTVLSEGNVEQELRASLAALRLASPEPLVAFSHHVLDKLVRLVIRPPIISGQIVNLGRGAFEAMAHVVSLVHRSLEAAQDARGHCPQLAAYVHYAFRLPGTEPSLPDGAPPVTVQAATLARGSGRPASLYLARSKSISSSNPDLAVAPGSVDDEVSRILASKLLHEELALQWVVSSSAVREAILQHAWFFFQLMVKSMALHLLLGQRLDTPRKLRFPGRFLDDITALVGSVGLEVITRVHKDVELAEHLNASLAFFLSDLLSLVDRGFVFSLVRAHYKQVATRLQSSPNPAALLTLRMEFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQSSTFSSQAPDPKVTSMFELSGPFRQQHFLAGLLLTELALALEPEAEGAFLLHKKAISAVHSLLCGHDTDPRYAEATVKARVAELYLPLLSIARDTLPRLHDFAEGPGQRSRLASMLDSDTEGEGDIAGTINPSVAMAIAGGPLAPGSRASISQGPPTASRAGCALSAESSRTLLACVLWVLKNTEPALLQRWATDLTLPQLGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKARLEEAILGTIGARQEMVRRSRERSPFGNPENVRWRKSVTHWKQTSDRVDKTKDEMEHEALVEGNLATEASLVVLDTLEIIVQTVMLSEARESVLGAVLKVVLYSLGSAQSALFLQHGLATQRALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRTHASASLYLLMRQNFEIGHNFARVKMQVTMSLSSLVGTTQNFSEEHLRRSLKTILTYAEEDMGLRDSTFAEQVQDLMFNLHMILTDTVKMKEHQEDPEMLIDLMYRIARGYQGSPDLRLTWLQNMAGKHAELGNHAEAAQCMVHAAALVAEYLALLEDHRHLPVGCVSFQNISSNVLEESAISDDILSPDEEGFCSGKHFTELGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVHGKLQEAFTKIMHQSSGWERVFGTYFRVGFYGAHFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVEIIKDSNPVDKSKLDSQKAYIQITYVEPYFDTYELKDRVTYFDRNYGLRTFLFCTPFTPDGRAHGELPEQHKRKTLLSTDHAFPYIKTRIRVCHREETVLTPVEVAIEDMQKKTRELAFATEQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLAEIPEDPKLFRHHNKLRLCFKDFCKKCEDALRKNKALIGPDQKEYHRELERNYCRLREALQPLLTQRLPQLMAPTPPGLRNSLNRASFRKADL
Protein: Proteasome subunit beta type-6 (EC 3.4.25.1) (20S proteasome beta subunit A-1) (Proteasome component D) (Proteasome subunit beta type-1) (Q8LD27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-3-B
- Proteasome subunit alpha type-4-A
- Proteasome subunit alpha type-6-B
- Proteasome subunit alpha type-5-B
- Proteasome subunit beta type-4
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3-A
- Proteasome subunit alpha type-7-B
- Proteasome subunit alpha type-1-B
Sequence:
MDLNLDAPHSMGTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSANLIRMLAYNNKNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKAVSLAIARDGASGGVVRTVIINSEGVTRNFYPGDKLQLWHEELEPQNSLLDILNAAGPEPMAM
Protein: Myelin expression factor 2 (MEF-2) (MyEF-2) (MST156) (Q9P2K5)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor of the myelin basic protein gene (MBP). Binds to the proximal MB1 element 5'-TTGTCC-3' of the MBP promoter. Its binding to MB1 and function are inhibited by PURA (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Cortexin-2
- Pre-mRNA-splicing factor SYF1
Sequence:
MADANKAEVPGATGGDSPHLQPAEPPGEPRREPHPAEAEKQQPQHSSSSNGVKMENDESAKEEKSDLKEKSTGSKKANRFHPYSKDKNSGAGEKKGPNRNRVFISNIPYDMKWQAIKDLMREKVGEVTYVELFKDAEGKSRGCGVVEFKDEEFVKKALETMNKYDLSGRPLNIKEDPDGENARRALQRTGGSFPGGHVPDMGSGLMNLPPSILNNPNIPPEVISNLQAGRLGSTIFVANLDFKVGWKKLKEVFSIAGTVKRADIKEDKDGKSRGMGTVTFEQAIEAVQAISMFNGQFLFDRPMHVKMDDKSVPHEEYRSHDGKTPQLPRGLGGIGMGLGPGGQPISASQLNIGGVMGNLGPGGMGMDGPGFGGMNRIGGGIGFGGLEAMNSMGGFGGVGRMGELYRGAMTSSMERDFGRGDIGINQGFGDSFGRLGSAMIGGFAGRIGSSNMGPVGSGISGGMGSMNSVTGGMGMGLDRMSSSFDRMGPGIGAILERSIDMDRGFLSGPMGSGMRERIGSKGNQIFVRNLPFDLTWQKLKEKFSQCGHVMFAEIKMENGKSKGCGTVRFDSPESAEKACRIMNGIKISGREIDVRLDRNA
Protein: Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (HsHPK) (PKU-alpha) (Tousled-like kinase 2) (Q86UE8)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A and ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy.
Subcellular location: Nucleus {ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:29955062, ECO:0000269|PubMed:33323470, ECO:0000269|PubMed:9427565}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:33323470}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:33323470}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10455159}. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle (PubMed:10455159). Present in the perinuclear region at S phase and in the nucleus at late G2 (PubMed:10455159). {ECO:0000269|PubMed:10455159}.
Interaction partners:
- Histone chaperone ASF1A
- Serine/threonine-protein kinase tousled-like 1
- Histone chaperone ASF1B
- Calcineurin-binding protein cabin-1
- Serine/arginine-rich splicing factor 1
Sequence:
MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYETSQGKGTPRGHKISDYFEFAGGSAPGTSPGRSVPPVARSSPQHSLSNPLPRRVEQPLYGLDGSAAKEATEEQSALPTLMSVMLAKPRLDTEQLAQRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETPSSGNTELKDTAPALGAHSLLRLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN
Protein: CDP-diacylglycerol--inositol 3-phosphatidyltransferase (EC 2.7.8.11) (Phosphatidylinositol synthase) (PI synthase) (PtdIns synthase) (Q10153)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the synthesis of phosphatidylinositol (PtdIns).
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:P06197}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P06197}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P06197}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P06197}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P06197}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P06197}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P06197}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P06197}.
Interaction partners:
- Putative phosphatidate cytidylyltransferase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase pik1
- Phosphatidylinositol 4-kinase stt4
- Phosphatidylinositol 3-kinase pik3
- Uncharacterized CDP-alcohol phosphatidyltransferase class-I family protein C22A12.10
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phosphatidylinositol 4-kinase lsb6
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase ptn1
- Uncharacterized protein C19F5.03
Sequence:
MGKNEQKDPNVYFFVPNLIGFTRVFLVLISLYFMSWHPNYCTIVYLYSSLLDAFDGWAARKLHQATNFGAILDMVTDRCATSCLLCFLCAAYPKYAIIFQLLVSLDLASHYMHMYSTLHQGASSHKTVTKKHNWMLRLYYGNNKVLFIFCAANEMFFVALYLLSFTPRTPPKLGYLPVPSFIYSTGELPLSYPTLLAVLCGPICLAKQIINVVQLVNAANALVKMDVEQRRAAKKLQ
Protein: Probable transcription factor At1g44810 (Storekeeper-like protein At1g44810) (Q9LPF0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Oxysterol-binding protein-related protein 4C
- GLABROUS1 enhancer-binding protein
Sequence:
MNKKLLNPLEDPPTASSSEDVDEEISSGEDEKEHISNSSSSEEENELKDLSTQTLNSPSTEAPTLDSGSETNSDSDKPIVLTSQKKKEGTDSSGTKRASEGTSSKDIKRAKKVSGDDDNKKFQSLWTKEDEISLLQGMIDFKAETGTSAHDDMNGFFDIAKRYISFDVSKIQFGDKIRGLKKKYFGVRKKKGLDLDHDKKCLGLAKSIWGLDGKEVVVLGGDSETSNWFEKSFLVRVVARLGVDECIVKWKWSKVSKETKKRIEEKMKMVEAKELELLSQKIDVLKEVASVIAETI
Protein: Striamin protein (Q9Z2R2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKGLAGEWHQDSGLDIREKAEDFSLPWLLPRLMALVMQEEGRFRSDRNHGYLREWLRIQALTACLPSPLGRVHYAQCSPKQKGRLPRGWASLPSLSVLVRALRASNAFSLGNYYCCPWRGTRWAKGQPGEWARPRASSPSAHREGVAVT
Protein: Kinetochore protein nsk1 (Nucleolus spindle kinetochore protein 1) (Q7LL22)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ensures chromosome alignment and accurate chromosome segregation during mitosis. Promotes proper kinetochore-microtubule (k-MT) interactions during anaphase B. The phosphorylation status of nsk1 affects the proper k-MT coupling, ensuring that it interacts stably only at the correct time during mitosis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:21965289}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21965289, ECO:0000269|PubMed:22065639}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21965289, ECO:0000269|PubMed:22065639}. Note=Undergoes cell cycle-dependent localization changes, nucleolar during interphase, distributed in the nucleoplasm during metaphase, and increased at kinetochores and the spindle during anaphase. {ECO:0000269|PubMed:21965289}.
Interaction partners:
- Dynein light chain Tctex-type
- Microtubule protein alp7
- DASH complex subunit dad1
- DASH complex subunit dad4
- DASH complex subunit spc19
- DASH complex subunit dam1
- DASH complex subunit duo1
- DASH complex subunit DAD5
- DASH complex subunit ask1
- DASH complex subunit spc34
Sequence:
MAYKLSLSAVEPLLIFPAAPFSTKKEKSTFQNNLISSDVFSSALKPLSPLKSLVADFSTHSNPSKDNQLISPPKINHREFLNEEKESDTQTRYLKQLINICNSPSKNHETSLSPSKSTIDNNERKLDNEIDNYKHDVKYSPYKGQGKTSNPSQGTTKCPGIFEEDNFFSVSPKRRKNLFEKYGKTDLGKPARVPSPKKSLSSTIKSPPSRVKLPTSILSKSPPLKVPNKNRSSTFSPLRTPTSSSKTFVIVDHSTPSPPSIRTKLEAFAPNSTFATQKRLRRLATLESSPALRSTLKSLQSKSSPVKLLKLKEEKAKIKNQLFKSEEEKDPVGKQKLPLESSLSPLDHSSAEKEMQKAPAKNKRRRTGSLETGLYPKESPTPSKKRSKRVLWSLKHIVSPGNREKHSLNSTPESIMKKDTKWPQNLAKNNINSEPNTPTKSNIDTGKAHSARAHKTRKNIQS
Protein: DEAD-box ATP-dependent RNA helicase 11 (EC 3.6.4.13) (Q8LA13)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein STABILIZED1
- Cell division cycle 5-like protein
- Polypyrimidine tract-binding protein homolog 2
- Annexin D2
- Tetraspanin-8
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
- 109 kDa U5 small nuclear ribonucleoprotein component GFL
- Annexin D1
- Tetraspanin-9
- At3g06330
Sequence:
MSASWADVADSEKAVSQSKPPYVPPHLRNRPSEPVAAPLPQNDHAGYGGQPAGSRWAPPSSGGGGASGGGYRNDGGRTGYGYGAGGGGGGGGGWNNRSGGWDRREREVNPFGDDAELEPVFTEQENTGINFDAYEDIPVETSGGDVPPPVNTFADIDLGDALNLNIRRCKYVRPTPVQRHAIPILLAERDLMACAQTGSGKTAAFCFPIISGIMKDQHVERPRGSRAVYPFAVILSPTRELACQIHDEAKKFSYQTGVKVVVAYGGTPIHQQLRELERGCDILVATPGRLNDLLERARVSMQMIRFLALDEADRMLDMGFEPQIRKIVEQMDMPPRGVRQTMLFSATFPSQIQRLAADFMSNYIFLAVGRVGSSTDLITQRVEFVQESDKRSHLMDLLHAQRETQDKQSLTLVFVETKRGADTLENWLCMNEFPATSIHGDRTQQEREVALRSFKTGRTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGIATAFFNENNAQLARSLAELMQEANQEVPEWLTRYASRASFGGGKKRSGGRFGGRDFRREGSYSRGGGGGGGGGGSDYYGGGGYGGGGYGGAPSGGYGAGVTSAWD