wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-conjugating enzyme E2 D3 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D3) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D3) (Phosphoarginine phosphatase) (PAPase) (Ubiquitin carrier protein D3) (Ubiquitin-conjugating enzyme E2(17)KB 3) (Ubiquitin-conjugating enzyme E2-17 kDa 3) (Ubiquitin-protein ligase D3) (P61078)
Organism: Rattus norvegicus (Rat)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction. Together with RNF135, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P61077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P61077}. Endosome membrane {ECO:0000250|UniProtKB:P61077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P61077}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D1
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-conjugating enzyme E2 D2B
- Ubiquitin conjugating enzyme E2 V1 like 1
- Polyubiquitin-C
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-ribosomal protein eL40 fusion protein
- STIP1 homology and U-Box containing protein 1, isoform CRA_b.
- E3 ubiquitin-protein ligase TRIP12
- E3 ubiquitin-protein ligase RING2
Sequence:
MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM
Protein: Carboxysome shell vertex protein CcmL (Carbon dioxide concentrating mechanism protein CcmL) (P72759)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Probably forms vertices in the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Has been modeled to induce curvature upon insertion into an otherwise flat hexagonal molecular layer of CcmK subunits.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00858, ECO:0000305|PubMed:18292340}. Note=This cyanobacterium makes beta-type carboxysomes (Probable). Probably forms vertices in the polyhedral carboxysome (Probable). {ECO:0000305|PubMed:17993516, ECO:0000305|PubMed:18292340}.
Interaction partners:
- Carboxysome shell protein CcmK1
- Carboxysome shell protein CcmK2
- Carboxysome shell protein CcmK4
- Carboxysome shell protein CcmK3
- Carboxysome assembly protein CcmM
- Carboxysome assembly protein CcmO
- Carboxysome assembly protein CcmN
- Ribulose bisphosphate carboxylase large chain
- Ribulose bisphosphate carboxylase small subunit
- Carboxysome shell protein CcmP
Sequence:
MQLAKVLGTVVSTSKTPNLTGVKLLLVQFLDTKGQPLERYEVAGDVVGAGLNEWVLVARGSAARKERGNGDRPLDAMVVGIIDTVNVASGSLYNKRDDGR
Protein: RNA polymerase sigma factor SigA (Q72B50)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963}.
Interaction partners:
- DNA primase
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit omega
- Transcription termination/antitermination protein NusA
- Transcriptional regulator, CarD family
- Chaperonin GroEL
- Transcriptional regulator, putative
- Transcriptional regulator, Crp/Fnr family
Sequence:
MSNIKEIQQIKSLIAKGKVSGFLTFDEVNKALPAEVNTPEQIEEIIGIFDQLDIAIVDSEKDGKKISMSPGESEEEAPSEGGLDLSDDEETVDYSSRSTDPVRMYLREMGSVPLLDRDGEVVIAKKIEMGEQDVLYALVEVPVAVEELVNVGEDLKQNRIKLKDVVKTIEEDDPSEDEMNQRQRVILLLEEIRTTFKKKRKVYSKLDECCTLERRVASVQREIMNYKEDIVSRLRDIKLEKTLIDRIIETVEDYVRQMHNCQRDLSAYILSTGKTQAEIQALFSGLEAREVSPVAASAALNMTVEELFSFKEMILGKIEILSRLQDKCCHNVNDLEEVLWRIKRGNSIAMRAKQELIRSNLRLVVSIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYQRGYKFSTYATWWIRQAITRAIADQARTIRIPVHMIETINKLIRTSRYLVQELGRDPTPEEIAERMDYPIDKVKKVLKIAKEPISLETPIGDEEDSSLGDFIEDKKAVAPAEEVVNTKLGEQIASVLADLTPREEQVLRKRFGIGEKSDHTLEEVGKLFNVTRERIRQIEAKALRKLRHPVRSQTLRSYYES
Protein: Large ribosomal subunit protein eL24z (60S ribosomal protein L24-1) (Q42347)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might have an extraribosomal function in reinitiation of translation.
Interaction partners:
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein uL22z
- Large ribosomal subunit protein eL31x
- Large ribosomal subunit protein uL30y
- Large ribosomal subunit protein eL28y
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein eL13x
Sequence:
MVLKTELCRFSGQKIYPGRGIRFIRSDSQVFLFLNSKCKRYFHNKLKPSKLCWTAMYRKQHKKDAAQEAVKRRRRATKKPYSRSIVGATLEVIQKKRAEKPEVRDAAREAALREIKERIKKTKDEKKAKKVEYASKQQKSQVKGNIPKSAAPKAAKMGGGGGRR
Protein: Synaptosomal-associated protein 25 (SNAP-25) (Super protein) (SUP) (Synaptosomal-associated 25 kDa protein) (P60879)
Organism: Mus musculus (Mouse)
Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16672379}. Cell membrane {ECO:0000269|PubMed:10413679, ECO:0000269|PubMed:9349529}; Lipid-anchor {ECO:0000269|PubMed:9349529}. Synapse, synaptosome {ECO:0000269|PubMed:2592413}. Photoreceptor inner segment {ECO:0000269|PubMed:26406599}. Note=Membrane association requires palmitoylation (PubMed:9349529). Expressed throughout cytoplasm, concentrating at the perinuclear region (PubMed:16672379). Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60881, ECO:0000269|PubMed:16672379, ECO:0000269|PubMed:9349529}.
Interaction partners:
- Vesicle-associated membrane protein 2
- Synaptotagmin-1
- Syntaxin-1A
- Complexin-1
- SNARE-associated protein Snapin
- Vesicle-associated membrane protein 3
- Alpha-soluble NSF attachment protein
- Beta-soluble NSF attachment protein
- Syntaxin-4
- Syntaxin-3
Sequence:
MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
Protein: Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha (GMP-PDE alpha) (EC 3.1.4.35) (P27664)
Organism: Mus musculus (Mouse)
Function: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP. This protein participates in processes of transmission and amplification of the visual signal.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P16499}; Lipid-anchor {ECO:0000250|UniProtKB:P16499}; Cytoplasmic side {ECO:0000250|UniProtKB:P16499}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P16499}.
Interaction partners:
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Guanine nucleotide-binding protein G
- Guanylate kinase
- Adenine phosphoribosyltransferase
- GMP synthase
- Inosine triphosphate pyrophosphatase
Sequence:
MGEVTAEEVEKFLDSNIGFAKQYYNFHYRGKVISDLLGAKEAAVDFSNYHDVNSVEESEIIFDLLRDVQENLQAEKCTFNVMKKLCFLLRADRMSLFMYRTRNGIAELATRLFNVHKDAVLEDCLVMPDSEIVFPLDMGVVGHVAHSKKIANVPNTEEDEHFCDFVDNLTEYQTKNILASPIMNGKDVVAIIMAVNKIDEPHFTKRDEEILLKYLNFVNLIMKVFHLSYLHNCETRRGQILLWSGSKVFEELTDIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEFFDVWPVLMGEAPAYSGPRTPDGREINFYKVIDYILHGKEDIKVIPNPPADHWALVSGLPTYVAQNGLICNIMNAPAEDFFEFQKEPLDESGWMIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDDMDETLMESLTQFLGWSVLNPDTYESMNKLENRKDIFQDIVKYHVKCDNEEIQKILKTREVYGKEPWECEEEELAEILQGELPDAESYEINKFHFSDLPLTELELVKCGIQMYYELRVVDKFHIPQEALVRFMYSLSKGYRRITYHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKTLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYESTQEWTQYMMLEQTRKEIVMAMMMTACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTVLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEITPMLDGITNNRKEWKALADEYEAKMKALEEEKQKQQAAKQAASGNQPGGNPLQGAPASKSCCIQ
Protein: Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Eukaryotic translation initiation factor 3 subunit 7) (eIF-3-zeta) (Q554U9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit L
Sequence:
MSLELNTIKVNPTGWGPVGKLEKFTDIPYAPFSKGDKIGKCSDWNSNVRNYQRQNYGSNAFNPFTFKLEDDEDSFTLVDYTRVQNKLKNKGKTYQKQFYQQNKRGGSNAGGRGGRGGMRGGRFGSNNKYWNDRRQRNRESSIEILSSWESKEEFDLSTFKQYTVEQLPEPETIGTYGQVKYYNKVYDRINAKNEKKLQKTENSVPLIPTSDDKVIRSEYMNGNVYATDSILAVLMSAQKSVYSWDIVVQKVGARLFFELRPGTSEHLTVNENLTAHHQDDKDPINTTSSLSQEATQVNLNYWQQVLSQNVEPFKFDNELPEGDEFENCVDVGYAYKKWDLGDDIVVLARTEIDGVVEGLPGQPPKFISIKAINEHDSNRFGIEFRKKLDSQRAAILATEIKNNSTKFAKWSIQSTLAGCEMLNLGFVSRDSIRDNNNHVILGTQFYPVADLNKQNGVDMKNCWGILKHIAQTCMKLANGKYLLHRDPNRNVINLYSVPENAFDQIEEETQEEEEEEQSKGWVEESRE
Protein: Bifunctional ligase/repressor BirA (Biotin operon repressor) (Biotin--[acetyl-CoA-carboxylase] ligase) (EC 6.3.4.15) (Biotin--protein ligase) (Biotin-[acetyl-CoA carboxylase] synthetase) (P06709)
Organism: Escherichia coli (strain K12)
Function: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
Interaction partners:
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- Biotin synthase
- Biotin carboxylase
- UDP-N-acetylenolpyruvoylglucosamine reductase
- tRNA-specific adenosine deaminase
- ATP-dependent dethiobiotin synthetase BioD 1
- Biotin sulfoxide reductase
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
- 8-amino-7-oxononanoate synthase
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
Sequence:
MKDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSVAVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAEK
Protein: Phosphatidic acid phosphatase, putative (EC 3.1.3.4) (Q388K6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Lipin, putative
- sphinganine-1-phosphate aldolase
- Acyltransferase
- Phospholipid:diacylglycerol acyltransferase-like protein
- Phosphatidate cytidylyltransferase
- 3-dehydrosphinganine reductase
- Ethanolaminephosphotransferase, putative
- sphingolipid 4-desaturase
- Phosphatidic acid phosphatase protein, putative
- Phosphatidylcholine:ceramide cholinephosphotransferase 4
Sequence:
MATGGRSSFAVYLYYAKVLRLLDYLVAFCFGATGFLLGRLIRPYCRTFSWDDLSINNSFAEKETFPDWSLVVMALVSCLFIFIIEKMRERYSPVGEWYMDEQLPEPSSNSITSSTNVLSEERAANRGGASVRERNGLENLPPAPSFERKVQRKFIVDQVINLWILSVVFAFFFSLGIVDVLKIYAGRLRPDFLDRLRREGFNATSPPSNACSLAREGRLSFPSGHSSCAFAAFTPLTMYFLGLSRAFNSGPVWRIILSMFPIYLAICVAASRTRDNRHHFSDILGGSVIGLVIGAFSVNIFFRVRSGEGYLVPRRLEPPRRRSGSPNDNDTV
Protein: Protein MAK11 (Maintenance of killer protein 11) (P20484)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for cell growth. Plays a role in assembly of 60S pre-ribosomal particles in the nucleolus. Also required for replication of the M1 double-stranded RNA of the L-A virus. This latter function may reflect an enhanced requirement for free 60S ribosomal particles for the translation of viral mRNAs which lack poly-A tails.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:2826479}. Nucleus membrane {ECO:0000269|PubMed:2826479}; Peripheral membrane protein {ECO:0000269|PubMed:2826479}. Note=Membrane associated.
Interaction partners:
- Ribosome biogenesis protein RLP24
- Ribosome biogenesis protein RPF2
- 25S rRNA
- 60S ribosome subunit biogenesis protein NIP7
- Ribosome biogenesis protein YTM1
- ATP-dependent RNA helicase HAS1
- Ribosomal RNA-processing protein 15
- Nucleolar GTP-binding protein 1
- Proteasome-interacting protein CIC1
- Ribosome biogenesis protein BRX1
Sequence:
MSAIGDKNQFRIIVGSYEHNILCLSLDIPNQKENDAAKTPHFMPIFHFQAHSLSIKCLAVSRRYLVSGSNDEHIRIYDLQKRKELGTLLSHQGSITALQFSHPASSSEDAAVSKGSKNSKWLLSASEDHKIMVWRVKDWETVGTLKGHTARVNDVDIHPTNRIAISVSDDHSIRLWNLMTLRNAAVLKLRKYNTNGTCVRWLGAKGDYFAVGLRDRVLIYETGSAKVFKEIVFQRKTLMHIETHILPFDNKEYLSVGISDGNVHFYPCEELFEKVEENEKQEDDDDKEDISPAFSLLGHTNRIKDFKFYTNEFGTYLVTIGSDGKIVVWDMSTKEQVAVYDCGERLNCLTLCDESIEKYNTMKKRDAETADIGDQSEVESDTEELKKIMFGEKKKLNKKKRKQLKKSKVSVELE
Protein: LD46453p (Q960L4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNPIVESVRPLHSSKVWEDISPQFLVTFWSLSMYDLHVPNESYQREVAKLKQLAQQAAEGKDSNQSKNKKEQERYIALMEKLNDERKKQHEHVDKISQRLQEQKDSWFLLRSGKSAKNDTITQFLQLCLFPRCTFTALDALYCAKFVHTIHNLKTSNFSTLLCYDRIFCDITYSVTSCTEGEATRYGRFLCAMLETVMRWHADQAVFNKECANYPGFVTKFRVSNQFSEANDHVGYENYRHVCHKWHYKITKAIVFCLDSKDFMQIRNALIILMRILPHYPVLSKLAQIIERKVDKVREEEKTKRPDLYAIASSYIGQLKLKTPHMLKESVFHQIAERPNKESPTSVGAPAAATRSDKLSPTSPSGNTQGTRAPGGAAPFYNSEQKSVIKEPDAKAASTTRESKSQRGEGNNVTLVSTATSTASNNERESKQRDLPAPRESQSRSKDDQQEQANNGSNGSRQSESRNRDVERDRHDQQDQRSISSHRSSRDIVRVKERTEAELHQRSRERSQRLEELEAQQRKREKTSRRGGEERIRHGDGVETVDLVGSTDNRHYEEFEGRMRDLSSVSNESNGSLHHRQRSHETIEFEKVDSKRRKLESSTSSSKKVEELVDSVKKARALKTKERNKDKLSDEEQDARKDRKLGRKRDRVDESNSNEHKRRREGQNGEEELRDRERHREKSPRERSHEKFDRERGGASGSRAEERQYISKSARSSRVNY
Protein: CUB-like domain-containing protein (Q19223)
Organism: Caenorhabditis elegans
Interaction partners:
- CUB-like domain-containing protein
- ShKT domain-containing protein
- CUB-like domain-containing protein
- Lysozyme-like protein 7
- Mitogen-activated protein kinase pmk-1
- CUB-like domain-containing protein
- CUB-like domain-containing protein
- CUB-like domain-containing protein
- Transcription factor atf-7
- CUB-like domain-containing protein
Sequence:
MKTLLWFLVFVGVSNALDCTQIPAGGIVPRHNATIPAGAKEPVLIPPNFNCLYNIKVPAMVYARVVLENGLNGNNDQITVTNEQNAKTFINSRSGKYATFYVFPNTLTSFLVSTKSVNMHSSFRMVVDYYSLNNATVTYLDNPDMQYSRLYTLQAEIGWSPRTIVAKERMSISIAYSGWTPYDNLYNFFLIEGDLENPLAIYRMTQFLYQNYISKGNKVTVLGLDNTFSRSSIVFVPLSQAQQYDSYTAASGYMNLNQVDIDATVGEKKKKIVTMISMRDYVMIWKMEKTSNPDCVLKAITSPPTSESKVLLDFSVETQFPTNITRPSFCIIAENCAASIQFIVL
Protein: Actin-binding LIM protein 1 (A0A8I5Y740)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVKEKVAHPQDPHHSSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGDYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKEATCSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGSPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPPNIPRSSSDFFYPKSLIRRTGRSPALQPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYEDKQDRQSLGESPRTLSPTPSAEGFQDGRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPGNEPSSGRNSPLPYRPDSRPLTPTYAQAPKHFHVPDQGINIYRKPPIYKQHGTDPRRRSSGREEDEEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKENRERASLLASRYDSPLHSASHAPSSKTSSLPGYGKSGLHRPVSTDFAQYNSYGDVSGGVRDYQTLPDGHMPAMRMDRGVSMPNMLEPKIFPYEMLMVTNRGRNKILRDVDRTRLERHLAPEVFWEIFGMSIQEFDKLPLWRRNDMKKKAKLF
Protein: Interleukin enhancer-binding factor 2 (Nuclear factor of activated T-cells 45 kDa) (Q9CXY6)
Organism: Mus musculus (Mouse)
Function: Chromatin-interacting protein that forms a stable heterodimer with interleukin enhancer-binding factor 3/ILF3 and plays a role in several biological processes including transcription, innate immunity or cell growth. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. Together with ILF3, forms an RNA-binding complex that is required for mitotic progression and cytokinesis by regulating the expression of a cluster of mitotic genes. Mechanistically, competes with STAU1/STAU2-mediated mRNA decay. Also plays a role in the inhibition of various viruses including Japanese encephalitis virus or enterovirus 71 (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q12905}. Cytoplasm {ECO:0000250|UniProtKB:Q12905}. Nucleus {ECO:0000250|UniProtKB:Q12905}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:Q12905}.
Interaction partners:
- Interleukin enhancer-binding factor 3
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Heterogeneous nuclear ribonucleoprotein M
- ATP-dependent RNA helicase A
- Heterogeneous nuclear ribonucleoprotein H
- Y-box-binding protein 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- Heterogeneous nuclear ribonucleoprotein Q
- Heterogeneous nuclear ribonucleoprotein U
- Heterogeneous nuclear ribonucleoprotein H2
Sequence:
MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE
Protein: Aphrodisin (Q9Z1I7)
Organism: Mesocricetus auratus (Golden hamster)
Function: Acts as an aphrodisiac pheromone, reliably eliciting copulatory behavior from male hamster.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MVKILVLALVFSLAHAQDFAELQGKWYTIVIAADNLEKIEEGGPLRFYFRHIDCYKNCSEMEITFYVITNNQCSKTTVIGYLKGNGTYQTQFEGNNIFQPLYITSDKIFFTNKNMDRAGQETNMIVVAGKGNALTPEENEILVQFAHEKKIPVENILNILATDTCPE
Protein: Glial fibrillary acidic protein (GFAP) (Q58EE9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12801639}. Note=Associated with intermediate filaments.
Interaction partners:
- Oligodendrocyte lineage transcription factor 2.
- ELAV-like protein
- Transcription factor Sox-2
- Brain-type fatty acid-binding protein
- DnaJ homolog subfamily C member 2
- Glutamine synthetase
- Glutamine synthetase
- Glutamine synthetase
- Protein S100-B
- Growth-associated protein 43.
Sequence:
MESQRSFSSYRKRFGTPGGSPSVGVTSRHSTGRLSLHSSPRHLTSSPLTLSTSRLSLGGERLDFSADSLLKAQYRETRTNEKVEMMGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGKEPSRLGDIYQEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKKVHEEEMRELHEQLMAQQVHVDLDVSKPDLTAALKEIRAQFEAMANSNMQETEEWYRSKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSNESLERQLREMEERFAIETAGYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEESRITVPVQNFTNLQFRDTSMDTKLTPEAHVKRSIVVRTVETRDGEIIKESTTERKDLP
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase (EC 2.4.1.109) (Q5BDC1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase
- Dolichyl-phosphate-mannose--protein mannosyltransferase
Sequence:
MSSSPSLRKRGGKREDTPVPSDRSFAPSASQLGAASRSSEWDYRLAITILTVLAFITRFYKISYPDQVVFDEVHFGKFASYYLRRTYFFDVHPPFAKLLLAFTGWLVGYDGHFLFENIGDSYIDNKVPYVALRAMPAVLGALTIPVVFLIMWESGYSLPACVLASGLVLFDNAHVGEDRLILLDSTLVITMALSILCYIRFYKLRHEPFGRKWWKWLLLTGVSLSCVISTKYVGVFTFVTIGSAVMVDLWNLLDIRRQGGALTMFEWTKHFAARFFSLIVVPFFFYLFWFQVHFAILTHSGPGDDFMTPAFQETLSDNAMAAQSVSIEYFDTITMRHKDTKVFLHSHSDTYPLRYDDGRISSQGQQVTGYPYNDTNNHWQIIPTVPLDETDEKSRKVRNGDIVQLRHVATDTILLTHDVASPYYPTNQEFTTVSHELADGKRHNDTLFEIRVEHGKSKQEFRTLSSQFKLVHVPTKVAMWTHTTPLPDWAYKQAEINGNKNVLQSSNIWYVEAIESLEEDSPRLKKEERKVKHLPFWRKYIELQRAMFFHNNALTSSHPYASEPFQWPFLLRGVSFWTKSDTREQIYFLGNPVGWWISSSLLAVFAGVIGADQLSLRRGVDAVEEIWGPGSRSRLYNSTGFLFLCWAAHYFPFWLMGRQRFLHHYLPAHVASALVTGALIEFIFNIQPISVPATIPVAADDPTGKGKTRRFVTARERMGVKSIVAGWIASLTILAATIWGFWFFAPLTYGTPGLDVAQVNARKWLGYDLHFAK
Protein: SET and MYND domain-containing protein 4 (Q7KMH5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- AT24727p
- SET and MYND domain containing, arthropod-specific, member 6
- SET and MYND domain containing, arthropod-specific, member 2
- GH11294p
- RE12806p
- SET and MYND domain containing, arthropod-specific, member 4, isoform A
- Protein-lysine N-trimethyltransferase SMYD5
Sequence:
MDVYDVSDDLIKKLQDWKLIGIISGKFNELKENHRKVDFVMRALIDFKYIEKIFLNVTLREDKCNKRSVEFRMLGNEQFSLKNRNYFQALELYNKSICYAEPNSEHLSIGYANRSAVLFEWKRYRQCLDNIKLARQANYPARLSHKLDKRERDCQQLLDQQPPDVVPYEFKLSFEPHAQVPFIADCLELRETAAEGRFVVTNRDLAVGDLVSVEEPFCSTLLTPMRYIRCATCKRENYLTLIPCDSCCSTMFCSEECKSIAMQTYHRYECPIIDFLNRMFNKIHCIALRTTLVALNIFPSIEELIDFCEQEQNQDKCAFDLNYNELTPEEHYRAIHGLVTNQHLRSVSDLFQRSVVCAVLKHFIIEYTPVKEYLGGEEGVNFFTDLLFRHLQTSPSNMHGIDLVEQVNETKDDQTHSSGAYAFLSLINHSCAPNTVRIYEGTKAYMFVLRPIKAGNVLYDNYGAHFAICSKEQRLKRLSLQYRFDCKCEGCELNYPMFGMMPHKATVPSVTDDTELALSSYNYDFAVSNYRKYCDFLTQYGDDYPCEQISSAEECLKMALHIMADAVPLKAKM