wanglab/gogpt-training-data huggingface dataset:
Protein: Histone deacetylase phd1 (EC 3.5.1.98) (O13298)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Is not essential.
Subcellular location: Nucleus {ECO:0000269|PubMed:9781677}.
Interaction partners:
- Set3 complex subunit hif2
- Uncharacterized protein C22E12.19
- SET domain-containing protein 3
- RbAp48-related WD40 repeat-containing protein prw1
- Paired amphipathic helix protein pst3
- Putative histone deacetylase complex subunit cti6
- Transcriptional regulatory protein rxt3
- Histone deacetylase clr6
- SWIRM domain-containing protein laf2
- SWIRM domain-containing protein laf1
Sequence:
MDTPETSTPYEQVEKGSFFSFRPQKKRVTYHLDEQVGNYHYGDKHPMKPHRITITNHLVMGYGLHNKMSVFSPRMATFGEMSEFHREDYLDFLKRVTPDNAEQFADKFQQFNIGDDCPVFDGTYEFSQRSAGASLDASRKLVQGQTDIAINWSGGLHHAKRGEASGFCYVNDIVLAILNMLRFFPRVLYIDIDIHHGDGVQQAFYESDRVLTVSFHKYNGDFFPATGNFDENGVKGGKYFALNVPLEDGIGDEQYTSLFKSIIEPTINTFQPSAIVLQCGADSLGYDRLGVFNLSIHAHGECVRFTRSFNIPMLVVGGGGYTLRNVARAWCYETSICVNEQIPSELPRETLYYEFFAPDYTLHPRLTTKIENKNTPKALEDLRIRALEQLRYLGGAPSVQMQQIPPDLTGHLEEEDERLNDEYLDKAVDVRVRG
Protein: Annexin A6 (Annexin VI) (Annexin-6) (Calcium-binding protein 65/67) (CBP 65/67) (P48037)
Organism: Rattus norvegicus (Rat)
Function: May associate with CD21. May regulate the release of Ca(2+) from intracellular stores.
Subcellular location: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}.
Interaction partners:
- Prolow-density lipoprotein receptor-related protein 1
Sequence:
MAKIAQGAMYRGSVHDFADFDANQDAEALYTAMKGFGSDKESILELITSRSNKQRQEICQSYKSLYGKDLIADLKYELTGKFERLIVNLMRPLAYCDAKEIKDAISGIGTDEKCLIEILASRTNEQIHQLVAAYKDAYERDLESDIIGDTSGHFQKMLVVLLQGTRENDDVVSEDLVQQDVQDLYEAGELKWGTDEAQFIYILGNRSKQHLRLVFDEYLKTTGKPIEASIRGELSGDFEKLMLAVVKCIRSTPEYFAERLFKAMKGLGTRDNTLIRIMVSRSELDMLDIREIFRTKYEKSLYSMIKNDTSGEYKKALLKLCGGDDDAAGQFFPEAAQVAYQMWELSAVSRVELKGTVRAANDFNPDADAKGLRKAMKGIGTDEATIIDIITQRSNVQRQQIRQTFKSHFGRDLMADLKSEISGDLARLILGLMMPPAHYDAKQLKKAMEGAGTDEKALIEILATRTNAEIRAINEAYKEDYHKSLEDALSSDTSGHFKRILISLATGNREEGGENRDQAQEDAQVAAEILEIADTPSGDKTSLETRFMTVLCTRSYPHLRRVFQEFIKKTNYDIEHVIKKEMSGDVKDAFVAIVQSVKNKPLFFADKLYKSMKGAGTDEKTLTRVMVSRSEIDLLNIRREFIEKYDKSPHQAIEGDTSGDFMKALLALCGGED
Protein: Transmembrane emp24 domain-containing protein p24beta3 (p24 family protein beta2) (p24beta2) (p24 family protein beta3) (p24beta3) (Q9LIL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side (By similarity).
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:22132757}; Single-pass type I membrane protein {ECO:0000269|PubMed:22132757}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:22132757}; Single-pass type I membrane protein {ECO:0000269|PubMed:22132757}. Note=Cycles between the endoplasmic reticulum and Golgi via COPI and COPII dependent pathways. {ECO:0000250}.
Interaction partners:
- Transmembrane emp24 domain-containing protein p24delta9
- Transmembrane emp24 domain-containing protein p24delta11
- Transmembrane emp24 domain-containing protein p24delta10
- Transmembrane emp24 domain-containing protein p24delta5
- Transmembrane emp24 domain-containing protein p24delta7
- Transmembrane emp24 domain-containing protein p24delta4
- Transmembrane emp24 domain-containing protein p24delta6
- Transmembrane emp24 domain-containing protein p24delta3
- Transmembrane emp24 domain-containing protein p24delta8
- ER lumen protein-retaining receptor A
Sequence:
MERRQAKIHVFVLIGLILLNSINQISSLSVTVNDEECVQEYVLYEGDTVSGNFVVVDHDIFWGSDHPGLDFTVTSPAGNIVQTLKGTSGDKFEFKAPKSGMYKFCFHNPYSTPETVSFYIHVGHIPNEHDLAKDEHLDPVNVKIAELREALESVVAEQKYLKARDTRHRHTNESTRKRVIFYTVGEYIFLAAASGLQVLYIRKLFSKSVAYNRV
Protein: Cyanocobalamin reductase / alkylcobalamin dealkylase (Alkylcobalamin:glutathione S-alkyltransferase) (EC 2.5.1.151) (CblC) (Cyanocobalamin reductase (cyanide-eliminating)) (EC 1.16.1.6) (Methylmalonic aciduria and homocystinuria type C protein) (MMACHC) (Q9CZD0)
Organism: Mus musculus (Mouse)
Function: Cobalamin (vitamin B12) cytosolic chaperone that catalyzes the reductive decyanation of cyanocob(III)alamin (cyanocobalamin, CNCbl) to yield cob(II)alamin and cyanide, using FAD or FMN as cofactors and NADPH as cosubstrate. Cyanocobalamin constitutes the inactive form of vitamin B12 introduced from the diet, and is converted into the active cofactors methylcobalamin (MeCbl) involved in methionine biosynthesis, and 5'-deoxyadenosylcobalamin (AdoCbl) involved in the TCA cycle. Forms a complex with the lysosomal transporter ABCD4 and its chaperone LMBRD1, to transport cobalamin across the lysosomal membrane into the cytosol. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR (methionine synthase) which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine. Also acts as a glutathione transferase by catalyzing the dealkylation of the alkylcob(III)alamins MeCbl and AdoCbl, using the thiolate of glutathione for nucleophilic displacement to generate cob(I)alamin and the corresponding glutathione thioether. The conversion of incoming MeCbl or AdoCbl into a common intermediate cob(I)alamin is necessary to meet the cellular needs for both cofactors. Cysteine and homocysteine cannot substitute for glutathione in this reaction.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y4U1}.
Interaction partners:
- Cobalamin trafficking protein CblD
- Methionine synthase reductase
- Methionine synthase
- Corrinoid adenosyltransferase MMAB
- Methylmalonic aciduria type A homolog, mitochondrial
- Methylmalonyl-CoA mutase, mitochondrial
- Diacylglycerol kinase epsilon
- Lysosomal cobalamin transport escort protein LMBD1
Sequence:
MEPRVAELKQKIEDTLCPFGFEVYPFQVAWYNELLPPAFHLPFPGPTLAFLVLSTPAMFDRALKPFLKSCHFQTLRDPVDQCVSYHLRSVTEKFPEVHMEVIADYEVHPNRRPKILAQTAAHVAGAAYYYQRQDVDADPWGTQHIAGVCIHPRFGGWFAIRGVMLLPGIEVPNLPPRKPPDCVPTRAGRITLLEGFNFHWRDWTYRDAVTPEERYSEEQKIYFSTPPAQRLALLGLAQPSEHPSTTSELPLSLLTKPQNSRRARSWLSPSVSPPVSPGP
Protein: Phosphoprotein (Protein P) (P04859)
Organism: Sendai virus (strain Harris) (SeV)
Function: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template.
Subcellular location: Host cytoplasm.
Interaction partners:
Sequence:
MDQDAFILKEDSEVEREAPGGRESLSDVIGFLDAVLSSEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQDNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHRAFGGRTGTNSVSQDLGDGGDSGILENPPNERGYPRSGIEDENREMAAHPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLTPATVPGTRSPPLNRYNSTGSPPGKPPSTQDEHINSGDTPAVRVKDRKPPIGTRSVSDCPANGRPIHPGLESDSTKKGIGENTSSMKEMATLLTSLGVIQSAQEFESSRDASYVFARRALKSANYAEMTFNVCGLILSAEKSSARKVDENKQLLKQIQESVESFRDIYKRFSEYQKEQNSLLMSNLSTLHIITDRGGKTDNTDSLTRSPSVFAKSKENKTKATRFDPSMETLEDMKYKPDLIREDEFRDEIRNPVYQERDTEPRASNASRLLPSKEKPTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELVEEDIESLTN
Protein: Translocator protein (Mitochondrial benzodiazepine receptor) (PKBS) (Peripheral-type benzodiazepine receptor) (PBR) (P30536)
Organism: Homo sapiens (Human)
Function: Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme (By similarity). Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism, but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis. Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:1847678}; Multi-pass membrane protein {ECO:0000269|PubMed:1847678}.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC1
- Steroidogenic acute regulatory protein, mitochondrial
- Peripheral-type benzodiazepine receptor-associated protein 1
- Golgi resident protein GCP60
- Non-selective voltage-gated ion channel VDAC3
- Non-selective voltage-gated ion channel VDAC2
- ADP/ATP translocase 3
- ADP/ATP translocase 2
- Acyl-CoA-binding protein
- ADP/ATP translocase 1
Sequence:
MAPPWVPAMGFTLAPSLGCFVGSRFVHGEGLRWYAGLQKPSWHPPHWVLGPVWGTLYSAMGYGSYLVWKELGGFTEKAVVPLGLYTGQLALNWAWPPIFFGARQMGWALVDLLLVSGAAAATTVAWYQVSPLAARLLYPYLAWLAFTTTLNYCVWRDNHGWRGGRRLPE
Protein: GrpE protein homolog (A0A178U8H4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion matrix {ECO:0000256|RuleBase:RU000640}.
Interaction partners:
Sequence:
MAGLLKTPSLHLTPTLLHAPSVPFKPFCVSFAGGRNVSVSLSRRASLRSVSSGYPLRLLNLVPFASGEAETTETEVESNEPEVQETDGAVDVENENASAEEGEAEEEEAAVITALLKSYKEALADNNEGKIAEIEASLKSIEDEKFLLADKVASLSNELSVERDRLIRISADFDNFRKRTERERLNLVSNAQGEVVENLLAVLDNFERAKSQIKVETEGEEKVTNSYQSIYKQFVEILGSLGVIHVETVGKQFDPMLHEAIMREDSAEYEEGIVLEEYRKGFLLGERLLRPSMVKVSAGPGPEKPLEAEGEEATAQGSAEEESSSS
Protein: FI21262p1 (Snazarus, isoform A) (Snazarus, isoform B) (Q9W3N0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- LD12265p
- Sorting nexin-3
- Sorting nexin
- FI18122p1
- LD15323p
- LD13361p
Sequence:
MESEEHAVDAMENRRLPLFPIEPEPSVTATQRLTLLATRLLRALQLNWRIIVSGITLTLLAVIWYYPTFFLFFAFVVYSLVLVFAAVAGTVYIHYIFTTNEPTPPSRVPSRLLYNATKSNIFDLPKPIKNPSNLPLIFGKTVDLQLQQIIEYVLRDFMLPWLGYVVTKPKLINDVVREDLWNAIQKIHERALRMDAAKIIAVDMVNRVTVHLEKIRIAEARAAETNTPPVFSTNSYLADEEKEMEFLRKLCEIMVILLLPRGYSLPPLKVLLSEILSYKIFFPMIKMLTAPDYINQKVVQNIETRLAAAAMSKRSYEYAASFEDFLKIINNSGNLEELSLIRKSIVNDLMHATTMQNLQRAKGLDPDHEDHSLSKSELTAAVRLKRYVRQLTMAKGECEKNLAKFGWNGNYSSDIDLTLVEILNTAVGRRYFTLFLEPLKASALIGFYLAVEEIKHAHKSASHQLGTEIFYTYIRVPKSEIQIDKHERKLIETFLLGDAEPDIFYDIQRNVLRTLEEKYYPPFVLSDQYRQLKEALDSNEIADPTLLMCHTIGDVQEPLADEQPGAADGLNGGAGGAIDVAAHTSYARRKLEQIQERIDKKNQALDALKYSVKPESKVLTILEKEMEWLKSEKRQTEAHLRRTDAWTEHLGKWKATIQSVEVSDEKESLQFMILVHVDEDINAPVQPTSSKNGDSGHANLRKRPSGISSGWVVMRSLNQVHELQRKLRHVSSNLKAIDLPTNFKFFFLKTDRHGQEKAKSQIQKFLNFILEDDHLNGSEAIYTFLSPSSDHLKQSLPSPKKSKFSLSTLFRSDAGKAHEASKATDPFWGLQRDDEDISTYLDGESGGEAKMLAADLDSKDSIAEPMYALMGEIFDMGGVFKWLRKSLISFVQITYGRTINRQIRESVAYLFEESMLHNYFSAILKSFWPGGVLASAYPTRSEDMREMTTTAAKALLTDHIPEVLCNLVGAQAAKRGVLKVFDALQNPAYNKQLFYELLEILMIEFFPEIRQLRVSNSNGTKLNTATAGAAAASAAAALVAATASASLPSLNHSGGGHSASTGGHQNHQGSSSASGSSAGASGATGGGAASHHQSHYHHGSHHHQQQQHHHSQAGSSK
Protein: H/ACA ribonucleoprotein complex subunit 2-like protein (Nhp2-like protein) (Q9LEY9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 3-like protein
- H/ACA ribonucleoprotein complex subunit 1-like protein 2
- Putative H/ACA ribonucleoprotein complex subunit 1-like protein 1
- Putative rRNA 2'-O-methyltransferase fibrillarin 3
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Ribosome assembly factor mrt4
- rRNA 2'-O-methyltransferase fibrillarin 2
- rRNA 2'-O-methyltransferase fibrillarin 1
- H/ACA ribonucleoprotein complex subunit 4
- Nucleolar protein 56
Sequence:
MGSDTEAEKSIQKEKKKYAITLAPIAKPLAGKKLQKRTFKLIQKAAGKKCLKRGVKEVVKSIRRGQKGLCVIAGNISPIDVITHLPILCEEAGVPYVYVPSKEDLAQAGATKRPTCCVLVMLKPAKGDLTAEELAKLKTDYEQVSDDIKELATSVI
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (A1Z8K9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMQYLVVSLALCATICSAAQTRNMPIQAIAYLIGPVQSDNTQVKGNVTFTQNDCGQNVHVRVQLEGLKEGKHGFHIHEKGDLTNGCISMGAHYNPDKVDHGGPDHEVRHVGDLGNLEANSTGIIDVTYTDQVITLTGKLGIIGRGVVVHELEDDLGLGNHTDSKKTGNAGGRIACGVIGINGPSVPAPAPPTPRHQPLYYVPHGEPQDHVVYPLQHYPLPYPHPYPYPHPYPYPYPLSHQLYL
Protein: Interleukin 6 signal transducer (Gp130, oncostatin M receptor) (Q17RA0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLTLQTWLVQALFIFLTTESTGELLDPCGYISPESPVVQLHSNFTAVCVLKEKCMDYFHVNANYIVWKTNHFTIPKEQYTIINRTASSVTFTDIASLNIQLTCNILTFGQLEQNVYGITIISGLPPEKPKNLSCIVNEGKKMRCEWDRGRETHLETNFTLKSEWATHKFADCKAKRDTPTSCTVDYSTVYFVNIEVWVEAENALGKVTSDHINFDPVYKVKPNPPHNLSVINSEELSSILKLTWTNPSIKSVIILKYNIQYRTKDASTWSQIPPEDTASTRSSFTVQDLKPFTEYVFRIRCMKEDGKGYWSDWSEEASGITYEDRPSKAPSFWYKIDPSHTQGYRTVQLVWKTLPPFEANGKILDYEVTLTRWKSHLQNYTVNATKLTVNLTNDRYVATLTVRNLVGKSDAAVLTIPACDFQATHPVMDLKAFPKDNMLWVEWTTPRESVKKYILEWCVLSDKAPCITDWQQEDGTVHRTYLRGNLAESKCYLITVTPVYADGPGSPESIKAYLKQAPPSKGPTVRTKKVGKNEAVLEWDQLPVDVQNGFIRNYTIFYRTIIGNETAVNVDSSHTEYTLSSLTSDTLYMVRMAAYTDEGGKDGPEFTFTTPKFAQGEIEAIVVPVCLAFLLTTLLGVLFCFNKRDLIKKHIWPNVPDPSKSHIAQWSPHTPPRHNFNSKDQMYSDGNFTDVSVVEIEANDKKPFPEDLKSLDLFKKEKINTEGHSSGIGGSSCMSSSRPSISSSDENESSQNTSSTVQYSTVVHSGYRHQVPSVQVFSRSESTQPLLDSEERPEDLQLVDHVDGGDGILPRQQYFKQNCSQHESSPDISHFERSKQVSSVNEEDFVRLKQQISDHISQSCGSGQMKMFQEVSAADAFGPGTEGQVERFETVGMEAATDEGMPKSYLPQTVRQGGYMPQ
Protein: Biosynthetic peptidoglycan transglycosylase (EC 2.4.99.28) (Glycan polymerase) (Monofunctional biosynthetic peptidoglycan transglycosylase) (Monofunctional glycosyltransferase) (Monofunctional GTase) (Peptidoglycan glycosyltransferase MtgA) (PGT) (P46022)
Organism: Escherichia coli (strain K12)
Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors. May play a role in peptidoglycan assembly during cell division in collaboration with other cell division proteins.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00766, ECO:0000269|PubMed:8772200}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00766}. Note=Localizes to the cell division site. {ECO:0000269|PubMed:18165305}.
Interaction partners:
- Peptidoglycan D,D-transpeptidase FtsI
- Peptidoglycan D,D-transpeptidase MrdA
- Probable peptidoglycan glycosyltransferase FtsW
- Penicillin-binding protein 1B
- Peptidoglycan glycosyltransferase MrdB
- Cell division protein FtsN
- Glyoxalase ElbB
- D-alanyl-D-alanine carboxypeptidase DacB
- Lipid II flippase MurJ
- Penicillin-binding protein 1A
Sequence:
MSKSRLTVFSFVRRFLLRLMVVLAVFWGGGIALFSVAPVPFSAVMVERQVSAWLHGNFRYVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSRQAWILRQMYQLGGEPFMQQHQLD
Protein: 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed] (Q9CQV8)
Organism: Mus musculus (Mouse)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P31946}. Melanosome {ECO:0000250|UniProtKB:P31946}.
Interaction partners:
- M-phase inducer phosphatase 2
- 14-3-3 protein zeta/delta
- Serine/threonine-protein kinase B-raf
- 14-3-3 protein theta
- Serine/threonine-protein kinase A-Raf
- Bcl2-associated agonist of cell death
- 14-3-3 protein epsilon
- RAF proto-oncogene serine/threonine-protein kinase
- M-phase inducer phosphatase 3
- Forkhead box protein O3
Sequence:
MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLILNATQAESKVFYLKMKGDYFRYLSEVASGENKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN
Protein: Poly(A) RNA polymerase gld-2 homolog A (DmGLD2) (EC 2.7.7.19) (Q9VD44)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Required for formation of long term memory.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18780789}. Nucleus {ECO:0000269|PubMed:18780789}. Note=Found in neuronal cytoplasm, present in discrete neuronal particles associated with mRNA control, and in nuclear puncta.
Interaction partners:
- Symplekin
- polynucleotide adenylyltransferase
- FI20148p1
- PAPS synthetase, isoform D
- Polyadenylate-binding protein
- Translational regulator orb2
- Protein bicaudal C
Sequence:
MSTAMAMAAAASSSAAAATATTTAISNSTNTTASPATTNTINTTTKTITTSEVPLEPASNMAPKALEIEDSGRNEPEDLEHGAAKPLEQRKTTVVHTCPRPPGGYKYSMEFLYGIGSGMAGIPLNIPTPSSITPRTVRSTAPLLTTHMPLLTNMGVAPSRPSGIRYPGSAGGSNGTTVAASTTPSTTVTTSSGSPGSGAEAITSSVSSSGLPAAGLQAAQFICQGYMPTGPQRRLWHAENAVWQFDRNYPYNQAYSPPYGIPMMPVGFEHPYGQRIIYPGYYNQTPPGINPAAVAGLTRTNRPVTQQPHILTQPAVGTTESSEEAPATLGNAPQVSSTWRYGRPGTHRGRHAVPTAAAPALLHRDSKSFYNSIGSGMANGPRFKAPFVANVRNFQAGAVATVAAGGAATTAVVGTSAPATGAASSSDQNVATKRNHQGAATQNNHRNRHNAKKGGKNSVGKELTSNSSESLSNSSSKSQLNKRPSSSSSISPIKHPHRNYRNRMRYTATEPTEQKAATTTVPISNYQPPQQSTSTVRRTSKFQGSNAYQAHTAAGRQQSRFYQSRHMDGYVFQSGHYMVYAAGAPPVGLRPGKSPVSEATGAPPGAAAATAAAATAVAATAAAAEGGGAAEGGGAAAAPVTASSATLEGEQPLDSDFDQRQEFADLGLDPANGGFSSDLEPNGIKQDTSELDTHSCLISHPNSEVDGDDNQSLASFAPSVESDDSDSELSDASVESVARDILVSCLAVATGAEEPDFSGPNLVPYGDMHYLKELDKKNPPTNGYRSHRPYHQSHYAYHSQMSPRGLSCCGDMLNQHSEDLVFKLDQNQPDGIESGKNIFLREITEQPDNISVASNLSCSPSASSSKSVLAPMASKSNITMPEENNDDDELPLVVHNRYWREFFGYTPADRFLLRAKFVEMRRPPKVMGCKNKWDPLSLSVWKKFLESQQTRHVYKIKMRLWRAIYTVAMKNYPRYGLYLVGSSISYFGSKCSDMDICMLACTNPNIDSRMEAVYHLHVMKELLGRTNMFQDFNLIEARVPILRFTDRCHKVEVDINFNNSVGIRNTHLLYCYSQLDWRVRPMALTVKQWAQYHNINNAKNMTISSYSLMLMVIHFLQVGASPPVLPCLHNLYPEKFGLLQPNDFGYVDMNEVMAPYQSDNSQTLGDLLLSFLHYYSVFDYGKYAISIRVGGVLPIEVCRAATAPKNDIHQWNELCIEEPFDQTNTARSVYDTDTFERIKTIFVASYRRLDSTRNLSAIFEDYDGPTILMQQPSVDSEIELYEGQHHRLLPNRGSSRSNSAIPSPRPSILMVDKATTAIWDDINNKPDHPVLSHSNNYDATNECTGNGSLMGLKDNSVADKPPIA
Protein: Cerebellin-1 (Precerebellin) [Cleaved into: Cerebellin (CER); [des-Ser1]-cerebellin] (P23435)
Organism: Homo sapiens (Human)
Function: Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post-synaptic components. On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2. NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). NRXN1-CBLN1-GRID2 complex mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis. Essential for long-term maintenance but not establishment of excitatory synapses (By similarity). Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9R171}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R171}.
Interaction partners:
- Glutamate receptor ionotropic, delta-2
- Neurexin-1
- Neurexin-2
- Glutamate dehydrogenase 1, mitochondrial
- Nucleoredoxin
- Leucine-rich repeat transmembrane neuronal protein 2
Sequence:
MLGVLELLLLGAAWLAGPARGQNETEPIVLEGKCLVVCDSNPTSDPTGTALGISVRSGSAKVAFSAIRSTNHEPSEMSNRTMIIYFDQVLVNIGNNFDSERSTFIAPRKGIYSFNFHVVKVYNRQTIQVSLMLNGWPVISAFAGDQDVTREAASNGVLIQMEKGDRAYLKLERGNLMGGWKYSTFSGFLVFPL
Protein: Pentatricopeptide repeat-containing protein At3g16010 (Q9LW84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MMYVSARSGSAKRSISSLPHLSQRFKQTENEIVQMFSVPNHEESEKPQEKWKLSRKDPSVRMLDERFIRIVKIFKWGPDAEKALEVLKLKVDHRLVRSILEIDVEINVKIQFFKWAGKRRNFQHDCSTYMTLIRCLEEARLYGEMYRTIQEVVRNTYVSVSPAVLSELVKALGRAKMVSKALSVFYQAKGRKCKPTSSTYNSVILMLMQEGQHEKVHEVYTEMCNEGDCFPDTITYSALISSYEKLGRNDSAIRLFDEMKDNCMQPTEKIYTTLLGIYFKVGKVEKALDLFEEMKRAGCSPTVYTYTELIKGLGKAGRVDEAYGFYKDMLRDGLTPDVVFLNNLMNILGKVGRVEELTNVFSEMGMWRCTPTVVSYNTVIKALFESKAHVSEVSSWFDKMKADSVSPSEFTYSILIDGYCKTNRVEKALLLLEEMDEKGFPPCPAAYCSLINALGKAKRYEAANELFKELKENFGNVSSRVYAVMIKHFGKCGKLSEAVDLFNEMKNQGSGPDVYAYNALMSGMVKAGMINEANSLLRKMEENGCRADINSHNIILNGFARTGVPRRAIEMFETIKHSGIKPDGVTYNTLLGCFAHAGMFEEAARMMREMKDKGFEYDAITYSSILDAVGNVDHEKDDVSSF
Protein: Protein FANTASTIC FOUR 4 (Q9SFG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates the size of the shoot meristem by modulating the CLV3-WUS feedback loop. Can repress WUS but is under negative control by CLV3.
Interaction partners:
- Germin-like protein subfamily 2 member 3
- Protein trichome birefringence-like 10
- Protein GOLVEN 5
- Protein GOLVEN 6
- F5I14.10
- Sugar transport protein 6
- CLAVATA3/ESR
Sequence:
MATVVYQSYFESQHFEPRALRLRLSSHTNPQLSTPLKSHFQNSSIAPQDNPITINAASLPSSSPNPSSNSDTNSGSWSFLESLSNSSSNDKEKKTLPLFQSPSSRRTLSDESLALCTESLGSETGSDIIHEDMFSISSELQTMETRTTSTTSNPSRQDRKRNTMASLPPPLTSMIGFDCIEVKSHRENGRLVMMATRPPPRNRCLQDRSNGCVRLAILIDSDDHIETETKEEKEEEEEETIETVRDNEEEIPEYKEEEEEKEEEIKVKGVEKVQRSRRCIEGDRENRGFLNWESLCVATS
Protein: Ribosome biogenesis protein tsr1 (O13956)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for 40S ribosomal subunit synthesis. Required for normal export of the pre-40S particles from the nucleus to the cytoplasm (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-rRNA-processing protein pno1
- 20S-pre-rRNA D-site endonuclease nob1
- Protein LTV1
- Serine/threonine-protein kinase rio2
- Uncharacterized protein C13G1.09
- Dimethyladenosine transferase
- Serine/threonine-protein kinase rio1
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS15
Sequence:
MAHHHRSTFKAKKPFKSKHASKSSLKEKYKNEVEPHRSGPKNIVHTSTKADRRNTAKQIQLNKRTEVAMNNRIFGGKNGAPKVITIVPLCNNVDSWNVLTNLLRSIDPEASLPKFDKDSISYSTTIDRFKQNLLFLLPKREFYSLIDACKVSDYVIFVLSAVQEVDEFGELIVRTTQGQGISSVLSMVHDLSEVDSLKTRNEVKKSLQSFMNFFFSDQERVFAADVSQDALNVMRALCTSHPRGIHWRDSRSYLLSQEISYSNGNLLVRGIVRGKGLDPNRLIHIQGFGDFAINRIYEAPQGIQNSRGISMDEDTNLTGGLVELCSPTQEQDSLESLGPIIDDMDTDMDSEVGKEASRGVRLDDFYYFDDEEEPVAVAKRVPKGTSTYQATWIPDEDEESDQYSDVEDTEVIIEDQDNQEISNHVAEEKIDSDEEETIDDAKSEMFVDLSEEEEVRQYEEYRKKQKELQEELEFPDEVELQPNELARERFKKYRGLRSLYTSQWDADEYDPNEPREWRQLFKFENYRNLKNKFLKQPFIGEAKPGKAVYVELRNVPIEIFEYYNKPWNLLVLYSLLQYENKLTVSQFTAMQHSEYEEPIESKEELLLQIGPRRFMVRPLYSDPTASGASNNLQKYHRYLPPKQAVIASVISPIVFGNVPIIMFKKSSDNSLRLAATGSYVNCDTNSVIAKRAVLTGHPFKVHKKLVTIRYMFFNPEDVIWFKPIQLFTKQGRTGYIKEPLGTHGYFKATFNGKITVQDTVAMSLYKRMYPLPCELFKVTDIDS