wanglab/gogpt-training-data huggingface dataset:
Protein: Tubulin beta-2B chain (Q9BVA1)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. Plays a critical role in proper axon guidance in both central and peripheral axon tracts. Implicated in neuronal migration.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23001566, ECO:0000269|PubMed:28013290}.
Interaction partners:
- Tubulin alpha-1B chain
- Tubulin alpha-1A chain
- Microtubule-associated protein tau
- Cytoplasmic dynein 1 heavy chain 1
- Kinesin-like protein KIF11
- Tubulin alpha-1C chain
- Tubulin alpha-3E chain
- Kinesin heavy chain isoform 5C
- Tubulin alpha-4A chain
- Tubulin alpha chain-like 3
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
Protein: Aspartate aminotransferase (Q964F2)
Organism: Crithidia fasciculata
Interaction partners:
Sequence:
MSGSPTDNFDGLSALPPDSIFFTSQKAKAAQGPKADLIIGAYRDEHGCPYPLKTVRKAERILLDMNLDYEYLPMTGYKPFVDEATKIIYADSVAPDHLVAVQTLSGTGAVYLGAAFLAEVYDPKTTPIYLPNPTWPNHPSILKLTGWKDIRTYNYYDPKTVALDFEGIKKDIQEAPECSVFLLHQCAHNPTGVDPSHAQWEEIADLMLAKKHQVFFDSAYQGYASGSLDEDAFAARLFVKKGVQFILAQSFSKNMGLYNERTGTLSVVLRNPERAAAVKTHLDLLIRANYSNPPAHGARLVHLVLSDKELRKEWEAELAEMANRIRTMRHTVYDELKRLGTPGTWEHIINQIGMFSFLGLSKEQCQYCQDHNVFILLSGRANMAGLTHDTALMLARTIDEAVRTV
Protein: ATPase family gene 2 protein homolog B (EC 3.6.4.10) (AFG2 AAA ATPase homolog B) (Ribosome biogenesis protein SPATA5L1) (Spermatogenesis-associated protein 5-like protein 1) (Q9BVQ7)
Organism: Homo sapiens (Human)
Function: ATP-dependent chaperone, which plays an essential role in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles. Acts together with SPATA5, C1orf109 and CINP.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18445686}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686}. Nucleus {ECO:0000250|UniProtKB:D4A2B7}.
Interaction partners:
- ATPase family gene 2 protein homolog A
- Cyclin-dependent kinase 2-interacting protein
- Ubiquitin recognition factor in ER-associated degradation protein 1
- AFG2-interacting ribosome maturation factor
- Phospholipase A-2-activating protein
- Derlin-1
- Proteasome subunit beta type-2
- UBX domain-containing protein 7
Sequence:
MAPDSDPFPEGPLLKLLPLDARDRGTQRCRLGPAALHALGARLGSAVKISLPDGGSCLCTAWPRRDGADGFVQLDPLCASPGAAVGASRSRRSLSLNRLLLVPCPPLRRVAVWPVLRERAGAPGARNTAAVLEAAQELLRNRPISLGHVVVAPPGAPGLVAALHIVGGTPSPDPAGLVTPRTRVSLGGEPPSEAQPQPEVPLGGLSEAADSLRELLRLPLRYPRALTALGLAVPRGVLLAGPPGVGKTQLVRAVAREAGAELLAVSAPALQGSRPGETEENVRRVFQRARELASRGPSLLFLDEMDALCPQRGSRAPESRVVAQVLTLLDGASGDREVVVVGATNRPDALDPALRRPGRFDREVVIGTPTLKQRKEILQVITSKMPISSHVDLGLLAEMTVGYVGADLTALCREAAMHALLHSEKNQDNPVIDEIDFLEAFKNIQPSSFRSVIGLMDIKPVDWEEIGGLEDVKLKLKQSIEWPLKFPWEFVRMGLTQPKGVLLYGPPGCAKTTLVRALATSCHCSFVSVSGADLFSPFVGDSEKVLSQIFRQARASTPAILFLDEIDSILGARSASKTGCDVQERVLSVLLNELDGVGLKTIERRGSKSSQQEFQEVFNRSVMIIAATNRPDVLDTALLRPGRLDKIIYIPPPDHKGRLSILKVCTKTMPIGPDVSLENLAAETCFFSGADLRNLCTEAALLALQENGLDATTVKQEHFLKSLKTVKPSLSCKDLALYENLFKKEGFSNVEGI
Protein: Collagen alpha-1(XXVII) chain B (A0MSJ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May play a role during the calcification of cartilage and the transition of cartilage to bone (By similarity). Together with col27a1a, plays a role in development of the notochord and axial skeleton.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
Sequence:
MEPDNTPSSRLRAAGVGGRAVFFCMVLYCTCCLRLAQAQSADVDVLQRLGLVGKRPPQGFIPIKSGVILTTRARIDVPVSSVIPVSLGSTFSIILSVCSHRINNAFLFTIVTKRKRLHLGVQFIPGQILVYLGQNSSVNFDYNVHNGQWHNLALEIQGQKVTLYTSCGNTSIQANLDFQNEETLDSEGSFRLGKMSQNSVQFEGAICQFDIHPSAQAAHNYCKYIKKQCREADTYRPNLPPLLPLLPLDPNRSTIQTPKVVTDINERHLSLTRDKMNINHEGQTTVPPMITQPTLQLPLQTTAQTTASIRNRTSQISPKPTQQNRKKAKKERNKLHILKEHQISVTDSPTSQQQNQVDIPTTTTPELSSTFRVSEMTTLAAQRPLPKETSFFEAKATFFESVTPAAMDGLQTFDLEPTQYSLLELTGLKGEPGLPGPPGPPGQPGLPGKRGPRGPSGPHGKPGPPGTPGPKGKKGNPGISPGRAPSGIKGDPGLVGLPGQPGQPGRKGQKGHPGPSGHPGDQGIRGPDGSPGAKGYPGRQGLPGPIGNMGPKGVRGFIGIPGIFGLPGADGERGLPGVPGKKGKMGRPGFPGDFGERGPPGPDGNPGEIGAPGPVGIPGFIGDMGPVGMVGPPGLIGPKGVPGNPGEPGLKGDKGELGLPGEPGEPGFQGDKGIQGSPGLPGVQGKPGPQGKIGDRGPDGLPGPLGPEGFPGDIGPPGQNGVEGPKGNAGVRGIPGPGGLPGLEGDQGPVGPAGAPGLEGRPGRKGISGNPGEEGMKGEPGMTGNPGMLGERGPVGFVGPFGEMGLAGEKGDRGETGQPGPPGEKGAMGHPGAPGERGLSGPAGAPGPHGSRGLSGTRGPKGTRGARGPDGPVGEKGMMGMKGPEGPPGKQGLSGQMGKIGETGEAGPTGFTGVQGPTGPPGAKGILGEPGPQGSPGVLGPLGEIGAIGLPGKAGDQGLPGEPGEKGAVGSPGNIGEQGLIGPRGDPGVDGEAGPSGPDGAKGEQGDVGLEGESGEKGVIGFKGTEGRTGDPGLIGVKGPEGKPGKIGERGKPGEKGSKGHQGQLGEMGALGEQGDTGFIGPKGSRGTTGFMGAPGKMGQQGEPGLVGYEGHQGPQGSLGSPGPKGEKGEQGDDGKVEGPPGPSGDIGPVGNRGDRGEPGDPGYPGLEGVQGERGKEGAPGVPGNSGPRGFPGPKGSKGNKGPKGKNSPRGESGNRGSPGPVGVPGPRGVIGREGFEGEPGLDGAAGKDGAKGMPGDLGRDGDVGLPGKPGPQGNAGAPGLPGVQGSFGPKGERGITGHSGPPGKRGLNGGMGFPGKQGDQGFKGQPGDAGEQGFPGVLGIFGPQGPPGDFGPVGIQGPKGPQGLMGMQGAIGPVGIIGPSGNPGPQGDKGNKGEMGVQGPRGPPGPRGPPGPPGLPAVAFSHENEALGAALHVFDSRSALRSEMYQDTDLPLLDQGSEIFKTLHYLSILIHSIKNPLGTQENPARMCRDLLECEHRLNDGTYWIDPNLGCSSDNIEVTCSFTSGGQTCLKPVTASKLEIGVSLIQMNFIHLLSSEAVQIITVHCLNVSVWASEDSKTPSSSMVYFKAWDGQIIEAGGFIEPDLLKDECWITDGRWHQTQFIFRTQDPNLLPIVEIYNLPSTKPGSHYHLEVGPVCFL
Protein: Photosystem I reaction center subunit psaK, chloroplastic (PSI-K) (Photosystem I subunit X) (Q9SUI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I chlorophyll a/b-binding protein 5, chloroplastic
- Photosystem I reaction center subunit II-2, chloroplastic
- Photosystem I reaction center subunit XI, chloroplastic
- Photosystem I reaction center subunit VIII
- Chlorophyll a-b binding protein 6, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 2, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit IV A, chloroplastic
- Chlorophyll a-b binding protein 4, chloroplastic
Sequence:
MASTMMTTLPQFNGLRATKISAAPVQGLASVQPMRRKGNGALGAKCDFIGSSTNLIMVTSTTLMLFAGRFGLAPSANRKATAGLRLEARDSGLQTGDPAGFTLADTLACGTVGHIIGVGVVLGLKNIGAI
Protein: ABC transporter expressed in trachea, isoform A (ABC transporter expressed in trachea, isoform B) (ABC transporter expressed in trachea, isoform D) (Q9VQY4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- UPF0585 protein CG18661
- Cytochrome b5 domain-containing protein 1
Sequence:
MNELQASSVPLVDKCSSHAVILPAAKSPNRVSDSAATTAPNAVLYTSGNMSLSTLSTGSGNPNPNPNASTNSRQEPVPLLSQLKLTNDLKQNSHGSQNNLCNGGLGSNNHALAPKVANNSGGSPNGQKKGTIALSHLPQRPPVDIEFCDISYSVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLINSKERNLRRFRKLSCYIMQDDVLIANLTVREAMMVAANLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEGRVKGLVPYLSSLGYECPSYHNPADYVLEVASGEYGDAVPKLVDAVKSGACKKYAHKDYVLTLAQKGCNNDIIKGSGSGAENAMAILTLEDEKPPLEDRQLEPSIPVDDPAELKPPKLETQQSQNSDCSVVNMPTNAVDDSCSFSSSKGTQNAVGGSGSGGPSAVVGCMTSLLDSHESVVTLPNKTGFPTSGWTQFWILLKRSFRTILRDKMLTHMRLFSHVIVGAIIGMIYYDVGNEASKIMSNAGCIFFVSLFTTFTAMMPTILTFPTEMSVFVREHLNYWYSLKAFYFAKTIADMPFQIVFSSVYVLVVYYLTSQPMELERVSMFVLICVLNSLVAQSLGLLIGAGMNIETGVFLGPVTTIPTILFSGFFVNFDTIPGYLQWVTYVSYVRYGFEGAMVAIYGMDRAKMQCNQMYCHYRVPKKFLEEMSMDNALFWVDAVALIGIFFALRIIAYFVLRWKLHMIR
Protein: Candida glabrata strain CBS138 chromosome D complete sequence (Q6FW29)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Ribonucleoside-diphosphate reductase
- Nucleoside diphosphate kinase
- Guanylate kinase
- Uridylate kinase
- Adenylate kinase
- GTP:AMP phosphotransferase, mitochondrial
- Candida glabrata strain CBS138 chromosome H complete sequence
- Thymidylate kinase
- Adenylate kinase isoenzyme 6 homolog
Sequence:
MTKETPSKVAASALSDLELKDSQSNLKKQLEVLREENREQIEALKAKLSTAAVEHKEYLKSHKVHRHELKELEKDEPLLNDDPDRLTLFPIKYHEIWQAYKRAEASFWTAEEIDLSKDLHDWNNRLNENERFFISRVLAFFAASDGIVNENLVENFSTEAVIPEAKAFYGFQIMIENIHSETYSLLIDTYIKDPKESEFLFNAIHTIPEIGEKAEWALRWIANSEALFAERLVAFAAIEGVFFSGSFASIFWLKKRGLMPGLTFSNELICRDEGLHTDFACLLFAHLNHKPDPEVVERIVTEAVEIEQRYFLDALPVALLGMNAQLMNQYVEFVADRLLVAFGNKKVYNVENPFDFMENISLAGKTNFFEKRVSDYQKAGVMSKAQNTEGGGAFSLDEDF
Protein: Small ribosomal subunit protein eS6 (40S ribosomal protein S6) (I2HAF9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKQGILTNGRVRLLLKKGQSCYRERKNGERKRKSVRGCIVDANMSALSLVIVKKGDGEIEGLTDSVLPRKLGPKRASKIRKLFNLTKHDDVTKYVITHDKTFPDGVTKTIAPKIQRLITPARIARKKYLLRQKRNQKIKMRDDAAAYHKLLAKYSKEEHDAKIARRRSSASHHSESEVKKTSKK
Protein: Host cell factor homolog hcf-1 (HCF homolog) (G5EC23)
Organism: Caenorhabditis elegans
Function: Transcriptional coregulator. Involved in control of the cell cycle and in modulating mitotic histone phosphorylation. Plays a role in modulating lifespan by regulating the transcriptional activity of daf-16/Forkhead box protein O, in concert with protein deacetylase sir-2.1/SIRT1, and perhaps acting independently of the Insulin/IGF-1-like signaling (IIS) mediated pathway. Negatively modulates responses to environmental stresses, including oxidative stress, heat stress, and exposure to heavy metals; acting via regulation of the transcription factors daf-16 and skn-1. May play a role in pharyngeal development via positive modulation of expression of sup-35.
Subcellular location: Nucleus {ECO:0000269|PubMed:14629117, ECO:0000269|PubMed:18043729, ECO:0000269|PubMed:18828672}. Note=Localizes to nucleus, except for nucleolus. {ECO:0000269|PubMed:14629117}.
Interaction partners:
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase
- Forkhead box protein O
- NAD-dependent protein deacetylase sir-2.1
- Set1/Ash2 histone methyltransferase complex subunit ash-2
- Retinoblastoma-binding protein homolog 5
- Histone-lysine N-methyltransferase set-2
- WD repeat-containing protein wdr-5.1
- Dosage compensation protein dpy-30
- Histone-lysine N-methyltransferase set-1
- CXXC-type zinc finger protein 1
Sequence:
MDEDVGLEATNYSRGDESRSEEQEKNVVRWRIVQQSTGPNPKPRHGHRAVVLKELIVIFGGGNEGMIDELHAYNTQKREWTAPQCCGDVPTPAAAFGAISLGNKIYRFGGMTEYGKYTNDLYELQSTRWEWRRLNPRVHSNGHLPCPRIGHSFVVSQKSQKAYVFGGLSNDLNDPKRNVPHYLDDLYVINLSGPQHLIWEKLNATGPGPISRESHTAVIYEKDSISRMVVYGGMNGVRLGDLWYLNLNTLHWTEIKFDDPRTGIPPMPRSLHSSVLIGDKMFVYGGWVPLLEHASTEQQTEKEWKCTSSLGCWNITEDRWVPLHLYCSDEDTIPRGRAGHCAAAVGDRMYIWSGRDGYRKAWSNQVCCRDMWLLDTILPEQPGKVQLGRAGFNSLEISWPIVQGASGYFLQIGFGDAKEQSVSPIKRATTSPRKQPSIVPPSQKETEQSPKKPQGTAPSIISTQGTTYTAPADPKPATDEGGLPQDLFEDTEKNETASPKRSNDAQSADSSTCEQKKTDESGLEEDSEKDQKPSDAGETDEMKEENGDDDLPWFDVGIIDKATINVTHYFNDRQQSLEKQLNDLIDHNAFKCVNDSVFTTEDKIPLINGQSYRFRVSAINGLGKGAWSETASCKTCVPGYPSAPSSIRITKSHEGAQLTWEPPSNTNISGKIIEYSVYLAVKNQSANSADSQLAFMRVYCGPQADCQVLQSNLGTAFVDQTNKPAIIFRIAARNEKGYGPATQVRWLQDQQKIPVRTNYPNNSGFIYQQHGGQQKRARFDHQ
Protein: EP2C protein (Q699T2)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
RQRLLPFFTSLLLVALLFPGLSQARHVNHSATEALRELREGATGQGTNGSQLLRHPGKRAPIIRRIPYYPEVESDLRIVDCKRSEGFCQEYCNYLETQVGYCSKKKDACCLH
Protein: Amyloid beta precursor like protein 1 (F1LRS5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Amyloid beta precursor protein binding family B member 1
- Contactin-5
- Low-density lipoprotein receptor-related protein 3
- Sialic acid binding Ig-like lectin 8
- Nicastrin
- Ribitol-5-phosphate transferase
- G1/S-specific cyclin-E1
- Beta-secretase 1
- Amyloid-beta A4 precursor protein-binding family A member 1
Sequence:
MGPSSPTTRGQGRRRGPPPLPLLLPLSLLLLRAQLAVGNLAGGSPSAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLLDPQRVLEYCRQMYPELHIARVEQAAQAIPMERWCGGTRSGRCAHPHHEVVPFHCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPPPATPNPSGMAVGDPSTRSWPLGGRAEGGEDEEEVESFPQPVDDYFVEPPQAEEEEEEEEERAPPPSSHTPVMVSRVTPTPRPTDGVDVYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADSQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQGDPPQAERVLMALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVQTHLQVVQERMNQSLGLLDQNPHLAQELRPQIQELLHAEHLGPSELEASVPGSSSEDKGSTDQESSSSGREKLTPLEQYEQKVNASAPRGFPFHSSDIQRDELAPAGTGVSREALSGLLIMGAGGGSLIVLSLLLLRKKKPYGTISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP
Protein: Histone RNA hairpin-binding protein (Histone stem-loop-binding protein) (Q14493)
Organism: Homo sapiens (Human)
Function: RNA-binding protein involved in the histone pre-mRNA processing. Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery. Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression. Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis (By similarity). Binds to the 5' side of the stem-loop structure of histone pre-mRNAs (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567}. Nucleus {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567}. Note=Polyribosome-associated (PubMed:12588979). Localizes predominantly in the nucleus at the G1/G2 phases and the beginning of S phase (PubMed:12588979). Through the S phase, partially redistributes to the cytoplasm (PubMed:12588979). Binding to histone mRNA is necessary for cytoplasmic localization (PubMed:12588979). Shuttles between the nucleus and the cytoplasm (PubMed:15829567). Imported in the nucleus by the Importin alpha/Importin beta receptor (PubMed:15829567). {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567}.
Interaction partners:
- MIF4G domain-containing protein
- 3'-5' exoribonuclease 1
- Regulator of nonsense transcripts 1
- U7 snRNA-associated Sm-like protein LSm11
- Nuclear cap-binding protein subunit 1
- Zinc finger protein 473
- Nuclear autoantigenic sperm protein
- Eukaryotic translation initiation factor 4E
- U7 snRNA-associated Sm-like protein LSm10
- CBP80/20-dependent translation initiation factor
Sequence:
MACRPRSPPRHQSRCDGDASPPSPARWSLGRKRRADGRRWRPEDAEEAEHRGAERRPESFTTPEGPKPRSRCSDWASAVEEDEMRTRVNKEMARYKRKLLINDFGRERKSSSGSSDSKESMSTVPADFETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPKTPNKFKKYSRRSWDQQIKLWKVALHFWDPPAEEGCDLQEIHPVDLESAESSSEPQTSSQDDFDVYSGTPTKVRHMDSQVEDEFDLEACLTEPLRDFSAMS
Protein: RNA-binding protein RBP6, putative (Q57ZL9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein RBP10, putative
Sequence:
MFYPNSPQTSPQLTQIPYGQQYAMMQRQIQQPYHPFATTEPQARLYPYHYQGPIQQEQGGFITQQSTAASPQYVQMRVTPVDQSIMSGYPNQTANGSSSSSFNYNIHPQQQQQQQQQQQLRHHAMPVGSVPLQDDRYRKQLIVNYLAPDVTSTDLHELFSRFGELDGARIIYDKQTNMSKGYGFVYFCHAEDAKEAVERMSGYEFHGKWLKVGYSTNPLNIVPSNSSPYVHAGSRGAAG
Protein: Leucine-rich repeat-containing protein 55 (BK channel auxiliary gamma subunit LRRC55) (Q6ZSA7)
Organism: Homo sapiens (Human)
Function: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Calcium-activated potassium channel subunit beta-1
Sequence:
MGDTWAQLPWPGPPHPAMLLISLLLAAGLMHSDAGTSCPVLCTCRNQVVDCSSQRLFSVPPDLPMDTRNLSLAHNRITAVPPGYLTCYMELQVLDLHNNSLMELPRGLFLHAKRLAHLDLSYNNFSHVPADMFQEAHGLVHIDLSHNPWLRRVHPQAFQGLMQLRDLDLSYGGLAFLSLEALEGLPGLVTLQIGGNPWVCGCTMEPLLKWLRNRIQRCTADSQLAECRGPPEVEGAPLFSLTEESFKACHLTLTLDDYLFIAFVGFVVSIASVATNFLLGITANCCHRWSKASEEEEI
Protein: Homeobox protein goosecoid (Q02591)
Organism: Mus musculus (Mouse)
Function: Regulates chordin (CHRD). May play a role in spatial programing within discrete embryonic fields or lineage compartments during organogenesis (By similarity). In concert with NKX3-2, plays a role in defining the structural components of the middle ear; required for the development of the entire tympanic ring. Goosecoid-expressing regions of the gastrulating mouse egg cylinder have organizer-like activity when transplanted into Xenopus embryos. Probably involved in the regulatory networks that define neural crest cell fate specification and determine mesoderm cell lineages in mammals (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Histone H4 transcription factor
- TAR DNA-binding protein 43
- Zinc finger protein 330
- Pre-mRNA-splicing factor ISY1 homolog
- WD repeat-containing protein 26
- Transcription elongation factor SPT6
- G protein pathway suppressor 2
- Tektin-2
- RRP15-like protein
- Centrosomal protein 20
Sequence:
MPASMFSIDNILAARPRCKDAVLPVAPSAAAPVVFPALHGDSLYGAGGGTSSDYGAFYPRPVAPGGAGLPAAVGSSRLGYNSYFYGQLHVQAAPVGPACCGAVPPLGAQQCSCVPTPPGYEGPGSVLVSPVPHQMLPYMNVGTLSRTELQLLNQLHCRRKRRHRTIFTDEQLEALENLFQETKYPDVGTREQLARKVHLREEKVEVWFKNRRAKWRRQKRSSSEESENAEKWNKTSSKASPEKREEEGKSDLDSDS
Protein: GYF domain-containing protein (Q9NAH3)
Organism: Caenorhabditis elegans
Interaction partners:
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Probable ATP-dependent RNA helicase DDX23
- Thioredoxin-like protein
- Pre-mRNA-splicing factor 8 homolog
- Probable small nuclear ribonucleoprotein-associated protein B
- Tr-type G domain-containing protein
- Pre-mRNA-processing factor 6
- SNU homolog
- Splicing factor 3B subunit 3
- Pre-mRNA-processing factor 17
Sequence:
MPKRAVSFADDIETRVFKRDKREIEDGILDIPMEEDVVKERPGNADEDEEEKKKFHTLESDEEEEEDHKRLDTRRVEGQEDCGVDFDGSIKITAFNMKEDEEEGHFDETGNFIFDKKTKDVQDAWLDGIDWSLVKKKAGDQWEGDEDKKSLEDEEPEPITMSDARKKEIFEQLVNLLKPNQTVAKALSELKKKKGLSAAEERKLRWAAKKAGKSFEPTDGQKETSQLSGLADELISAGIMDAYEWHREKFNFQLQKMISTAADELDMFSDEPTSTGAARAAGAPMEQEEEEADDSVKWEYKANEEAKIEGPIPTSEMMDRQSKGLLSAEGVARRSGTNGHFNPVARIDFELYL
Protein: Mucus adhesion promoting protein (Q9FCU5)
Organism: Limosilactobacillus reuteri (Lactobacillus reuteri)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
Sequence:
MKFWKKALLTIVALTVGTPAGITSVSAASSAVNSELVHKGELTIGLEGTYSPYSYRKNNKLTGFEVDLGKAVAKKMGLKANFVPTKWDSLIAGLGSGKFDVVMNNITQTPERAKQYNFSTPYIKSRFALIVPTDSNIKSLKNIKGKKIIAGTGTNNANVVKKYKGNLTPNGDFASSLDMIKQGRAAGTINSREAWYAYSKKNSTKGLKMIDVSSEQDPAKISALFNKKDTAIQSSYNKALKELQQDGTVKKLSEKYFGADITE
Protein: kinetoplast-associated protein 2-1 (Histone H1-like protein p18-1) (Q9TY83)
Organism: Crithidia fasciculata
Function: Histone H1-like DNA-binding protein involved in the organization and segregation of kinetoplast DNA (kDNA). The mitochondrial DNA of kinetoplastid protozoa consists of about 5,000 minicircles and 20 to 30 maxicircles. These circular DNAs are held together by catenation into a highly organized compact disk structure referred to as a kinetoplast DNA (kDNA) network. Binds preferentially to a specific fragment of minicircle DNA and is able to compact kDNA networks through DNA charge neutralization and condensation.
Subcellular location: Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:8446592, ECO:0000269|PubMed:8552084}.
Interaction partners:
Sequence:
MLRRTVSNFAMSPYMLFISDLAKTGKLKGIRTPGKFVGKKYRQLSAKEKAALQQRAKQASTPAMTAYRRMAHREMSNKSVPIEQRRANLTKKWNETKQAQREKAQKAQKKTKSAKSKVKKAAKKSKKSKK
Protein: Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase (Pyr2C/Pip2C reductase) (EC 1.5.1.21) (Delta(1)-pyrroline-(4S)-hydroxy-2-carboxylate reductase) (Pyr4SH2C reductase) (EC 1.5.1.-) (Proline ketimine reductase) (Q9I492)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the reduction of both Delta(1)-pyrroline-2-carboxylate (Pyr2C) and Delta(1)-piperideine-2-carboxylate (Pip2C) to L-proline and L-pipecolate, respectively, using NADPH as the electron donor. Cannot use NADH instead of NADPH. Is likely involved in a degradation pathway that converts trans-3-hydroxy-L-proline (t3LHyp) to L-proline, which would allow P.aeruginosa to grow on t3LHyp as a sole carbon source. Can also catalyze the reverse oxidation reactions, albeit at a much lower rate. Is also able to use Delta(1)-pyrroline-(4S)-hydroxy-2-carboxylate (Pyr4SH2C) and cis-4-hydroxy-L-proline (c4LHyp) as substrates, and might be involved in the metabolism of c4LHyp, a compound which is generated by the hydroxylation of free L-proline in bacteria.
Interaction partners:
- Cis-3-hydroxy-L-proline dehydratase
- Bifunctional trans-3-hydroxy-L-proline dehydratase/2-epimerase
- Probable dihydrodipicolinate synthetase
- NADP-dependent malic enzyme
- Glycine oxidase
- Uncharacterized protein PA2026
- NAD-dependent malic enzyme
Sequence:
MIRMTLDEVRELAVRILRRHAFSEAHVQAVADTLVAGERDECASHGIWRLLGCIATLKAGKVSADAEPELHDIAPGLLRVDAHGGFSQCAFRLGLPHLLEKARSQGIAAMAVNRCVHFSALWVEVEALTEAGLVALATTPSHAWVAPAGGRKPIFGTNPIAFGWPRPDGPPFVFDFATSAVARGEIQLHERAGKPIPLGWGVDEQGEPTTDASAALRGAMLTFGGHKGSALAAMVELLAGPLIGDLTSAESLAYDEGSRSSPYGGELLIAIDPRRMLGASAEEHLARAETLFEGIVEQGARLPSQRRFEARERSARDGVTIPEALHRELLALLE
Protein: Zinc finger protein 143 (Zfp-143) (Selenocysteine tRNA gene transcription-activating factor) (mStaf) (O70230)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8 (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein SIX5
- Double-strand-break repair protein rad21 homolog
- THAP domain-containing protein 11
- POU domain, class 5, transcription factor 1
- Histone-lysine N-methyltransferase EZH2
- Histone-lysine N-methyltransferase EZH1
- Transcriptional repressor protein YY1
Sequence:
MLLAQINRDSQGMTEFPGGGMEAQHVTLCLTEAVTVADGDNLENMEGVSLQAVTLADGSTAYIQHNSKDGRLIDGQVIQLEDGSAAYVQHVPIPKSTGDSLRLEDGQAVQLEDGTTAFIHHTSKDSYDQSSLQAVQLEDGTTAYIHHAVQVPQSDTILAIQADGTVAGLHTGDATIDPDTISALEQYAAKVSIDGSDGVTSTGMIGENEQEKKMQIVLQGHATRVTPKSQQSGEKAFRCKYDGCGKLYTTAHHLKVHERSHTGDRPYQCEHSGCGKAFATGYGLKSHFRTHTGEKPYRCSEDNCTKSFKTSGDLQKHIRTHTGERPFKCPIEGCGRSFTTSNIRKVHIRTHTGERPYYCTEPGCGRAFASATNYKNHVRIHTGEKPYVCTVPGCDKRFTEYSSLYKHHVVHTHSKPYNCNHCGKTYKQISTLAMHKRTAHNDTEPIEEEQEAFFEPPPGQGDDVLKGSQITYVTGVDGEDIVSTQVATVTQSGLSQQVTLISQDGTQHVNISQADMQAIGNTITMVTQDGTPITVPTHDAVISSAGTHSVAMVTAEGTEGQQVAIVAQDLAAFHTASSEMGHQQHSHHLVTTETRPLTLVATSNGTQIAVQLGEQPSLEEAIRIASRIQQGETPGLDD