wanglab/gogpt-training-data huggingface dataset:
Protein: Exocrine gland secreted peptide 31 (Exocrine gland-secreting peptide 31) (A8R0W3)
Organism: Mus musculus (Mouse)
Interaction partners:
- Exocrine gland secreted peptide 4
Sequence:
MDSFPVMCFLLILLLSSMFTEGAVLKNDQEELIDSEDEQLIFIECGYIQGILHNPEMSFNLNDYEQKFENINNRVFFLCVSRTYVCLKYPKTRLLLQVMDPVRFINMTQSRDFC
Protein: t-SNARE VTI1 (Qb-SNARE VTI1) (VPS10-interacting protein 1) (Vesicle transport v-SNARE protein VTI1) (Q04338)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse.
Subcellular location: Prevacuolar compartment membrane; Single-pass type IV membrane protein. Golgi apparatus membrane; Single-pass type IV membrane protein. Note=A small portion is localized in the Golgi apparatus, the majority is localized in the PVC.
Interaction partners:
- Synaptobrevin homolog 2
- Syntaxin VAM3
- Synaptobrevin homolog YKT6
- Vacuolar protein sorting-associated protein 33
- t-SNARE affecting a late Golgi compartment protein 1
- Vacuolar v-SNARE NYV1
- t-SNARE affecting a late Golgi compartment protein 2
- Protein transport protein SEC22
- Alpha-soluble NSF attachment protein
- Integral membrane protein SED5
Sequence:
MSSLLISYESDFKTTLEQAKASLAEAPSQPLSQRNTTLKHVEQQQDELFDLLDQMDVEVNNSIGDASERATYKAKLREWKKTIQSDIKRPLQSLVDSGDRDRLFGDLNASNIDDDQRQQLLSNHAILQKSGDRLKDASRIANETEGIGSQIMMDLRSQRETLENARQTLFQADSYVDKSIKTLKTMTRRLVANKFISYAIIAVLILLILLVLFSKFK
Protein: EBP cholestenol delta-isomerase (C9J719)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHP
Protein: Thiamine thiazole synthase (EC 2.4.2.60) (Thiazole biosynthetic enzyme) (P40998)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03158, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03158, ECO:0000269|PubMed:16823372}.
Interaction partners:
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
- Thiamine pyrophosphokinase
- Probable thiamine biosynthetic bifunctional enzyme
- Thiamine repressible genes regulatory protein thi1
- Thiamine repressible genes regulatory protein thi5
- Thiamine-repressible acid phosphatase pho4
- Thiamine transporter thi9
- Vitamin B6 transporter bsu1
- Uncharacterized amino-acid permease C794.03
Sequence:
MAPATAVVTPQTAFKTDLPVEKTAHNTVVKSEMGALSKAYPTYSLDESFSFAPIRESTVSRAMTRRYFSDLDKYAESDIVIVGAGSAGLTAAYYIGTRRPDLKIAIIEASVAPGGGAWLGGQLFSAMVVRKPADLFLNEIGVPYEDEGDYVVVKHAALFTSTVMARTLALPNVKLFNATAVEDLIVKEGKDGKQRIAGVVTNWTLVSLNHGLQSCMDPNTINAHLVVSATGHDGPFGAFCVKRLASAQLVSNLHDMRPLDMNRAEDLIVKGTREVFPGMIVGGMELSEFDGANRMGPTFGGMMFSGIKAAQEALAIFDERKAVNEKYL
Protein: Palmitoyltransferase ZDHHC19 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 19) (DHHC-19) (Q8WVZ1)
Organism: Homo sapiens (Human)
Function: Palmitoyltransferase that mediates palmitoylation of RRAS, leading to increased cell viability.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:20074548, ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20074548}.
Interaction partners:
Sequence:
MTLLTDATPLVKEPHPLPLVPRPWFLPSLFAAFNVVLLVFFSGLFFAFPCRWLAQNGEWAFPVITGSLFVLTFFSLVSLNFSDPGILHQGSAEQGPLTVHVVWVNHGAFRLQWCPKCCFHRPPRTYHCPWCNICVEDFDHHCKWVNNCIGHRNFRFFMLLVLSLCLYSGAMLVTCLIFLVRTTHLPFSTDKAIAIVVAVSAAGLLVPLSLLLLIQALSVSSADRTYKGKCRHLQGYNPFDQGCASNWYLTICAPLGPKYMAEAVQLQRVVGPDWTSMPNLHPPMSPSALNPPAPTSGSLQSREGTPGAW
Protein: Divalent cation tolerance protein, putative (Q57Y36)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFSVCYVTTPTSEVAREISRILVSSNKAACVNIVPSVTSVYRWEGQLCEEQECLMMIKTRTELLQEVIDSVKKNHPYSTPEVVSVPISSGSEEYLKWVEENTMPTSSNNNSGCSCR
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (A0A8I6A2G7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MVKGAALFLQQGNSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESVWTDRVRYMVVVYTSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKEFKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYQFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAFNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQPADDTIAEPSEFLPETLDGALDTQLPCLEDATHPGLPRSLPSGGPSLPCCFRRLSDPLLLPHRDGAGGLVHLEDLERDALLEDEAQPVEVRKLVPSSQEGDRLCEKDVKRKLEFGSPKARSGSLPQVEELEKDGSPRPGRWRRASTQLERGLLDQENLNNNNSKRSCPDDFERDAVFGILSKVKPPYTSCADCMYPAAGAPEAFMERHEDPSSSAICTQPTFLPHVTSSPMAHTSNRSRAPERPTSGPANTSPFLLPAGSRKPDVSGSGAGVAPEPPASLPEPSRETSKALQKSLLSKNSHCDKNAANTEAAAKEELSTKKDPKPSKDLRLLFSQEGEKPTANSYLMQHQESIIQLQKAGLVRKHTKELERLKSLPSDSPSTCRDSAASRLEASIPEEGQEPAHPALDSQAGTEEKPVGGASQKSPPPTLLLRLDHTSKDFSKDFLKSACYTPTPSSISSNLTRSSSSDSIHSVRGKPGLVKQRAQEIETRLRLAGLTVSSPLKRSHSLAKLGSLNFSTEDLSSEADTSTIADSQDAKCTLSSFLPEPQAAPRNPSATSKPSGKSAPENLKIPVRVNKS
Protein: Regulatory protein SWI6 (Cell-cycle box factor subunit SWI6) (MBF subunit P90) (Trans-acting activator of HO endonuclease gene) (P09959)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of a complex involved in cell-cycle-dependent transcription. SWI4 and SWI6 are required for formation of the cell-cycle box factor-DNA complex. The repeated element in the upstream region of HO (5'-CACGAAAA-3') is called the cell cycle box (CCB).
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- Regulatory protein SWI4
- S-phase entry cyclin-5
- G1/S-specific cyclin CLN2
- Protein STB1
- G1/S-specific cyclin CLN1
- Transcription factor MBP1
- Cyclin-dependent kinase 1
- G1/S-specific cyclin CLN3
- G1-specific transcriptional repressor WHI5
- Transcription factor NRM1
Sequence:
MALEEVVRYLGPHNEIPLTLTRDSETGHFLLKHFLPILQQYHDTGNINETNPDSFPTDEERNKLLAHYGIAVNTDDRGELWIELEKCLQLLNMLNLFGLFQDAFEFEEPETDQDEEDPSHSKLPENKTKSENSKDNISSKRINNLQDMSLDSDAHRELGSPLKKLKIDTSVIDAESDSTPNTARGKPNDDINKGPSGDNENNGTDDNDRTAGPIITFTHDLTSDFLSSPLKIMKALPSPVVNDNEQKMKLEAFLQRLLFPEIQEMPTSLNNDSSNRNSEGGSSNQQQQHVSFDSLLQEVNDAFPNTQLNLNIPVDEHGNTPLHWLTSIANLELVKHLVKHGSNRLYGDNMGESCLVKAVKSVNNYDSGTFEALLDYLYPCLILEDSMNRTILHHIIITSGMTGCSAAAKYYLDILMGWIVKKQNRPIQSGTNEKESKPNDKNGERKDSILENLDLKWIIANMLNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDFGAGTSKLQNTNGGDENSKMVSKGDYDGQKNGKAKKIRSQLLKNPPETTSLINDVQNLLNSISKDYENETVQYNEKLEKLHKELNEQREELANSREQLANVKQLKDEYSLMQEQLTNLKAGIEEEEESFREESKKLGIIADESSGIDWDSSEYDADEPFKVEFLSDFLEDKLQKNYEGDISKLLEAESKEQIMEQIRNQLPAEKIQSMLPPTVLLKARINAYKRNDKHLTNVLDTISTKQSELENKFRRVLSLCLKIDENKVDNMLDGLLQAISSEDPQDIDTDEMQDFLKKHAS
Protein: Protein RRP6-like 3 (AtRRP6L3) (A9LLI8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18285452}.
Interaction partners:
- Exosome complex component RRP4 homolog
- Exosome complex component RRP41 homolog
- Exosome complex exonuclease RRP46 homolog
- DExH-box ATP-dependent RNA helicase DExH9
- Exosome complex component RRP45B
- Nuclear nucleic acid-binding protein C1D
- Inactive exonuclease DIS3L2
- Ribonuclease II, chloroplastic/mitochondrial
- DExH-box ATP-dependent RNA helicase DExH10
- Exosome complex exonuclease RRP44 homolog A
Sequence:
MELKEKAKVVITVASLVAVTILFVTEYRRRRQRRKQTSSLSSCYLHSELKPQFGFKRVLADNSYSEFKHLKLVDASSSSLEKPSNGHPYETEITVLLENPQIEFGFLRGECSLEMSDSYVWVETESQLKELAEILAKEQVFAVDTEQHSLRSFLGFTALIQISTHEEDFLVDTIALHDVMSILRPVFSDPNICKVFHGADNDVIWLQRDFHIYVVNMFDTAKACEVLSKPQRSLAYLLETVCGVATNKLLQREDWRQRPLSEEMVRYARTDAHYLLYIADSLTTELKQLATEDSSSPDDRFHFLLEASRRSNMTCLQLYTKETEDFPGSAASSSIIYRHLNGHGDKSNISLNAEELVRKLCAWRDLMGRIHDESTRYVLSDQAIVGLSCKQPTTTEEIYDTIAHIDLATESSPSLSSSVQSPYPVICSHLDDIYKMILDKLAKLDDLLPVVLKKCLGTNGTCPISVFNYSLLVNFKTKLSSHSAPKQNGHKNFKQQFTRKASRELFVKKFSCKAPVYHNCRIYANDGRLLCYCDKRKLEWYLNRGLAKLVEENPPAIMLLFEPKGRPEDEGNDFYIQTKRNICVGCGEGKHYLRYRIIPSCYRVHFPEHLKSHRSHDIVLLCVDCHEVAHAAAERYKKQIATEFGIPLFVRRVLDSKEAQGTSSLVEDESTGDSEDAGVSPLHLRSAAMALLRHGNRMPSSRREELLQTVKMYYGGRDLSEEDLEKALLIGLSPHERRKLERKKGVSFKHSAEVAGMDKQEDENNDGEALADFEKIMTVERSTVVDDSGDGTSEGDGAKELNDTQCNGNTLHQQNSKLSLLGHGPHGKQIVEYLLREHGEDGVRDFCQRWRKVFVDAVHPRHLPGGWNVSHSGRRDFGEFSVYNPTKRLSTE
Protein: Copper-transporting ATPase-like protein, putative (EC 3.6.3.4) (Q387C6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
- Intraflagellar transport
Sequence:
MEENNATTGQKRRRRKNKRGREAQRPTDSDELQPLVSYGSLAQTPLLAEEQSVGAVSLSAQTAAAPSPVVVPEFTEAAKSSPSSVQLLGGSTVALVDKTVESHFSLHGLPCASCASHIESHIGEMGGVAQVTVNFASSHAVVVHNPHVVGASRITEEMEAMGYTAVLISAHSDDAEQLDNLGVREFELLIGGMTCGSCVSRVQSALLEIDVVKSCTINFSTGTCKLTMTGGRDSLNCVQEEVKKLGYTATPLEERGSGNAVDVMKEALERTKEIQAHKRAFVLSAVLATPLAVFMILMTVTKYFEDITTMVIVNTIQLYLATPIVFYCGSGFFSRAWVNLKHRTFTMDTLVALGAGCSYLYSVAGLITMFLMKRHVTTYFDTAGMLVAFMLLGRYLEAYAKRHTNDALIKLMNLVPPTSLVVTPAGDVSMPSSTVKKGMRVRVLAGDRVPVDGVLVEGNSDVDEQMVTGESVPKPVSAGGTVVGGTTNLTAMIVIEATKVGEEAVLSQILRVVREAQNSKPAIQRIADKVAARFVPAVIIFSLVVLAVWLLLGAFNLYPSEWRGNNESTTVFAFDFFIATIVAACPCALGLATPTAIMVGTGVGAKHGILVKCGMTLEAMRRTRCVVFDKTGTITNGTLCVVFQRRWGNGADAAVDAVGAVEQRSNHPISRAIAVCVASDPKSQVAAYEVVTSTVHSGLGVKATVQRKDSGHQLNVFIGNMDMMLSSGIDVSGEVAKVVRWQMGLGRTVTLAAVDGSVRFLAALADEPKAEAAGVIRFLKRQNIRVFMVTGDNPGVAAAVAQAVGISQEDVYAGALPVTKAAVVKAFQEEYRDVVFVGDGINDGPALAQASVGVALGAGTEIAIEAADAVLVRNSLVDLLNLRALSITTVRHVYGNFMWAFGYNVLILPLASGMLYPFLHVRVPPVVAGVAMILSSLSVLMSSLSIRCFSPYKREQFIDII
Protein: LS1-like protein (Putative LS1) (Putative macrophage migration inhibitory factor (MIF)) (Tautomerase/MIF superfamily protein) (Q8LG92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT5g64160/MHJ24_14
- At5g57910
- At1g01170)
- Stress up-regulated Nod 19 protein
- Pathogenesis-related thaumatin superfamily protein
- Heavy metal transport/detoxification superfamily protein
- Protein TIC 20-II, chloroplastic
- Protein FATTY ACID EXPORT 5
- Pathogenesis-related thaumatin superfamily protein
Sequence:
MPCLYITTNVNFDGVNTDPFYSEVTKAVASIVGRPQNLVMVVLKGSVEIVFGGNKEAAAYAEIVSMGGITKQVKRELIATVGSILHTHFSIHPTRFIFKVFDINSLPLPSKL
Protein: Carboxypeptidase (EC 3.4.16.-) (Q59EV6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTSSPRAPPGEQGRGGAEMIRAAPPPLFLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY
Protein: Auxin-responsive protein IAA3 (Indoleacetic acid-induced protein 3) (Short hypocotyl) (Suppressor of HY2) (Q38822)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Plays a central role in auxin regulation of root growth, in gravitropism, and in lateral root formation. Regulated by an auxin-induced protein turnover. Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression. When activated by cytokinin, restricts the expression of the PIN genes to the vascular transition zone. Induction of SHY2 in the vascular transition zone restricts BRX expression to down-regulate PIN3 and thus limit meristem growth, but proper SHY2 expression requires BRX. Involved in meristem growth and in determining its size. May participate in strigolactone signaling to regulate meristem size and lateral root formation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin response factor 5
- Auxin response factor 7
- Auxin response factor 19
- Auxin transporter protein 1
- Two-component response regulator ARR1
- Protein AUXIN SIGNALING F-BOX 2
- Auxin response factor 8
- Auxin response factor 6
- Auxin-responsive protein IAA1
Sequence:
MDEFVNLKETELRLGLPGTDNVCEAKERVSCCNNNNKRVLSTDTEKEIESSSRKTETSPPRKAQIVGWPPVRSYRKNNIQSKKNESEHEGQGIYVKVSMDGAPYLRKIDLSCYKGYSELLKALEVMFKFSVGEYFERDGYKGSDFVPTYEDKDGDWMLIGDVPWEMFICTCKRLRIMKGSEAKGLGCGV
Protein: Snt1p (A0A1D8PFD3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- SIR4-interacting protein SIF2
- Histone-binding protein
- Histone deacetylase
- Histone acetyltransferase
- Transcription initiation factor TFIID subunit 9
- SAGA histone acetyltransferase complex subunit
- Deubiquitination module subunit
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 6
Sequence:
MSSSNSSGGGGPPSSRYNNDYLDYGKQRRKNFYSSNLTSSTSPTTSSTNLNSNTHISSNTVPGLSRRDFKNNGSGSSSIPHSKDSNSIPTTSRNGSYSSSSHYSNYGNYHDYYSGHGRNDTWRKSSSGAGDSRLTASNSSNAPGSGPGPGSGSSSSSSSSSYQQYRPNGDYRIKDRYDSYTGHDGSINTSKWKMSRSSVGSRYSAKDRMRGKQSSFTSGSNSIPLGSSSLVNSTNYRSTSGGGSGGDSYYGSGRSNGYSSSMNSMYSNPKAVDRYSSLSKNGGYSKPRDYKYRYVNKDYNRSTLITPVDKELKKEYEDRESPTPRDEDEEEEEEDEEEAEEEQEETNDSIQTIETKDKAENKLESDKTEIVKPVLENGLESKEIKAETEPETKAEIKPETKPIEQLNESVEKPTLEVTVGYKPTPEMIEKATLEAATQLCRYPLTKIEYEFEELKKKFTQETKHHESGANYLKYSLARPIVDFNEFPFFSNNYQSFIKSKDSLIESFQKKHNVINKKKKSLWKDYKQGLEVWETEQLKMDQQLRVLHPPNDEMRREIDSSDNRKQYQQQQQQLQQQQQQQQQNQQQQQFNDSNSGDNIHFSTRRNRRHGDLVTTEAEFQEILLSLGQEDDENPLVKAERVAAKIPDMILDPVKRDKVLFMDSNNIVRDKNEWAQRVKHDFMNNFSEREHELFCEGFCLHPKRFGAIARHMGGLRSASECVVHYYMTKKKVNYKELLIKSRKKSKPRRKQKAAASKKEAVPVSTTVESGETEIELPPSSIVPVEQLVSEELYTETGRRKRAAAPVFDGKEKEKEKKKQRKDGTNIVVVNEPTSVNTAGGTAIATATTANTTTTTTTPTIDNTPTATTVITTPNLAPNVNPALAHVNNTNIINDSNSAVTMNIPVAGSAVSSSEIPVPTTTTEENKDNKRKVISSYWSITEANAFPKLLEEFGMNWGLISDKLATKSTTMVRNYFQRNAEKNGWDAIVANQKSSKMSIMSLLN
Protein: Protein POST-ILLUMINATION CHLOROPHYLL FLUORESCENCE INCREASE, chloroplastic (Q9LVZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required during nonphotochemical quenching. Involved in NAD(P)H dehydrogenase complex-mediated chlororespiratory electron transport which mediates electron flow from stromal reductants to the plastoquinone (PQ) pool during chlorophyll fluorescence increase after turning off actinic light, in response to photoinhibition conditions (e.g. high light intensities), and upon long-term mild heat stress.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:17573537}.
Interaction partners:
- Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
Sequence:
MAAAANTSAVFASPSQPLSSKRSFLYSSRIGPILRRFPRKKLDLQVKAVATTLAPLEEIKEYKLPSWAMFEMGTAPVYWKTMNGLPPTSGEKLKLFYNPAASKLTLNEDYGVAFNGGFNQPIMCGGEPRAMLKKDRGKADSPIYTMQICIPKHAVNLIFSFTNGVDWDGPYRLQFQVPKRWQNKPIEFFNEGLANELSQDGACERAIFPDSNVVPTRCTMIANLTVEGGDRCNLDLVPGCMDTNSEHFNPYANVDDGSCPLELSDSDE
Protein: Probable splicing factor, arginine/serine-rich 1 (CeSRp75) (RNA-binding protein srp-5) (Q23121)
Organism: Caenorhabditis elegans
Function: Plays a functionally redundant role in spermatogenesis and growth rate control.
Subcellular location: Nucleus {ECO:0000269|PubMed:10906451}.
Interaction partners:
- SpoU_methylase domain-containing protein
- RRM domain-containing protein
- Cell division cycle 5-like protein
- Probable splicing factor, arginine/serine-rich 6
- Uncharacterized protein
- Probable small nuclear ribonucleoprotein F
Sequence:
MAARIYIGRLTSRVSEKDIEHFFRGYGQIRDVLLKNGFGFVEFDDKRDAEDAVHDLNGKELGGERVILDYSKPRGGGGDRGGFGGGGRGGARVSSYSGGGGGGRDRFDRYDRGPPRRESRYGRPYSTRHRVVVENLSSRISWQDLKDQVRRQGVEPTYAEAHKRPNEALLCFATPSDLKRCIEKCDGMDLNGRKIKMIDDSQAGRSRSRSNSRSRSRSRSRDRRRSRSRSSSRSKSRSRSPPKRSRRESKSKSRSRSRSRSADNRKSRSPSRSPKKVDRSPSPPRGSRSPSEKGSPRRSRSASPMDNGDGDN
Protein: Homeobox protein Nkx-2.5 (Homeobox protein NK-2 homolog E) (Q98872)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MAMFSSQMTSTPFSVRDILNLEQNQEDMVSLDMSQRLDSALIPTSSCMLSTFKQEQFMEMPSGSSLFSEDLQEDKGNKINSLNFSASGFYAKNFLEMDYVKDAKTDDTFEDKEKKDIGFCQEDPGEDLKLDDAERPKQRKRRKPRVLFSQAQVYELERRFKQQKYLSAPERDHLANVLKLTSTQVKIWFQNRRYKCKRQRQDQTLEMVGIAPPRRISVPVLVRDGKPCLGDTSTYNTSYNVGINHFTYNTYPAFSNFPSPGNSNYSCNYPSSMSSIQPSQSNSNYMNFGVGDLNNVQASFQSSSVPSLHGIRAW
Protein: Barttin (Q8WZ55)
Organism: Homo sapiens (Human)
Function: Functions as a beta-subunit for CLCNKA and CLCNKB chloride channels. In the kidney CLCNK/BSND heteromers mediate chloride reabsorption by facilitating its basolateral efflux. In the stria, CLCNK/BSND channels drive potassium secretion by recycling chloride for the basolateral SLC12A2 cotransporter.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:18776122}; Multi-pass membrane protein {ECO:0000255}. Note=Mostly sorted at the basolateral membrane. A significant amount also observed intracellularly. Staining in membranes of the renal tubule and of potassium-secreting epithelia of the inner ear is basolateral (By similarity). {ECO:0000250}.
Interaction partners:
- Chloride channel protein ClC-Kb
- Chloride channel protein ClC-Ka
- Solute carrier family 12 member 1-chloride cotransporter 1)
- ATP-sensitive inward rectifier potassium channel 1
- Solute carrier family 12 member 3
- H
- Chloride channel protein 1
Sequence:
MADEKTFRIGFIVLGLFLLALGTFLMSHDRPQVYGTFYAMGSVMVIGGIIWSMCQCYPKITFVPADSDFQGILSPKAMGLLENGLAAEMKSPSPQPPYVRLWEEAAYDQSLPDFSHIQMKVMSYSEDHRSLLAPEMGQPKLGTSDGGEGGPGDVQAWMEAAVVIHKGSDESEGERRLTQSWPGPLACPQGPAPLASFQDDLDMDSSEGSSPNASPHDREEACSPQQEPQGCRCPLDRFQDFALIDAPTLEDEPQEGQQWEIALPNNWQRYPRTKVEEKEASDTGGEEPEKEEEDLYYGLPDGAGDLLPDKELGFEPDTQG
Protein: Vitamin D 25-hydroxylase (EC 1.14.14.24) (Cytochrome P450 2R1) (Q6VVX0)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in activation of vitamin D precursors. Catalyzes hydroxylation at C-25 of both forms of vitamin D, vitamin D(2) and D(3) (calciol). Can metabolize vitamin D analogs/prodrugs 1alpha-hydroxyvitamin D(2) (doxercalciferol) and 1alpha-hydroxyvitamin D(3) (alfacalcidol) forming 25-hydroxy derivatives. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15465040}; Peripheral membrane protein. Microsome membrane {ECO:0000305|PubMed:15465040}; Peripheral membrane protein.
Interaction partners:
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
- 1,25-dihydroxyvitamin D
- 7-dehydrocholesterol reductase
- Vitamin D-binding protein
- Glutamine-dependent NAD
- Sterol 26-hydroxylase, mitochondrial
- Probable imidazolonepropionase
Sequence:
MWKLWRAEEGAAALGGALFLLLFALGVRQLLKQRRPMGFPPGPPGLPFIGNIYSLAASSELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQKSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLICAERR
Protein: Threonine--tRNA ligase 1, cytoplasmic (EC 6.1.1.3) (Threonine--tRNA ligase, cytoplasmic) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase 1) (Q9D0R2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29579307}.
Interaction partners:
- Leucine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase 2, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase, mitochondrial
- Probable leucine--tRNA ligase, mitochondrial
- Valine--tRNA ligase
- Asparagine--tRNA ligase, cytoplasmic
Sequence:
MSQEKASSPSGKMDGEKPVDASEEKRKEGGKKKSKDGGGDGGRAELNPWPEYINTRLDMYNKLKAEHDSILAEKAAKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVVAKVNKVVWDLDRPLETDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIENGFYYDMYLEEGGVSSNDFSSLETLCKKIIKEKQTFERLEVKKETLLEMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKTLKIHKNSSTYWEGKADMETLQRIYGISFPDPKLLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNTLMEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKEQFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGDIEIWNQAEKQLENSLNEFGEKWELNPGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADTDLDPGCTLNKKIRNAQLAQYNFILVVGEKEKASGTVNIRTRDNKVHGERTVEETVRRLQQLKQTRSKQAEEEF
Protein: Ovocleidin-17 (OC-17) (Q9PRS8)
Organism: Gallus gallus (Chicken)
Function: May form proteinaceous networks during the construction of the eggshell which then may control the deposition of the mineral phase.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:7648490}. Note=Eggshell matrix. Mostly in the mammillary bodies.
Interaction partners:
Sequence:
DPDGCGPGWVPTPGGCLGFFSRELSWSRAESFCRRWGPGSHLAAVRSAAELRLLAELLNASRGGDGSGEGADGRVWIGLHRPAGSRSWRWSDGTAPRFASWHRTAKARRGGRCAALRDEEAFTSWAARPCTERNAFVCKAAA
Protein: Cilia- and flagella-associated protein 206 (Q57VI3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
- BRCT domain-containing protein
- EGF-like domain-containing protein
Sequence:
MDVTPVVAREIVRRFGKLTAGGSSMSLTTELASFVLRLQLRNSPFRDAKGDVEMTPEAIETMVEDVANFLVTCSEDLMATLSLQCRTLSLPTKLKAKRHKERVKFETVTLKLLTSLCDNSERLPEELLGEMTFFILHCYGQAEESQSNLPARKETALVLTAVLPKSQVPAFASQPPEEKKRQLQELRRIVWGIRLHNVACGKSVGTGITPPRDKAELLMSSLREHIEKELEEAISACARYVAVLRSPSTPVEGSMREAICAEYHRQLQLLLNIRMAKQQLDTLNNQIFGELLPSYEAALEAVKDVLGTRSMRSDGVSLRKNVSKATVYPKFIELAEVYEEAQRSFQSFEDIKALMTLSLSLGKVSNSSLPPTLLQEAINLEKEDGPADRCSTEARFESIVTASLPTKLDRVFYARDAETLRARSAVCALNGMCPVTLLEDGLCVEGRVGSRDPAFPGFVMRSEVDNERVEWYAFQTASKLLRFAASSQRFVDHAKTLVKSNMVMVGLFGLVDLLPRELYIEGTRRYEHQQEEALAARQTVSTQTGQIDSYIDRNYRWNEWDLRRQALKLVNLLDMRTHSTQTIASHFRRDNATQCRPPRDDSTQTMQDIAVQPPRTVQYLKGLRGTKTSAIETVQKTFLY