wanglab/gogpt-training-data huggingface dataset:
Protein: ABC transporter A family member 9 (ABC transporter ABCA.9) (AtABCA9) (ABC2 homolog 11) (Q9FLT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the transport of acyl-CoAs and/or free fatty acids to the endoplasmic reticulum. Has no effect on the selectivity of fatty acid incorporation into triacylglycerol or further desaturation steps.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23269834}; Multi-pass membrane protein {ECO:0000269|PubMed:23269834}.
Interaction partners:
- Protein FATTY ACID EXPORT 1, chloroplastic
- Putative defensin-like protein 234
- Protein FATTY ACID EXPORT 2, chloroplastic
- Putative defensin-like protein 235
- Protein FATTY ACID EXPORT 4, chloroplastic
- ABC transporter D family member 1
Sequence:
MTLREGLPLFHQQFTALFKKNLLLSWRNKRATCLHLFSSFFFILLIFSIEESSKASDLTSTRHKNVTDPKALVSLPILPCEDKFFVRLPCFDFVWSGNQSRRVTDIVSAIMANNPGRPIPTNKVQSFTKPEEVDAWFMSHPSQVTGALHFVEKNATVISYGIQTNSSSEKKRGRREDPTFKFLVPLQIAAEREIARSLIGDPKFSWDFGFKEFARPAIGGEVIISAFYLMGPVFFLAFSMFGFVLQLGSVVTEKELKLREAMTTMGVYESAYWLSWLIWEGILTFVSSLFLVLFGMMFQFEFFLKNSFVLVFLLFFLFQFNMIGLAFALSSIISKSSSATTVGFLVFLVGFITQIVTTAGFPYSSAYSIGSRVIWSLFPPNTFSAGLQLLLEATSSPGDSGISWSERAICAGGESTCVITTNKIYIWLVGTFFFWFVLALYFDNIIPNASGVRKSIFYFLKPSYWTGKEGNKVEEGSICSCIGSVPPVEHITPEDEDVLEEEILVKQQAMDGRVDPNIAVQIHGLAKTYPGTTKLGCCKCTKTSPFHAVKGLWMNIAKDQLFCLLGPNGAGKTTTISCLTGINPVTGGDAKIYGNSIRSSVGMSNIRKMIGVCPQFDILWDALSSEEHLHLFASIKGLPPSSIKSIAEKLLVDVKLTGSAKIRAGSYSGGMKRRLSVAIALIGDPKLVFLDEPTTGMDPITRRHVWDIIQESKKGRAIILTTHSMEEADILSDRIGIMAKGRLRCIGTSIRLKSRFGTGFVATVSFIENKKDGAPEPLKRFFKERLKVEPTEENKAFMTFVIPHDKEQLLKGFFAELQDRESEFGIADIQLGLATLEEVFLNIARRAELESATVEGTMVTLELESGIAVEIPVGARFVGIPGTENAENPRGLMVEVYWQQDGSGSMCISGHSAEMRIPENVSVIYEPSSQVLGHGQRRVRGIVIDYESNN
Protein: Guanine nucleotide-binding protein alpha-2 subunit (P22454)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Involved in behavioral responses to P.aeruginosa by controlling the expression of daf-7, a member of the TGF-beta family, in ASJ sensory neurons.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha
- C2H2-type domain-containing protein
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit beta-1
- Receptor-type guanylate cyclase daf-11
- Guanine nucleotide-binding protein subunit gamma
- SRBC-64)
- Serpentine Receptor, class BC
- Cyclic nucleotide-binding domain-containing protein
- G protein gamma domain-containing protein
Sequence:
MGLCQSEEEKVGTLKSRAIDKEIKQLQTSEERTVKLLLLGAGECGKSTVLKQMRLLTSKQYTDEELLTQAKLVYTNIVIEMDHLVKAMPAAGLNFSDPMREHDVHMLTLYIKDMQHKNFQQDAADHVEKLWKDPVVKRLYAERKELNIRDIGDNTEYFFENLPRISKEDYHPNATDTLLLRTKTTGIVEVGFEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESMRLFESICNSRWFHNTNIILFLNKKDLFEEKIKKENIHKAFPEYRGEQNYAETVAFIKTKFEALSNNPKKTFYVHETCATDTNQVQKILDSVISMIIQSNLHKSGLY
Protein: Sorting nexin mvp1 (O14120)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for vacuolar protein sorting.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P40959}. Endosome membrane {ECO:0000250|UniProtKB:P40959}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40959}; Cytoplasmic side {ECO:0000250|UniProtKB:P40959}. Note=Localizes throughout the endosomal system binding to phosphatidylinositol 3-phosphate (PtdIns3P). Enriched on retromer SNX-BAR-decorated endosomes. {ECO:0000250|UniProtKB:P40959}.
Interaction partners:
- DNA mismatch repair protein msh3
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d
- Uncharacterized pyrophosphatase/phosphodiesterase C725.05c
Sequence:
MGDNVFLEPDPWASSSNWGSPVKPLNYKTAIGNSSIPLQYRNYWDVFQANNVLLFPEEESYSDIFHVPQDVMKEFFTLIESSSNQPLRQIQFFVLLALVACYQLGVPSTLEQIFKQRNVLPILQRFNPELFNRSSDNETPLFPNNSPPASTTALNLSSNIVPSINESKILEQEDDDVSNKSLPHAQQSIIRSFPDIQKQPKGFFSYPSSTVSSIAPSTLEAGNLHSQQPPKFSVDSSVDDNAITPRKPFSKIPNRLSPSTQPLLSNSRHSSFRLASSSTSFPASLEMNVDIDLEPSGYFFYRHNNYIISDSSNTREVLRRYSDFFWLHSYLMKKYPFRRVPLIPLKKFHFAKRNASTQNSFLEHRRQELSDFVNDLSHHPIFSNDEVVRVFFTEPNVFKNWRRENQKRIDQEIEQFLVVPQSQVPDASETVKERLLKLNMSTTTAINNQLNIFRIFEKMIFTLQHFHEDFLRLQNSFNCLLDSGLYHQVFTSTFAQNESKIMSMASGHFYNIDSLLHQQNDAVKHTFLLGLSKEIKILISLRLLIERISEVFSTDLTKVRHTISNDENLLRETANSDESGRNRTFLNRSSKKRAENSLKSKKELYLKNLNQRYQIAHELEQELSYLQDYVFSLGNPYVEYCKQHVKLEEESLKIWHTLESDFSRLET
Protein: Pentraxin family member (Q2TS39)
Organism: Carcinoscorpius rotundicauda (Mangrove horseshoe crab) (Limulus rotundicauda)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362112}.
Interaction partners:
Sequence:
KVKFPPSSSPSFPRLVMVGTLPDLQEITLCYWFKLHRLKGTPHIFSYANSETDNEILTSLNEQNDFLFNIHGKTQLNVQCNNKIHAGRWHHVCHTWSSWEGEATTAVDGFRCKGNATGKAMGVTFRQGGLVVLGQDQDSVGGGFDAKQSLVGELSELNLWDMVLNHEQIKHLSECVHPSERHIYGNVIHWDKTQFQAYDGVALSPNEICA
Protein: ADP-ribosylation factor 1 (AtARF1) (EC 3.6.5.2) (Protein BFA-VISUALIZED EXOCYTIC TRAFFICKING DEFECTIVE 1) (P36397)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTP-binding protein involved in protein trafficking; required for the sequence-specific vacuolar sorting route to the lytic vacuole, for the ER-to-Golgi transport and for the Golgi-derived transport to the plasma membrane. Involved in the recruitment of COPI and GDAP1 to membranes. Required for recycling of PIN auxin transporters (e.g. PIN1 and PIN2) in a fungal toxin brefeldin A (BFA)-dependent manner. Involved in various auxin-dependent developmental processes.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:11090220, ECO:0000269|PubMed:15659621, ECO:0000269|PubMed:24369434}. Endosome {ECO:0000269|PubMed:11090220, ECO:0000269|PubMed:15659621}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21105926, ECO:0000269|PubMed:24369434}. Early endosome {ECO:0000269|PubMed:24369434}. Note=Colocalizes with AGD5 at trans-Golgi network. {ECO:0000269|PubMed:21105926}.
Interaction partners:
- Coatomer subunit gamma
- ARF guanine-nucleotide exchange factor GNL1
- Coatomer subunit delta
- Brefeldin A-inhibited guanine nucleotide-exchange protein 3
- ARF guanine-nucleotide exchange factor GNL2
- Brefeldin A-inhibited guanine nucleotide-exchange protein 4
- Probable ADP-ribosylation factor GTPase-activating protein AGD9
- Brefeldin A-inhibited guanine nucleotide-exchange protein 5
- Ras-related protein RABA1b
- Kinesin-like protein KIN-14E
Sequence:
MGLSFGKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIASKA
Protein: polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Q9V9X7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- ATP-dependent RNA helicase SUV3 homolog, mitochondrial
- CTP synthase
- Poly
- Elongation factor Ts, mitochondrial
- Ribonuclease Z, mitochondrial
- FI21480p1
- Eukaryotic translation initiation factor 5B
- DNA-directed RNA polymerase II subunit RPB3
- rRNA biogenesis protein RRP5
- U3 small nucleolar ribonucleoprotein protein IMP3
Sequence:
MAMIFTRKSLKLLNYRLKCLSLSCPGGRRGIQSSSNGEAPSVEVNFSNGRNMTFSSGRLARFANGTAVCQMGDTAVMVTAVAKAKPNPGQGFMPLVVDYRLKNAASGRIPMNFMRRELGPSEKEILSARLIDRSLRPLFHKDYRTETQLVCNMLAMDAVHSPDVLAINAASMALSLSDIPWNGPIGAVRVGLCDGEVLINPTRRELQTSQLDLVVSATKQNLVVMLEGKGNVVLQQDLLKAIKQGTREAQFIIHEIERLQKAYGRQKREVEVAAEVDPELGKAVRSMCEMRLREIFQDSTHDKMSRDNAVNEVRSNVIDKVWSSFPDTEPSLITEQFNQTSRTIFRELIFERGLRCDGRDYDQLRNISCQVDMYKPLHGSALFQRGQTQVFCTVSLDSQESAMKLDSLAALDSGGLKAKNFMLHYEFPPYATGEVGRIGPVGRREMGHGALAERSLLPTLPNDYPFTVRLTSEVLESNGSSSMASVCGGSLALMDAGVPVSAPAAGVAIGLVTKFENDDTKHLQDYRILTDILGIEDYMGDMDMKVAGTRKGFTAIQADLKIPGIPLKVVMESLQKATDAKSNILDIMSEAIREPRKYPKESWPVSETLTVEPQQRAQLIGPSGLHMKRIYLETGTSLTAVDETHFNVFAPSQAAMDEAKELIEGYMVKERVPDLEFGGIYTAKITELRDTGVMVILYPSMPPALLHNSQLDQRKIAHPSALNLEVGQEIQVKYFGRDPVSGFMRLSRKVLQGPALGIPRSLNKSAGESGT
Protein: MIOREX complex component 2 (Mitochondrial organization of gene expression protein 2) (Q05892)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression. Component of a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Ubiquinone biosynthesis protein COQ9
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Atypical kinase COQ8, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein COQ4, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Hexaprenyl pyrophosphate synthase, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MIPKLIVFGGNGFLGKRICQEAVTSGYQVVSVSRSGKAPHSNELNDKQWMQEVQWTAADIFKPDSYHELLNNATNVVHSLGILLENENYKQTLSKSPTYDSKSRLLSFGAGPNPLKKSSPYFTYEMMNKQSAIILADTFKQKILKKSKKEQEKANQRSFTYISADKGFPLIPSGYINSKREAEIELEKMQRYFRPIIVRPGFMFDEHRNAIGPRSFIHTALELLYCGNKFLLRNKLQLLNDLIRPTVSTQQVSKSVLKNIENPDFKGVVTLEEILKA
Protein: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type III) (3-beta-HSD III) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)] (P26150)
Organism: Mus musculus (Mouse)
Function: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Cytochrome P450 7B1
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Cytochrome P450 7A1
- Aldo-keto reductase family 1 member D1
- 17-beta-hydroxysteroid dehydrogenase type 3
- Steroid 21-hydroxylase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- steroid 11beta-monooxygenase
- Aromatase
Sequence:
MPGWSCLVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAIIDVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLNGHEDEHRESTWSDPYPYSKKMAEKAVLAANGSMLKNGGTLQTCALRPMCIYGERSQFLSNTIIKALKNKFILRGGGKFSTANPVYVGNVAWAHILAARGLRNPKKSPNIQGEFYYISDDTPHQSYDDLNYTLSKEWGFCLNSRWYLPVPILYWLAFLLETVSFLLSPIYRYIPPFNRHLVTLTASTFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWIGTLVEQHRETLDTKSQ
Protein: F-box/kelch-repeat protein At3g04660 (Q9SR08)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Integral membrane HRF1 family protein
- F-box protein At5g52880
- F-box/kelch-repeat protein At3g24760
- F-box/kelch-repeat protein At2g24250
- F-box/LRR-repeat protein At1g67190
- Protein STABILIZED1
- F-box/kelch-repeat protein At2g43270
- F-box/kelch-repeat protein At2g22030
- F-box/kelch-repeat protein At4g29370
- Putative F-box only protein 10
Sequence:
MKKRGRKSKKPEEKRAEYDPSSILPLELKIEILMKSPPKSIAKLGFVSNHWSSIIRGQVFTDLYMRRSLAHPRLLFSVYRPNMQMQFFHSCSQEDPSSDHRSVSYTLNSDLRYSFSPPIGGLIFGQNNTKAMIGNPSTGQFVPLPRIKTQRKHIFSIFGYDPVNDLYKVLCMTVRTLRGPHYFRWEDPMWEEPMTEEHQVFTLGPKQKWRMLECKYLHRHHSGSQGICRDGVMYYLASFNDKRSLMSFDLSSEEFNVTKLPEDYILQQFGNMVDHSGKIAIVSQAYSGPMDLWVLEDVSKEEWSKVAAIVPSITDIVGNDQRVIFRGILSTGEIILSLLPTPKPPFFFLCYDPKEKTARKVVIQGIGEDYAAINVFFDHVESHMVLSKLT
Protein: Bifunctional (p)ppGpp synthase/hydrolase SpoT [Includes: GTP pyrophosphokinase (EC 2.7.6.5) ((p)ppGpp synthase) (ATP:GTP 3'-pyrophosphotransferase) (Stringent response-like protein) (ppGpp synthase II); Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase (EC 3.1.7.2) (Penta-phosphate guanosine-3'-pyrophosphohydrolase) ((ppGpp)ase)] (P0AG24)
Organism: Escherichia coli (strain K12)
Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response which coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the synthesis and degradation of ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c-di-GMP induces it. ppGpp activates transcription of CsrA-antagonistic small RNAs CsrB and CsrC, which down-regulate CsrA's action on translation during the stringent response.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17616600}. Note=Is associated with pre-50S ribosomal subunits in a salt-dependent manner.
Interaction partners:
- tRNA
- Guanylate kinase
- ATP-dependent DNA helicase RecG
- Nucleoside triphosphate pyrophosphohydrolase
- GTP pyrophosphokinase
- Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
- Pyruvate kinase I
- Nucleoside diphosphate kinase
- Exopolyphosphatase
- Adenylate cyclase
Sequence:
MYLFESLNQLIQTYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMKLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKFRDKKEAQAENFRKMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRYRVIKEVVKAARGNRKEMIQKILSEIEGRLQEAGIPCRVSGREKHLYSIYCKMVLKEQRFHSIMDIYAFRVIVNDSDTCYRVLGQMHSLYKPRPGRVKDYIAIPKANGYQSLHTSMIGPHGVPVEVQIRTEDMDQMAEMGVAAHWAYKEHGETSTTAQIRAQRWMQSLLELQQSAGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGHACVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAAWLNFVVSSKARAKIRQLLKNLKRDDSVSLGRRLLNHALGGSRKLNEIPQENIQRELDRMKLATLDDLLAEIGLGNAMSVVVAKNLQHGDASIPPATQSHGHLPIKGADGVLITFAKCCRPIPGDPIIAHVSPGKGLVIHHESCRNIRGYQKEPEKFMAVEWDKETAQEFITEIKVEMFNHQGALANLTAAINTTTSNIQSLNTEEKDGRVYSAFIRLTARDRVHLANIMRKIRVMPDVIKVTRNRN
Protein: FCS-Like Zinc finger 8 (Q8L471)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway.
Interaction partners:
- FCS-Like Zinc finger 17
- FCS-Like Zinc finger 16
- FCS-Like Zinc finger 1
- Regulatory-associated protein of TOR 1
Sequence:
MLKKRSRSKQALMAETNQSQNQKQSKTTPFPRLFTAFSSFKSFTENDAVASPTSILDTKPFSVLKNPFGSDNPKTQEPETRLKLEPKRIGLAIVDSLIQDETPEPGPRSGTILFGSQLRIRVPDSPISSSDFGIKTRNSQPETKKPGSESGLGSPRIISGYFPASDMELSEDYTCVTCHGPNPRTIHIFDNCIVESQPGVVFFRSSDPVNESDSDYSPPDSFLSCCCNCKKSLGPRDDIFMYRGDRAFCSSECRSIEMMMSEENDTK
Protein: BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3) (GAOB1) (Q9H6U6)
Organism: Homo sapiens (Human)
Function: Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy. Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures.
Subcellular location: Nucleus {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17505058}. Cytoplasm {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:18030336, ECO:0000269|PubMed:33499712}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8CCN5}. Preautophagosomal structure {ECO:0000269|PubMed:33499712}. Note=Localizes in the cytoplasm in stationary cells. Translocates from the cytoplasm to the leading edge in motile cells. Colocalizes with microtubules and intermediate filaments in both stationary and motile cells (By similarity). Associates with chromatin. Recruited to estrogen receptor-induced promoters in a PELP1-dependent manner. The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner (PubMed:33499712). {ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:33499712}.
Interaction partners:
- Breast carcinoma-amplified sequence 4
- Phagosome assembly factor 1
- WD repeat domain phosphoinositide-interacting protein 2
- Metastasis-associated protein MTA1
Sequence:
MNEAMATDSPRRPSRCTGGVVVRPQAVTEQSYMESVVTFLQDVVPQAYSGTPLTEEKEKIVWVRFENADLNDTSRNLEFHEIHSTGNEPPLLIMIGYSDGMQVWSIPISGEAQELFSVRHGPIRAARILPAPQFGAQKCDNFAEKRPLLGVCKSIGSSGTSPPYCCVDLYSLRTGEMVKSIQFKTPIYDLHCNKRILVVVLQEKIAAFDSCTFTKKFFVTSCYPCPGPNMNPIALGSRWLAYAENKLIRCHQSRGGACGDNIQSYTATVISAAKTLKSGLTMVGKVVTQLTGTLPSGVTEDDVAIHSNSRRSPLVPGIITVIDTETVGEGQVLVSEDSDSDGIVAHFPAHEKPVCCMAFNTSGMLLVTTDTLGHDFHVFQILTHPWSSSQCAVHHLYTLHRGETEAKVQDICFSHDCRWVVVSTLRGTSHVFPINPYGGQPCVRTHMSPRVVNRMSRFQKSAGLEEIEQELTSKQGGRCSPVPGLSSSPSGSPLHGKLNSQDSYNNFTNNNPGNPRLSPLPSLMVVMPLAQIKQPMTLGTITKRTGPYLFGAGCFSIKAPCKVKPPPQISPSKSMGGEFCVAAIFGTSRSWFANNAGLKREKDQSKQVVVESLYIISCYGTLVEHMMEPRPLSTAPKISDDTPLEMMTSPRASWTLVRTPQWNELQPPFNANHPLLLAADAVQYYQFLLAGLVPPGSPGPITRHGSYDSLASDHSGQEDEEWLSQVEIVTHTGPHRRLWMGPQFQFKTIHPSGQTTVISSSSSVLQSHGPSDTPQPLLDFDTDDLDLNSLRIQPVRSDPVSMPGSSRPVSDRRGVSTVIDAASGTFDRSVTLLEVCGSWPEGFGLRHMSSMEHTEEGLRERLADAMAESPSRDVVGSGTELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPLSLFPTGFP
Protein: CKLF-like MARVEL transmembrane domain-containing protein 8 (Chemokine-like factor superfamily member 8) (Q8IZV2)
Organism: Homo sapiens (Human)
Subcellular location: [Isoform 1]: Membrane; Multi-pass membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.
Interaction partners:
- CKLF-like MARVEL transmembrane domain-containing protein 7
- CKLF-like MARVEL transmembrane domain-containing protein 6
- Chemokine-like factor
- CKLF-like MARVEL transmembrane domain-containing protein 3
- CKLF-like MARVEL transmembrane domain-containing protein 1
- CKLF-like MARVEL transmembrane domain-containing protein 5
- CKLF-like MARVEL transmembrane domain-containing protein 2
Sequence:
MEEPQRARSHTVTTTASSFAENFSTSSSSFAYDREFLRTLPGFLIVAEIVLGLLVWTLIAGTEYFRVPAFGWVMFVAVFYWVLTVFFLIIYITMTYTRIPQVPWTTVGLCFNGSAFVLYLSAAVVDASSVSPERDSHNFNSWAASSFFAFLVTICYAGNTYFSFIAWRSRTIQ
Protein: Endoplasmic reticulum oxidoreductin, putative (Q57UW3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004367}; Lumenal side {ECO:0000256|ARBA:ARBA00004367}.
Interaction partners:
- Ribosomal protein L7Ae/L30e/S12e/Gadd45 domain-containing protein
- Protein disulfide isomerase
- Sulfhydryl oxidase
- Uncharacterized protein
- Derlin
- Derlin
- alpha-1,2-Mannosidase
- UDP-glucose:glycoprotein glucosyltransferase, putative
- Nucleoside diphosphate kinase-like domain-containing protein
Sequence:
MLKMRLLIVVPVLLGLVWQILLRAELDGVSFFGMYISANNSGAGSYVRTKKGNALKEGFCSLTMDEVSQNTEGITGLLNNITSHPYFRYFKVNLDRECRYWVAEASCTCDSNGCQICTCDDSGIPETLKYPYDMSDVSTVERRAAPDKHAAKGFEDEIKPIDPDRDATYVDLLQNPEANTGYSGPKAARVWQAVYNNCNIDGLPSNDTAGVENREKALLRQLLSGLHTSITMHVAAFFYNDTKGDSPLRSLGVLNNPNISFYPNCGMFRRIVKNDEFIRNLFVVYQFVLRALAKTKRAFLANSSLYNSGFNGAATDGDVRLYSNIGELFSSKLFRVATFDEQKFFESPGAHLLVRQMKRVVHNVTTLMDCVTCEKCRAWGKLETAALATALKIVFGSAENVVELNRGERVALINFARQLAISVKNVRSLAAVCEKFNYTAMS
Protein: Daf-12-interacting protein 1 (G5EGK6)
Organism: Caenorhabditis elegans
Function: Probable transcriptional corepressor which modulates activity of the nuclear hormone receptor daf-12 to regulate the dauer diapause.
Subcellular location: Nucleus {ECO:0000269|PubMed:15314028}.
Interaction partners:
- Nuclear hormone receptor family member daf-12
- 3-ketosteroid oxygenase
- Suppressor of hairless protein homolog
- LIPaSe related
- Cholesterol 7-desaturase
- Nuclear hormone receptor family member nhr-48
Sequence:
MVQVPSTNTVKESRHVAISGLPSTLPDDRLQLHFTKFGEIQRLVRQHGNPEIVLVSYMDARGALRARSTKPQFEDSIEYKISAYIPEPTQNSSMASMSSTPSSGQSSSPRNAELSPQRYGDTRGAEVKSPSFRNQMEARRGGPHLSVQSQQRHSREYWPIPEFPSESTACVVYEIQSGSTPERDLFELVKKHSKRSGVPIDIQLESTTEPGWKKARVHYYRLDTDGLKADKSLILGRPPKFRVYYPTSGEQKHPQCHPSTSYAIPKLKGDHLLKASCSVHVPHLDRHSPDHYRRRFESYGQVIDVDMVKSNDNKAFAVVQFTNIDDAQKALQDTNIPKPMSYQSRPSHRIIIFYLPIECTNEEIMLIIRSLSDRIVDICVDWWDRSAVITLDDMEPANLLLKRMKLVGRNNFGEHKVAVDFCSDRFNLYFINRKKENIEVAARSSSPTSKSENDQGSSSPSSSRDRQNLHDPLQTRSSVEHHTNQEDQENNASGSDSSSDSDSEEGSSSSNEDSDEQNDVDEEDDEDVVSEEKRHEPEEGKSSSPGNGHRDESNGDKDHEDSSERFSQPSTSSHHETSHSPEKDSEAYQSRSFSPLNYQSQSPGYEFLESKEIKQEFSPTTSSASSSDLELDMEMPDNPLTRMLERMHWRPFIDVSSFVNRIDEIVELNQKARASYEKFTGRPFPKCNNDEVLSIQKIVFHEPRDYYYYENPCSELEVRIRDWRKLSDTADLDDFRATDSKELGRDQPAGGRTSGRPSLDESRTNRLSFDSTHHPAELAQRSHSLCIGPMTPSTPFPTSQPLLVNTTHLPGTSQPSTSGGITTPRSSQPPPLMSPVSRHNSMSSTGRPASIQTLRHQSVMFPPDVSIPPPPIPPTHDEMMAPRGTPPSRRSSETMVPLRSPPFGTPIQNLLTMPIVPPPHLIAATSTGTHSVSSSAHSTPRHSISGTPVHCEPSNSKTSQPPTPKSRPEKVQIRHDTISKSGPSNAINALQARSQSMTSGDPKKSAPSTPVVRDAGSDLVAQIMSNQPNLGLRKLPRIEKKSSALQNIQNHQPPHSNANSTPSTPSTSTHQAMFKDKEKERKKKEKEKEEREREARREMKRKETKEERNKRKEMERAKRLEDERQERKREKKKERDERKKEKEKVRKKAEKEKLKKKKHRKGDSSDESDSDSNDELDLDVRKSTKEMTQEEKDHQLALLLSKGGIIENLKSRRRSDKRAHDSFEKMQQKSQQRRVLIESSDDEGGKDGDKGNSSNGEESDSEKADLPPPPAPPSLSESADQRLKVLKEREKGELTTSSDDEDHNDAGEIHQQRLTEDRENRKRQKSLTAYSSDEQGERKNVPKRMRRDDSEDAAAKHPGWSAKDDQKQRKRKLEHRRSSEDESKKNAKRDFRDIPHEDVSDEEETEDGSRSRRQSTSSTISNVTAKERKEKSGKTPLRIVPEPTGTPLLSPKILSPKHLSPKTSTSSTKRSSISDHENLISPRQRNRTTSSTSTATTSSKHEALSIPEKPLSPPVTAKSSVSSIDDPSIRDEFSMNSAADSPMSTTGRPMVLTKAAMKAFNSTPPKKKNSSSGQHDSSSGSSSDSSSSDGSTSSDDSSDDEVPKQTEPVTSIPVVASDNGSPENVVVETPSIVSQTPREPEPFTISEQSSESEPEAVPECPEASVEPQMETSQNVEPVSEEHEDSHEHGDSEVAVESQQQPLEHQEEKEELENKILDVAAEHHEEQVQGDEDSVESSIPAPSDEPDPVTQAQEKSAHTLISDQETDQAVQSIFDEEEADEFPQYPDFGISTNEKEVSGKDPHNIKPTEPLNNGHTDLLFSPSSSAHASEKQSTKSEDDMEEDSELVVMEKEVPMEQVIAQEVHVPSEPSPMEEEVKLETSPVPKEEPIKMEESPEQTPTPDLISNNESQDTPGAVNNHLHENHDAVQTPIQLQPASQHQVAQPSPRPAVAPDSQQNGPVLVSQQSQPSPMSSQQSDMAQNLILSSKDINDLAAKLHKNPEALAQATRGDCSGIFQHLLLHAQGNGQNMTPEMLQLKAAFFAQQQENEANQMMQAKMKQQTINKDRIKEQERVKRMYEENERKVEEDRREKQRKEEERQRLAAATAAATMATQKAAEALKQKQEVPRHGFQHVLSMMTPEARSLYEQFPGLSSYINRDSIGATNGVLHLPTQSIQRPSSTASTSSNPPKAPLQPSASVNQNTIDPAEIEEIRVQRWFYKHFPMVWTGRLALKSTEAMINLHLINGSETFLNDVLGRQVTEENPRRDSVKILQRLRLDNGQVEHIYRILTNPEYACCLALSSVNNIENLKENDTNLKSHFIDYLINKKIAGISSLGEVETKFKSARVHVFAPGEIVNRYLSELATSLHDYLQNTDTRYLLIVFTNDKADPNMTGPPSVASLAVPPVSST
Protein: Prolactin-releasing peptide (PrRP) (Prolactin-releasing hormone) [Cleaved into: Prolactin-releasing peptide PrRP31; Prolactin-releasing peptide PrRP20] (P81277)
Organism: Homo sapiens (Human)
Function: Stimulates prolactin (PRL) release and regulates the expression of prolactin through its receptor GPR10. May stimulate lactotrophs directly to secrete PRL.
Subcellular location: Secreted.
Interaction partners:
- Prolactin-releasing peptide receptor
- Pro-FMRFamide-related neuropeptide FF
- Neuropeptide FF receptor 2
- Orexigenic neuropeptide QRFP
- Prolactin
- Pro-FMRFamide-related neuropeptide VF
Sequence:
MKVLRAWLLCLLMLGLALRGAASRTHRHSMEIRTPDINPAWYASRGIRPVGRFGRRRATLGDVPKPGLRPRLTCFPLEGGAMSSQDG