wanglab/gogpt-training-data huggingface dataset:
Protein: Sperm-associated antigen 4 (Q9VKG2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Muscle-specific protein 300 kDa, isoform G
- E3 SUMO-protein ligase NSE2
- DNA repair protein Rad60
- Structural maintenance of chromosomes protein 5
Sequence:
MAHNSRNNLGIMRLREDVDDISHILRQQQIDSKVAQGSCKFNCLGGEPKGVGSGMCNNRDVSAYVDTLFKRKIGHLMDDVYNLKKQVMSADCSSKSAQSTPKPESVALAKPRINYASEELGARIINVKAHSIDGTNIIRSLLGLDFSTNPPVNMIRTGLSPGSCFGFNGSRATVTLHLARTIIVEAITLTHVAREMTPDLCVKSAPKNFDVYGLRSENSKRELLGQWSYDNAANKRTQSYSVRSDTFFRNLDFSFNSNHGANSTCIYRVEVYGRL
Protein: Doublesex- and mab-3-related transcription factor 2b (Doublesex-and mab-3-related transcription factor 2b) (A0SDZ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00070}.
Interaction partners:
Sequence:
MSTKADRGAQVDATHLECLKAEWVADCAGREVMGTDEAPAARRLSRSPKCARCRNHGVVSRLKGHKRLCRWRDCQCANCLLVVERQRVMAAQVALRRQQATEGKKGQKNSAVLRRTAYQRYTRAPSLLAKSILEGYKPPVPEDWPKRLHQPPVSVRMRKRRAFADKELETVMLERELRQREIEELPSLLLQAVVPSAPSPYFFPLSDPIMPTFVPVSKNSPPLTDCDLRQHGLKSKTLDTLTDDVSLRVCKNWDIFSSIQSPLQCYNSTSPGVNLVKNTPDRSFSDLYVKPKFAVADIMSKQDIPPILNMADVLIHAKSPHKRCRSLGHEASVRLDCVEGASKDPVKKAVTRPLPFSVEALLMR
Protein: Neurolysin, mitochondrial (EC 3.4.24.16) (Microsomal endopeptidase) (MEP) (Mitochondrial oligopeptidase M) (Neurotensin endopeptidase) (Q91YP2)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1.
Subcellular location: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P42676}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P42676}.
Interaction partners:
- Neurotensin/neuromedin N
Sequence:
MITLCLSALRGLHRAGGSRIRLRMTLGREAASPLQAMSSYTAAGRNVLRWDLSPEQIRTRTEELIAQTKQVYDTVGTINLEDVTYENCLQVLADIEVKYIVERTMLDFPQHVSSDREVRAASTEADKRLSRFDIEMSMREDVFQRIVHLQETCDLEKIKPEARRYLEKSIKMGKRNGLHLPEHVKNEIKSMKKRMSELCIDFNKNLNEDDTSLVFSKAELGALPDDFIDSLEKTDEDKYKVTLKYPHYFPVMKKCCVPETRRKMEMAFHTRCKEENTIILQQLLPLRAQVAKLLGYNTHADFVLELNTAKSTSHVATFLDDLSQKLKPLGEAEREFILSLKKKECEERGFAYDGKINAWDLHYYMTQTEELKYSVDQESLKEYFPIEVVTEGLLSIYQELLGLSFEQVADAHVWNKSVSLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMSVAALVVNFSQPIAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDIDSLRKLSKHYRDGHPITDELLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNASLDAASEYAKYCTEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFHSCFRKEGIMNPEVGMKYRNLILKPGGSLDGMDMLQNFLQREPNQKAFLMSRGLNAS
Protein: Anaerobic nitric oxide reductase flavorubredoxin (FlRd) (FlavoRb) (Q46877)
Organism: Escherichia coli (strain K12)
Function: Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase.
Subcellular location: Cytoplasm.
Interaction partners:
- Nitric oxide reductase FlRd-NAD
- Anaerobic nitric oxide reductase transcription regulator NorR
- Flavohemoprotein
- 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD
- Hydroxylamine reductase
- Nitrite reductase large subunit
- Cytochrome c-552
- Iron-sulfur cluster repair protein YtfE
- HTH-type transcriptional repressor NsrR
Sequence:
MSIVVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVELYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMMPKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDQDALKLCREHGREIARQWALAPLPQSTVNTVVKEETSATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFEELASEAK
Protein: Guanine nucleotide-binding protein alpha-12 subunit (Q19572)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (Probable). May play a role in resistance to fungal infection in the epidermis by regulating the up-regulation of several antimicrobial peptides of the NLP and CNC families. Upstream of plc-3, tpa-1 and the p38-like pathway, required for the expression of antimicrobial peptide nlp-29 in the epidermis in response to fungal infection or physical injury.
Interaction partners:
- Guanine nucleotide exchange factor
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit beta-1
- G-protein coupled receptors family 1 profile domain-containing protein
- Guanine nucleotide-binding protein alpha-9 subunit
- G Protein, Alpha subunit
- Ras-like GTP-binding protein rhoA
- GPS domain-containing protein
- Small ribosomal subunit protein RACK1
- Protein kinase C-like 1
Sequence:
MVCCFGKKDERTKTIEKELHKERKIMRRQINLLLLGSGESGKSTFVKQMHIIHGAGEFTADEVRAYRQQIYQNAISAMRVLLDARNKLGIAWEDPKRQVEVEKVMRFSVGDLLKGIDFTTFVEVAPIISDFWNDAAIRKTYEQRNLFQISDSCQYFFEHIPRIAMPDFYPTNRDILFCRKATRGISEHIFEINKIPFRFIDVGGQRSQRQKWFQCFTDITSILFMVASNEYDQVILEDRRTNRVVESRSVFETIVNNRAFSNVSIILFMNKNDLLQEKVPKSDIRQYFTDFTGDHTLVRDVQFFLVDKFEASRRDRARPFFYHFTTAVDTENIRRVFRDVRESILEQNLKTLMMQ
Protein: Hybrid signal transduction histidine kinase E (EC 2.7.13.3) (Q55E44)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May act in a signal transduction pathway. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDKLKINNNLSPPSSPSSSTTTPNLSSTNLENNLNSNINNNINNFNLNNSTNTFNNSNNIIINNNNNNNNNNNNNNNNNNNNSNNNNNNINNNNPNVNSPNEVILNNNFLKQNKKGFFKRNKKMIEIFLPPKFKSPIYRRCCILLGECGVYVFIYMFFLIFLRSFYPIFICGIVSMIVLYIVSTKTTKYKLVALIYIFVQSILNFTFFLQITNNFNNNTVNINNTDDYSNEVIEFSKLNFLFIMNLILSLISIQIFFPKFTFSITLTCSLNIFNIIIHLISIYSLNTKKLIVFQNLIVPITVSFLLSFYSYILSIDNQEIEAKEKRFRNIFDTSSEALVIHKNGLIIDVNSTFEKIFQIKQSDLINGTIWEYLPELESFFQNTNGNSKYTNQSLQQQLQQQQQQQQQLYNTITNGGNNKQTSTTSANSTPRYNNYNNNNINSNNLNNLNVFNNLNNLNNLNNNNNNHHIHKVSRSNTGLSDSSSIFDDSDSVDFFSMKNINKCPIVLDTVGITPCGSEFCAQVKIERKKDMLIGSGTSSFNLLNNNNNNNNNNNNNNNNNNNNNNNNNNSNNNNNNNSNNNNNNNNINNNISNNIINNNNNNNNSGIITNLSQQSNNLSTTNLNTSSKIINHKHKNSKQDFDVMSIVDISAKKKLMIADQALRRAEELNQAKINFLTTVSHEVRTPINGILASVEILDGSQLDVTQRDFLSCIKQSADYLLDLITDILDFSKIEAGKFELDRVEFNLITMLEESINIVYRTAQERGIEVLTFIDPDVPIILIGDPYRVKQCVLNFLSNAIKFTHKGQVMVKVSIVDQINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKIVGFSNNNNNNNNNNNNGNNGILNFKLSFSVEDSGVGIKEEVLDCLFTPFHQLGGSPRKYLGTGLGLSISKKLTTLMGGEIGVKSVYGVGSAFSFTSILSTTSTTPISLQSLGSSLSIALNNLSPTIPKISGFIYDDNIHTSNSLFNFLKLMNINLKIINPIINNNNNNNNNNNNNNNNNNNNNNNNNNNNNDNNNNNNNNNDNNIDQQQLKFEFENEIDKYCNVEDDNNNVILIITNQLSNDNLNYFKDKINQLNNSIYWFVLCDNGLKAIDPFYYGIVKKPNNLLNLVDTVFKVYNCQLPQDLYQLLTNGSKDDYKNYLKYRNVVIKKITEDNEKKQQQQQQQQQQMGDTLSSTKSPQYTNLPPLDISSSSNGSLNKSNRSNLLRKSSSVYSDHVAITRGMVQVNRSPRPSTPPPLFNLKGNNSNPNSTELNSTNSVNGNPNNDSTLETIEPLNISETVGDLCSSGSVINNSNFIINNNFLTSSPYGSCLTPNSGTTSPSIPININNNDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSFKKLEPDNFSPPPSILINDNNIIPALNVTTPITISTSTSSSSSLLINNEINNKSTTSKRPSFIPPLDIQSKKLIINTADENHKNNCIIDFEQIFGQDGKQQPQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQKLNIGNQQQQQILSSPRLQSQLLSNCDSLGNTPPVTPHRRNALIVDDTELNRKVLAQLLRRMDWSVSFAENGIEALKEITSERCFDIIFMDCQMPILDGFETTKLLRLRELENNWKPLNIVALSADSSSSFGQVCFDCGMNGYLGKPITLITLKDTLLKWGGYRD
Protein: Uncharacterized protein C553.06 (O74943)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Probable protein transport protein Sec61 subunit gamma
- Uncharacterized protein C19G7.17
- Protein transport protein sec61 subunit alpha
- UDP-N-acetylglucosamine transferase subunit alg13
- UDP-N-acetylglucosamine transferase subunit alg14
Sequence:
MKGFFLIAGFLLFARALCASWNVEEGTLQLSSQDLESENAYDLKFSQIQSSTVYELTGDETLNLKFTCILNGTGAIPHQAHLLLSDTEHPTLAVIYPASVSQGGVASLELRLFDIPTSLLRSDSTLTAKLLVASFGETIPFSLPLGQLSINVPPSLYHKAEFSPLDELSPKEVILHTFSPPPKRANYFLSICFSVSVVVSLIGLLGVWQKLLPKSNVYSVSSSSFARTFGFASLAVAEILLFIYWTSLSIFQFGAYAAGVAIMCGIAAKSL
Protein: Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) (P83777)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378761}.
Interaction partners:
- inorganic diphosphatase
- Plasma membrane ATPase
- Adenylyl-sulfate kinase
- H
- ATP synthase subunit 5
- ATP synthase subunit alpha
- ATP synthase subunit gamma
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase proteolipid subunit
- Eukaryotic translation initiation factor 5A
Sequence:
MSSYSTRQVGAANTLDYKVYIEKDGKLVSPFHDIPLYANEEKTILNMIVEVPRWTNAKLEISKEQKLNPIIQDTKKGKLRFVRNCFPHHGYIHNYGAFPQTWEDPNQSHPETKAKGDNDPLDVCEIGEKVATVGEVKQVKVLGVMALLDEGETDWKVIVIDVNDPLAPKLNDIEDVETHLPGLLRATNEWFRIYKIPDGKPENQFAFSGECKNKKYAEEVIGECAEAWEKLIKGESVDSKGIDLTNTTLSSTPSYSDAAAQEIPSASPAPAAPIDKSIDKWFFISGAH
Protein: Probable phospholipase YOR022C, mitochondrial (EC 3.1.1.-) (Q12204)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable phospholipase that hydrolyzes phosphatidic acid.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Uncharacterized protein YNL146W
Sequence:
MLRFTHRGLPSSTRFRNIFVRLNHIYVPWFYAIDVPNSKPYLPTYQTLHSPKKFKPFSVDDSNRLEKASKRQERRPVLVNEDYLFKVDLSHMELSPTYWEGPTYQVRRGVWFDSSNQPLSSDLTSEIEGLYKQLKFDDSNDDPTTTPPAESQDIFRLKGKYPVDKENEGEQKNGSSNKDENESTFKFILFANKQTAFLLSDLDGGKLQLAFLRSNLAQSLPINATMITRSYKYSSSATTKQTSTSFKAAKTPQTEVADGSNSSKSRSIETKLEKKVSNLFNLSDFLQLFNGNASKDQDDAQSLEKQMETDYNNADNSQGANASSKIEDGKNSGASDRQIRSNRRDVDNLILCVHGIGQTLGKKYEYVNFAHTVNLLRSNMKKIYNNSEKLQSLNTAPDYKSNCNVQVLPITWRHSISFQTDAKEENIENPDLPTLSQVTVNGVLPLRKLLADGLLDILLYVEPYYQDMILQQVTSQLNKTYRIFKEFNPEFDGKVHLVGHSLGSMILFDILSKQKKYELEFQVDNLFFIGSPIGLLKLIQRTKIGDRPEFPNDLERKLTVQRPQCKDIYNVYHVCDPISYRMEPLVSKEMAHYEQTYLPHCSEAYGLTSKVLEFGENIWKDLPGTDENNLQSKKTSPEKKEVKLSENLTRMLTGLNYTGRLDYAMSPSLLEVDFISAIKSHVSYFEEPDIAAFILKEILSKHENASEIYVKRKTG
Protein: MyoD family inhibitor domain-containing protein (I-mfa domain-containing protein) (hIC) (Q9P1T7)
Organism: Homo sapiens (Human)
Function: Required to control the activity of various transcription factors through their sequestration in the cytoplasm. Retains nuclear Zic proteins ZIC1, ZIC2 and ZIC3 in the cytoplasm and inhibits their transcriptional activation (By similarity). Modulates the expression from both cellular and viral promoters. Down-regulates Tat-dependent transcription of the human immunodeficiency virus type 1 (HIV-1) LTR by interacting with HIV-1 Tat and Rev and impairing their nuclear import, probably by rendering the NLS domains inaccessible to importin-beta. Also stimulates activation of human T-cell leukemia virus type I (HTLV-I) LTR. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin regulation of the WNT and JNK signaling pathways. Has a role in the development of lymphatic vessel valves. It is required to promote lymphatic endothelial cell migration, in a process that involves down-regulation of integrin beta 1 activation and control of cell adhesion to the extracellular matrix (By similarity).
Subcellular location: [Isoform 1]: Nucleus, nucleolus. Note=Also shows a granular distribution in the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:10671520, ECO:0000269|PubMed:11139147, ECO:0000269|PubMed:12944466, ECO:0000269|PubMed:16260749, ECO:0000269|PubMed:35235341}. Cell membrane {ECO:0000250|UniProtKB:Q8BX65}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BX65}. Secreted {ECO:0000250|UniProtKB:Q8BX65}.
Interaction partners:
- Transcriptional repressor CTCF
- Acidic mammalian chitinase
Sequence:
MSGAGEALAPGPVGPQRVAEAGGGQLGSTAQGKCDKDNTEKDITQATNSHFTHGEMQDQSIWGNPSDGELIRTQPQRLPQLQTSAQVPSGEEIGKIKNGHTGLSNGNGIHHGAKHGSADNRKLSAPVSQKMHRKIQSSLSVNSDISKKSKVNAVFSQKTGSSPEDCCVHCILACLFCEFLTLCNIVLGQASCGICTSEACCCCCGDEMGDDCNCPCDMDCGIMDACCESSDCLEICMECCGICFPS
Protein: Aromatic amino acid aminotransferase 2 (EC 2.6.1.57) (Aromatic amino acid aminotransferase II) (Aromatic amino acid-requiring protein 9) (Kynurenine aminotransferase I) (KAT I) (EC 2.6.1.7) (P38840)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Mainly involved in tryptophan degradation. Active with phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate and pyruvate as amino acceptors. Does not accept glutamate or 2-oxoglutarate as substrates. Also active with methionine, leucine, glutamine and kynurenine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as the amino donors. Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) with pyruvate as amino acceptor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transaminated amino acid decarboxylase
- Probable prephenate dehydratase
- Prephenate dehydrogenase [NADP
- Aromatic/aminoadipate aminotransferase 1
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Branched-chain-amino-acid aminotransferase, cytosolic
- Transcriptional activator ARO80
- Chorismate mutase
- Histidinol-phosphate aminotransferase
Sequence:
MTAGSAPPVDYTSLKKNFQPFLSRRVENRSLKSFWDASDISDDVIELAGGMPNERFFPIESMDLKISKVPFNDNPKWHNSFTTAHLDLGSPSELPIARSFQYAETKGLPPLLHFVKDFVSRINRPAFSDETESNWDVILSGGSNDSMFKVFETICDESTTVMIEEFTFTPAMSNVEATGAKVIPIKMNLTFDRESQGIDVEYLTQLLDNWSTGPYKDLNKPRVLYTIATGQNPTGMSVPQWKREKIYQLAQRHDFLIVEDDPYGYLYFPSYNPQEPLENPYHSSDLTTERYLNDFLMKSFLTLDTDARVIRLETFSKIFAPGLRLSFIVANKFLLQKILDLADITTRAPSGTSQAIVYSTIKAMAESNLSSSLSMKEAMFEGWIRWIMQIASKYNHRKNLTLKALYETESYQAGQFTVMEPSAGMFIIIKINWGNFDRPDDLPQQMDILDKFLLKNGVKVVLGYKMAVCPNYSKQNSDFLRLTIAYARDDDQLIEASKRIGSGIKEFFDNYKS
Protein: Zinc transporter ZIP9 (Solute carrier family 39 member 9) (Zrt- and Irt-like protein 9) (ZIP-9) (Q3KR82)
Organism: Rattus norvegicus (Rat)
Function: Transports zinc ions across cell and organelle membranes into the cytoplasm and regulates intracellular zinc homeostasis. Participates in the zinc ions efflux out of the secretory compartments. Regulates intracellular zinc level, resulting in the enhancement of AKT1 and MAPK3/MAPK1 (Erk1/2) phosphorylation in response to the BCR activation (By similarity). Also functions as membrane androgen receptor that mediates, through a G protein, the non-classical androgen signaling pathway, characterized by the activation of MAPK3/MAPK1 (Erk1/2) and transcription factors CREB1 or ATF1. This pathway contributes to CLDN1 and CLDN5 expression and tight junction formation between adjacent Sertoli cells. Mediates androgen-induced vascular endothelial cell proliferation through activation of an inhibitory G protein leading to the AKT1 and MAPK3/MAPK1 (Erk1/2) activation which in turn modulate inhibition (phosphorylation) of GSK3B and CCND1 transcription. Moreover, has dual functions as membrane-bound androgen receptor and as an androgen-dependent zinc transporter both of which are mediated through an inhibitory G protein (Gi) that mediates both MAP kinase and zinc signaling leading to the androgen-dependent apoptotic process (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NUM3}. Cell membrane {ECO:0000250|UniProtKB:Q9NUM3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NUM3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NUM3}. Mitochondrion {ECO:0000250|UniProtKB:Q9NUM3}. Nucleus {ECO:0000250|UniProtKB:Q9NUM3}.
Interaction partners:
- Zinc transporter ZIP11
- Zinc transporter ZIP13
- Zinc transporter 7
- Metal cation symporter ZIP8
- Proton-coupled zinc antiporter SLC30A1
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Probable proton-coupled zinc antiporter SLC30A4
- Solute carrier family 39 member 10
- Zinc transporter ZIP4
Sequence:
MDDFLSISLLSLAMLVGCYVAGIIPLAVNFSEERLKLVTVLGAGLLCGTALAVIVPEGVHALYEEVLEGKHHQASEAKQNVIASDKAAEISVVHEHEHSHDHTQLHAYIGVSLVLGFVFMLLVDQIGSSHVHSTDDPESARPSSSKITTTLGLVVHAAADGVALGAAASTSQTSVQLIVFVAIMLHKAPAAFGLVSFLMHAGLERNRIRKHLLVFALAAPAMSMLTYLGLSKSSKEALSEVNATGVAMLFSAGTFLYVATVHVLPEDTSTNQSGSSLSPRPLPSGKN
Protein: Programmed cell death protein 7 (ES18) (Q9WTY1)
Organism: Mus musculus (Mouse)
Function: Promotes apoptosis when overexpressed.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- U11/U12 small nuclear ribonucleoprotein 48 kDa protein
- U11/U12 small nuclear ribonucleoprotein 25 kDa protein
- Y-box-binding protein 1
- Zinc finger matrin-type protein 5
- U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
- U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2-like
- Transcription initiation factor TFIID subunit 5
Sequence:
MALPPFFAQSRQGPPPPQPPPSAPFGCPPPPLPSPAFPPPLPQRPGPFPGASAPFLQPPLALQPRAPAEASRGGGGGGAFFPVPPPPLPPPPPQCRPFPGPDAVERPRPPPPGPGPPWSPRWAEAPPPPDVLGDAALQRLRDRQWLEAVFGNPRRPGGLRTPRTPAGPSLGEVRARLRSALRLVRRLRSLGQSLREAEADGAAWASLHAQAAPLRAELAERLQPLRQAAYVGEARRRLERVRRRVRVRERARDRRLSGRRGAQRTEREQEIDRWRVKCVQEVEEKKRDEELKAAADGVLAEVRKKQSDTKRMVDILRALEKLRKLRKEAAARKGVCPPASADETFEHHLQRLRKLIKKRSELYEAEERALRVMLEGEQEEERRRELEKKQRKEKEKLLLQKREIESKLFGDPDEFPLAHLLQPFRQYYLQAEHSLPALIQIRHDWDQYLVPSDHPKGNSVPQGWVLPPLPSNDIWATAIQLH
Protein: MAGE domain-containing protein (Q54PA3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Non-structural maintenance of chromosomes element 1 homolog
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6
- SP-RING-type domain-containing protein
- Non-structural maintenance of chromosomes element 4
Sequence:
MSRRSQQSQQRKPARRDEISSSSSEEEEEEEEEEEESPEEFSEGEEEEVGNKRKRATPRKTTQSQQSSTSTTTTTTTTTRSELTEEERYKLVYEYVRLLLFSNRKKVPITKTEINKIILARFKDKSLQGFVYKAGREYLKEFFGYEVVELKKKGKESSTYILKNLNDYEAVRQLDSIDPIENRESMIQKENLTLLTIILSIIFLENGHVESPQLLQFLSVLGFSQNEPHPVYGDLEKLLEKFCREQYLTRRKNVVDNQIIWVYEMGQRSSTESSKRFILNSISDIYGSEPDSIILKEIEQKEKDEGTFDPQNVNSTRGRTPKTNKNTQFNQNNNQNNNQNNNNNNNNNNNNNNNNNEDEEEESQQRVQKRPQQRGNLRKQVTIEEDEEEEEEPQQSQRMSQRSTRR
Protein: Phosphatidate cytidylyltransferase 1 (EC 2.7.7.41) (CDP-DAG synthase 1) (CDP-DG synthase 1) (CDP-diacylglycerol synthase 1) (CDS 1) (CDP-diglyceride pyrophosphorylase 1) (CDP-diglyceride synthase 1) (CTP:phosphatidate cytidylyltransferase 1) (O35052)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol. Exhibits almost no acyl chain preference for PA, showing no discrimination for the sn-1/sn-2 acyl chain composition of PAs (By similarity). Plays an important role in regulatinng the growth of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (By similarity). Positively regulates the differentiation and development of adipocytes (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29253589, ECO:0000269|PubMed:6271231, ECO:0000269|PubMed:9083091}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Cardiolipin synthase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Lysocardiolipin acyltransferase 1
- Phospholipase D1
- Phospholipase D2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Membrane-bound glycerophospholipid O-acyltransferase 2
Sequence:
MLELRHRGGCPGPGGAGTPPPREGEAAGGDHETESTSDKETDIDDRYGDLDARGDSDVPEVPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQVKCFQEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLIRYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMIWFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVIFGFIAAYVLSKYQYFVCPVEYRSDVNSFVTECEPSELFQLQNYSLPPFLQAVLSRETVSLYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRGPNPSKVLQQLLVLQPEQQLNIYRTLKIHLTEKGILQPTWKV
Protein: 17.4 kDa class I heat shock protein (17.4 kDa heat shock protein) (OsHsp17.4) (P31673)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MSMIRRSNVFDPFSLDLWDPFDGFPFGSGSGSLFPRANSDAAAFAGARIDWKETPEAHVFKADVPGLKKEEVKVEVEDGNVLQISGERIKEQEEKTDKWHRVERSSGKFLRRFRLPENTKPEQIKASMENGVLTVTVPKEEPKKPDVKSIQITG
Protein: Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) (P20536)
Organism: Vaccinia virus (strain Copenhagen) (VACV)
Function: Plays an essential role in viral replication as a component of the DNA polymerase processivity factor. Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Interaction partners:
Sequence:
MNSVTVSHAPYTITYHDDWEPVMSQLVEFYNEVASWLLRDETSPIPDKFFIQLKQPLRNKRVCVCGIDPYPKDGTGVPFESPNFTKKSIKEIASSISRLTGVIDYKGYNLNIIDGVIPWNYYLSCKLGETKSHAIYWDKISKLLLQHITKHVSVLYCLGKTDFSNIRAKLESPVTTIVGYHPAARDRQFEKDRSFEIINVLLELDNKVPINWAQGFIY
Protein: Pleckstrin homology domain containing, family A member 5 (A0A1L1SQF5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKENEPIITMVHTMIENSALRPQLYQQMAVGLLFLRQKNKISLYCLSQDECRGTLYKYRPEEAGIDAKLSRLCEQDKVVRALEEKLQQLHKEKYTLEQALLSASQEIEMNADNPAAIQTVVLQRDDLQNGLLSTCRELSRATAELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQSESAGIQRAQIQKELWRIQDVMEGLSKHKQQRGSSETGLAGSKPFSSVKYKSEEEEVVPPRPPLPRSYDFTEQPPIIPPLPSDSSSLLCYSRGPVHLPEDKKIHQVQGYPRNGSHCGPDYRLYKSEPELTTVAEVDESNGEEKSEPVSETEAPVVKGSHFPVGVPLRTKSPTPESSTIASYVTLRKTKKMVELRTERPRSAVEQLCLAESARPRMTVEEQLERIRRHQQACLREKKKGLSVLGASDPSDVRDSPLRLTQTLRRDDNVKELDTVHRENDVKPDYETPAAQCAHLEDAEPQNADIGRKLKRSEMLYTPEPNGMASEEVTEKERQKEQVHADGSCSPQEETAMTEHQMEGPPEEAESLHEEEETLASCEPAPEIPRENQTTVRSLSPSPDSSTAADPPTPPQLREGSHFMCV
Protein: Light-regulated protein, chloroplastic (Q03200)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Thylakoid-determinant subunit of high molecular weight LFNRs-containing protein complexes.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:26941088}; Peripheral membrane protein {ECO:0000269|PubMed:26941088}; Stromal side {ECO:0000269|PubMed:26941088}. Plastid, chloroplast envelope {ECO:0000269|PubMed:26941088}. Plastid, chloroplast stroma {ECO:0000269|PubMed:26941088}.
Interaction partners:
- Protein TIC 62, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic
Sequence:
MQTAASSVVGLSAVLPAAVKGRSLQIQAPRRVALRVRAAAAAVAVEAAEVDYSSNISVFPMEACDLIGGEACNVQMYPEAKLSSSAAVAVSRAAAEEVDRDYLSYDEPTTVFPEEACDDLGGEFCKAT