wanglab/gogpt-training-data huggingface dataset:
Protein: SI:bY184L24.2.2 (Transcription factor spi1) (Spi-1 proto-oncogene b) (Transcription factor PU.1b isoform 3) (Q8AW41)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MLHPYRMEGYIIPPQTEEMFETEIYRPPMEYQYIIDDSQNDHSWDYNTHHIHPVDFENLPESHFTELQSVQSLHAASVHRFPDVESSHFMDPGLGSHHIPLTNPQMTYLPRTSVCYPHNVQPSPLQRSSDEEDPSSRSPPLEVSDEECMRDHISSTTGGEHGNKKKIRLYQFLLDLLRNGDMKDSIWWVDREKGTFQFSSKHKEVLANRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKIKKKLTYQFSGEVLGKSHTDRKHYM
Protein: UPF0690 protein C1orf52 (BCL10-associated gene protein) (Q8N6N3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAEEKDPLSYFAAYGSSSSGSSDEEDNIEPEETSRRTPDPAKSAGGCRNKAEKRLPGPDELFRSVTRPAFLYNPLNKQIDWERHVVKAPEEPPKEFKIWKSNYVPPPETYTTEKKPPPPELDMAIKWSNIYEDNGDDAPQNAKKARLLPEGEETLESDDEKDEHTSKKRKVEPGEPAKKKK
Protein: Uncharacterized protein (Q386V7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSECVTVKVKLGGAALPAHDLMQLERRLIGARSLMQATEKTLKETVVVVSPNLRKDGDERRDHILNDGMVSKHTQLSWYIVEDVLAVYYRLSTLIEEEERQARIRVERFHSSTINQMRRRHNADHLSSAKCVYERSCVEEDAHWALKLVAQEHSDYLFSIKILEEDERQDIARRVGLPMQNSTPLLGWSRTPNTVWQQPELAPWWDHLEGPAGYFWGVSPSGGVEMPQWSHVHWGDNPASGGFQCVPGEWCHRSNLQ
Protein: Cadherin-11 (OSF-4) (Osteoblast cadherin) (OB-cadherin) (P55287)
Organism: Homo sapiens (Human)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Required for proper focal adhesion assembly. Involved in the regulation of cell migration.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin beta-1
- Cadherin-2
- Catenin delta-1
- Catenin alpha-1
- Junction plakoglobin
- Cadherin-3
- Cadherin-15
- Cadherin-1
- Cadherin-13
- Cadherin-20
Sequence:
MKENYCLQAALVCLGMLCHSHAFAPERRGHLRPSFHGHHEKGKEGQVLQRSKRGWVWNQFFVIEEYTGPDPVLVGRLHSDIDSGDGNIKYILSGEGAGTIFVIDDKSGNIHATKTLDREERAQYTLMAQAVDRDTNRPLEPPSEFIVKVQDINDNPPEFLHETYHANVPERSNVGTSVIQVTASDADDPTYGNSAKLVYSILEGQPYFSVEAQTGIIRTALPNMDREAKEEYHVVIQAKDMGGHMGGLSGTTKVTITLTDVNDNPPKFPQSVYQMSVSEAAVPGEEVGRVKAKDPDIGENGLVTYNIVDGDGMESFEITTDYETQEGVIKLKKPVDFETKRAYSLKVEAANVHIDPKFISNGPFKDTVTVKISVEDADEPPMFLAPSYIHEVQENAAAGTVVGRVHAKDPDAANSPIRYSIDRHTDLDRFFTINPEDGFIKTTKPLDREETAWLNITVFAAEIHNRHQEAKVPVAIRVLDVNDNAPKFAAPYEGFICESDQTKPLSNQPIVTISADDKDDTANGPRFIFSLPPEIIHNPNFTVRDNRDNTAGVYARRGGFSRQKQDLYLLPIVISDGGIPPMSSTNTLTIKVCGCDVNGALLSCNAEAYILNAGLSTGALIAILACIVILLVIVVLFVTLRRQKKEPLIVFEEEDVRENIITYDDEGGGEEDTEAFDIATLQNPDGINGFIPRKDIKPEYQYMPRPGLRPAPNSVDVDDFINTRIQEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESATTDSDLDYDYLQNWGPRFKKLADLYGSKDTFDDDS
Protein: V-type proton ATPase subunit E (V-ATPase subunit E) (Vacuolar proton pump subunit E) (O00780)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
Interaction partners:
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase subunit B
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d
- V-type proton ATPase subunit C
- V-type proton ATPase catalytic subunit A
Sequence:
MDDTQVNAQLDQMKNFILQEAQDKANEIKTKATQEFTSEKGRIFQNEKIKIIKEYEKKQKLIEVQKKINLSNELNKSRLSVLKVREECLRDVIKEAQKKLATISDDKDKYQTILKNLIYQGFVKLNENKIQVVGRKEDAGLLEKATTEAAAQYKKNVGKSIDVSVDKERFLPQGPKSDYNGPTCCGGVILSALEGRIICKNTLDSRLEICFDQLTPVIRTQLYGASTSRKFFD
Protein: Glia-derived nexin (GDN) (Peptidase inhibitor 7) (PI-7) (Protease nexin 1) (PN-1) (Protease nexin I) (Serine protease-inhibitor 4) (Serpin E2) (Q07235)
Organism: Mus musculus (Mouse)
Function: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Urokinase-type plasminogen activator
- Tissue-type plasminogen activator
- Prothrombin
- Vitronectin
- Urokinase plasminogen activator surface receptor
- Plasminogen
- Vacuolar protein sorting-associated protein 29
- Prolow-density lipoprotein receptor-related protein 1
- Fibronectin
- Coagulation factor V
Sequence:
MNWHFPFFILTTVTLYSVHSQFNSLSLEELGSNTGIQVFNQIIKSRPHENVVVSPHGIASILGMLQLGADGKTKKQLSTVMRYNVNGVGKVLKKINKAIVSKKNKDIVTVANAVFLRNGFKMEVPFAVRNKDVFQCEVQNVNFQDPASASESINFWVKNETRGMIDNLLSPNLIDGALTRLVLVNAVYFKGLWKSRFQPESTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTRTPNGLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHITTKTIDSWMNTMVPKRMQLVLPKFTAVAQTDLKEPLKALGITEMFEPSKANFTKITRSESLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFSIRHNPTGAILFLGQVNKP
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (Q4U0S6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU367045}.
Interaction partners:
Sequence:
MAGRQMQAARCPTDELSLTNCVVASEKDFKSGQHLTIKTTPTQKFVFTVRTHPSVVPGTIAFSLPQRKWAGLSLNQDVEVSVYNFDPSRQYVGTMTIEIDFLQKKSIDSNPYDSDKMAIEFIQCFTAQAFSMSQQFVFSFCDKLFALVIKDIEAMDPSILRGEQNSSKKHKIDIGLLHGNSQVIFEKAESSSVNLIGKAKTKGSRQSIINPDWNFERMGIGGLDKEFSDIFRRAFASRVFPPDIVEQMGCKHVKGILLFGPPGCGKTLMARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFADAEEEQKRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDETGRVQILNIHTAKMKQSNMLAKDVDVKELAVETKNYSGAELEGLVRAAQSTAMNRHIKATTQVEVDTEKAQTLQVSRSDFLASLNNDIKPAFGSNQEDYSSYIMNGIVKWSNAVSDILGDGELLVQQTKNSERTPLVTVLLEGPAHSGKTALAAKIAEQSQFPFIKICSPDKMIGFTETAKCQAIKKIFEDAYKSQLSCVVVDDIERLLDFVPIGPRFSNLVLQALLVLLKKPPPRGRKLLILGTTSRKDVLQEMGMSDSFSTTIHIPNISRGEHLMEALELLGGFQEEERANIGKQVKGQSVWLGIKKLQMLIEMSLQMPLEYRVQKFLALLKEEGALGPDKHVAF
Protein: Transmembrane protein 242 (Q9NWH2)
Organism: Homo sapiens (Human)
Function: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC3. Participates in the incorporation of the c-ring into vestigial complexes. Additionally influences the incorporation of subunits MT-ATP6, MT-ATP8, ATP5MJ, and ATP5MK in the ATP synthase.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:33753518}; Multi-pass membrane protein {ECO:0000269|PubMed:33753518}.
Interaction partners:
- Transmembrane protein 70
Sequence:
METAGAATGQPASGLEAPGSTNDRLFLVKGGIFLGTVAAAGMLAGFITTLSLAKKKSPEWFNKGSMATAALPESGSSLALRALGWGSLYAWCGVGVISFAVWKALGVHSMNDFRSKMQSIFPTIPKNSESAVEWEETLKSK
Protein: GATOR1 complex protein NPRL3 (Nitrogen permease regulator 3-like protein) (Q8VIJ8)
Organism: Mus musculus (Mouse)
Function: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway.
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q12980}. Note=Localization to lysosomes is mediated by the KICSTOR complex and is amino acid-independent. {ECO:0000250|UniProtKB:Q12980}.
Interaction partners:
- GATOR1 complex protein NPRL2
- GATOR1 complex protein DEPDC5
- GATOR2 complex protein WDR59
- GATOR2 complex protein WDR24
- GATOR2 complex protein MIOS
- Ras-related GTP-binding protein C
- Nucleoporin SEH1
- KICSTOR complex protein SZT2
- Ras-related GTP-binding protein B
- Ras-related GTP-binding protein A
Sequence:
MGDNTSPISVILVSSGSRGNKLLFRYPFQRSQEHPASQTNKPRSRYAVNNTGEHADDQDGDSRFSDVILATILATKSEMCGQKFELKIDNVRFVGHPTLLQHALGQVSKTDPSPKREAPTMILFNVVFALRANADPSVINCLHNLSRRIATVLQHEERRCQYLTREAKLILALQDEVSAMADANEGPQSPFQHILPKCKLARDLKEAYDSLCTSGVVRLHINSWLEVSFCLPHKIHYAASSLIPPEAIERSLKAIRPYHALLLLSDEKSLLSELPIDCSPALVRVIKTTSAVKNLQQLAQDADLALLQVFQLAAHLVYWGKAVIIYPLCENNVYVMSPNASVCLYSPLAEQFSRQFPSHDLPSVLAKFSLPVSLSEFRSPLAPPAQETQLIQMVVWMLQRRLLIQLHTYVCLMASPSEEEPRLREDDVPFTARVGGRSLSTPNALSFGSPTSSDDMTLTSPSMDNSSAELLPSGDSPLNKRMTENLLASLSEHERAAILNVPAAQNPEDLRMFARLLHYFRGRHHLEEIMYNENTRRSQLLMLFDKFRSVLVVTTHEDPVIAVFQALLT
Protein: Protein PopA1 [Cleaved into: Protein PopA2; Protein PopA3] (Q9RBS0)
Organism: Ralstonia nicotianae (strain ATCC BAA-1114 / GMI1000) (Ralstonia solanacearum)
Function: Acts as a specific hypersensitive response (HR) elicitor. Has activity on tobacco (non-host plant) and petunia but is without activity on tomato (host plant); PopA3 seems to be more active than a PopA1-PopA2 mixture.
Subcellular location: Secreted {ECO:0000269|PubMed:10430949, ECO:0000269|PubMed:8313899}. Note=Probably secreted via a type III secretion system (T3SS). {ECO:0000269|PubMed:10430949, ECO:0000269|PubMed:8313899}.
Interaction partners:
Sequence:
MSVGNIQSPSNLPGLQNLNLNTNTNSQQSGQSVQDLIKQVEKDILNIIAALVQKAAQSAGGNTGNTGNAPAKDGNANAGANDPSKNDPSKSQGPQSANKTGNVDDANNQDPMQALMQLLEDLVKLLKAALHMQQPGGNDKGNGVGGANGAKGAGGQGGLAEALQEIEQILAQLGGGGAGAGGAGGGVGGAGGADGGSGAGGAGGANGADGGNGVNGNQANGPQNAGDVNGANGADDGSEDQGGLTGVLQKLMKILNALVQMMQQGGLGGGNQAQGGSKGAGNASPASGANPGANQPGSADDQSSGQNNLQSQIMDVVKEVVQILQQMLAAQNGGSQQSTSTQPM
Protein: Acyl-coenzyme A oxidase (Acyl-CoA oxidase) (EC 1.3.3.6) (P13711)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Peroxisome.
Interaction partners:
- Peroxisomal hydratase-dehydrogenase-epimerase
- 3-ketoacyl-CoA thiolase, peroxisomal
- Acetyl-coenzyme A synthetase 1
- Long-chain-fatty-acid--CoA ligase 2
- Potassium-activated aldehyde dehydrogenase, mitochondrial
- Magnesium-activated aldehyde dehydrogenase, cytosolic
- Acetyl-CoA acetyltransferase
- Acetyl-coenzyme A synthetase 2
- Aldehyde dehydrogenase [NAD
- Peroxisomal targeting signal receptor
Sequence:
MTRRTTINPDSVVLNPQKFIQKERADSKIKVDQVNTFLESSPERRTLTHALIDQIVNDPILKTDTDYYDAKKMQEREITAKKIARLASYMEHDIKTVRKHFRDTDLMKELQANDPDKASPLTNKDLFIFDKRLSLVANIDPQLGTRVGVHLGLFGNCIKGNGTDEQIRYWLQERGATLMKGIYGCFAMTELGHGSNVAQLQTRAVYDKQNDTFVIDTPDLTATKWWIGGAAHSATHAAVYARLIVEGKDYGVKTFVVPLRDPSTFQLLAGVSIGDIGAKMGRDGIDNGWIQFRNVVIPREFMLSRFTKVVRSPDGSVTVKTEPQLDQISGYSALLSGRVNMVMDSFRFGSKFATIAVRYAVGRQQFAPRKGLSETQLIDYPLHQYRVLPQLCVPYLVSPVAFKLMDNYYSTLDELYNASSSAYKAALVTVSKKLKNLFIDSASLKATNTWLIATLIDELRQTCGGHGYSQYNGFGKGYDDWVVQCTWEGDNNVLSLTSAKSILKKFIDSATKGRFDNTLDVDSFSYLKPQYIGSVVSGEIKSGLKELGDYTEIWSITLIKLLAHIGTLVEKSRSIDSVSKLLVLVSKFHALRCMLKTYYDKLNSRDSHISDEITKESMWNVYKLFSLYFIDKHSGEFQQFKIFTPDQISKVVQPQLLALLPIVRKDCIGLTDSFELPDAMLNSPIGYFDGDIYHNYFNEVCRNNPVEADGAGKPSYHALLSSMLGRGFEFDQKLGGAANAEILSKINK
Protein: Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnE (L-Ara4N-phosphoundecaprenol flippase subunit ArnE) (Undecaprenyl phosphate-aminoarabinose flippase subunit ArnE) (Q47377)
Organism: Escherichia coli (strain K12)
Function: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD
- Bifunctional polymyxin resistance protein ArnA
- Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
- UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase aminotransferase)
- UDP-glucose 6-dehydrogenase
Sequence:
MIWLTLVFASLLSVAGQLCQKQATCFVAINKRRKHIVLWLGLALACLGLAMVLWLLVLQNVPVGIAYPMLSLNFVWVTLAAVKLWHEPVSPRHWCGVAFIIGGIVILGSTV
Protein: Poly(rC) binding protein 2 (H3BSS4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XLESPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSAGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS
Protein: Complement component C8 alpha chain (Complement component 8 subunit alpha) (P07357)
Organism: Homo sapiens (Human)
Function: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C8A inserts into the target membrane, but does not form pores by itself.
Subcellular location: Secreted. Cell membrane; Multi-pass membrane protein. Note=Secreted as soluble protein. Inserts into the cell membrane of target cells.
Interaction partners:
- Complement component C8 beta chain
- Complement component C8 gamma chain
- Complement C5
- Complement component C9
- Complement component C6
- Complement component C7
- Complement C4-A
- Non-selective voltage-gated ion channel VDAC1
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Mitochondrial inner membrane m-AAA protease component paraplegin
Sequence:
MFAVVFFILSLMTCQPGVTAQEKVNQRVRRAATPAAVTCQLSNWSEWTDCFPCQDKKYRHRSLLQPNKFGGTICSGDIWDQASCSSSTTCVRQAQCGQDFQCKETGRCLKRHLVCNGDQDCLDGSDEDDCEDVRAIDEDCSQYEPIPGSQKAALGYNILTQEDAQSVYDASYYGGQCETVYNGEWRELRYDSTCERLYYGDDEKYFRKPYNFLKYHFEALADTGISSEFYDNANDLLSKVKKDKSDSFGVTIGIGPAGSPLLVGVGVSHSQDTSFLNELNKYNEKKFIFTRIFTKVQTAHFKMRKDDIMLDEGMLQSLMELPDQYNYGMYAKFINDYGTHYITSGSMGGIYEYILVIDKAKMESLGITSRDITTCFGGSLGIQYEDKINVGGGLSGDHCKKFGGGKTERARKAMAVEDIISRVRGGSSGWSGGLAQNRSTITYRSWGRSLKYNPVVIDFEMQPIHEVLRHTSLGPLEAKRQNLRRALDQYLMEFNACRCGPCFNNGVPILEGTSCRCQCRLGSLGAACEQTQTEGAKADGSWSCWSSWSVCRAGIQERRRECDNPAPQNGGASCPGRKVQTQAC
Protein: Migration and invasion enhancer 1 (Q9CQ86)
Organism: Mus musculus (Mouse)
Function: Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17503775}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Concentrates at the leading edge of migrating cells. Localizes outside membrane raft regions (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MSGEPAPVSVVPPPGEVEAGSGVHIVVEYCKPCGFEATYLELASAVKEEYPGIEIESRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLMEAIRRASNGEPVEKITNSRPPCVIL
Protein: Zinc finger protein 486 (KRAB domain only protein 2) (Q96H40)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MPGPLRSLEMESLQFRDVAVEFSLEEWHCLDTAQQNLYRDVMLENYRHLVFLGIIVSKPDLITCLEQGIKPLTMKRHEMIAKPPVVCSHFAQDLWPEQSIKDSYQKVILRKFEKCGHGNLHFKKGCESVDECKLHKRGYNGLNQCLTTTQSKIFQCGKYVKVFHQFSNSKRHKRRHTEKKPLKYIEGDKAFNQSSTHTTHKKIDTGEKPYKCEECGKAFNRSSHLTTHKITHTREKPYKCEECGKVFKYFSSFTTHKKIHSGEKPYICEECGKAFMYPYTLTTHKIIHTGEQPYKCKECDKAFNHPATLSSHKKIHTGEKPYTCDKCGKAFISSSILSKHEKIHTGEKPYKCEECGKAFTRSSHLTMHKIIHTGEKPYKCEECGKAFTWSAGLHKHRRTHTGEKPYKCEECGKAYTTSSNLTEHKTTHTGEKPYKCKECGKAFNWSSDLNKHKRIHIGQKPRT
Protein: Major urinary protein (MUP) (Allergen Rat n I) (Alpha(2)-euglobulin) (Alpha-2u-globulin) (alpha-2u globulin PGCL1) (allergen Rat n 1) [Cleaved into: 15.5 kDa fatty acid-binding protein (15.5 kDa FABP)] (P02761)
Organism: Rattus norvegicus (Rat)
Function: Major urinary proteins (Mups) bind and release pheromones. They may also protect pheromones from oxidation. In this context, they play a role in the regulation of social behaviors, such as aggression, mating, pup-suckling, territory establishment and dominance. Acts as a kairomone, detected by the prey vomeronasal organ and inducing fear reactions in mice.
Subcellular location: [15.5 kDa fatty acid-binding protein]: Cytoplasm, cytosol. Note=It is probably taken up from the urinary lumen by endocytosis.; SUBCELLULAR LOCATION: Secreted.
Interaction partners:
Sequence:
MKLLLLLLCLGLTLVCGHAEEASSTRGNLDVAKLNGDWFSIVVASNKREKIEENGSMRVFMQHIDVLENSLGFKFRIKENGECRELYLVAYKTPEDGEYFVEYDGGNTFTILKTDYDRYVMFHLINFKNGETFQLMVLYGRTKDLSSDIKEKFAKLCEAHGITRDNIIDLTKTDRCLQARG
Protein: Sodium bicarbonate cotransporter 3 (Solute carrier family 4 member 7) (Q8BTY2)
Organism: Mus musculus (Mouse)
Function: Electroneutral sodium- and bicarbonate-dependent cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry. Mediates the sodium-dependent bicarbonate transport important for pH recovery after acid load as well as for regulation of steady-state pH in the duodenum and vascular smooth muscle cells. Plays a key role in macrophage acidification, mediating bicarbonate import into the cytoplasm which is crucial for net acid extrusion and maintenance of cytoplasmic pH during phagocytosis (By similarity). Provides cellular bicarbonate for de novo purine and pyrimidine synthesis and is a key mediator of de novo nucleotide synthesis downstream of mTORC1 signaling in proliferating cells (By similarity). May be involved in maintaining locomotor activity, exploratory behavior, and hearing.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:22586225, ECO:0000269|PubMed:23401617}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9R1N3}; Multi-pass membrane protein {ECO:0000255}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q9R1N3}. Cell membrane {ECO:0000269|PubMed:16439691}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the stereocilia of cochlear outer hair cells and to the lateral membrane of cochlear inner hair cells (By similarity). {ECO:0000250|UniProtKB:Q9R1N3}.
Interaction partners:
- Carbonic anhydrase 2
- Sodium/hydrogen exchanger 1
- Solute carrier family 12 member 2
Sequence:
MEADGAGEQMRPLLTRGPDEEAVVDLGKTSSTVNTKFEKEELESHRAVYVGVHVPFSKESRRRHKHRGHKHHHRRRKDKDSDKEDGRESPSYDTPSQRVQFILGTEDDDEEHIPHDLFTEMDELCYRDGEEYEWKETARWLKFEEDVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRASTLDEIADMVLDNMIASGQLDDSIRENVREALLKRHHHQNEKRFTSRIPLVRSFADIGILASPQSAPGNLDNSKSGEMKGNGSGGSRENSTVDFSKVDMNFMRKIPTGAEASNVLVGEVDFLERPIIAFVRLAPAVLLSGLTEVPVPTRFLFLLLGPAGKAPQYHEIGRSIATLMTDEIFHDVAYKAKDRNDLLSGIDEFLDQVTVLPPGEWDPSIRIEPPKSVPSQEKRKIPVFPNGSAAMSVGPPKEDDHHAGPELQRTGRLFGGLILDIKRKAPFFLSDFKDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESLFGASLTGIAYSLFAGQPLTILGSTGPVLVFEKILFKFCRDYHLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYITRFTEEAFAALICIIFIYEALEKLFHLGEIYAFNMHNNLDELTSYTCVCAEPSNPSNETLELWKRKNITAYSVSWGNLTVSECKTFHGMFVGSACGPHGPYVPDVLFWCVVLFFTTFFLSSFLKQFKTKGYFPTKVRSTISDFAVFLTIVIMVAIDYLVGIPSPKLHVPEKFEPTDPSRGWIISPLGDNPWWTLLIAAVPALLCTILIFMDQQITAVIINRKEHKLKFIPMPVLYGVFLYMGVSSLKGIQFFDRIKLFGMPAKHQPDLIYLRYVPLWKVHVFTVVQLTCLVLLWVIKASAAAVVFPMMVLALVFVRKLMDLCFTKRELSWLDDLMPESKKKKEDDKKKKEKEEAERMLQDDEDTVHLPFERGSLLQIPVKTLKYSIDPSVVNISDEMAKTAQWKALSMNTENAKVTRPNTSPEKPVSVTINFEDEPSKKYMDAETSL
Protein: Calpastatin (Calpain inhibitor) (P12675)
Organism: Sus scrofa (Pig)
Function: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
Interaction partners:
- Calpain-1 catalytic subunit
- Calpain-2 catalytic subunit
- Calpain small subunit 1
- Calpain-3
- Calpain 11
- Calpain 8
- Calpain-5
- Calpain-12
- Calpain 10
- Calpain-7
Sequence:
MNPTETKAIPVSKQLEGPHSPNKKRHKKQAVKTEPEKKSQSTKPSVVHEKKTQEVKPKEHPEPKSLPTHSADAGSKRAHKEKAVSRSNEQPTSEKSTKPKAKPQDPTPSDGKLSVTGVSAASGKPAETKKDDKSLTSSVPAESKSSKPSGKSDMDAALDDLIDTLGGPEETEEDNTTYTGPEVLDPMSSTYIEELGKREVTLPPKYRELLDKKEGIPVPPPDTSKPLGPDDAIDALSLDLTCSSPTADGKKTEKEKSTGEVLKAQSVGVIKSAAAPPHEKKRRVEEDTMSDQALEALSASLGSRKSEPELDLSSIKEIDEAKAKEEKLKKCGEDDETVPPEYRLKPAMDKDGKPLLPEAEEKPKPLSESELIDELSEDFDQSKRKEKQSKPTEKTKESQATAPTPVGEAVSRTSLCCVQSAPPKPATGMVPDDAVEALAGSLGKKEADPEDGKPVEDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKTLPHKDPKEPVLPLSEDFVLDALSQDFAGPPAASSLFEDAKLSAAVSEVVSQTSAPTTHSAGPPPDTVSDDKKLDDALDQLSDSLGQRQPDPDENKPIEDKVKEKAEAEHRDKLGERDDTIPPEYRHLLDKDEEGKSTKPPTKKPEAPKKPEAAQDPIDALSGDFDRCPSTTETSENTTKDKDKKTASKSKAPKNGGKAKDSTKAKEETSKQKSDGKSTS
Protein: Peroxin 3-1 (F4J7K3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDLVRCVLNSDLLMYSFLSLLVSSSVGKHRRKILVTTTCLGSGYLLYKLYNAHTRKLADLERELANERENDEIIKTQMKAHFDNIQMIADTTTLPHAIHHLSSRVVEEIDVSSIMDKLSKGKGILIPSEKLQLWNELKILSFTRMVLSLWSVTMLSLYIRVQVNILGRHLYIDTARGLGSSHLLDELDLIERDDEQKFLTSADFLATSGMPSLISNMQNAVKEVLKGKQLKDVLTTSALRETVMRILDVFMSTGSPHHWVDYLMMSQDATTDVSSSDATVTKFHLLITETREVLTSNDFSNVAEISLKCCAVALVEEMETQTGLATGMQLAKLLPQIEKTMPEISAEPEKNRFLQLIRDLPEVKLFFTLLYANMPQ
Protein: Homeobox protein DLX-1 (Q64317)
Organism: Mus musculus (Mouse)
Function: Plays a role as a transcriptional activator or repressor. Inhibits several cytokine signaling pathways, such as TGFB1, activin-A/INHBA and BMP4 by interfering with the transcriptional stimulatory activity of transcription factors, such as MSX2, FAST2, SMAD2 and SMAD3 during hematopoietic cell differentiation (By similarity). Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina. Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis and may be involved in the early development of diencephalic subdivisions.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P56177}.
Interaction partners:
- Homeobox protein DLX-2
- LIM/homeobox protein Lhx6
- Achaete-scute homolog 1
- Sonic hedgehog protein
- Forkhead box protein G1
- Glutamate decarboxylase 1
- T-box brain protein 1
- LIM/homeobox protein Lhx8
Sequence:
MTMTTMPESLNSPVSGKAVFMEFGPPNQQMSPSPMSHGHYSMHCLHSAGHSQPDGAYSSASSFSRPLGYPYVNSVSSHASSPYISSVQSYPGSASLAQSRLEDPGADSEKSTVVEGGEVRFNGKGKKIRKPRTIYSSLQLQALNRRFQQTQYLALPERAELAASLGLTQTQVKIWFQNKRSKFKKLMKQGGAALEGSALANGRALSAGSPPVPPGWNPNSSSGKGSGSSAGSYVPSYTSWYPSAHQEAMQQPQLM
Protein: Macoilin (P91193)
Organism: Caenorhabditis elegans
Function: Plays a role in the regulation of neuronal activity. In AWA and AWC neurons, plays a role in regulating olfactory adaptation by controlling the forgetting sensory responses to odorants such as diacetyl and isoamyl alcohol. May play a role in regulating daf-7 expression in ASI neurons in response to bacterial small RNAs. In ASI neurons, promotes dauer formation in response to pheromones such as the ascarosides ascr#2 and ascr#3.
Subcellular location: Rough endoplasmic reticulum membrane {ECO:0000269|PubMed:21437263, ECO:0000269|PubMed:21589894}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:21437263}; Multi-pass membrane protein {ECO:0000255}. Note=Restricted to neuronal cell bodies, absent from dendrites and axons (PubMed:21437263). {ECO:0000269|PubMed:21437263}.
Interaction partners:
- Alpha-2-macroglobulin RAP C-terminal domain-containing protein)
- CTLH domain-containing protein
- Protein CNPPD1
- DUF5523 domain-containing protein
- Williams-Beuren syndrome chromosomal region 16 protein
- Small integral membrane protein 14
Sequence:
MMQQQKPGKPKKINRIDKIKRLQINRSRRPDINQTVPSPLFYVRIVVTWLGMVSLDAMTGFRFELLWPTWLMIRAAAESIQMRNQHCVTTIANPTAARFSVLFICVTATSDLICYLFIPIRMLIFLATTYVWISLYYHTQGGFLRSLATVYGGERLQSWPIVFITCFIVIFELFLRIRSHPILISFFPNVAEYAGVSPVWPRSLNAFFGAHSIGYPVILITVSMHYYFNEWKLRRKQCDVSNRNEQLFRILVEGLPAEYEGPKDYTSQQCLEDDLYYLDPPVQTLQPMQAIQAASATPPTSSKKNGIHKRNGDVTSSTTTSSRKKKHNGNSGFNSTPPNDKKKGKSIRDVDMDDGDDSDDDYSYRDTSSSTIEDQRRGGGISIIRFIFSSAAWLFSFVFESSTPSENSLSNQQIDDDEDYEDGDGDKKNGRTDSMTSTTKGRANTMPSTTRSQNNNNSQKQQKQSNGKSHHQHSSHQNNHQKSNGNSNGHARGFAAVRDSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEFQIKNGSSIGGGSSETLMNGRSSTEANNENDTTASDQSSPHQHSAMGSPVPFAKMPLSVNVSNRHGSPFNGKVSPIASIGSVLAAAGGPAPPDYMMAVGANVTATTGPVPQKQPRAGFHGISRYNEFTNIASGGEHRLFDTPASAISASAINGSNPEDDFLMNKGKFGAPSQPAARLA
Protein: Lymphocyte antigen 6D (Ly-6D) (Thymocyte B-cell antigen) (ThB) (P35459)
Organism: Mus musculus (Mouse)
Function: May act as a specification marker at earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
Sequence:
MKTALLVLLVLAVATSPAWALRCHVCTNSANCKNPQVCPSNFYFCKTVTSVEPLNGNLVRKECANSCTSDYSQQGHVSSGSEVTQCCQTDLCNERLVSAAPGHALLSSVTLGLATSLSLLTVMALCL