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Q8BJL0

- SMAL1_MOUSE

UniProt

Q8BJL0 - SMAL1_MOUSE

Protein

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1

Gene

Smarcal1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi417 – 4248ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. annealing helicase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. DNA binding Source: InterPro
    4. DNA-dependent ATPase activity Source: UniProtKB
    5. helicase activity Source: UniProtKB-KW

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. chromatin modification Source: InterPro
    4. DNA metabolic process Source: UniProtKB
    5. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    6. replication fork processing Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (EC:3.6.4.-)
    Alternative name(s):
    HepA-related protein
    Short name:
    mharp
    Sucrose nonfermenting protein 2-like 1
    Gene namesi
    Name:Smarcal1
    Synonyms:Harp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1859183. Smarcal1.

    Subcellular locationi

    Nucleus By similarity
    Note: Recruited to damaged DNA regions.By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB
    2. site of double-strand break Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 910909SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1PRO_0000074349Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity

    Post-translational modificationi

    DNA damage-regulated phosphorylation by kinases that may include ATM, ATR and PRKDC.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ8BJL0.
    PRIDEiQ8BJL0.

    PTM databases

    PhosphoSiteiQ8BJL0.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with high levels in brain, heart, kidney, liver and testis.1 Publication

    Gene expression databases

    BgeeiQ8BJL0.
    GenevestigatoriQ8BJL0.

    Interactioni

    Subunit structurei

    Interacts with RPA2; the interaction is direct and mediates the recruitment by the RPA complex of SMARCAL1 to sites of DNA damage.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000047589.

    Structurei

    Secondary structure

    1
    910
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi203 – 2108
    Beta strandi213 – 2186
    Helixi222 – 2309
    Beta strandi235 – 2373
    Turni238 – 2414
    Beta strandi242 – 2465
    Helixi247 – 2493
    Helixi250 – 2578
    Beta strandi263 – 2664

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4O66X-ray1.90A/B/C/D197-268[»]
    ProteinModelPortaliQ8BJL0.
    SMRiQ8BJL0. Positions 393-807.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini199 – 26971HARP 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini286 – 35772HARP 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini404 – 559156Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini674 – 827154Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 2928Mediates interaction with RPA2By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili3 – 3432Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi508 – 5114DESH box

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family. SMARCAL1 subfamily.PROSITE-ProRule annotation
    Contains 2 HARP domains.PROSITE-ProRule annotation
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00630000089754.
    HOVERGENiHBG054110.
    InParanoidiQ3TEQ9.
    KOiK14440.
    OMAiSIHYLVA.
    OrthoDBiEOG7XSTD5.
    PhylomeDBiQ8BJL0.
    TreeFamiTF106474.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR010003. HARP_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF07443. HARP. 2 hits.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51467. HARP. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BJL0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSLPLTEEQR KKIEENRQKA LARRAEKLSE QPQSAASGSS AAGPSQSKQG    50
    SLLNLLAEPS KPVGHASIFK QQNLSNSFPT DQRPHSSRCS QPSPAEETTG 100
    LWKTQGEMST ACPKPNPSPP GASNQPLLGY KSSEGQPQAT WDTGASSSGP 150
    FPRDPELEAK AARPSTSRQS ISDSFYVLGG KTPRTEGRPP NILQTTPQNT 200
    GFLRGACIKT GDRFRVKIGY NQELIAVFKS LPSRHYDSFT KTWDFSMSDY 250
    RALMKAVERL STVSLKPLDE AGGSVGGQTS LPSAPSLTFV TGKCMLISRV 300
    RFEVDIGYSE AVIGLFKQME SRSYDIKTRK WSFLLEEHNK LIARSRELKQ 350
    VQLDPLPKTV TLAFASQLEK TSPKLKADVP EADLSGVDAK LVSSLMPFQR 400
    EGVSFAISKR GRLLLADDMG LGKTVQAICI AAFYRKEWPL LVVVPSSVRF 450
    TWEQAFLRWL PSLSPENINV VVTGKGRLTA GLVNIVSFDL LCKLERQLKT 500
    PFKVVIIDES HFLKNIKTAR CRAAVPILKV AKRVILLSGT PAMSRPAELY 550
    TQIIAVKPTF FPQFHAFGLR YCDAKRLPWG WDYSGSSNLG ELKLLLEEAI 600
    MLRRLKSDVL SQLPAKQRKM VVVNPGRISS RAKAALDAAA KEMTKDKTKQ 650
    QQKEALLVFF NRTAEAKIPC VVEYILDLLD SGREKFLVFA HHKVILDAVA 700
    KELERKNVQH IRIDGSTPSA DREAQCQRFQ LSKGHTVALL SITAANMGLT 750
    FSTADLVVFA ELFWNPGVLI QAEDRVHRIG QTNSVSIHYL VAKGTADDYL 800
    WPLIQEKIKV LGEAGLSETN FSEMTEATDY VHKDPKQKTI YDLFQQSFED 850
    DGNDMEFLEA AESFELGSTS GTSGNISQDL GDLLDEDEGS PPKKSRFEFF 900
    DNWDSFSSPF 910
    Length:910
    Mass (Da):100,840
    Last modified:March 1, 2003 - v1
    Checksum:iF6B28F847BD6FC18
    GO
    Isoform 2 (identifier: Q8BJL0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         769-788: LIQAEDRVHRIGQTNSVSIH → GNVARVPLGMPRAEKYKIRK
         789-910: Missing.

    Note: May be due to an intron retention.

    Show »
    Length:788
    Mass (Da):87,126
    Checksum:iAE70BAB0A799A3F8
    GO
    Isoform 3 (identifier: Q8BJL0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         508-574: DESHFLKNIK...HAFGLRYCDA → VSNGIALKYF...QPLSLCARLS
         575-910: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:574
    Mass (Da):63,218
    Checksum:i0E8930A229E115E8
    GO
    Isoform 4 (identifier: Q8BJL0-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         404-404: S → R
         405-910: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:404
    Mass (Da):44,190
    Checksum:i92E5249A242D75A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351A → T in AAH29078. (PubMed:15489334)Curated
    Sequence conflicti78 – 781F → L in AAH29078. (PubMed:15489334)Curated
    Sequence conflicti529 – 5291K → N in BAE32320. (PubMed:16141072)Curated
    Sequence conflicti685 – 6851K → R in BAC31469. (PubMed:16141072)Curated
    Sequence conflicti717 – 7259Missing in AAG47648. (PubMed:10857751)Curated
    Sequence conflicti717 – 7171T → R in AAF24985. (PubMed:10857751)Curated
    Sequence conflicti719 – 7213SAD → TRA in AAF24985. (PubMed:10857751)Curated
    Sequence conflicti724 – 7252AQ → LK in AAF24985. (PubMed:10857751)Curated
    Sequence conflicti743 – 7431T → P in AAF24985. (PubMed:10857751)Curated
    Sequence conflicti834 – 8341D → A in AAF24985. (PubMed:10857751)Curated
    Sequence conflicti834 – 8341Missing in AAG47648. (PubMed:10857751)Curated
    Sequence conflicti866 – 8683LGS → IKN in AAF24985. (PubMed:10857751)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei404 – 4041S → R in isoform 4. 1 PublicationVSP_036216
    Alternative sequencei405 – 910506Missing in isoform 4. 1 PublicationVSP_036217Add
    BLAST
    Alternative sequencei508 – 57467DESHF…RYCDA → VSNGIALKYFVCLDTRKGST DLGICVLLGPLWALRREGNR NRCLSFIENDFFIPFLKQPL SLCARLS in isoform 3. 1 PublicationVSP_036218Add
    BLAST
    Alternative sequencei575 – 910336Missing in isoform 3. 1 PublicationVSP_036219Add
    BLAST
    Alternative sequencei769 – 78820LIQAE…SVSIH → GNVARVPLGMPRAEKYKIRK in isoform 2. 1 PublicationVSP_012919Add
    BLAST
    Alternative sequencei789 – 910122Missing in isoform 2. 1 PublicationVSP_012920Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF088884 mRNA. Translation: AAF24985.1.
    AF209773 Genomic DNA. Translation: AAG47648.1.
    AK042332 mRNA. Translation: BAE20630.1.
    AK043129 mRNA. Translation: BAC31469.1.
    AK077878 mRNA. Translation: BAC37047.1.
    AK083488 mRNA. Translation: BAC38933.1.
    AK154020 mRNA. Translation: BAE32320.1.
    AK169465 mRNA. Translation: BAE41189.1.
    BC029078 mRNA. Translation: AAH29078.1.
    CCDSiCCDS35609.1. [Q8BJL0-1]
    RefSeqiNP_061287.2. NM_018817.2. [Q8BJL0-1]
    XP_006496204.1. XM_006496141.1. [Q8BJL0-1]
    XP_006496205.1. XM_006496142.1. [Q8BJL0-1]
    XP_006496206.1. XM_006496143.1. [Q8BJL0-1]
    XP_006496207.1. XM_006496144.1. [Q8BJL0-1]
    UniGeneiMm.274232.

    Genome annotation databases

    EnsembliENSMUST00000047615; ENSMUSP00000047589; ENSMUSG00000039354. [Q8BJL0-1]
    ENSMUST00000152225; ENSMUSP00000137833; ENSMUSG00000039354. [Q8BJL0-1]
    GeneIDi54380.
    KEGGimmu:54380.
    UCSCiuc007bko.2. mouse. [Q8BJL0-4]
    uc007bkq.2. mouse. [Q8BJL0-3]
    uc007bkr.2. mouse. [Q8BJL0-2]
    uc007bks.2. mouse. [Q8BJL0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF088884 mRNA. Translation: AAF24985.1 .
    AF209773 Genomic DNA. Translation: AAG47648.1 .
    AK042332 mRNA. Translation: BAE20630.1 .
    AK043129 mRNA. Translation: BAC31469.1 .
    AK077878 mRNA. Translation: BAC37047.1 .
    AK083488 mRNA. Translation: BAC38933.1 .
    AK154020 mRNA. Translation: BAE32320.1 .
    AK169465 mRNA. Translation: BAE41189.1 .
    BC029078 mRNA. Translation: AAH29078.1 .
    CCDSi CCDS35609.1. [Q8BJL0-1 ]
    RefSeqi NP_061287.2. NM_018817.2. [Q8BJL0-1 ]
    XP_006496204.1. XM_006496141.1. [Q8BJL0-1 ]
    XP_006496205.1. XM_006496142.1. [Q8BJL0-1 ]
    XP_006496206.1. XM_006496143.1. [Q8BJL0-1 ]
    XP_006496207.1. XM_006496144.1. [Q8BJL0-1 ]
    UniGenei Mm.274232.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4O66 X-ray 1.90 A/B/C/D 197-268 [» ]
    ProteinModelPortali Q8BJL0.
    SMRi Q8BJL0. Positions 393-807.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000047589.

    PTM databases

    PhosphoSitei Q8BJL0.

    Proteomic databases

    PaxDbi Q8BJL0.
    PRIDEi Q8BJL0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000047615 ; ENSMUSP00000047589 ; ENSMUSG00000039354 . [Q8BJL0-1 ]
    ENSMUST00000152225 ; ENSMUSP00000137833 ; ENSMUSG00000039354 . [Q8BJL0-1 ]
    GeneIDi 54380.
    KEGGi mmu:54380.
    UCSCi uc007bko.2. mouse. [Q8BJL0-4 ]
    uc007bkq.2. mouse. [Q8BJL0-3 ]
    uc007bkr.2. mouse. [Q8BJL0-2 ]
    uc007bks.2. mouse. [Q8BJL0-1 ]

    Organism-specific databases

    CTDi 50485.
    MGIi MGI:1859183. Smarcal1.

    Phylogenomic databases

    eggNOGi COG0553.
    GeneTreei ENSGT00630000089754.
    HOVERGENi HBG054110.
    InParanoidi Q3TEQ9.
    KOi K14440.
    OMAi SIHYLVA.
    OrthoDBi EOG7XSTD5.
    PhylomeDBi Q8BJL0.
    TreeFami TF106474.

    Miscellaneous databases

    NextBioi 311200.
    PROi Q8BJL0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BJL0.
    Genevestigatori Q8BJL0.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR010003. HARP_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF07443. HARP. 2 hits.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51467. HARP. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of HARP/SMARCAL1: a prokaryotic HepA-related SNF2 helicase protein from human and mouse."
      Coleman M.A., Eisen J.A., Mohrenweiser H.W.
      Genomics 65:274-282(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
      Strain: C57BL/6J and NOD.
      Tissue: Cerebellum, Embryo, Testis and Thymus.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: Czech II.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiSMAL1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BJL0
    Secondary accession number(s): Q3TEQ9
    , Q3U4W0, Q3V3A8, Q8BVK7, Q8BXW4, Q8K309, Q9EQK8, Q9QYC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3