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P38935

- SMBP2_HUMAN

UniProt

P38935 - SMBP2_HUMAN

Protein

DNA-binding protein SMUBP-2

Gene

IGHMBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    5' to 3' helicase that unwinds RNA and DNA duplices in an ATP-dependent reaction. Acts as a transcription regulator. Required for the transcriptional activation of the flounder liver-type antifreeze protein gene. Exhibits strong binding specificity to the enhancer element B of the flounder antifreeze protein gene intron. Binds to the insulin II gene RIPE3B enhancer region. May be involved in translation By similarity. DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region. Preferentially binds to the 5'-GGGCT-3' motif. Interacts with tRNA-Tyr. Stimulates the transcription of the human neurotropic virus JCV.By similarity2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi214 – 2218ATPBy similarity
    Zinc fingeri894 – 94047AN1-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. ATP-dependent 5'-3' DNA helicase activity Source: UniProtKB
    3. ATP-dependent 5'-3' RNA helicase activity Source: UniProtKB
    4. DNA binding Source: UniProtKB
    5. DNA-dependent ATPase activity Source: UniProtKB
    6. DNA helicase activity Source: ProtInc
    7. protein binding Source: UniProtKB
    8. ribosome binding Source: UniProtKB
    9. RNA binding Source: UniProtKB
    10. RNA-dependent ATPase activity Source: UniProtKB
    11. single-stranded DNA binding Source: ProtInc
    12. transcription factor binding Source: UniProtKB
    13. tRNA binding Source: UniProtKB
    14. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cell death Source: UniProtKB-KW
    3. DNA duplex unwinding Source: GOC
    4. DNA recombination Source: ProtInc
    5. DNA repair Source: ProtInc
    6. DNA replication Source: ProtInc
    7. protein homooligomerization Source: MGI
    8. regulation of transcription, DNA-templated Source: UniProtKB-KW
    9. transcription, DNA-templated Source: UniProtKB-KW
    10. translation Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Helicase, Hydrolase, Ribonucleoprotein

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-binding protein SMUBP-2 (EC:3.6.4.12, EC:3.6.4.13)
    Alternative name(s):
    ATP-dependent helicase IGHMBP2
    Glial factor 1
    Short name:
    GF-1
    Immunoglobulin mu-binding protein 2
    Gene namesi
    Name:IGHMBP2
    Synonyms:SMBP2, SMUBP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:5542. IGHMBP2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Cell projectionaxon By similarity
    Note: Colocalizes with the translation initiation factor EIF4G2.By similarity

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. growth cone Source: UniProtKB
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Neuronopathy, distal hereditary motor, 6 (HMN6) [MIM:604320]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171L → P in HMN6. 1 Publication
    VAR_058497
    Natural varianti192 – 1921L → P in HMN6. 1 Publication
    VAR_022321
    Natural varianti196 – 1961Q → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_058498
    Natural varianti213 – 2131H → R in HMN6. 1 Publication
    VAR_022322
    Natural varianti216 – 2161P → L in HMN6. 1 Publication
    VAR_058499
    Natural varianti221 – 2211T → A in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022323
    Natural varianti241 – 2411C → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022324
    Natural varianti251 – 2511L → P in HMN6. 1 Publication
    VAR_058500
    Natural varianti334 – 3341E → K in HMN6. 1 Publication
    VAR_022325
    Natural varianti361 – 3611L → P in HMN6. 2 Publications
    VAR_022326
    Natural varianti364 – 3641L → P in HMN6. 1 Publication
    VAR_022327
    Natural varianti382 – 3821E → K in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022328
    Natural varianti386 – 3861W → R in HMN6. 1 Publication
    VAR_058501
    Natural varianti426 – 4261L → P in HMN6. 1 Publication
    VAR_022329
    Natural varianti445 – 4451H → P in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_058502
    Natural varianti472 – 4721L → P in HMN6. 1 Publication
    VAR_058503
    Natural varianti493 – 4931T → I in HMN6; does not affect activity; reduces protein steady-state levels. 1 Publication
    VAR_058504
    Natural varianti514 – 5141E → K in HMN6. 1 Publication
    VAR_022330
    Natural varianti565 – 5651D → N in HMN6; does not affect ATPase activity; loss of helicase activity on RNA duplices. 2 Publications
    VAR_022331
    Natural varianti572 – 5721Missing in HMN6. 1 Publication
    VAR_022332
    Natural varianti577 – 5771L → P in HMN6. 2 Publications
    VAR_022333
    Natural varianti580 – 5801V → I in HMN6. 1 Publication
    VAR_022334
    Natural varianti581 – 5811R → S in HMN6. 1 Publication
    VAR_058505
    Natural varianti583 – 5831N → I in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022335
    Natural varianti586 – 5861G → C in HMN6. 1 Publication
    VAR_022336
    Natural varianti603 – 6031R → C in HMN6. 1 Publication
    VAR_058506
    Natural varianti603 – 6031R → H in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022337
    Natural varianti637 – 6371R → C in HMN6. 2 Publications
    VAR_022338
    Natural varianti879 – 8791T → K in HMN6. 1 Publication
    Corresponds to variant rs17612126 [ dbSNP | Ensembl ].
    VAR_022339
    Natural varianti974 – 9741D → E in HMN6. 1 Publication
    Corresponds to variant rs147674615 [ dbSNP | Ensembl ].
    VAR_022340

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi604320. phenotype.
    Orphaneti98920. Spinal muscular atrophy with respiratory distress.
    PharmGKBiPA29731.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 993992DNA-binding protein SMUBP-2PRO_0000080701Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP38935.
    PaxDbiP38935.
    PRIDEiP38935.

    PTM databases

    PhosphoSiteiP38935.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined.

    Gene expression databases

    ArrayExpressiP38935.
    BgeeiP38935.
    CleanExiHS_IGHMBP2.
    GenevestigatoriP38935.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with RUVBL1, RUVBL2, GTF3C1 and ABT1. Is part of large cytosolic ribonucleoprotein complexes Probable. Associates with the ribosomes.2 PublicationsCurated

    Protein-protein interaction databases

    BioGridi109728. 1 interaction.
    IntActiP38935. 1 interaction.
    STRINGi9606.ENSP00000255078.

    Structurei

    Secondary structure

    1
    993
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 3330
    Helixi37 – 404
    Helixi41 – 433
    Beta strandi45 – 5713
    Beta strandi59 – 613
    Beta strandi63 – 708
    Beta strandi71 – 744
    Beta strandi88 – 936
    Turni94 – 974
    Beta strandi102 – 1109
    Beta strandi113 – 1175
    Beta strandi134 – 1396
    Helixi142 – 15615
    Beta strandi160 – 1623
    Helixi164 – 1707
    Beta strandi172 – 1743
    Helixi194 – 20512
    Beta strandi207 – 2137
    Helixi220 – 23314
    Beta strandi238 – 2447
    Helixi245 – 25713
    Beta strandi262 – 2643
    Helixi273 – 2764
    Helixi280 – 2845
    Turni285 – 2884
    Helixi293 – 3008
    Beta strandi302 – 3043
    Turni305 – 3084
    Helixi320 – 34425
    Beta strandi346 – 3516
    Turni352 – 3554
    Beta strandi357 – 3593
    Helixi360 – 3634
    Beta strandi370 – 3745
    Helixi377 – 3793
    Helixi382 – 3854
    Turni386 – 3883
    Helixi389 – 3913
    Beta strandi392 – 3998
    Helixi411 – 4155
    Turni416 – 4194
    Helixi422 – 4309
    Helixi431 – 4333
    Beta strandi435 – 4373
    Beta strandi440 – 4445
    Helixi446 – 45611
    Turni465 – 4695
    Helixi472 – 4743
    Turni482 – 4854
    Beta strandi487 – 4926
    Helixi512 – 52716
    Helixi532 – 5343
    Beta strandi535 – 5406
    Helixi542 – 55211
    Turni553 – 5553
    Beta strandi560 – 5634
    Helixi564 – 5674
    Beta strandi572 – 5787
    Turni589 – 5924
    Helixi594 – 6029
    Beta strandi604 – 6129
    Helixi614 – 6174
    Helixi621 – 63212
    Beta strandi633 – 6386
    Helixi639 – 6413
    Helixi727 – 73913
    Beta strandi742 – 7465
    Helixi753 – 76412
    Beta strandi767 – 7726
    Beta strandi774 – 7763
    Beta strandi779 – 7846

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MSZNMR-A711-786[»]
    2LRRNMR-A711-786[»]
    4B3FX-ray2.50X3-648[»]
    4B3GX-ray2.85A/B3-648[»]
    ProteinModelPortaliP38935.
    SMRiP38935. Positions 3-648, 717-786.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38935.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini723 – 78664R3HPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni638 – 785148SS DNA-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi864 – 8685Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi251 – 426176Leu-richAdd
    BLAST
    Compositional biasi795 – 85965Gln/Pro-richAdd
    BLAST
    Compositional biasi864 – 8707Poly-Lys

    Sequence similaritiesi

    Belongs to the DNA2/NAM7 helicase family.Curated
    Contains 1 AN1-type zinc finger.PROSITE-ProRule annotation
    Contains 1 R3H domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri894 – 94047AN1-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1112.
    HOGENOMiHOG000185831.
    HOVERGENiHBG077019.
    InParanoidiP38935.
    OMAiLSHHIPE.
    OrthoDBiEOG7M6D6M.
    PhylomeDBiP38935.
    TreeFamiTF105388.

    Family and domain databases

    Gene3Di3.30.1370.50. 1 hit.
    3.40.50.300. 3 hits.
    4.10.1110.10. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR014001. Helicase_ATP-bd.
    IPR027417. P-loop_NTPase.
    IPR001374. R3H_ss-bd.
    IPR004483. SMUBP-2/Hcs1_like.
    IPR000058. Znf_AN1.
    [Graphical view]
    PfamiPF01424. R3H. 1 hit.
    PF01428. zf-AN1. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00487. DEXDc. 1 hit.
    SM00393. R3H. 1 hit.
    SM00154. ZnF_AN1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF82708. SSF82708. 1 hit.
    TIGRFAMsiTIGR00376. TIGR00376. 1 hit.
    PROSITEiPS51061. R3H. 1 hit.
    PS51039. ZF_AN1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P38935-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASAAVESFV TKQLDLLELE RDAEVEERRS WQENISLKEL QSRGVCLLKL    50
    QVSSQRTGLY GRLLVTFEPR RYGSAAALPS NSFTSGDIVG LYDAANEGSQ 100
    LATGILTRVT QKSVTVAFDE SHDFQLSLDR ENSYRLLKLA NDVTYRRLKK 150
    ALIALKKYHS GPASSLIEVL FGRSAPSPAS EIHPLTFFNT CLDTSQKEAV 200
    LFALSQKELA IIHGPPGTGK TTTVVEIILQ AVKQGLKVLC CAPSNIAVDN 250
    LVERLALCKQ RILRLGHPAR LLESIQQHSL DAVLARSDSA QIVADIRKDI 300
    DQVFVKNKKT QDKREKSNFR NEIKLLRKEL KEREEAAMLE SLTSANVVLA 350
    TNTGASADGP LKLLPESYFD VVVIDECAQA LEASCWIPLL KARKCILAGD 400
    HKQLPPTTVS HKAALAGLSL SLMERLAEEY GARVVRTLTV QYRMHQAIMR 450
    WASDTMYLGQ LTAHSSVARH LLRDLPGVAA TEETGVPLLL VDTAGCGLFE 500
    LEEEDEQSKG NPGEVRLVSL HIQALVDAGV PARDIAVVSP YNLQVDLLRQ 550
    SLVHRHPELE IKSVDGFQGR EKEAVILSFV RSNRKGEVGF LAEDRRINVA 600
    VTRARRHVAV ICDSRTVNNH AFLKTLVEYF TQHGEVRTAF EYLDDIVPEN 650
    YSHENSQGSS HAATKPQGPA TSTRTGSQRQ EGGQEAAAPA RQGRKKPAGK 700
    SLASEAPSQP SLNGGSPEGV ESQDGVDHFR AMIVEFMASK KMQLEFPPSL 750
    NSHDRLRVHQ IAEEHGLRHD SSGEGKRRFI TVSKRAPRPR AALGPPAGTG 800
    GPAPLQPVPP TPAQTEQPPR EQRGPDQPDL RTLHLERLQR VRSAQGQPAS 850
    KEQQASGQQK LPEKKKKKAK GHPATDLPTE EDFEALVSAA VKADNTCGFA 900
    KCTAGVTTLG QFCQLCSRRY CLSHHLPEIH GCGERARAHA RQRISREGVL 950
    YAGSGTKNGS LDPAKRAQLQ RRLDKKLSEL SNQRTSRRKE RGT 993
    Length:993
    Mass (Da):109,149
    Last modified:January 11, 2011 - v3
    Checksum:iDE785579EE60E26F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti292 – 2921I → N in AAA53082. (PubMed:8349627)Curated
    Sequence conflicti461 – 4611L → V in AAA53082. (PubMed:8349627)Curated
    Sequence conflicti491 – 4944VDTA → GGRV in AAA58611. (PubMed:1714899)Curated
    Sequence conflicti863 – 8631E → K in AAA58611. (PubMed:1714899)Curated
    Sequence conflicti866 – 8661K → T in AAA58611. (PubMed:1714899)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171L → P in HMN6. 1 Publication
    VAR_058497
    Natural varianti75 – 751A → T.
    Corresponds to variant rs2228206 [ dbSNP | Ensembl ].
    VAR_055225
    Natural varianti192 – 1921L → P in HMN6. 1 Publication
    VAR_022321
    Natural varianti196 – 1961Q → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_058498
    Natural varianti201 – 2011L → S.1 Publication
    Corresponds to variant rs560096 [ dbSNP | Ensembl ].
    VAR_024242
    Natural varianti213 – 2131H → R in HMN6. 1 Publication
    VAR_022322
    Natural varianti216 – 2161P → L in HMN6. 1 Publication
    VAR_058499
    Natural varianti221 – 2211T → A in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022323
    Natural varianti241 – 2411C → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022324
    Natural varianti251 – 2511L → P in HMN6. 1 Publication
    VAR_058500
    Natural varianti275 – 2751I → V.1 Publication
    Corresponds to variant rs10896380 [ dbSNP | Ensembl ].
    VAR_024243
    Natural varianti334 – 3341E → K in HMN6. 1 Publication
    VAR_022325
    Natural varianti361 – 3611L → P in HMN6. 2 Publications
    VAR_022326
    Natural varianti364 – 3641L → P in HMN6. 1 Publication
    VAR_022327
    Natural varianti382 – 3821E → K in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022328
    Natural varianti386 – 3861W → R in HMN6. 1 Publication
    VAR_058501
    Natural varianti426 – 4261L → P in HMN6. 1 Publication
    VAR_022329
    Natural varianti445 – 4451H → P in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_058502
    Natural varianti472 – 4721L → P in HMN6. 1 Publication
    VAR_058503
    Natural varianti493 – 4931T → I in HMN6; does not affect activity; reduces protein steady-state levels. 1 Publication
    VAR_058504
    Natural varianti514 – 5141E → K in HMN6. 1 Publication
    VAR_022330
    Natural varianti557 – 5571P → A.
    Corresponds to variant rs7122089 [ dbSNP | Ensembl ].
    VAR_055226
    Natural varianti565 – 5651D → N in HMN6; does not affect ATPase activity; loss of helicase activity on RNA duplices. 2 Publications
    VAR_022331
    Natural varianti572 – 5721Missing in HMN6. 1 Publication
    VAR_022332
    Natural varianti577 – 5771L → P in HMN6. 2 Publications
    VAR_022333
    Natural varianti580 – 5801V → I in HMN6. 1 Publication
    VAR_022334
    Natural varianti581 – 5811R → S in HMN6. 1 Publication
    VAR_058505
    Natural varianti583 – 5831N → I in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022335
    Natural varianti586 – 5861G → C in HMN6. 1 Publication
    VAR_022336
    Natural varianti603 – 6031R → C in HMN6. 1 Publication
    VAR_058506
    Natural varianti603 – 6031R → H in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 1 Publication
    VAR_022337
    Natural varianti637 – 6371R → C in HMN6. 2 Publications
    VAR_022338
    Natural varianti671 – 6711T → A.
    Corresponds to variant rs622082 [ dbSNP | Ensembl ].
    VAR_020147
    Natural varianti694 – 6941R → W.
    Corresponds to variant rs2236654 [ dbSNP | Ensembl ].
    VAR_021899
    Natural varianti879 – 8791T → K in HMN6. 1 Publication
    Corresponds to variant rs17612126 [ dbSNP | Ensembl ].
    VAR_022339
    Natural varianti928 – 9281E → K.
    Corresponds to variant rs2275996 [ dbSNP | Ensembl ].
    VAR_021900
    Natural varianti974 – 9741D → E in HMN6. 1 Publication
    Corresponds to variant rs147674615 [ dbSNP | Ensembl ].
    VAR_022340

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14754 mRNA. Translation: AAA53082.1.
    L24544 Genomic DNA. Translation: AAA70430.1.
    AP000808 Genomic DNA. No translation available.
    BC025299 mRNA. Translation: AAH25299.1.
    M64979 mRNA. Translation: AAA58611.1.
    CCDSiCCDS8187.1.
    PIRiA47500.
    RefSeqiNP_002171.2. NM_002180.2.
    UniGeneiHs.503048.

    Genome annotation databases

    EnsembliENST00000255078; ENSP00000255078; ENSG00000132740.
    GeneIDi3508.
    KEGGihsa:3508.
    UCSCiuc001ook.1. human.

    Polymorphism databases

    DMDMi317373494.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14754 mRNA. Translation: AAA53082.1 .
    L24544 Genomic DNA. Translation: AAA70430.1 .
    AP000808 Genomic DNA. No translation available.
    BC025299 mRNA. Translation: AAH25299.1 .
    M64979 mRNA. Translation: AAA58611.1 .
    CCDSi CCDS8187.1.
    PIRi A47500.
    RefSeqi NP_002171.2. NM_002180.2.
    UniGenei Hs.503048.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MSZ NMR - A 711-786 [» ]
    2LRR NMR - A 711-786 [» ]
    4B3F X-ray 2.50 X 3-648 [» ]
    4B3G X-ray 2.85 A/B 3-648 [» ]
    ProteinModelPortali P38935.
    SMRi P38935. Positions 3-648, 717-786.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109728. 1 interaction.
    IntActi P38935. 1 interaction.
    STRINGi 9606.ENSP00000255078.

    PTM databases

    PhosphoSitei P38935.

    Polymorphism databases

    DMDMi 317373494.

    Proteomic databases

    MaxQBi P38935.
    PaxDbi P38935.
    PRIDEi P38935.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255078 ; ENSP00000255078 ; ENSG00000132740 .
    GeneIDi 3508.
    KEGGi hsa:3508.
    UCSCi uc001ook.1. human.

    Organism-specific databases

    CTDi 3508.
    GeneCardsi GC11P068671.
    H-InvDB HIX0009884.
    HIX0171377.
    HGNCi HGNC:5542. IGHMBP2.
    MIMi 600502. gene.
    604320. phenotype.
    neXtProti NX_P38935.
    Orphaneti 98920. Spinal muscular atrophy with respiratory distress.
    PharmGKBi PA29731.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1112.
    HOGENOMi HOG000185831.
    HOVERGENi HBG077019.
    InParanoidi P38935.
    OMAi LSHHIPE.
    OrthoDBi EOG7M6D6M.
    PhylomeDBi P38935.
    TreeFami TF105388.

    Miscellaneous databases

    EvolutionaryTracei P38935.
    GeneWikii IGHMBP2.
    GenomeRNAii 3508.
    NextBioi 13764.
    PROi P38935.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P38935.
    Bgeei P38935.
    CleanExi HS_IGHMBP2.
    Genevestigatori P38935.

    Family and domain databases

    Gene3Di 3.30.1370.50. 1 hit.
    3.40.50.300. 3 hits.
    4.10.1110.10. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR014001. Helicase_ATP-bd.
    IPR027417. P-loop_NTPase.
    IPR001374. R3H_ss-bd.
    IPR004483. SMUBP-2/Hcs1_like.
    IPR000058. Znf_AN1.
    [Graphical view ]
    Pfami PF01424. R3H. 1 hit.
    PF01428. zf-AN1. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00487. DEXDc. 1 hit.
    SM00393. R3H. 1 hit.
    SM00154. ZnF_AN1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF82708. SSF82708. 1 hit.
    TIGRFAMsi TIGR00376. TIGR00376. 1 hit.
    PROSITEi PS51061. R3H. 1 hit.
    PS51039. ZF_AN1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human S mu bp-2, a DNA-binding protein specific to the single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region."
      Fukita Y., Mizuta T.-R., Shirozu M., Ozawa K., Shimizu A., Honjo T.
      J. Biol. Chem. 268:17463-17470(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-201 AND VAL-275.
    2. "Smubp-2 represses the Epstein-Barr virus lytic switch promoter."
      Zhang Q., Wang Y.C., Montalvo E.A.
      Virology 255:160-170(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] OF 1-868.
      Tissue: Brain.
    5. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 221-233 AND 824-831, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    6. "A recombinant cDNA derived from human brain encodes a DNA binding protein that stimulates transcription of the human neurotropic virus JCV."
      Kerr D., Khalili K.
      J. Biol. Chem. 266:15876-15881(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 491-866.
      Tissue: Brain.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. "IGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1)."
      Guenther U.P., Handoko L., Laggerbauer B., Jablonka S., Chari A., Alzheimer M., Ohmer J., Ploettner O., Gehring N., Sickmann A., von Au K., Schuelke M., Fischer U.
      Hum. Mol. Genet. 18:1288-1300(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ATP-DEPENDENT HELICASE, INTERACTION WITH RIBOSOMES, CHARACTERIZATION OF VARIANTS HMN6 ARG-196; ALA-221; ARG-241; LYS-382; PRO-445; ILE-493; ASN-565; ILE-583 AND HIS-603.
    9. "Biochemical and genetic evidence for a role of IGHMBP2 in the translational machinery."
      de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A., Mourelatos Z.
      Hum. Mol. Genet. 18:2115-2126(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH RUVBL1; RUVBL2; GTF3C1 AND ABT1, TRNA-BINDING.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure of the R3H domain from human Smubp-2."
      Liepinsh E., Leonchiks A., Sharipo A., Guignard L., Otting G.
      J. Mol. Biol. 326:217-223(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 709-794.
    15. Cited for: VARIANTS HMN6 ARG-213; LYS-514 AND ILE-580.
    16. Cited for: VARIANTS HMN6 PRO-192; ALA-221; ARG-241; LYS-334; PRO-361; PRO-364; LYS-382; PRO-426; ASN-565; LYS-572 DEL; PRO-577; ILE-583; CYS-586; HIS-603; CYS-637 AND GLU-974.
    17. Cited for: VARIANTS HMN6 ARG-196; LEU-216; PRO-251; ASN-565; PRO-577; CYS-603 AND CYS-637.
    18. "A new mutation of IGHMBP2 gene in spinal muscular atrophy with respiratory distress type 1."
      Tachi N., Kikuchi S., Kozuka N., Nogami A.
      Pediatr. Neurol. 32:288-290(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HMN6 LYS-879.
    19. "Clinical and mutational profile in spinal muscular atrophy with respiratory distress (SMARD): defining novel phenotypes through hierarchical cluster analysis."
      Guenther U.P., Varon R., Schlicke M., Dutrannoy V., Volk A., Huebner C., von Au K., Schuelke M.
      Hum. Mutat. 28:808-815(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HMN6 PRO-17; PRO-361; ARG-386; PRO-445; PRO-472 AND SER-581.
    20. "Clinical variability in distal spinal muscular atrophy type 1 (DSMA1): determination of steady-state IGHMBP2 protein levels in five patients with infantile and juvenile disease."
      Guenther U.P., Handoko L., Varon R., Stephani U., Tsao C.Y., Mendell J.R., Luetzkendorf S., Huebner C., von Au K., Jablonka S., Dittmar G., Heinemann U., Schuetz A., Schuelke M.
      J. Mol. Med. 87:31-41(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HMN6 ILE-493, CHARACTERIZATION OF VARIANT HMN6 ILE-493.

    Entry informationi

    Entry nameiSMBP2_HUMAN
    AccessioniPrimary (citable) accession number: P38935
    Secondary accession number(s): A0PJD2, Q00443, Q14177
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3