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P38935 (SMBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:IGHMBP2
Synonyms:SMBP2, SMUBP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length993 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Homooligomer. Interacts with RUVBL1, RUVBL2, GTF3C1 and ABT1. Is part of large cytosolic ribonucleoprotein complexes Probable. Associates with the ribosomes. Ref.8 Ref.9

Subcellular location

Nucleus. Cytoplasm. Cell projectionaxon By similarity. Note: Colocalizes with the translation initiation factor EIF4G2 By similarity. Ref.9

Tissue specificity

Expressed in all tissues examined.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Sequence similarities

Belongs to the DNA2/NAM7 helicase family.

Contains 1 AN1-type zinc finger.

Contains 1 R3H domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell projection
Cytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Neurodegeneration
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
RNA-binding
tRNA-binding
Zinc
   Molecular functionActivator
Helicase
Hydrolase
Ribonucleoprotein
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.8. Source: GOC

DNA duplex unwinding

Inferred from direct assay Ref.8. Source: GOC

DNA recombination

Traceable author statement Ref.1. Source: ProtInc

DNA repair

Traceable author statement PubMed 8493094. Source: ProtInc

DNA replication

Traceable author statement PubMed 8493094. Source: ProtInc

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

protein homooligomerization

Inferred from physical interaction Ref.9. Source: MGI

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Non-traceable author statement Ref.9. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.8. Source: UniProtKB

ATP-dependent 5'-3' DNA helicase activity

Inferred from direct assay Ref.8. Source: UniProtKB

ATP-dependent 5'-3' RNA helicase activity

Inferred from direct assay Ref.8. Source: UniProtKB

DNA binding

Inferred from direct assay Ref.8. Source: UniProtKB

DNA helicase activity

Traceable author statement Ref.1. Source: ProtInc

DNA-dependent ATPase activity

Inferred from direct assay Ref.8. Source: UniProtKB

RNA binding

Inferred from direct assay Ref.8. Source: UniProtKB

RNA-dependent ATPase activity

Inferred from direct assay Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

ribosome binding

Inferred from direct assay Ref.8. Source: UniProtKB

single-stranded DNA binding

Traceable author statement Ref.1PubMed 8493094. Source: ProtInc

tRNA binding

Inferred from direct assay Ref.9. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.9. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 993992DNA-binding protein SMUBP-2
PRO_0000080701

Regions

Domain723 – 78664R3H
Nucleotide binding214 – 2218ATP By similarity
Zinc finger894 – 94047AN1-type
Region638 – 785148SS DNA-binding By similarity
Motif864 – 8685Nuclear localization signal Potential
Compositional bias251 – 426176Leu-rich
Compositional bias795 – 85965Gln/Pro-rich
Compositional bias864 – 8707Poly-Lys

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.12 Ref.13

Natural variations

Natural variant171L → P in HMN6. Ref.19
VAR_058497
Natural variant751A → T.
Corresponds to variant rs2228206 [ dbSNP | Ensembl ].
VAR_055225
Natural variant1921L → P in HMN6. Ref.16
VAR_022321
Natural variant1961Q → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.17
VAR_058498
Natural variant2011L → S. Ref.1
Corresponds to variant rs560096 [ dbSNP | Ensembl ].
VAR_024242
Natural variant2131H → R in HMN6. Ref.15
VAR_022322
Natural variant2161P → L in HMN6. Ref.17
VAR_058499
Natural variant2211T → A in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.16
VAR_022323
Natural variant2411C → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.16
VAR_022324
Natural variant2511L → P in HMN6. Ref.17
VAR_058500
Natural variant2751I → V. Ref.1
Corresponds to variant rs10896380 [ dbSNP | Ensembl ].
VAR_024243
Natural variant3341E → K in HMN6. Ref.16
VAR_022325
Natural variant3611L → P in HMN6. Ref.16 Ref.19
VAR_022326
Natural variant3641L → P in HMN6. Ref.16
VAR_022327
Natural variant3821E → K in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.16
VAR_022328
Natural variant3861W → R in HMN6. Ref.19
VAR_058501
Natural variant4261L → P in HMN6. Ref.16
VAR_022329
Natural variant4451H → P in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.19
VAR_058502
Natural variant4721L → P in HMN6. Ref.19
VAR_058503
Natural variant4931T → I in HMN6; does not affect activity; reduces protein steady-state levels. Ref.8 Ref.20
VAR_058504
Natural variant5141E → K in HMN6. Ref.15
VAR_022330
Natural variant5571P → A.
Corresponds to variant rs7122089 [ dbSNP | Ensembl ].
VAR_055226
Natural variant5651D → N in HMN6; does not affect ATPase activity; loss of helicase activity on RNA duplices. Ref.8 Ref.16 Ref.17
VAR_022331
Natural variant5721Missing in HMN6. Ref.16
VAR_022332
Natural variant5771L → P in HMN6. Ref.16 Ref.17
VAR_022333
Natural variant5801V → I in HMN6. Ref.15
VAR_022334
Natural variant5811R → S in HMN6. Ref.19
VAR_058505
Natural variant5831N → I in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.16
VAR_022335
Natural variant5861G → C in HMN6. Ref.16
VAR_022336
Natural variant6031R → C in HMN6. Ref.17
VAR_058506
Natural variant6031R → H in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.16
VAR_022337
Natural variant6371R → C in HMN6. Ref.16 Ref.17
VAR_022338
Natural variant6711T → A.
Corresponds to variant rs622082 [ dbSNP | Ensembl ].
VAR_020147
Natural variant6941R → W.
Corresponds to variant rs2236654 [ dbSNP | Ensembl ].
VAR_021899
Natural variant8791T → K in HMN6. Ref.18
Corresponds to variant rs17612126 [ dbSNP | Ensembl ].
VAR_022339
Natural variant9281E → K.
Corresponds to variant rs2275996 [ dbSNP | Ensembl ].
VAR_021900
Natural variant9741D → E in HMN6. Ref.16
Corresponds to variant rs147674615 [ dbSNP | Ensembl ].
VAR_022340

Experimental info

Sequence conflict2921I → N in AAA53082. Ref.1
Sequence conflict4611L → V in AAA53082. Ref.1
Sequence conflict491 – 4944VDTA → GGRV in AAA58611. Ref.6
Sequence conflict8631E → K in AAA58611. Ref.6
Sequence conflict8661K → T in AAA58611. Ref.6

Secondary structure

............................................................................................................................. 993
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38935 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: DE785579EE60E26F

FASTA993109,149
        10         20         30         40         50         60 
MASAAVESFV TKQLDLLELE RDAEVEERRS WQENISLKEL QSRGVCLLKL QVSSQRTGLY 

        70         80         90        100        110        120 
GRLLVTFEPR RYGSAAALPS NSFTSGDIVG LYDAANEGSQ LATGILTRVT QKSVTVAFDE 

       130        140        150        160        170        180 
SHDFQLSLDR ENSYRLLKLA NDVTYRRLKK ALIALKKYHS GPASSLIEVL FGRSAPSPAS 

       190        200        210        220        230        240 
EIHPLTFFNT CLDTSQKEAV LFALSQKELA IIHGPPGTGK TTTVVEIILQ AVKQGLKVLC 

       250        260        270        280        290        300 
CAPSNIAVDN LVERLALCKQ RILRLGHPAR LLESIQQHSL DAVLARSDSA QIVADIRKDI 

       310        320        330        340        350        360 
DQVFVKNKKT QDKREKSNFR NEIKLLRKEL KEREEAAMLE SLTSANVVLA TNTGASADGP 

       370        380        390        400        410        420 
LKLLPESYFD VVVIDECAQA LEASCWIPLL KARKCILAGD HKQLPPTTVS HKAALAGLSL 

       430        440        450        460        470        480 
SLMERLAEEY GARVVRTLTV QYRMHQAIMR WASDTMYLGQ LTAHSSVARH LLRDLPGVAA 

       490        500        510        520        530        540 
TEETGVPLLL VDTAGCGLFE LEEEDEQSKG NPGEVRLVSL HIQALVDAGV PARDIAVVSP 

       550        560        570        580        590        600 
YNLQVDLLRQ SLVHRHPELE IKSVDGFQGR EKEAVILSFV RSNRKGEVGF LAEDRRINVA 

       610        620        630        640        650        660 
VTRARRHVAV ICDSRTVNNH AFLKTLVEYF TQHGEVRTAF EYLDDIVPEN YSHENSQGSS 

       670        680        690        700        710        720 
HAATKPQGPA TSTRTGSQRQ EGGQEAAAPA RQGRKKPAGK SLASEAPSQP SLNGGSPEGV 

       730        740        750        760        770        780 
ESQDGVDHFR AMIVEFMASK KMQLEFPPSL NSHDRLRVHQ IAEEHGLRHD SSGEGKRRFI 

       790        800        810        820        830        840 
TVSKRAPRPR AALGPPAGTG GPAPLQPVPP TPAQTEQPPR EQRGPDQPDL RTLHLERLQR 

       850        860        870        880        890        900 
VRSAQGQPAS KEQQASGQQK LPEKKKKKAK GHPATDLPTE EDFEALVSAA VKADNTCGFA 

       910        920        930        940        950        960 
KCTAGVTTLG QFCQLCSRRY CLSHHLPEIH GCGERARAHA RQRISREGVL YAGSGTKNGS 

       970        980        990 
LDPAKRAQLQ RRLDKKLSEL SNQRTSRRKE RGT 

« Hide

References

« Hide 'large scale' references
[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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in the gene encoding immunoglobulin mu-binding protein 2 cause spinal muscular atrophy with respiratory distress type 1."
Grohmann K., Schuelke M., Diers A., Hoffmann K., Lucke B., Adams C., Bertini E., Leonhardt-Horti H., Muntoni F., Ouvrier R., Pfeufer A., Rossi R., Van Maldergem L., Wilmshurst J.M., Wienker T.F., Sendtner M., Rudnik-Schoeneborn S., Zerres K., Huebner C.
Nat. Genet. 29:75-77(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HMN6 ARG-213; LYS-514 AND ILE-580.
[16]"Infantile spinal muscular atrophy with respiratory distress type 1 (SMARD1)."
Grohmann K., Varon R., Stolz P., Schuelke M., Janetzki C., Bertini E., Bushby K., Muntoni F., Ouvrier R., Van Maldergem L., Goemans N.M.L.A., Lochmueller H., Eichholz S., Adams C., Bosch F., Grattan-Smith P., Navarro C., Neitzel H. expand/collapse author list , Polster T., Topaloglu H., Steglich C., Guenther U.P., Zerres K., Rudnik-Schoeneborn S., Huebner C.
Ann. Neurol. 54:719-724(2003) [PubMed] [Europe PMC] [Abstract]
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]"Allelic heterogeneity of SMARD1 at the IGHMBP2 locus."
Maystadt I., Zarhrate M., Landrieu P., Boespflug-Tanguy O., Sukno S., Collignon P., Melki J., Verellen-Dumoulin C., Munnich A., Viollet L.
Hum. Mutat. 23:525-526(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8187.1.
PIRA47500.
RefSeqNP_002171.2. NM_002180.2.
UniGeneHs.503048.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MSZNMR-A711-786[»]
2LRRNMR-A711-786[»]
4B3FX-ray2.50X3-648[»]
4B3GX-ray2.85A/B3-648[»]
ProteinModelPortalP38935.
SMRP38935. Positions 3-648, 717-786.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109728. 1 interaction.
IntActP38935. 1 interaction.
STRING9606.ENSP00000255078.

PTM databases

PhosphoSiteP38935.

Polymorphism databases

DMDM317373494.

Proteomic databases

MaxQBP38935.
PaxDbP38935.
PRIDEP38935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255078; ENSP00000255078; ENSG00000132740.
GeneID3508.
KEGGhsa:3508.
UCSCuc001ook.1. human.

Organism-specific databases

CTD3508.
GeneCardsGC11P068671.
H-InvDBHIX0009884.
HIX0171377.
HGNCHGNC:5542. IGHMBP2.
MIM600502. gene.
604320. phenotype.
neXtProtNX_P38935.
Orphanet98920. Spinal muscular atrophy with respiratory distress.
PharmGKBPA29731.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1112.
HOGENOMHOG000185831.
HOVERGENHBG077019.
InParanoidP38935.
OMALSHHIPE.
OrthoDBEOG7M6D6M.
PhylomeDBP38935.
TreeFamTF105388.

Gene expression databases

ArrayExpressP38935.
BgeeP38935.
CleanExHS_IGHMBP2.
GenevestigatorP38935.

Family and domain databases

Gene3D3.30.1370.50. 1 hit.
3.40.50.300. 3 hits.
4.10.1110.10. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR014001. Helicase_ATP-bd.
IPR027417. P-loop_NTPase.
IPR001374. R3H_ss-bd.
IPR004483. SMUBP-2/Hcs1_like.
IPR000058. Znf_AN1.
[Graphical view]
PfamPF01424. R3H. 1 hit.
PF01428. zf-AN1. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00487. DEXDc. 1 hit.
SM00393. R3H. 1 hit.
SM00154. ZnF_AN1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF82708. SSF82708. 1 hit.
TIGRFAMsTIGR00376. TIGR00376. 1 hit.
PROSITEPS51061. R3H. 1 hit.
PS51039. ZF_AN1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38935.
GeneWikiIGHMBP2.
GenomeRNAi3508.
NextBio13764.
PROP38935.
SOURCESearch...

Entry information

Entry nameSMBP2_HUMAN
AccessionPrimary (citable) accession number: P38935
Secondary accession number(s): A0PJD2, Q00443, Q14177
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM