P38935 (SMBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	IGHMBP2
Synonyms:	SMBP2, SMUBP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	993 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 projection › axon By similarity. Note: Colocalizes with the traslation initiation factor EIF4G2 By similarity. Ref.9
Tissue specificity	Expressed in all tissues examined.
Involvement in disease	Distal hereditary motor neuronopathy 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.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
Sequence similarities	Belongs to the DNA2/NAM7 helicase family. Contains 1 AN1-type zinc finger. Contains 1 R3H domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell projection Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Neurodegeneration
Domain	Zinc-finger
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Activator Helicase Hydrolase Ribonucleoprotein
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW translation Non-traceable author statement Ref.9. Source: UniProtKB
Cellular_component	axon 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_function	ATP 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 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 zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 993

992

DNA-binding protein SMUBP-2

PRO_0000080701

Regions

Domain

723 – 786

64

R3H

Nucleotide binding

214 – 221

8

ATP By similarity

Zinc finger

894 – 940

47

AN1-type

Region

638 – 785

148

SS DNA-binding By similarity

Motif

864 – 868

5

Nuclear localization signal Potential

Compositional bias

251 – 426

176

Leu-rich

Compositional bias

795 – 859

65

Gln/Pro-rich

Compositional bias

864 – 870

7

Poly-Lys

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Natural variations

Natural variant

17

1

L → P in HMN6. Ref.17

VAR_058497

Natural variant

75

1

A → T.
Corresponds to variant rs2228206 [ dbSNP | Ensembl ].

VAR_055225

Natural variant

192

1

L → P in HMN6. Ref.14

VAR_022321

Natural variant

196

1

Q → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.15

VAR_058498

Natural variant

201

1

L → S. Ref.1
Corresponds to variant rs560096 [ dbSNP | Ensembl ].

VAR_024242

Natural variant

213

1

H → R in HMN6. Ref.13

VAR_022322

Natural variant

216

1

P → L in HMN6. Ref.15

VAR_058499

Natural variant

221

1

T → A in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.14

VAR_022323

Natural variant

241

1

C → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.14

VAR_022324

Natural variant

251

1

L → P in HMN6. Ref.15

VAR_058500

Natural variant

275

1

I → V. Ref.1
Corresponds to variant rs10896380 [ dbSNP | Ensembl ].

VAR_024243

Natural variant

334

1

E → K in HMN6. Ref.14

VAR_022325

Natural variant

361

1

L → P in HMN6. Ref.14 Ref.17

VAR_022326

Natural variant

364

1

L → P in HMN6. Ref.14

VAR_022327

Natural variant

382

1

E → K in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.14

VAR_022328

Natural variant

386

1

W → R in HMN6. Ref.17

VAR_058501

Natural variant

426

1

L → P in HMN6. Ref.14

VAR_022329

Natural variant

445

1

H → P in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.17

VAR_058502

Natural variant

472

1

L → P in HMN6. Ref.17

VAR_058503

Natural variant

493

1

T → I in HMN6; does not affect activity; reduces protein steady-state levels. Ref.8 Ref.18

VAR_058504

Natural variant

514

1

E → K in HMN6. Ref.13

VAR_022330

Natural variant

557

1

P → A.
Corresponds to variant rs7122089 [ dbSNP | Ensembl ].

VAR_055226

Natural variant

565

1

D → N in HMN6; does not affect ATPase activity; loss of helicase activity on RNA duplices. Ref.8 Ref.14 Ref.15

VAR_022331

Natural variant

572

1

Missing in HMN6. Ref.14

VAR_022332

Natural variant

577

1

L → P in HMN6. Ref.14 Ref.15

VAR_022333

Natural variant

580

1

V → I in HMN6. Ref.13

VAR_022334

Natural variant

581

1

R → S in HMN6. Ref.17

VAR_058505

Natural variant

583

1

N → I in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.14

VAR_022335

Natural variant

586

1

G → C in HMN6. Ref.14

VAR_022336

Natural variant

603

1

R → C in HMN6. Ref.15

VAR_058506

Natural variant

603

1

R → H in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. Ref.8 Ref.14

VAR_022337

Natural variant

637

1

R → C in HMN6. Ref.14 Ref.15

VAR_022338

Natural variant

671

1

T → A.
Corresponds to variant rs622082 [ dbSNP | Ensembl ].

VAR_020147

Natural variant

694

1

R → W.
Corresponds to variant rs2236654 [ dbSNP | Ensembl ].

VAR_021899

Natural variant

879

1

T → K in HMN6. Ref.16
Corresponds to variant rs17612126 [ dbSNP | Ensembl ].

VAR_022339

Natural variant

928

1

E → K.
Corresponds to variant rs2275996 [ dbSNP | Ensembl ].

VAR_021900

Natural variant

974

1

D → E in HMN6. Ref.14

VAR_022340

Experimental info

Sequence conflict

292

1

I → N in AAA53082. Ref.1

Sequence conflict

461

1

L → V in AAA53082. Ref.1

Sequence conflict

491 – 494

4

VDTA → GGRV in AAA58611. Ref.6

Sequence conflict

863

1

E → K in AAA58611. Ref.6

Sequence conflict

866

1

K → T in AAA58611. Ref.6

Secondary structure

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993

Helix Strand Turn

Details...

Helix

4 – 33

30

Helix

37 – 40

4

Helix

41 – 43

3

Beta strand

45 – 57

13

Beta strand

59 – 61

3

Beta strand

63 – 70

8

Beta strand

71 – 74

4

Beta strand

88 – 93

6

Turn

94 – 97

4

Beta strand

102 – 110

9

Beta strand

113 – 117

5

Beta strand

134 – 139

6

Helix

142 – 156

15

Beta strand

160 – 162

3

Helix

164 – 170

7

Beta strand

172 – 174

3

Helix

194 – 205

12

Beta strand

207 – 213

7

Helix

220 – 233

14

Beta strand

238 – 244

7

Helix

245 – 257

13

Beta strand

262 – 264

3

Helix

273 – 276

4

Helix

280 – 284

5

Turn

285 – 288

4

Helix

293 – 300

8

Beta strand

302 – 304

3

Turn

305 – 308

4

Helix

320 – 344

25

Beta strand

346 – 351

6

Turn

352 – 355

4

Beta strand

357 – 359

3

Helix

360 – 363

4

Beta strand

370 – 374

5

Helix

377 – 379

3

Helix

382 – 385

4

Turn

386 – 388

3

Helix

389 – 391

3

Beta strand

392 – 399

8

Helix

411 – 415

5

Turn

416 – 419

4

Helix

422 – 430

9

Helix

431 – 433

3

Beta strand

435 – 437

3

Beta strand

440 – 444

5

Helix

446 – 456

11

Turn

465 – 469

5

Helix

472 – 474

3

Turn

482 – 485

4

Beta strand

487 – 492

6

Helix

512 – 527

16

Helix

532 – 534

3

Beta strand

535 – 540

6

Helix

542 – 552

11

Turn

553 – 555

3

Beta strand

560 – 563

4

Helix

564 – 567

4

Beta strand

572 – 578

7

Turn

589 – 592

4

Helix

594 – 602

9

Beta strand

604 – 612

9

Helix

614 – 617

4

Helix

621 – 632

12

Beta strand

633 – 638

6

Helix

639 – 641

3

Helix

727 – 739

13

Beta strand

742 – 746

5

Helix

753 – 764

12

Beta strand

767 – 772

6

Beta strand

774 – 776

3

Beta strand

779 – 784

6

Sequences

	Sequence		Length	Mass (Da)
	P38935 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: DE785579EE60E26F	FASTA	993	109,149
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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]	"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.
[13]	"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.
[14]	"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. , 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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.

Web resources

GeneReviews

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.

IPI

IPI00009379.

PIR

A47500.

RefSeq

NP_002171.2. NM_002180.2.

UniGene

Hs.503048.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P38935.

SMR

P38935. Positions 3-648, 717-786.

ModBase

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Protein-protein interaction databases

IntAct

P38935. 1 interaction.

STRING

9606.ENSP00000255078.

PTM databases

PhosphoSite

P38935.

Polymorphism databases

DMDM

229462778.

Proteomic databases

PaxDb

P38935.

PRIDE

P38935.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000255078; ENSP00000255078; ENSG00000132740.

GeneID

3508.

KEGG

hsa:3508.

UCSC

uc001ook.1. human.

Organism-specific databases

CTD

3508.

GeneCards

GC11P068671.

H-InvDB

HIX0009884.
HIX0171377.

HGNC

HGNC:5542. IGHMBP2.

MIM

600502. gene.
604320. phenotype.

neXtProt

NX_P38935.

Orphanet

98920. Spinal muscular atrophy with respiratory distress.

PharmGKB

PA29731.

GenAtlas

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Phylogenomic databases

eggNOG

COG1112.

HOGENOM

HOG000185831.

HOVERGEN

HBG077019.

InParanoid

P38935.

OMA

HARQRIS.

OrthoDB

EOG4GHZNJ.

PhylomeDB

P38935.

Gene expression databases

ArrayExpress

P38935.

Bgee

P38935.

CleanEx

HS_IGHMBP2.

Genevestigator

P38935.

GermOnline

ENSG00000132740. Homo sapiens.

Family and domain databases

Gene3D

4.10.1110.10. 1 hit.

InterPro

IPR003593. AAA+_ATPase.
IPR004483. DNA_helicase_put.
IPR014001. Helicase_ATP-bd.
IPR001374. R3H_ss-bd.
IPR026853. SMUBP-2.
IPR000058. Znf_AN1.
[Graphical view]

PANTHER

PTHR10887:SF23. PTHR10887:SF23. 1 hit.

Pfam

PF01424. R3H. 1 hit.
PF01428. zf-AN1. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
SM00487. DEXDc. 1 hit.
SM00393. R3H. 1 hit.
SM00154. ZnF_AN1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00376. TIGR00376. 1 hit.

PROSITE

PS51061. R3H. 1 hit.
PS51039. ZF_AN1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P38935.

GenomeRNAi

3508.

NextBio

13764.

SOURCE

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Entry information

Entry name

SMBP2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 141 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.