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Protein

DNA-binding protein SMUBP-2

Gene

IGHMBP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 221ATPBy similarity8
Zinc fingeri894 – 940AN1-typePROSITE-ProRule annotationAdd BLAST47

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • ATP-dependent 5'-3' DNA helicase activity Source: UniProtKB
  • ATP-dependent 5'-3' RNA helicase activity Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA-dependent ATPase activity Source: UniProtKB
  • DNA helicase activity Source: ProtInc
  • ribosome binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA-dependent ATPase activity Source: UniProtKB
  • single-stranded DNA binding Source: ProtInc
  • transcription factor binding Source: UniProtKB
  • tRNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • DNA recombination Source: ProtInc
  • DNA repair Source: ProtInc
  • DNA replication Source: ProtInc
  • protein homooligomerization Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: InterPro
  • transcription, DNA-templated Source: UniProtKB-KW
  • translation Source: UniProtKB
Complete GO annotation...

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000132740-MONOMER.
BRENDAi3.6.4.12. 2681.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:5542. IGHMBP2.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • growth cone Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Neuronopathy, distal hereditary motor, 6 (HMN6)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:604320
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05849717L → P in HMN6. 1 Publication1
Natural variantiVAR_022321192L → P in HMN6. 1 Publication1
Natural variantiVAR_058498196Q → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_022322213H → R in HMN6. 1 PublicationCorresponds to variant rs137852666dbSNPEnsembl.1
Natural variantiVAR_058499216P → L in HMN6. 1 Publication1
Natural variantiVAR_022323221T → A in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_022324241C → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_058500251L → P in HMN6. 1 Publication1
Natural variantiVAR_022325334E → K in HMN6. 1 Publication1
Natural variantiVAR_022326361L → P in HMN6. 2 PublicationsCorresponds to variant rs201060167dbSNPEnsembl.1
Natural variantiVAR_022327364L → P in HMN6. 1 Publication1
Natural variantiVAR_072695369F → L in HMN6. 1 PublicationCorresponds to variant rs137852670dbSNPEnsembl.1
Natural variantiVAR_022328382E → K in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_058501386W → R in HMN6. 1 PublicationCorresponds to variant rs759641927dbSNPEnsembl.1
Natural variantiVAR_022329426L → P in HMN6. 1 Publication1
Natural variantiVAR_058502445H → P in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 PublicationsCorresponds to variant rs571142182dbSNPEnsembl.1
Natural variantiVAR_058503472L → P in HMN6. 1 Publication1
Natural variantiVAR_058504493T → I in HMN6; does not affect activity; reduces protein steady-state levels. 2 PublicationsCorresponds to variant rs780594709dbSNPEnsembl.1
Natural variantiVAR_022330514E → K in HMN6. 1 PublicationCorresponds to variant rs137852665dbSNPEnsembl.1
Natural variantiVAR_022331565D → N in HMN6; does not affect ATPase activity; loss of helicase activity on RNA duplices. 3 PublicationsCorresponds to variant rs770111639dbSNPEnsembl.1
Natural variantiVAR_022332572Missing in HMN6. 1 Publication1
Natural variantiVAR_022333577L → P in HMN6. 2 Publications1
Natural variantiVAR_022334580V → I in HMN6. 1 PublicationCorresponds to variant rs137852667dbSNPEnsembl.1
Natural variantiVAR_058505581R → S in HMN6. 1 Publication1
Natural variantiVAR_022335583N → I in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_022336586G → C in HMN6. 1 Publication1
Natural variantiVAR_058506603R → C in HMN6. 1 Publication1
Natural variantiVAR_022337603R → H in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 PublicationsCorresponds to variant rs151079750dbSNPEnsembl.1
Natural variantiVAR_022338637R → C in HMN6. 2 PublicationsCorresponds to variant rs201563456dbSNPEnsembl.1
Natural variantiVAR_022339879T → K in HMN6. 1 PublicationCorresponds to variant rs17612126dbSNPEnsembl.1
Natural variantiVAR_022340974D → E in HMN6. 1 PublicationCorresponds to variant rs147674615dbSNPEnsembl.1
Charcot-Marie-Tooth disease 2S (CMT2S)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy.
See also OMIM:616155
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072694202F → V in CMT2S. 1 PublicationCorresponds to variant rs724159958dbSNPEnsembl.1
Natural variantiVAR_072696373V → G in CMT2S. 1 PublicationCorresponds to variant rs724159959dbSNPEnsembl.1
Natural variantiVAR_072697528A → T in CMT2S. 1 PublicationCorresponds to variant rs724159960dbSNPEnsembl.1

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

DisGeNETi3508.
MalaCardsiIGHMBP2.
MIMi604320. phenotype.
616155. phenotype.
OpenTargetsiENSG00000132740.
Orphaneti98920. Spinal muscular atrophy with respiratory distress type 1.
PharmGKBiPA29731.

Polymorphism and mutation databases

BioMutaiIGHMBP2.
DMDMi317373494.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000807012 – 993DNA-binding protein SMUBP-2Add BLAST992

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP38935.
MaxQBiP38935.
PaxDbiP38935.
PeptideAtlasiP38935.
PRIDEiP38935.

PTM databases

iPTMnetiP38935.
PhosphoSitePlusiP38935.

Expressioni

Tissue specificityi

Expressed in all tissues examined. Expressed in the developing and adult human brain, with highest expression in the cerebellum. Moderately expressed in fibroblasts.1 Publication

Gene expression databases

BgeeiENSG00000132740.
CleanExiHS_IGHMBP2.
ExpressionAtlasiP38935. baseline and differential.
GenevisibleiP38935. HS.

Organism-specific databases

HPAiHPA060994.

Interactioni

Subunit structurei

Homooligomer. Interacts with RUVBL1, RUVBL2, GTF3C1 and ABT1. Is part of large cytosolic ribonucleoprotein complexes (Probable). Associates with the ribosomes.Curated2 Publications

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109728. 14 interactors.
IntActiP38935. 5 interactors.
STRINGi9606.ENSP00000255078.

Structurei

Secondary structure

1993
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 33Combined sources30
Helixi37 – 40Combined sources4
Helixi41 – 43Combined sources3
Beta strandi45 – 57Combined sources13
Beta strandi59 – 61Combined sources3
Beta strandi63 – 70Combined sources8
Beta strandi71 – 74Combined sources4
Beta strandi88 – 93Combined sources6
Turni94 – 97Combined sources4
Beta strandi102 – 110Combined sources9
Beta strandi113 – 117Combined sources5
Beta strandi134 – 139Combined sources6
Helixi142 – 156Combined sources15
Beta strandi160 – 162Combined sources3
Helixi164 – 170Combined sources7
Beta strandi172 – 174Combined sources3
Helixi194 – 205Combined sources12
Beta strandi207 – 213Combined sources7
Helixi220 – 233Combined sources14
Beta strandi238 – 244Combined sources7
Helixi245 – 257Combined sources13
Beta strandi262 – 264Combined sources3
Helixi273 – 276Combined sources4
Helixi280 – 284Combined sources5
Turni285 – 288Combined sources4
Helixi293 – 300Combined sources8
Beta strandi302 – 304Combined sources3
Turni305 – 308Combined sources4
Helixi320 – 344Combined sources25
Beta strandi346 – 351Combined sources6
Turni352 – 355Combined sources4
Beta strandi357 – 359Combined sources3
Helixi360 – 363Combined sources4
Beta strandi370 – 374Combined sources5
Helixi377 – 379Combined sources3
Helixi382 – 385Combined sources4
Turni386 – 388Combined sources3
Helixi389 – 391Combined sources3
Beta strandi392 – 399Combined sources8
Helixi411 – 415Combined sources5
Turni416 – 419Combined sources4
Helixi422 – 430Combined sources9
Helixi431 – 433Combined sources3
Beta strandi435 – 437Combined sources3
Beta strandi440 – 444Combined sources5
Helixi446 – 456Combined sources11
Turni465 – 469Combined sources5
Helixi472 – 474Combined sources3
Turni482 – 485Combined sources4
Beta strandi487 – 492Combined sources6
Helixi512 – 527Combined sources16
Helixi532 – 534Combined sources3
Beta strandi535 – 540Combined sources6
Helixi542 – 552Combined sources11
Turni553 – 555Combined sources3
Beta strandi560 – 563Combined sources4
Helixi564 – 567Combined sources4
Beta strandi572 – 578Combined sources7
Turni589 – 592Combined sources4
Helixi594 – 602Combined sources9
Beta strandi604 – 612Combined sources9
Helixi614 – 617Combined sources4
Helixi621 – 632Combined sources12
Beta strandi633 – 638Combined sources6
Helixi639 – 641Combined sources3
Helixi727 – 739Combined sources13
Beta strandi742 – 746Combined sources5
Helixi753 – 764Combined sources12
Beta strandi767 – 772Combined sources6
Beta strandi774 – 776Combined sources3
Beta strandi779 – 784Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MSZNMR-A711-786[»]
2LRRNMR-A711-786[»]
4B3FX-ray2.50X3-648[»]
4B3GX-ray2.85A/B3-648[»]
ProteinModelPortaliP38935.
SMRiP38935.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38935.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini723 – 786R3HPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni638 – 785SS DNA-bindingBy similarityAdd BLAST148

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi864 – 868Nuclear localization signalSequence analysis5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi251 – 426Leu-richAdd BLAST176
Compositional biasi795 – 859Gln/Pro-richAdd BLAST65
Compositional biasi864 – 870Poly-Lys7

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)DescriptionActionsGraphical viewLength
Zinc fingeri894 – 940AN1-typePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1803. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00820000127110.
HOGENOMiHOG000185831.
HOVERGENiHBG077019.
InParanoidiP38935.
KOiK19036.
OMAiYCLSHHI.
OrthoDBiEOG091G01DF.
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.
IPR033098. IGHMBP2.
IPR027417. P-loop_NTPase.
IPR001374. R3H_dom.
IPR004483. SMUBP-2/Hcs1-like.
IPR000058. Znf_AN1.
[Graphical view]
PANTHERiPTHR10887:SF375. PTHR10887:SF375. 1 hit.
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

        10         20         30         40         50
MASAAVESFV TKQLDLLELE RDAEVEERRS WQENISLKEL QSRGVCLLKL
60 70 80 90 100
QVSSQRTGLY GRLLVTFEPR RYGSAAALPS NSFTSGDIVG LYDAANEGSQ
110 120 130 140 150
LATGILTRVT QKSVTVAFDE SHDFQLSLDR ENSYRLLKLA NDVTYRRLKK
160 170 180 190 200
ALIALKKYHS GPASSLIEVL FGRSAPSPAS EIHPLTFFNT CLDTSQKEAV
210 220 230 240 250
LFALSQKELA IIHGPPGTGK TTTVVEIILQ AVKQGLKVLC CAPSNIAVDN
260 270 280 290 300
LVERLALCKQ RILRLGHPAR LLESIQQHSL DAVLARSDSA QIVADIRKDI
310 320 330 340 350
DQVFVKNKKT QDKREKSNFR NEIKLLRKEL KEREEAAMLE SLTSANVVLA
360 370 380 390 400
TNTGASADGP LKLLPESYFD VVVIDECAQA LEASCWIPLL KARKCILAGD
410 420 430 440 450
HKQLPPTTVS HKAALAGLSL SLMERLAEEY GARVVRTLTV QYRMHQAIMR
460 470 480 490 500
WASDTMYLGQ LTAHSSVARH LLRDLPGVAA TEETGVPLLL VDTAGCGLFE
510 520 530 540 550
LEEEDEQSKG NPGEVRLVSL HIQALVDAGV PARDIAVVSP YNLQVDLLRQ
560 570 580 590 600
SLVHRHPELE IKSVDGFQGR EKEAVILSFV RSNRKGEVGF LAEDRRINVA
610 620 630 640 650
VTRARRHVAV ICDSRTVNNH AFLKTLVEYF TQHGEVRTAF EYLDDIVPEN
660 670 680 690 700
YSHENSQGSS HAATKPQGPA TSTRTGSQRQ EGGQEAAAPA RQGRKKPAGK
710 720 730 740 750
SLASEAPSQP SLNGGSPEGV ESQDGVDHFR AMIVEFMASK KMQLEFPPSL
760 770 780 790 800
NSHDRLRVHQ IAEEHGLRHD SSGEGKRRFI TVSKRAPRPR AALGPPAGTG
810 820 830 840 850
GPAPLQPVPP TPAQTEQPPR EQRGPDQPDL RTLHLERLQR VRSAQGQPAS
860 870 880 890 900
KEQQASGQQK LPEKKKKKAK GHPATDLPTE EDFEALVSAA VKADNTCGFA
910 920 930 940 950
KCTAGVTTLG QFCQLCSRRY CLSHHLPEIH GCGERARAHA RQRISREGVL
960 970 980 990
YAGSGTKNGS LDPAKRAQLQ RRLDKKLSEL SNQRTSRRKE RGT
Length:993
Mass (Da):109,149
Last modified:January 11, 2011 - v3
Checksum:iDE785579EE60E26F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti292I → N in AAA53082 (PubMed:8349627).Curated1
Sequence conflicti461L → V in AAA53082 (PubMed:8349627).Curated1
Sequence conflicti491 – 494VDTA → GGRV in AAA58611 (PubMed:1714899).Curated4
Sequence conflicti863E → K in AAA58611 (PubMed:1714899).Curated1
Sequence conflicti866K → T in AAA58611 (PubMed:1714899).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05849717L → P in HMN6. 1 Publication1
Natural variantiVAR_05522575A → T.Corresponds to variant rs2228206dbSNPEnsembl.1
Natural variantiVAR_022321192L → P in HMN6. 1 Publication1
Natural variantiVAR_058498196Q → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_024242201L → S.1 PublicationCorresponds to variant rs560096dbSNPEnsembl.1
Natural variantiVAR_072694202F → V in CMT2S. 1 PublicationCorresponds to variant rs724159958dbSNPEnsembl.1
Natural variantiVAR_022322213H → R in HMN6. 1 PublicationCorresponds to variant rs137852666dbSNPEnsembl.1
Natural variantiVAR_058499216P → L in HMN6. 1 Publication1
Natural variantiVAR_022323221T → A in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_022324241C → R in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_058500251L → P in HMN6. 1 Publication1
Natural variantiVAR_024243275I → V.1 PublicationCorresponds to variant rs10896380dbSNPEnsembl.1
Natural variantiVAR_022325334E → K in HMN6. 1 Publication1
Natural variantiVAR_022326361L → P in HMN6. 2 PublicationsCorresponds to variant rs201060167dbSNPEnsembl.1
Natural variantiVAR_022327364L → P in HMN6. 1 Publication1
Natural variantiVAR_072695369F → L in HMN6. 1 PublicationCorresponds to variant rs137852670dbSNPEnsembl.1
Natural variantiVAR_072696373V → G in CMT2S. 1 PublicationCorresponds to variant rs724159959dbSNPEnsembl.1
Natural variantiVAR_022328382E → K in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_058501386W → R in HMN6. 1 PublicationCorresponds to variant rs759641927dbSNPEnsembl.1
Natural variantiVAR_022329426L → P in HMN6. 1 Publication1
Natural variantiVAR_058502445H → P in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 PublicationsCorresponds to variant rs571142182dbSNPEnsembl.1
Natural variantiVAR_058503472L → P in HMN6. 1 Publication1
Natural variantiVAR_058504493T → I in HMN6; does not affect activity; reduces protein steady-state levels. 2 PublicationsCorresponds to variant rs780594709dbSNPEnsembl.1
Natural variantiVAR_022330514E → K in HMN6. 1 PublicationCorresponds to variant rs137852665dbSNPEnsembl.1
Natural variantiVAR_072697528A → T in CMT2S. 1 PublicationCorresponds to variant rs724159960dbSNPEnsembl.1
Natural variantiVAR_055226557P → A.Corresponds to variant rs7122089dbSNPEnsembl.1
Natural variantiVAR_022331565D → N in HMN6; does not affect ATPase activity; loss of helicase activity on RNA duplices. 3 PublicationsCorresponds to variant rs770111639dbSNPEnsembl.1
Natural variantiVAR_022332572Missing in HMN6. 1 Publication1
Natural variantiVAR_022333577L → P in HMN6. 2 Publications1
Natural variantiVAR_022334580V → I in HMN6. 1 PublicationCorresponds to variant rs137852667dbSNPEnsembl.1
Natural variantiVAR_058505581R → S in HMN6. 1 Publication1
Natural variantiVAR_022335583N → I in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 Publications1
Natural variantiVAR_022336586G → C in HMN6. 1 Publication1
Natural variantiVAR_058506603R → C in HMN6. 1 Publication1
Natural variantiVAR_022337603R → H in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices. 2 PublicationsCorresponds to variant rs151079750dbSNPEnsembl.1
Natural variantiVAR_022338637R → C in HMN6. 2 PublicationsCorresponds to variant rs201563456dbSNPEnsembl.1
Natural variantiVAR_020147671T → A.Corresponds to variant rs622082dbSNPEnsembl.1
Natural variantiVAR_021899694R → W.Corresponds to variant rs2236654dbSNPEnsembl.1
Natural variantiVAR_022339879T → K in HMN6. 1 PublicationCorresponds to variant rs17612126dbSNPEnsembl.1
Natural variantiVAR_021900928E → K.Corresponds to variant rs2275996dbSNPEnsembl.1
Natural variantiVAR_022340974D → E in HMN6. 1 PublicationCorresponds to variant rs147674615dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MSZNMR-A711-786[»]
2LRRNMR-A711-786[»]
4B3FX-ray2.50X3-648[»]
4B3GX-ray2.85A/B3-648[»]
ProteinModelPortaliP38935.
SMRiP38935.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109728. 14 interactors.
IntActiP38935. 5 interactors.
STRINGi9606.ENSP00000255078.

PTM databases

iPTMnetiP38935.
PhosphoSitePlusiP38935.

Polymorphism and mutation databases

BioMutaiIGHMBP2.
DMDMi317373494.

Proteomic databases

EPDiP38935.
MaxQBiP38935.
PaxDbiP38935.
PeptideAtlasiP38935.
PRIDEiP38935.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255078; ENSP00000255078; ENSG00000132740.
GeneIDi3508.
KEGGihsa:3508.
UCSCiuc001ook.2. human.

Organism-specific databases

CTDi3508.
DisGeNETi3508.
GeneCardsiIGHMBP2.
H-InvDBHIX0009884.
HIX0171377.
HGNCiHGNC:5542. IGHMBP2.
HPAiHPA060994.
MalaCardsiIGHMBP2.
MIMi600502. gene.
604320. phenotype.
616155. phenotype.
neXtProtiNX_P38935.
OpenTargetsiENSG00000132740.
Orphaneti98920. Spinal muscular atrophy with respiratory distress type 1.
PharmGKBiPA29731.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1803. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00820000127110.
HOGENOMiHOG000185831.
HOVERGENiHBG077019.
InParanoidiP38935.
KOiK19036.
OMAiYCLSHHI.
OrthoDBiEOG091G01DF.
PhylomeDBiP38935.
TreeFamiTF105388.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000132740-MONOMER.
BRENDAi3.6.4.12. 2681.

Miscellaneous databases

ChiTaRSiIGHMBP2. human.
EvolutionaryTraceiP38935.
GeneWikiiIGHMBP2.
GenomeRNAii3508.
PROiP38935.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132740.
CleanExiHS_IGHMBP2.
ExpressionAtlasiP38935. baseline and differential.
GenevisibleiP38935. HS.

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.
IPR033098. IGHMBP2.
IPR027417. P-loop_NTPase.
IPR001374. R3H_dom.
IPR004483. SMUBP-2/Hcs1-like.
IPR000058. Znf_AN1.
[Graphical view]
PANTHERiPTHR10887:SF375. PTHR10887:SF375. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 179 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.