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P38935

- SMBP2_HUMAN

UniProt

P38935 - SMBP2_HUMAN

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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

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. ribosome binding Source: UniProtKB
  8. RNA binding Source: UniProtKB
  9. RNA-dependent ATPase activity Source: UniProtKB
  10. single-stranded DNA binding Source: ProtInc
  11. transcription factor binding Source: UniProtKB
  12. tRNA binding Source: UniProtKB
  13. 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
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

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
Complete GO annotation...

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 type 1.
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

BgeeiP38935.
CleanExiHS_IGHMBP2.
ExpressionAtlasiP38935. baseline and differential.
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. 2 interactions.
IntActiP38935. 1 interaction.
STRINGi9606.ENSP00000255078.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00730000111172.
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

        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)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:
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.1. human.

Polymorphism databases

DMDMi317373494.

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 .
CCDSi CCDS8187.1.
PIRi A47500.
RefSeqi NP_002171.2. NM_002180.2.
UniGenei Hs.503048.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 2 interactions.
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 type 1.
PharmGKBi PA29731.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1112.
GeneTreei ENSGT00730000111172.
HOGENOMi HOG000185831.
HOVERGENi HBG077019.
InParanoidi P38935.
OMAi LSHHIPE.
OrthoDBi EOG7M6D6M.
PhylomeDBi P38935.
TreeFami TF105388.

Miscellaneous databases

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

Gene expression databases

Bgeei P38935.
CleanExi HS_IGHMBP2.
ExpressionAtlasi P38935. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 157 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

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