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O75147

- OBSL1_HUMAN

UniProt

O75147 - OBSL1_HUMAN

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Protein

Obscurin-like protein 1

Gene

OBSL1

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

Functioni

Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons.3 Publications

GO - Molecular functioni

  1. cytoskeletal adaptor activity Source: BHF-UCL

GO - Biological processi

  1. cardiac myofibril assembly Source: BHF-UCL
  2. cytoskeleton organization Source: BHF-UCL
  3. Golgi organization Source: UniProtKB
  4. microtubule cytoskeleton organization Source: UniProtKB
  5. positive regulation of dendrite morphogenesis Source: UniProtKB
  6. protein localization to Golgi apparatus Source: UniProtKB
  7. regulation of mitosis Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Obscurin-like protein 1
Gene namesi
Name:OBSL1
Synonyms:KIAA0657
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:29092. OBSL1.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmperinuclear region. Golgi apparatus
Note: Colocalizes with CUL7 at the Golgi apparatus in neurons.

GO - Cellular componenti

  1. 3M complex Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. Golgi apparatus Source: UniProtKB
  5. intercalated disc Source: BHF-UCL
  6. M band Source: BHF-UCL
  7. perinuclear region of cytoplasm Source: UniProtKB
  8. Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

Pathology & Biotechi

Involvement in diseasei

3M syndrome 2 (3M2) [MIM:612921]: An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171F → R: Diminishes binding affinity for TTN. 1 Publication

Keywords - Diseasei

Dwarfism

Organism-specific databases

MIMi612921. phenotype.
Orphaneti2616. 3M syndrome.
PharmGKBiPA142671235.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18961896Obscurin-like protein 1PRO_0000247959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine1 Publication
Disulfide bondi33 ↔ 84PROSITE-ProRule annotation
Disulfide bondi149 ↔ 209PROSITE-ProRule annotation
Disulfide bondi267 ↔ 319PROSITE-ProRule annotation
Disulfide bondi362 ↔ 412PROSITE-ProRule annotation
Disulfide bondi738 ↔ 788PROSITE-ProRule annotation
Disulfide bondi829 ↔ 879PROSITE-ProRule annotation
Disulfide bondi920 ↔ 970PROSITE-ProRule annotation
Disulfide bondi1011 ↔ 1061PROSITE-ProRule annotation
Disulfide bondi1103 ↔ 1153PROSITE-ProRule annotation
Disulfide bondi1195 ↔ 1245PROSITE-ProRule annotation
Disulfide bondi1381 ↔ 1522PROSITE-ProRule annotation
Disulfide bondi1650 ↔ 1700PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiO75147.
PaxDbiO75147.
PRIDEiO75147.

PTM databases

PhosphoSiteiO75147.

Expressioni

Tissue specificityi

Widely expressed, with predominant levels found in the heart.1 Publication

Gene expression databases

BgeeiO75147.
CleanExiHS_OBSL1.
ExpressionAtlasiO75147. baseline and differential.
GenevestigatoriO75147.

Organism-specific databases

HPAiHPA036404.
HPA036405.

Interactioni

Subunit structurei

Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Interacts with CCDC8. Interacts with CUL7; the interaction is direct. Interacts with FBXW8. Interacts (via N-terminal Ig-like domain) with TTN/titin (via C-terminal Ig-like domain); the interaction is direct.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TTNQ8WZ428EBI-1223896,EBI-681210

Protein-protein interaction databases

BioGridi116944. 25 interactions.
DIPiDIP-38340N.
IntActiO75147. 11 interactions.
MINTiMINT-7979572.
STRINGi9606.ENSP00000385636.

Structurei

Secondary structure

1
1896
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 167Combined sources
Beta strandi21 – 244Combined sources
Beta strandi29 – 3911Combined sources
Beta strandi42 – 476Combined sources
Beta strandi56 – 594Combined sources
Beta strandi66 – 738Combined sources
Helixi76 – 783Combined sources
Beta strandi80 – 889Combined sources
Beta strandi91 – 10212Combined sources
Beta strandi618 – 6203Combined sources
Beta strandi625 – 6284Combined sources
Beta strandi632 – 64110Combined sources
Beta strandi646 – 6516Combined sources
Beta strandi669 – 6724Combined sources
Beta strandi678 – 6858Combined sources
Beta strandi692 – 6998Combined sources
Beta strandi702 – 71110Combined sources
Beta strandi724 – 7329Combined sources
Beta strandi748 – 7514Combined sources
Beta strandi762 – 7676Combined sources
Beta strandi770 – 7778Combined sources
Turni780 – 7823Combined sources
Beta strandi784 – 7896Combined sources
Beta strandi797 – 8026Combined sources
Beta strandi815 – 8184Combined sources
Beta strandi825 – 8306Combined sources
Beta strandi839 – 8424Combined sources
Beta strandi854 – 8585Combined sources
Beta strandi861 – 8688Combined sources
Helixi871 – 8733Combined sources
Beta strandi875 – 8806Combined sources
Beta strandi885 – 8917Combined sources
Beta strandi898 – 9025Combined sources
Beta strandi906 – 9116Combined sources
Beta strandi916 – 9238Combined sources
Beta strandi930 – 9334Combined sources
Beta strandi944 – 9485Combined sources
Beta strandi950 – 95910Combined sources
Turni962 – 9643Combined sources
Beta strandi966 – 9749Combined sources
Beta strandi976 – 9849Combined sources
Beta strandi1279 – 12813Combined sources
Beta strandi1287 – 12904Combined sources
Beta strandi1301 – 13044Combined sources
Beta strandi1313 – 13197Combined sources
Beta strandi1324 – 13307Combined sources
Beta strandi1337 – 13426Combined sources
Turni1344 – 13463Combined sources
Beta strandi1348 – 13547Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPCNMR-A893-992[»]
2E6PNMR-A714-804[»]
2E6QNMR-A615-713[»]
2LU7NMR-A1277-1357[»]
2LVCNMR-A805-892[»]
2WP3X-ray1.48O1-106[»]
2WWKX-ray1.70O1-106[»]
2WWMX-ray2.30C/O1-106[»]
3KNBX-ray1.40B1-105[»]
ProteinModelPortaliO75147.
SMRiO75147. Positions 8-103, 608-1074, 1277-1357.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75147.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 10089Ig-like 1Add
BLAST
Domaini128 – 22598Ig-like 2Add
BLAST
Domaini243 – 33088Ig-like 3Add
BLAST
Domaini339 – 42587Ig-like 4Add
BLAST
Domaini517 – 61599Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST
Domaini714 – 80087Ig-like 5Add
BLAST
Domaini804 – 89390Ig-like 6Add
BLAST
Domaini902 – 98281Ig-like 7Add
BLAST
Domaini986 – 107590Ig-like 8Add
BLAST
Domaini1078 – 117295Ig-like 9Add
BLAST
Domaini1174 – 126188Ig-like 10Add
BLAST
Domaini1265 – 135793Ig-like 11Add
BLAST
Domaini1357 – 1534178Ig-like 12Add
BLAST
Domaini1628 – 172093Ig-like 13Add
BLAST
Domaini1794 – 1896103Ig-like 14Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 193Interaction with TTN
Regioni85 – 9410Interaction with TTN

Sequence similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119215.
HOGENOMiHOG000263472.
HOVERGENiHBG082081.
InParanoidiO75147.
OMAiETSFIYR.
OrthoDBiEOG744T84.
PhylomeDBiO75147.

Family and domain databases

Gene3Di2.60.40.10. 20 hits.
InterProiIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF07679. I-set. 15 hits.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 12 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
PROSITEiPS50853. FN3. 1 hit.
PS50835. IG_LIKE. 14 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75147-3) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKASSGDQGS PPCFLRFPRP VRVVSGAEAE LKCVVLGEPP PVVVWEKGGQ
60 70 80 90 100
QLAASERLSF PADGAEHGLL LTAALPTDAG VYVCRARNAA GEAYAAAAVT
110 120 130 140 150
VLEPPASDPE LQPAERPLPS PGSGEGAPVF LTGPRSQWVL RGAEVVLTCR
160 170 180 190 200
AGGLPEPTLY WEKDGMALDE VWDSSHFALQ PGRAEDGPGA SLALRILAAR
210 220 230 240 250
LPDSGVYVCH ARNAHGHAQA GALLQVHQPP ESPPADPDEA PAPVVEPLKC
260 270 280 290 300
APKTFWVNEG KHAKFRCYVM GKPEPEIEWH WEGRPLLPDR RRLMYRDRDG
310 320 330 340 350
GFVLKVLYCQ AKDRGLYVCA ARNSAGQTLS AVQLHVKEPR LRFTRPLQDV
360 370 380 390 400
EGREHGIAVL ECKVPNSRIP TAWFREDQRL LPCRKYEQIE EGTVRRLIIH
410 420 430 440 450
RLKADDDGIY LCEMRGRVRT VANVTVKGPI LKRLPRKLDV LEGENAVLLV
460 470 480 490 500
ETLEAGVEGR WSRDGEELPV ICQSSSGHMH ALVLPGVTRE DAGEVTFSLG
510 520 530 540 550
NSRTTTLLRV KCVKHSPPGP PILAEMFKGH KNTVLLTWKP PEPAPETPFI
560 570 580 590 600
YRLERQEVGS EDWIQCFSIE KAGAVEVPGD CVPSEGDYRF RICTVSGHGR
610 620 630 640 650
SPHVVFHGSA HLVPTARLVA GLEDVQVYDG EDAVFSLDLS TIIQGTWFLN
660 670 680 690 700
GEELKSNEPE GQVEPGALRY RIEQKGLQHR LILHAVKHQD SGALVGFSCP
710 720 730 740 750
GVQDSAALTI QESPVHILSP QDRVSLTFTT SERVVLTCEL SRVDFPATWY
760 770 780 790 800
KDGQKVEESE LLVVKMDGRK HRLILPEAKV QDSGEFECRT EGVSAFFGVT
810 820 830 840 850
VQDPPVHIVD PREHVFVHAI TSECVMLACE VDREDAPVRW YKDGQEVEES
860 870 880 890 900
DFVVLENEGP HRRLVLPATQ PSDGGEFQCV AGDECAYFTV TITDVSSWIV
910 920 930 940 950
YPSGKVYVAA VRLERVVLTC ELCRPWAEVR WTKDGEEVVE SPALLLQKED
960 970 980 990 1000
TVRRLVLPAV QLEDSGEYLC EIDDESASFT VTVTEPPVRI IYPRDEVTLI
1010 1020 1030 1040 1050
AVTLECVVLM CELSREDAPV RWYKDGLEVE ESEALVLERD GPRCRLVLPA
1060 1070 1080 1090 1100
AQPEDGGEFV CDAGDDSAFF TVTVTAPPER IVHPAARSLD LHFGAPGRVE
1110 1120 1130 1140 1150
LRCEVAPAGS QVRWYKDGLE VEASDALQLG AEGPTRTLTL PHAQPEDAGE
1160 1170 1180 1190 1200
YVCETRHEAI TFNVILAEPP VQFLALETTP SPLCVAPGEP VVLSCELSRA
1210 1220 1230 1240 1250
GAPVVWSHNG RPVQEGEGLE LHAEGPRRVL CIQAAGPAHA GLYTCQSGAA
1260 1270 1280 1290 1300
PGAPSLSFTV QVAEPPVRVV APEAAQTRVR STPGGDLELV VHLSGPGGPV
1310 1320 1330 1340 1350
RWYKDGERLA SQGRVQLEQA GARQVLRVQG ARSGDAGEYL CDAPQDSRIF
1360 1370 1380 1390 1400
LVSVEEPLLV KLVSELTPLT VHEGDDATFR CEVSPPDADV TWLRNGAVVT
1410 1420 1430 1440 1450
PGPQVEMAQN GSSRILTLRG CQLGDAGTVT LRAGSTATSA RLHVRETELL
1460 1470 1480 1490 1500
FLRRLQDVRA EEGQDVCLEV ETGRVGAAGA VRWVRGGQPL PHDSRLSMAQ
1510 1520 1530 1540 1550
DGHIHRLFIH GVILADQGTY GCESHHDRTL ARLSVRPRQL RVLRPLEDVT
1560 1570 1580 1590 1600
ISEGGSATFQ LELSQEGVTG EWARGGVQLY PGPKCHIHSD GHRHRLVLNG
1610 1620 1630 1640 1650
LGLADSGCVS FTADSLRCAA RLIVREVPVT IVRGPHDLEV TEGDTATFEC
1660 1670 1680 1690 1700
ELSQALADVT WEKDGNALTP SPRLRLQALG TRRLLQLRRC GPSDAGTYSC
1710 1720 1730 1740 1750
AVGTARAGPV RLTVRERTVA VLSELRSVSA REGDGATFEC TVSEVETTGR
1760 1770 1780 1790 1800
WELGGRPLRP GARVRIRQEG KKHILVLSEL RAEDAGEVRF QAGPAQSLAL
1810 1820 1830 1840 1850
LEVEALPLQM CRHPPREKTV LVGRRAVLEV TVSRSGGHVC WLREGAELCP
1860 1870 1880 1890
GDKYEMRSHG PTHSLVIHDV RPEDQGTYCC QAGQDSTHTR LLVEGN
Length:1,896
Mass (Da):206,947
Last modified:April 5, 2011 - v4
Checksum:i6D592AC3E30E9ACA
GO
Isoform 2 (identifier: O75147-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     986-1025: PPVRIIYPRD...EDAPVRWYKD → SYQSQDSSNN...PPWRRTAGTE
     1026-1896: Missing.

Show »
Length:1,025
Mass (Da):113,273
Checksum:iCAF2D3D8E1920335
GO
Isoform 3 (identifier: O75147-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1076-1167: Missing.
     1405-1493: VEMAQNGSSR...VRGGQPLPHD → RQSCCSYGGC...TTIAPWPGSA
     1494-1896: Missing.

Show »
Length:1,401
Mass (Da):152,925
Checksum:i3AE3886DF8C0B8A8
GO
Isoform 4 (identifier: O75147-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1537-1543: PRQLRVL → RECPVLS
     1544-1896: Missing.

Show »
Length:1,543
Mass (Da):168,521
Checksum:i8DAB399C567C8CDD
GO

Sequence cautioni

The sequence AAH07201.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651G → R in BAA31632. (PubMed:9734811)Curated
Sequence conflicti512 – 5121C → CG in ABO42327. (PubMed:17289344)Curated
Sequence conflicti723 – 7231R → K in AAH07201. (PubMed:15489334)Curated
Sequence conflicti723 – 7231R → K in BAA31632. (PubMed:9734811)Curated
Sequence conflicti1365 – 13651E → D in BAA31632. (PubMed:9734811)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei986 – 102540PPVRI…RWYKD → SYQSQDSSNNNPELCVLLKK PKTRRLWSRFPPWRRTAGTE in isoform 2. 1 PublicationVSP_040784Add
BLAST
Alternative sequencei1026 – 1896871Missing in isoform 2. 1 PublicationVSP_040785Add
BLAST
Alternative sequencei1076 – 116792Missing in isoform 3. 1 PublicationVSP_040786Add
BLAST
Alternative sequencei1405 – 149389VEMAQ…PLPHD → RQSCCSYGGCRMCGQRKART CVSKWRQAEWVQRGPCAGCE VGSPCPTTLACPWPRMGTST ASSSMVSYWPTRAPTAARAT TIAPWPGSA in isoform 3. 1 PublicationVSP_040787Add
BLAST
Alternative sequencei1494 – 1896403Missing in isoform 3. 1 PublicationVSP_040788Add
BLAST
Alternative sequencei1537 – 15437PRQLRVL → RECPVLS in isoform 4. 1 PublicationVSP_054755
Alternative sequencei1544 – 1896353Missing in isoform 4. 1 PublicationVSP_054756Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF063637 mRNA. Translation: ABO42327.1.
EF063638 mRNA. Translation: ABO42328.1.
AC009955 Genomic DNA. No translation available.
BC007201 mRNA. Translation: AAH07201.1. Different initiation.
AB014557 mRNA. Translation: BAA31632.2.
CCDSiCCDS46520.1. [O75147-3]
CCDS54433.1. [O75147-2]
CCDS63134.1. [O75147-4]
RefSeqiNP_001166879.1. NM_001173408.1. [O75147-2]
NP_001166902.1. NM_001173431.1. [O75147-4]
NP_056126.1. NM_015311.2. [O75147-3]
UniGeneiHs.526594.

Genome annotation databases

EnsembliENST00000373873; ENSP00000362980; ENSG00000124006. [O75147-2]
ENST00000404537; ENSP00000385636; ENSG00000124006. [O75147-3]
ENST00000603926; ENSP00000474519; ENSG00000124006. [O75147-4]
GeneIDi23363.
KEGGihsa:23363.
UCSCiuc002vmi.3. human. [O75147-2]
uc010fwk.3. human. [O75147-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF063637 mRNA. Translation: ABO42327.1 .
EF063638 mRNA. Translation: ABO42328.1 .
AC009955 Genomic DNA. No translation available.
BC007201 mRNA. Translation: AAH07201.1 . Different initiation.
AB014557 mRNA. Translation: BAA31632.2 .
CCDSi CCDS46520.1. [O75147-3 ]
CCDS54433.1. [O75147-2 ]
CCDS63134.1. [O75147-4 ]
RefSeqi NP_001166879.1. NM_001173408.1. [O75147-2 ]
NP_001166902.1. NM_001173431.1. [O75147-4 ]
NP_056126.1. NM_015311.2. [O75147-3 ]
UniGenei Hs.526594.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CPC NMR - A 893-992 [» ]
2E6P NMR - A 714-804 [» ]
2E6Q NMR - A 615-713 [» ]
2LU7 NMR - A 1277-1357 [» ]
2LVC NMR - A 805-892 [» ]
2WP3 X-ray 1.48 O 1-106 [» ]
2WWK X-ray 1.70 O 1-106 [» ]
2WWM X-ray 2.30 C/O 1-106 [» ]
3KNB X-ray 1.40 B 1-105 [» ]
ProteinModelPortali O75147.
SMRi O75147. Positions 8-103, 608-1074, 1277-1357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116944. 25 interactions.
DIPi DIP-38340N.
IntActi O75147. 11 interactions.
MINTi MINT-7979572.
STRINGi 9606.ENSP00000385636.

PTM databases

PhosphoSitei O75147.

Proteomic databases

MaxQBi O75147.
PaxDbi O75147.
PRIDEi O75147.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373873 ; ENSP00000362980 ; ENSG00000124006 . [O75147-2 ]
ENST00000404537 ; ENSP00000385636 ; ENSG00000124006 . [O75147-3 ]
ENST00000603926 ; ENSP00000474519 ; ENSG00000124006 . [O75147-4 ]
GeneIDi 23363.
KEGGi hsa:23363.
UCSCi uc002vmi.3. human. [O75147-2 ]
uc010fwk.3. human. [O75147-3 ]

Organism-specific databases

CTDi 23363.
GeneCardsi GC02M220415.
GeneReviewsi OBSL1.
H-InvDB HIX0002869.
HIX0161860.
HGNCi HGNC:29092. OBSL1.
HPAi HPA036404.
HPA036405.
MIMi 610991. gene.
612921. phenotype.
neXtProti NX_O75147.
Orphaneti 2616. 3M syndrome.
PharmGKBi PA142671235.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000119215.
HOGENOMi HOG000263472.
HOVERGENi HBG082081.
InParanoidi O75147.
OMAi ETSFIYR.
OrthoDBi EOG744T84.
PhylomeDBi O75147.

Miscellaneous databases

ChiTaRSi OBSL1. human.
EvolutionaryTracei O75147.
GeneWikii OBSL1.
GenomeRNAii 23363.
NextBioi 45409.
PROi O75147.
SOURCEi Search...

Gene expression databases

Bgeei O75147.
CleanExi HS_OBSL1.
ExpressionAtlasi O75147. baseline and differential.
Genevestigatori O75147.

Family and domain databases

Gene3Di 2.60.40.10. 20 hits.
InterProi IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view ]
Pfami PF07679. I-set. 15 hits.
[Graphical view ]
SMARTi SM00060. FN3. 1 hit.
SM00409. IG. 12 hits.
SM00408. IGc2. 6 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
PROSITEi PS50853. FN3. 1 hit.
PS50835. IG_LIKE. 14 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Obscurin-like 1, OBSL1, is a novel cytoskeletal protein related to obscurin."
    Geisler S.B., Robinson D., Hauringa M., Raeker M.O., Borisov A.B., Westfall M.V., Russell M.W.
    Genomics 89:521-531(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), TISSUE SPECIFICITY.
    Tissue: Heart.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 2).
    Tissue: Muscle.
  4. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-1896 (ISOFORM 3).
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "The primordial growth disorder 3-M syndrome connects ubiquitination to the cytoskeletal adaptor OBSL1."
    Hanson D., Murray P.G., Sud A., Temtamy S.A., Aglan M., Superti-Furga A., Holder S.E., Urquhart J., Hilton E., Manson F.D.C., Scambler P., Black G.C.M., Clayton P.E.
    Am. J. Hum. Genet. 84:801-806(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN 3M2.
  8. "Exome sequencing identifies CCDC8 mutations in 3-M syndrome, Suggesting that CCDC8 Contributes in a Pathway with CUL7 and OBSL1 to Control Human Growth."
    Hanson D., Murray P.G., O'Sullivan J., Urquhart J., Daly S., Bhaskar S.S., Biesecker L.G., Skae M., Smith C., Cole T., Kirk J., Chandler K., Kingston H., Donnai D., Clayton P.E., Black G.C.
    Am. J. Hum. Genet. 89:148-153(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC8 AND CUL7.
  9. "An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterning."
    Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E., Gygi S.P., Harper J.W., Bonni A.
    PLoS Biol. 9:E1001060-E1001060(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FBXW8 AND CUL7, SUBCELLULAR LOCATION.
  10. Cited for: FUNCTION, IDENTIFICATION IN THE 3M COMPLEX, SUBCELLULAR LOCATION.
  11. "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin to maintain genome integrity."
    Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., Xiong Y.
    Mol. Cell 54:805-819(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: INVOLVEMENT IN 3M2.
  13. "Solution structure of Ig-like domains from human obscurin-like protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 615-992.
  14. "Molecular basis of the head-to-tail assembly of giant muscle proteins obscurin-like 1 and titin."
    Sauer F., Vahokoski J., Song Y.H., Wilmanns M.
    EMBO Rep. 11:534-540(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-105 IN COMPLEX WITH THE C-TERMINAL IG-LIKE DOMAIN OF TTN, INTERACTION WITH TTN.
  15. "Structural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complex."
    Pernigo S., Fukuzawa A., Bertz M., Holt M., Rief M., Steiner R.A., Gautel M.
    Proc. Natl. Acad. Sci. U.S.A. 107:2908-2913(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 1-106 OF WILD-TYPE AND MUTANT ARG-17 IN COMPLEX WITH THE C-TERMINAL IG-LIKE DOMAIN OF TTN, INTERACTION WITH TTN, MUTAGENESIS OF PHE-17.
  16. "Solution NMR structure of Ig like domain (805-892) of obscurin-like protein 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8578K (CASP Target)."
    Northeast structural genomics consortium (NESG)
    Submitted (JUN-2012) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 805-892.
  17. "Solution NMR Structure of Ig like domain (1277-1357) of Obscurin-like protein 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8578D (CASP Target)."
    Northeast structural genomics consortium (NESG)
    Submitted (JUN-2012) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1277-1357.

Entry informationi

Entry nameiOBSL1_HUMAN
AccessioniPrimary (citable) accession number: O75147
Secondary accession number(s): A4KVA4
, A4KVA5, Q96IW3, S4R3M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2006
Last sequence update: April 5, 2011
Last modified: November 26, 2014
This is version 121 of the entry and version 4 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, Reference proteome

Documents

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

External Data

Dasty 3