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O75147 (OBSL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Obscurin-like protein 1
Gene names
Name:OBSL1
Synonyms:KIAA0657
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1896 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates CUL7-FBXW8-containing ubiquitin ligase complex, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Localizes CUL7 to the Golgi apparatus in neurons. Ref.9

Subunit structure

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. Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Golgi apparatus. Note: Colocalizes with CUL7 at the Golgi apparatus in neurons. Ref.9

Tissue specificity

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Contains 1 fibronectin type-III domain.

Contains 14 Ig-like (immunoglobulin-like) domains.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TTNQ8WZ428EBI-1223896,EBI-681210

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75147-3)

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.
Isoform 2 (identifier: O75147-2)

The sequence of this isoform differs from the canonical sequence as follows:
     986-1025: PPVRIIYPRD...EDAPVRWYKD → SYQSQDSSNN...PPWRRTAGTE
     1026-1896: Missing.
Isoform 3 (identifier: O75147-1)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18961896Obscurin-like protein 1
PRO_0000247959

Regions

Domain12 – 10089Ig-like 1
Domain128 – 22598Ig-like 2
Domain243 – 33088Ig-like 3
Domain339 – 42587Ig-like 4
Domain517 – 61599Fibronectin type-III
Domain714 – 80087Ig-like 5
Domain804 – 89390Ig-like 6
Domain902 – 98281Ig-like 7
Domain986 – 107590Ig-like 8
Domain1078 – 117295Ig-like 9
Domain1174 – 126188Ig-like 10
Domain1265 – 135793Ig-like 11
Domain1357 – 1534178Ig-like 12
Domain1628 – 172093Ig-like 13
Domain1794 – 1896103Ig-like 14
Region17 – 193Interaction with TTN
Region85 – 9410Interaction with TTN

Amino acid modifications

Modified residue101Phosphoserine Ref.6
Disulfide bond33 ↔ 84 By similarity
Disulfide bond149 ↔ 209 By similarity
Disulfide bond267 ↔ 319 By similarity
Disulfide bond362 ↔ 412 By similarity
Disulfide bond738 ↔ 788 By similarity
Disulfide bond829 ↔ 879 By similarity
Disulfide bond920 ↔ 970 By similarity
Disulfide bond1011 ↔ 1061 By similarity
Disulfide bond1103 ↔ 1153 By similarity
Disulfide bond1195 ↔ 1245 By similarity
Disulfide bond1381 ↔ 1522 By similarity
Disulfide bond1650 ↔ 1700 By similarity

Natural variations

Alternative sequence986 – 102540PPVRI…RWYKD → SYQSQDSSNNNPELCVLLKK PKTRRLWSRFPPWRRTAGTE in isoform 2.
VSP_040784
Alternative sequence1026 – 1896871Missing in isoform 2.
VSP_040785
Alternative sequence1076 – 116792Missing in isoform 3.
VSP_040786
Alternative sequence1405 – 149389VEMAQ…PLPHD → RQSCCSYGGCRMCGQRKART CVSKWRQAEWVQRGPCAGCE VGSPCPTTLACPWPRMGTST ASSSMVSYWPTRAPTAARAT TIAPWPGSA in isoform 3.
VSP_040787
Alternative sequence1494 – 1896403Missing in isoform 3.
VSP_040788

Experimental info

Mutagenesis171F → R: Diminishes binding affinity for TTN. Ref.12
Sequence conflict1651G → R in BAA31632. Ref.4
Sequence conflict7231R → K in AAH07201. Ref.3
Sequence conflict7231R → K in BAA31632. Ref.4
Sequence conflict13651E → D in BAA31632. Ref.4

Secondary structure

................................................................................................... 1896
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 5, 2011. Version 4.
Checksum: 6D592AC3E30E9ACA

FASTA1,896206,947
        10         20         30         40         50         60 
MKASSGDQGS PPCFLRFPRP VRVVSGAEAE LKCVVLGEPP PVVVWEKGGQ QLAASERLSF 

        70         80         90        100        110        120 
PADGAEHGLL LTAALPTDAG VYVCRARNAA GEAYAAAAVT VLEPPASDPE LQPAERPLPS 

       130        140        150        160        170        180 
PGSGEGAPVF LTGPRSQWVL RGAEVVLTCR AGGLPEPTLY WEKDGMALDE VWDSSHFALQ 

       190        200        210        220        230        240 
PGRAEDGPGA SLALRILAAR LPDSGVYVCH ARNAHGHAQA GALLQVHQPP ESPPADPDEA 

       250        260        270        280        290        300 
PAPVVEPLKC APKTFWVNEG KHAKFRCYVM GKPEPEIEWH WEGRPLLPDR RRLMYRDRDG 

       310        320        330        340        350        360 
GFVLKVLYCQ AKDRGLYVCA ARNSAGQTLS AVQLHVKEPR LRFTRPLQDV EGREHGIAVL 

       370        380        390        400        410        420 
ECKVPNSRIP TAWFREDQRL LPCRKYEQIE EGTVRRLIIH RLKADDDGIY LCEMRGRVRT 

       430        440        450        460        470        480 
VANVTVKGPI LKRLPRKLDV LEGENAVLLV ETLEAGVEGR WSRDGEELPV ICQSSSGHMH 

       490        500        510        520        530        540 
ALVLPGVTRE DAGEVTFSLG NSRTTTLLRV KCVKHSPPGP PILAEMFKGH KNTVLLTWKP 

       550        560        570        580        590        600 
PEPAPETPFI YRLERQEVGS EDWIQCFSIE KAGAVEVPGD CVPSEGDYRF RICTVSGHGR 

       610        620        630        640        650        660 
SPHVVFHGSA HLVPTARLVA GLEDVQVYDG EDAVFSLDLS TIIQGTWFLN GEELKSNEPE 

       670        680        690        700        710        720 
GQVEPGALRY RIEQKGLQHR LILHAVKHQD SGALVGFSCP GVQDSAALTI QESPVHILSP 

       730        740        750        760        770        780 
QDRVSLTFTT SERVVLTCEL SRVDFPATWY KDGQKVEESE LLVVKMDGRK HRLILPEAKV 

       790        800        810        820        830        840 
QDSGEFECRT EGVSAFFGVT VQDPPVHIVD PREHVFVHAI TSECVMLACE VDREDAPVRW 

       850        860        870        880        890        900 
YKDGQEVEES DFVVLENEGP HRRLVLPATQ PSDGGEFQCV AGDECAYFTV TITDVSSWIV 

       910        920        930        940        950        960 
YPSGKVYVAA VRLERVVLTC ELCRPWAEVR WTKDGEEVVE SPALLLQKED TVRRLVLPAV 

       970        980        990       1000       1010       1020 
QLEDSGEYLC EIDDESASFT VTVTEPPVRI IYPRDEVTLI AVTLECVVLM CELSREDAPV 

      1030       1040       1050       1060       1070       1080 
RWYKDGLEVE ESEALVLERD GPRCRLVLPA AQPEDGGEFV CDAGDDSAFF TVTVTAPPER 

      1090       1100       1110       1120       1130       1140 
IVHPAARSLD LHFGAPGRVE LRCEVAPAGS QVRWYKDGLE VEASDALQLG AEGPTRTLTL 

      1150       1160       1170       1180       1190       1200 
PHAQPEDAGE YVCETRHEAI TFNVILAEPP VQFLALETTP SPLCVAPGEP VVLSCELSRA 

      1210       1220       1230       1240       1250       1260 
GAPVVWSHNG RPVQEGEGLE LHAEGPRRVL CIQAAGPAHA GLYTCQSGAA PGAPSLSFTV 

      1270       1280       1290       1300       1310       1320 
QVAEPPVRVV APEAAQTRVR STPGGDLELV VHLSGPGGPV RWYKDGERLA SQGRVQLEQA 

      1330       1340       1350       1360       1370       1380 
GARQVLRVQG ARSGDAGEYL CDAPQDSRIF LVSVEEPLLV KLVSELTPLT VHEGDDATFR 

      1390       1400       1410       1420       1430       1440 
CEVSPPDADV TWLRNGAVVT PGPQVEMAQN GSSRILTLRG CQLGDAGTVT LRAGSTATSA 

      1450       1460       1470       1480       1490       1500 
RLHVRETELL FLRRLQDVRA EEGQDVCLEV ETGRVGAAGA VRWVRGGQPL PHDSRLSMAQ 

      1510       1520       1530       1540       1550       1560 
DGHIHRLFIH GVILADQGTY GCESHHDRTL ARLSVRPRQL RVLRPLEDVT ISEGGSATFQ 

      1570       1580       1590       1600       1610       1620 
LELSQEGVTG EWARGGVQLY PGPKCHIHSD GHRHRLVLNG LGLADSGCVS FTADSLRCAA 

      1630       1640       1650       1660       1670       1680 
RLIVREVPVT IVRGPHDLEV TEGDTATFEC ELSQALADVT WEKDGNALTP SPRLRLQALG 

      1690       1700       1710       1720       1730       1740 
TRRLLQLRRC GPSDAGTYSC AVGTARAGPV RLTVRERTVA VLSELRSVSA REGDGATFEC 

      1750       1760       1770       1780       1790       1800 
TVSEVETTGR WELGGRPLRP GARVRIRQEG KKHILVLSEL RAEDAGEVRF QAGPAQSLAL 

      1810       1820       1830       1840       1850       1860 
LEVEALPLQM CRHPPREKTV LVGRRAVLEV TVSRSGGHVC WLREGAELCP GDKYEMRSHG 

      1870       1880       1890 
PTHSLVIHDV RPEDQGTYCC QAGQDSTHTR LLVEGN 

« Hide

Isoform 2 [UniParc].

Checksum: CAF2D3D8E1920335
Show »

FASTA1,025113,273
Isoform 3 [UniParc].

Checksum: 3AE3886DF8C0B8A8
Show »

FASTA1,401152,925

References

« Hide 'large scale' references
[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] (ISOFORM 1), 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF063638 mRNA. Translation: ABO42328.1.
AC009955 Genomic DNA. No translation available.
BC007201 mRNA. Translation: AAH07201.1. Different initiation.
AB014557 mRNA. Translation: BAA31632.2.
RefSeqNP_001166879.1. NM_001173408.1.
NP_056126.1. NM_015311.2.
UniGeneHs.526594.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO75147.
SMRO75147. Positions 8-103, 608-1074, 1277-1357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116944. 13 interactions.
DIPDIP-38340N.
IntActO75147. 8 interactions.
MINTMINT-7979572.
STRING9606.ENSP00000385636.

PTM databases

PhosphoSiteO75147.

Proteomic databases

PaxDbO75147.
PRIDEO75147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373873; ENSP00000362980; ENSG00000124006. [O75147-2]
ENST00000404537; ENSP00000385636; ENSG00000124006. [O75147-3]
GeneID23363.
KEGGhsa:23363.
UCSCuc002vmi.3. human. [O75147-2]
uc010fwk.3. human. [O75147-3]

Organism-specific databases

CTD23363.
GeneCardsGC02M220415.
H-InvDBHIX0002869.
HIX0161860.
HGNCHGNC:29092. OBSL1.
HPAHPA036404.
HPA036405.
MIM610991. gene.
612921. phenotype.
neXtProtNX_O75147.
Orphanet2616. 3M syndrome.
PharmGKBPA142671235.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000263472.
HOVERGENHBG082081.
OMAETSFIYR.
OrthoDBEOG744T84.
PhylomeDBO75147.

Gene expression databases

ArrayExpressO75147.
BgeeO75147.
CleanExHS_OBSL1.
GenevestigatorO75147.

Family and domain databases

Gene3D2.60.40.10. 20 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF07679. I-set. 15 hits.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
SM00409. IG. 12 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
PROSITEPS50853. FN3. 1 hit.
PS50835. IG_LIKE. 14 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75147.
GeneWikiOBSL1.
GenomeRNAi23363.
NextBio45409.
PROO75147.
SOURCESearch...

Entry information

Entry nameOBSL1_HUMAN
AccessionPrimary (citable) accession number: O75147
Secondary accession number(s): A4KVA5, Q96IW3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2006
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM