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Protein

U2 snRNP-associated SURP motif-containing protein

Gene

U2SURP

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

Functioni

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
U2 snRNP-associated SURP motif-containing protein
Alternative name(s):
140 kDa Ser/Arg-rich domain protein
U2-associated protein SR140
Gene namesi
Name:U2SURP
Synonyms:KIAA0332, SR140
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:30855. U2SURP.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Polymorphism and mutation databases

BioMutaiU2SURP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10291028U2 snRNP-associated SURP motif-containing proteinPRO_0000280070Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei67 – 671Phosphoserine1 Publication
Modified residuei202 – 2021Phosphoserine1 Publication
Modified residuei485 – 4851Phosphoserine2 Publications
Modified residuei719 – 7191Phosphothreonine1 Publication
Modified residuei760 – 7601N6-acetyllysine1 Publication
Modified residuei788 – 7881Phosphoserine3 Publications
Modified residuei800 – 8001Phosphoserine2 Publications
Modified residuei811 – 8111Phosphoserine3 Publications
Modified residuei931 – 9311Phosphothreonine1 Publication
Modified residuei946 – 9461Phosphoserine1 Publication
Modified residuei948 – 9481Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO15042.
PaxDbiO15042.
PRIDEiO15042.

PTM databases

PhosphoSiteiO15042.

Miscellaneous databases

PMAP-CutDBO15042.

Expressioni

Gene expression databases

BgeeiO15042.
ExpressionAtlasiO15042. baseline and differential.
GenevisibleiO15042. HS.

Organism-specific databases

HPAiHPA037545.

Interactioni

Subunit structurei

Interacts with ERBB4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RBM10P981752EBI-310697,EBI-721525
RBM5P527562EBI-310697,EBI-714003

Protein-protein interaction databases

BioGridi116932. 38 interactions.
IntActiO15042. 18 interactions.
MINTiMINT-2795506.
STRINGi9606.ENSP00000322376.

Structurei

3D structure databases

ProteinModelPortaliO15042.
SMRiO15042. Positions 276-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini274 – 35582RRMPROSITE-ProRule annotationAdd
BLAST
Repeati430 – 47344SURP motifAdd
BLAST
Domaini534 – 679146CIDPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili92 – 12130Sequence AnalysisAdd
BLAST
Coiled coili192 – 23241Sequence AnalysisAdd
BLAST
Coiled coili837 – 91579Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi357 – 40246Pro-richAdd
BLAST
Compositional biasi689 – 74658Asp-richAdd
BLAST
Compositional biasi762 – 917156Glu-richAdd
BLAST
Compositional biasi922 – 100180Arg/Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 CID domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation
Contains 1 SURP motif repeat.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG307351.
GeneTreeiENSGT00390000010687.
HOGENOMiHOG000286037.
HOVERGENiHBG093996.
InParanoidiO15042.
KOiK12842.
OMAiNSPTKWR.
OrthoDBiEOG74FF05.
PhylomeDBiO15042.
TreeFamiTF318729.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR013170. mRNA_splic_Cwf21.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000061. Surp.
[Graphical view]
PfamiPF08312. cwf21. 1 hit.
PF00076. RRM_1. 1 hit.
PF01805. Surp. 1 hit.
[Graphical view]
SMARTiSM00582. RPR. 1 hit.
SM00360. RRM. 1 hit.
SM00648. SWAP. 1 hit.
[Graphical view]
SUPFAMiSSF109905. SSF109905. 1 hit.
SSF48464. SSF48464. 1 hit.
PROSITEiPS51391. CID. 1 hit.
PS50102. RRM. 1 hit.
PS50128. SURP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15042-1) [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
MADKTPGGSQ KASSKTRSSD VHSSGSSDAH MDASGPSDSD MPSRTRPKSP
60 70 80 90 100
RKHNYRNESA RESLCDSPHQ NLSRPLLENK LKAFSIGKMS TAKRTLSKKE
110 120 130 140 150
QEELKKKEDE KAAAEIYEEF LAAFEGSDGN KVKTFVRGGV VNAAKEEHET
160 170 180 190 200
DEKRGKIYKP SSRFADQKNP PNQSSNERPP SLLVIETKKP PLKKGEKEKK
210 220 230 240 250
KSNLELFKEE LKQIQEERDE RHKTKGRLSR FEPPQSDSDG QRRSMDAPSR
260 270 280 290 300
RNRSSGVLDD YAPGSHDVGD PSTTNLYLGN INPQMNEEML CQEFGRFGPL
310 320 330 340 350
ASVKIMWPRT DEERARERNC GFVAFMNRRD AERALKNLNG KMIMSFEMKL
360 370 380 390 400
GWGKAVPIPP HPIYIPPSMM EHTLPPPPSG LPFNAQPRER LKNPNAPMLP
410 420 430 440 450
PPKNKEDFEK TLSQAIVKVV IPTERNLLAL IHRMIEFVVR EGPMFEAMIM
460 470 480 490 500
NREINNPMFR FLFENQTPAH VYYRWKLYSI LQGDSPTKWR TEDFRMFKNG
510 520 530 540 550
SFWRPPPLNP YLHGMSEEQE TEAFVEEPSK KGALKEEQRD KLEEILRGLT
560 570 580 590 600
PRKNDIGDAM VFCLNNAEAA EEIVDCITES LSILKTPLPK KIARLYLVSD
610 620 630 640 650
VLYNSSAKVA NASYYRKFFE TKLCQIFSDL NATYRTIQGH LQSENFKQRV
660 670 680 690 700
MTCFRAWEDW AIYPEPFLIK LQNIFLGLVN IIEEKETEDV PDDLDGAPIE
710 720 730 740 750
EELDGAPLED VDGIPIDATP IDDLDGVPIK SLDDDLDGVP LDATEDSKKN
760 770 780 790 800
EPIFKVAPSK WEAVDESELE AQAVTTSKWE LFDQHEESEE EENQNQEEES
810 820 830 840 850
EDEEDTQSSK SEEHHLYSNP IKEEMTESKF SKYSEMSEEK RAKLREIELK
860 870 880 890 900
VMKFQDELES GKRPKKPGQS FQEQVEHYRD KLLQREKEKE LERERERDKK
910 920 930 940 950
DKEKLESRSK DKKEKDECTP TRKERKRRHS TSPSPSRSSS GRRVKSPSPK
960 970 980 990 1000
SERSERSERS HKESSRSRSS HKDSPRDVSK KAKRSPSGSR TPKRSRRSRS
1010 1020
RSPKKSGKKS RSQSRSPHRS HKKSKKNKH
Length:1,029
Mass (Da):118,292
Last modified:March 6, 2007 - v2
Checksum:i7AB9235C63299714
GO
Isoform 2 (identifier: O15042-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     256-256: Missing.

Show »
Length:1,028
Mass (Da):118,235
Checksum:i626B4D73CC24A992
GO
Isoform 3 (identifier: O15042-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-409: Missing.
     410-424: KTLSQAIVKVVIPTE → MLLCYRHLKTKRILR

Show »
Length:620
Mass (Da):72,523
Checksum:iBA78B39559885CBC
GO

Sequence cautioni

The sequence AAH16323.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI05605.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 409409Missing in isoform 3. 1 PublicationVSP_023522Add
BLAST
Alternative sequencei256 – 2561Missing in isoform 2. 1 PublicationVSP_023523
Alternative sequencei410 – 42415KTLSQ…VIPTE → MLLCYRHLKTKRILR in isoform 3. 1 PublicationVSP_023524Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC018450 Genomic DNA. No translation available.
AC026304 Genomic DNA. No translation available.
BC006474 mRNA. Translation: AAH06474.1.
BC016323 mRNA. Translation: AAH16323.1. Sequence problems.
BC105604 mRNA. Translation: AAI05605.1. Sequence problems.
BC111692 mRNA. Translation: AAI11693.1.
AB002330 mRNA. Translation: BAA20790.1.
BK000564 mRNA. Translation: DAA00075.1.
CCDSiCCDS46928.1. [O15042-1]
RefSeqiNP_001073884.1. NM_001080415.1. [O15042-1]
XP_005247303.1. XM_005247246.3. [O15042-2]
XP_005247306.1. XM_005247249.3. [O15042-3]
UniGeneiHs.596572.

Genome annotation databases

EnsembliENST00000473835; ENSP00000418563; ENSG00000163714.
GeneIDi23350.
KEGGihsa:23350.
UCSCiuc003evh.1. human. [O15042-1]
uc003evi.1. human. [O15042-3]
uc003evk.1. human. [O15042-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC018450 Genomic DNA. No translation available.
AC026304 Genomic DNA. No translation available.
BC006474 mRNA. Translation: AAH06474.1.
BC016323 mRNA. Translation: AAH16323.1. Sequence problems.
BC105604 mRNA. Translation: AAI05605.1. Sequence problems.
BC111692 mRNA. Translation: AAI11693.1.
AB002330 mRNA. Translation: BAA20790.1.
BK000564 mRNA. Translation: DAA00075.1.
CCDSiCCDS46928.1. [O15042-1]
RefSeqiNP_001073884.1. NM_001080415.1. [O15042-1]
XP_005247303.1. XM_005247246.3. [O15042-2]
XP_005247306.1. XM_005247249.3. [O15042-3]
UniGeneiHs.596572.

3D structure databases

ProteinModelPortaliO15042.
SMRiO15042. Positions 276-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116932. 38 interactions.
IntActiO15042. 18 interactions.
MINTiMINT-2795506.
STRINGi9606.ENSP00000322376.

PTM databases

PhosphoSiteiO15042.

Polymorphism and mutation databases

BioMutaiU2SURP.

Proteomic databases

MaxQBiO15042.
PaxDbiO15042.
PRIDEiO15042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000473835; ENSP00000418563; ENSG00000163714.
GeneIDi23350.
KEGGihsa:23350.
UCSCiuc003evh.1. human. [O15042-1]
uc003evi.1. human. [O15042-3]
uc003evk.1. human. [O15042-2]

Organism-specific databases

CTDi23350.
GeneCardsiGC03P142683.
H-InvDBHIX0003746.
HGNCiHGNC:30855. U2SURP.
HPAiHPA037545.
neXtProtiNX_O15042.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG307351.
GeneTreeiENSGT00390000010687.
HOGENOMiHOG000286037.
HOVERGENiHBG093996.
InParanoidiO15042.
KOiK12842.
OMAiNSPTKWR.
OrthoDBiEOG74FF05.
PhylomeDBiO15042.
TreeFamiTF318729.

Miscellaneous databases

ChiTaRSiU2SURP. human.
GenomeRNAii23350.
NextBioi45335.
PMAP-CutDBO15042.
PROiO15042.

Gene expression databases

BgeeiO15042.
ExpressionAtlasiO15042. baseline and differential.
GenevisibleiO15042. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR013170. mRNA_splic_Cwf21.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000061. Surp.
[Graphical view]
PfamiPF08312. cwf21. 1 hit.
PF00076. RRM_1. 1 hit.
PF01805. Surp. 1 hit.
[Graphical view]
SMARTiSM00582. RPR. 1 hit.
SM00360. RRM. 1 hit.
SM00648. SWAP. 1 hit.
[Graphical view]
SUPFAMiSSF109905. SSF109905. 1 hit.
SSF48464. SSF48464. 1 hit.
PROSITEiPS51391. CID. 1 hit.
PS50102. RRM. 1 hit.
PS50128. SURP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1029 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-189 (ISOFORMS 1/2).
    Tissue: Lung and Urinary bladder.
  3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1029 (ISOFORM 1).
    Tissue: Brain.
  4. "Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein."
    Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.
    EMBO J. 21:4978-4988(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND SER-800, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND SER-800, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-760, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
    Gilmore-Hebert M., Ramabhadran R., Stern D.F.
    Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; SER-811; THR-931; SER-946 AND SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-485; SER-788 AND SER-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND THR-719, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSR140_HUMAN
AccessioniPrimary (citable) accession number: O15042
Secondary accession number(s): A0PJ60
, Q0D2M1, Q2NKQ7, Q9BR70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: July 22, 2015
This is version 114 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.