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Q6PKG0 (LARP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
La-related protein 1
Alternative name(s):
La ribonucleoprotein domain family member 1
Gene names
Name:LARP1
Synonyms:KIAA0731, LARP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1096 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the LARP family.

Contains 1 HTH La-type RNA-binding domain.

Sequence caution

The sequence AAH33856.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA34451.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of macroautophagy

Inferred from mutant phenotype PubMed 22354037. Source: BHF-UCL

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PKG0-1)

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: Q6PKG0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.
     78-144: PLQLPGAEGP...VLTTVNGQSP → MLWRVLLSKR...PFPVLAPFSN

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 10961095La-related protein 1
PRO_0000207609

Regions

Domain397 – 48791HTH La-type RNA-binding
Compositional bias1044 – 10507Poly-Gly

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue751Phosphoserine Ref.11 Ref.15
Modified residue901Phosphoserine Ref.6 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.19
Modified residue1431Phosphoserine Ref.13 Ref.17 Ref.19
Modified residue1651Phosphoserine Ref.13
Modified residue2151Phosphoserine Ref.19
Modified residue2201Phosphoserine Ref.17 Ref.19
Modified residue2281Phosphoserine By similarity
Modified residue3241Phosphoserine By similarity
Modified residue3271Phosphoserine By similarity
Modified residue3761Phosphothreonine Ref.17
Modified residue5171Phosphoserine Ref.13
Modified residue5211Phosphoserine Ref.6 Ref.13 Ref.17 Ref.19
Modified residue5261Phosphothreonine Ref.3 Ref.6 Ref.13 Ref.14 Ref.17 Ref.19
Modified residue5481Phosphoserine Ref.17 Ref.19
Modified residue6271Phosphoserine Ref.6 Ref.12 Ref.13 Ref.15 Ref.17 Ref.19
Modified residue6311Phosphoserine Ref.13 Ref.15 Ref.17 Ref.19
Modified residue6491Phosphothreonine Ref.13 Ref.17
Modified residue7241Phosphothreonine Ref.13 Ref.15
Modified residue7661Phosphoserine Ref.6 Ref.17 Ref.19
Modified residue7741Phosphoserine Ref.3 Ref.6 Ref.13 Ref.14 Ref.17 Ref.19
Modified residue7771Phosphotyrosine Ref.19
Modified residue8241Phosphoserine Ref.13 Ref.15
Modified residue8451Phosphothreonine Ref.7
Modified residue8511Phosphoserine Ref.13
Modified residue8651Phosphothreonine Ref.15
Modified residue8681Phosphoserine Ref.15
Modified residue8921N6-acetyllysine Ref.16
Modified residue10171N6-acetyllysine Ref.16
Modified residue10561Phosphoserine By similarity

Natural variations

Alternative sequence1 – 7777Missing in isoform 2.
VSP_015114
Alternative sequence78 – 14467PLQLP…NGQSP → MLWRVLLSKRPPFPHPELDF QEAPIPSCPGRLPGRKNSVA LAAAPRKEPTGDREKPLPFP VLAPFSN in isoform 2.
VSP_015115

Experimental info

Sequence conflict778 – 7803RNT → TRP in AAH33856. Ref.1
Sequence conflict9791V → L in CAB61364. Ref.5

Sequences

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

Last modified August 16, 2005. Version 2.
Checksum: CA3E9D30BBC101B7

FASTA1,096123,510
        10         20         30         40         50         60 
MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD GSARRPRPPC 

        70         80         90        100        110        120 
AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG AGGGAAGAAG AGRRDFVEAP 

       130        140        150        160        170        180 
PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP AKVVRAAVPK QRKGSKVGDF GDAINWPTPG 

       190        200        210        220        230        240 
EIAHKSVQPQ SHKPQPTRKL PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR 

       250        260        270        280        290        300 
GGQKKKGNKH KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA 

       310        320        330        340        350        360 
PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR GRGGTRTHFD 

       370        380        390        400        410        420 
YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ ELLKDYIKRQ IEYYFSVDNL 

       430        440        450        460        470        480 
ERDFFLRRKM DADGFLPITL IASFHRVQAL TTDISLIFAA LKDSKVVEIV DEKVRRREEP 

       490        500        510        520        530        540 
EKWPLPPIVD YSQTDFSQLL NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT 

       550        560        570        580        590        600 
LPKGLSASLP DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD 

       610        620        630        640        650        660 
EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP HYMRRHPGGD 

       670        680        690        700        710        720 
RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS QIKQEVENFK KVNMISREQF 

       730        740        750        760        770        780 
DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL ANKLFGAPEP STIARSLPTT VPESPNYRNT 

       790        800        810        820        830        840 
RTPRTPRTPQ LKDSSQTSRF YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE 

       850        860        870        880        890        900 
HRPRTASISS SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE 

       910        920        930        940        950        960 
RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG LECLFRYYSY 

       970        980        990       1000       1010       1020 
GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS KAKNLDIDPK LQEYLGKFRR 

      1030       1040       1050       1060       1070       1080 
LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG RKRCPSQSSS RPAAMISQPP TPPTGQPVRE 

      1090 
DAKWTSQHSN TQTLGK 

« Hide

Isoform 2 [UniParc].

Checksum: 64982CA22171B0E6
Show »

FASTA1,019116,465

References

« Hide 'large scale' references
[1]"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: Cervix and Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-816 (ISOFORM 1).
Tissue: Brain.
[3]Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W., Heiserich L., Boulahbel H., Gottlieb E.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-26; 115-123; 167-185; 252-265; 357-366; 410-422; 429-473; 524-539; 579-597; 643-654; 695-703; 718-778; 904-924; 937-944; 949-964 AND 1004-1017, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT THR-526 AND SER-774, MASS SPECTROMETRY.
Tissue: Cervix carcinoma, Colon carcinoma and Mammary carcinoma.
[4]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1096 (ISOFORM 1).
Tissue: Brain.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1096.
Tissue: Mammary cancer.
[6]"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-90; SER-521; THR-526; SER-627; SER-766 AND SER-774, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-845, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"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-90; SER-143; SER-165; SER-517; SER-521; THR-526; SER-627; SER-631; THR-649; THR-724; SER-774; SER-824 AND SER-851, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-526 AND SER-774, MASS SPECTROMETRY.
[15]"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-75; SER-90; SER-627; SER-631; THR-724; SER-824; THR-865 AND SER-868, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[16]"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-892 AND LYS-1017, MASS SPECTROMETRY.
[17]"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-143; SER-220; THR-376; SER-521; THR-526; SER-548; SER-627; SER-631; THR-649; SER-766 AND SER-774, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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-90; SER-143; SER-215; SER-220; SER-521; THR-526; SER-548; SER-627; SER-631; SER-766; SER-774 AND TYR-777, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC001460 mRNA. Translation: AAH01460.2.
BC033856 mRNA. Translation: AAH33856.1. Different initiation.
AK091465 mRNA. Translation: BAC03668.1.
AB018274 mRNA. Translation: BAA34451.1. Sequence problems.
AL133034 mRNA. Translation: CAB61364.1.
IPIIPI00185919.
IPI00411690.
PIRT42646.
RefSeqNP_056130.2. NM_015315.3.
UniGeneHs.292078.

3D structure databases

ProteinModelPortalQ6PKG0.
ModBaseSearch...

Protein-protein interaction databases

IntActQ6PKG0. 12 interactions.
MINTMINT-1631511.
STRING9606.ENSP00000366871.

PTM databases

PhosphoSiteQ6PKG0.

Polymorphism databases

DMDM73621135.

Proteomic databases

PaxDbQ6PKG0.
PRIDEQ6PKG0.

Protocols and materials databases

DNASU23367.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336314; ENSP00000336721; ENSG00000155506.
ENST00000518297; ENSP00000428589; ENSG00000155506.
GeneID23367.
KEGGhsa:23367.
UCSCuc003lvo.3. human.
uc010jie.1. human.

Organism-specific databases

CTD23367.
GeneCardsGC05P154092.
HGNCHGNC:29531. LARP1.
HPACAB015222.
MIM612059. gene.
neXtProtNX_Q6PKG0.
PharmGKBPA142671564.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5193.
HOGENOMHOG000113283.
HOVERGENHBG054322.
InParanoidQ6PKG0.
OMAGSEPATY.

Gene expression databases

ArrayExpressQ6PKG0.
BgeeQ6PKG0.
CleanExHS_LARP1.
GenevestigatorQ6PKG0.
GermOnlineENSG00000155506. Homo sapiens.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR006607. DM15.
IPR006630. Lupus_La_RNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF05383. La. 1 hit.
[Graphical view]
SMARTSM00684. DM15. 3 hits.
SM00715. LA. 1 hit.
[Graphical view]
PROSITEPS50961. HTH_LA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLARP1. human.
GenomeRNAi23367.
NextBio45430.
PMAP-CutDBQ6PKG0.
SOURCESearch...

Entry information

Entry nameLARP1_HUMAN
AccessionPrimary (citable) accession number: Q6PKG0
Secondary accession number(s): O94836 expand/collapse secondary AC list , Q8N4M2, Q8NB73, Q9UFD7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: May 1, 2013
This is version 97 of the entry and version 2 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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families