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Q9H0F6 (SHRPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Sharpin
Alternative name(s):
Shank-associated RH domain-interacting protein
Shank-interacting protein-like 1
Short name=hSIPL1
Gene names
Name:SHARPIN
Synonyms:SIPL1
ORF Names:PSEC0216
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Ref.10 Ref.11 Ref.12

Subunit structure

Monomer and homodimer. Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of approximative 600 kDa suggesting a heteromultimeric assembly of its subunits. Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner. Interacts with EYA1, EYA2, SHANK1 and SHANK3 (via ANK repeats). Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasmcytosol. Cell junctionsynapse By similarity. Note: Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1 By similarity. Ref.2

Tissue specificity

Highly expressed in skeletal muscle and placenta and at lower levels in brain, heart, colon without mucosa, thymus, spleen, kidney, liver, small intestine, lung and peripheral blood leukocytes. Up-regulated in various tumor tissues such as kidney, liver, ovary and pancreas tumors. Ref.2

Domain

The Ubiquitin-like domain is required for the interaction with RNF31. Ref.10 Ref.11 Ref.12

The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. Binds preferentially linear polyubiquitin chains and 'Lys-63'-linked polyubiquitin chains over 'Lys-48'-linked polyubiquitin chains. Also binds monoubiquitin. Ref.10 Ref.11 Ref.12

Sequence similarities

Contains 1 RanBP2-type zinc finger.

Contains 1 ubiquitin-like domain.

Sequence caution

The sequence BAC11666.1 differs from that shown. Reason: Frameshift at position 334.

The sequence BAC53797.1 differs from that shown. Reason: Frameshift at position 218.

The sequence BAC53798.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCell junction
Cytoplasm
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic nuclear changes

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

keratinization

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.10. Source: UniProtKB

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein linear polyubiquitination

Inferred from direct assay Ref.10Ref.11Ref.12. Source: UniProtKB

regulation of CD40 signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of tumor necrosis factor-mediated signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

   Cellular_componentLUBAC complex

Inferred from direct assay Ref.10Ref.11Ref.12. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Inferred from direct assay Ref.2. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionpolyubiquitin binding

Inferred from direct assay Ref.10Ref.12. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H0F6-1)

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: Q9H0F6-2)

Also known as: hSIPL1A;

The sequence of this isoform differs from the canonical sequence as follows:
     309-326: TGPSPQHPQKMDGELGRL → QLVLSFLHLHQCPRPPWL
     327-387: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Sharpin
PRO_0000280634

Regions

Domain219 – 28870Ubiquitin-like
Zinc finger348 – 37730RanBP2-type
Region1 – 180180Self-association By similarity
Region175 – 310136Interaction with SHANK1 By similarity

Amino acid modifications

Modified residue1651Phosphoserine Ref.8
Modified residue3121Phosphoserine Ref.9

Natural variations

Alternative sequence309 – 32618TGPSP…ELGRL → QLVLSFLHLHQCPRPPWL in isoform 2.
VSP_023837
Alternative sequence327 – 38761Missing in isoform 2.
VSP_023838
Natural variant2821S → T.
Corresponds to variant rs11541804 [ dbSNP | Ensembl ].
VAR_047799
Natural variant2941P → S.
Corresponds to variant rs34674752 [ dbSNP | Ensembl ].
VAR_047800
Natural variant3111P → R.
Corresponds to variant rs35844464 [ dbSNP | Ensembl ].
VAR_047801

Experimental info

Mutagenesis1141V → D: Abolishes homodimerization. Ref.13
Mutagenesis2721I → A: Abolishes interaction with RNF31 and ability to mediate linear polyubiquitination. Ref.12
Mutagenesis3541C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-357. Ref.10
Mutagenesis3571C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-354. Ref.10
Mutagenesis358 – 3592TF → LV: Abolishes binding to ubiquitin and ability to mediate linear polyubiquitination.
Mutagenesis3681C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-371. Ref.10
Mutagenesis3711C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-368. Ref.10
Sequence conflict2381A → P in AAH02688. Ref.6
Sequence conflict2431Q → R in BAC11666. Ref.3
Sequence conflict2571V → A in AAH02688. Ref.6

Secondary structure

................. 387
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 33EE4BF66936AB60

FASTA38739,949
        10         20         30         40         50         60 
MAPPAGGAAA AASDLGSAAV LLAVHAAVRP LGAGPDAEAQ LRRLQLSADP ERPGRFRLEL 

        70         80         90        100        110        120 
LGAGPGAVNL EWPLESVSYT IRGPTQHELQ PPPGGPGTLS LHFLNPQEAQ RWAVLVRGAT 

       130        140        150        160        170        180 
VEGQNGSKSN SPPALGPEAC PVSLPSPPEA STLKGPPPEA DLPRSPGNLT EREELAGSLA 

       190        200        210        220        230        240 
RAIAGGDEKG AAQVAAVLAQ HRVALSVQLQ EACFPPGPIR LQVTLEDAAS AASAASSAHV 

       250        260        270        280        290        300 
ALQVHPHCTV AALQEQVFSE LGFPPAVQRW VIGRCLCVPE RSLASYGVRQ DGDPAFLYLL 

       310        320        330        340        350        360 
SAPREAPATG PSPQHPQKMD GELGRLFPPS LGLPPGPQPA ASSLPSPLQP SWSCPSCTFI 

       370        380 
NAPDRPGCEM CSTQRPCTWD PLAAAST 

« Hide

Isoform 2 (hSIPL1A) [UniParc].

Checksum: C92FE8845FD1EC3E
Show »

FASTA32633,878

References

« Hide 'large scale' references
[1]"Novel human and mouse genes encoding a shank-interacting protein and its upregulation in gastric fundus of W/WV mouse."
Daigo Y., Takayama I., Ward S.M., Sanders K.M., Fujino M.A.
J. Gastroenterol. Hepatol. 18:712-718(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Newly identified tumor-associated role of human Sharpin."
Jung J., Kim J.M., Park B., Cheon Y., Lee B., Choo S.H., Koh S.S., Lee S.J.
Mol. Cell. Biochem. 340:161-167(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"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] (ISOFORM 1).
Tissue: Embryo.
[5]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORMS 1 AND 2).
Tissue: Pancreas, Prostate and Uterus.
[8]"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-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Linear ubiquitination prevents inflammation and regulates immune signalling."
Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E., Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W., Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J., Walczak H.
Nature 471:591-596(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, DOMAIN UBIQUITIN-LIKE, UBIQUITIN-BINDING, MUTAGENESIS OF CYS-354; CYS-357; CYS-368 AND CYS-371.
[11]"SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex."
Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M., Sakata S., Tanaka K., Nakano H., Iwai K.
Nature 471:633-636(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN UBIQUITIN-LIKE.
[12]"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis."
Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C., Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J., Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K., Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I.
Nature 471:637-641(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, DOMAIN UBIQUITIN-LIKE, UBIQUITIN-BINDING, MUTAGENESIS OF ILE-272 AND 358-THR-PHE-359.
[13]"Structural analysis of SHARPIN, a subunit of a large multi-protein E3 ubiquitin ligase, reveals a novel dimerization function for the pleckstrin homology superfold."
Stieglitz B., Haire L.F., Dikic I., Rittinger K.
J. Biol. Chem. 287:20823-20829(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-127, MUTAGENESIS OF VAL-114, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB052764 mRNA. Translation: BAC53797.1. Frameshift.
AB052765 mRNA. Translation: BAC53798.1. Sequence problems.
FJ655995 mRNA. Translation: ACN38058.1.
AL136816 mRNA. Translation: CAB66750.1.
AK075518 mRNA. Translation: BAC11666.1. Frameshift.
AC104592 Genomic DNA. No translation available.
CH471162 Genomic DNA. Translation: EAW82152.1.
CH471162 Genomic DNA. Translation: EAW82153.1.
CH471162 Genomic DNA. Translation: EAW82150.1.
CH471162 Genomic DNA. Translation: EAW82151.1.
BC002688 mRNA. Translation: AAH02688.2.
BC025244 mRNA. Translation: AAH25244.1.
BC034028 mRNA. Translation: AAH34028.1.
RefSeqNP_112236.3. NM_030974.3.
UniGeneHs.529755.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4EMOX-ray2.00A/B/C/D1-127[»]
ProteinModelPortalQ9H0F6.
SMRQ9H0F6. Positions 18-121, 219-302, 348-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123608. 17 interactions.
DIPDIP-57842N.
IntActQ9H0F6. 11 interactions.
MINTMINT-7034570.
STRING9606.ENSP00000381698.

PTM databases

PhosphoSiteQ9H0F6.

Polymorphism databases

DMDM74733523.

Proteomic databases

PaxDbQ9H0F6.
PRIDEQ9H0F6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359551; ENSP00000352551; ENSG00000179526. [Q9H0F6-2]
ENST00000398712; ENSP00000381698; ENSG00000179526. [Q9H0F6-1]
GeneID81858.
KEGGhsa:81858.
UCSCuc003zba.3. human. [Q9H0F6-1]

Organism-specific databases

CTD81858.
GeneCardsGC08M145153.
H-InvDBHIX0017281.
HIX0124604.
HGNCHGNC:25321. SHARPIN.
HPAHPA044453.
MIM611885. gene.
neXtProtNX_Q9H0F6.
PharmGKBPA142670925.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278522.
HOVERGENHBG093954.
OMAHELQPPP.
PhylomeDBQ9H0F6.
TreeFamTF323486.

Gene expression databases

ArrayExpressQ9H0F6.
BgeeQ9H0F6.
CleanExHS_SHARPIN.
GenevestigatorQ9H0F6.

Family and domain databases

InterProIPR026168. SHARPIN.
IPR001876. Znf_RanBP2.
[Graphical view]
PANTHERPTHR22770:SF11. PTHR22770:SF11. 1 hit.
PfamPF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi81858.
NextBio72187.
PROQ9H0F6.
SOURCESearch...

Entry information

Entry nameSHRPN_HUMAN
AccessionPrimary (citable) accession number: Q9H0F6
Secondary accession number(s): A6NEG3 expand/collapse secondary AC list , C0L3L2, D3DWL3, Q8IXF5, Q8IXF6, Q8N2E7, Q8TB25, Q9BUE4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 95 of the entry and version 1 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM