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Q9H0F6

- SHRPN_HUMAN

UniProt

Q9H0F6 - SHRPN_HUMAN

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Protein

Sharpin

Gene

SHARPIN

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

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri348 – 37730RanBP2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. polyubiquitin binding Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic nuclear changes Source: Ensembl
  2. brain development Source: Ensembl
  3. keratinization Source: Ensembl
  4. mitochondrion organization Source: Ensembl
  5. negative regulation of inflammatory response Source: UniProtKB
  6. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  7. protein homooligomerization Source: Ensembl
  8. protein linear polyubiquitination Source: UniProtKB
  9. regulation of CD40 signaling pathway Source: UniProtKB
  10. regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Sharpin
Alternative name(s):
Shank-associated RH domain-interacting protein
Shank-interacting protein-like 1
Short name:
hSIPL1
Gene namesi
Name:SHARPIN
Synonyms:SIPL1
ORF Names:PSEC0216
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:25321. SHARPIN.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Cell junctionsynapse By similarity
Note: Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytosol Source: UniProtKB
  3. dendrite Source: Ensembl
  4. LUBAC complex Source: UniProtKB
  5. postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141V → D: Abolishes homodimerization. 1 Publication
Mutagenesisi272 – 2721I → A: Abolishes interaction with RNF31 and ability to mediate linear polyubiquitination. 1 Publication
Mutagenesisi354 – 3541C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-357. 1 Publication
Mutagenesisi357 – 3571C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-354. 1 Publication
Mutagenesisi358 – 3592TF → LV: Abolishes binding to ubiquitin and ability to mediate linear polyubiquitination. 1 Publication
Mutagenesisi368 – 3681C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-371. 1 Publication
Mutagenesisi371 – 3711C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-368. 1 Publication

Organism-specific databases

PharmGKBiPA142670925.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387SharpinPRO_0000280634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei312 – 3121Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H0F6.
PaxDbiQ9H0F6.
PRIDEiQ9H0F6.

PTM databases

PhosphoSiteiQ9H0F6.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ9H0F6.
CleanExiHS_SHARPIN.
ExpressionAtlasiQ9H0F6. baseline.
GenevestigatoriQ9H0F6.

Organism-specific databases

HPAiHPA044453.

Interactioni

Subunit structurei

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).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKGQ9Y6K94EBI-3942966,EBI-81279
ITGA2P173015EBI-3942966,EBI-702960
ITGA5P086484EBI-3942966,EBI-1382311
RNF31Q96EP02EBI-3942966,EBI-948111

Protein-protein interaction databases

BioGridi123608. 21 interactions.
DIPiDIP-57842N.
IntActiQ9H0F6. 12 interactions.
MINTiMINT-7034570.
STRINGi9606.ENSP00000381698.

Structurei

Secondary structure

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 3011
Helixi31 – 333
Beta strandi40 – 489
Beta strandi56 – 605
Beta strandi70 – 734
Helixi74 – 763
Beta strandi77 – 837
Beta strandi86 – 905
Beta strandi99 – 1057
Helixi106 – 11914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EMOX-ray2.00A/B/C/D1-127[»]
ProteinModelPortaliQ9H0F6.
SMRiQ9H0F6. Positions 18-121, 219-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini219 – 28870Ubiquitin-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 180180Self-associationBy similarityAdd
BLAST
Regioni175 – 310136Interaction with SHANK1By similarityAdd
BLAST

Domaini

The Ubiquitin-like domain is required for the interaction with RNF31.
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.

Sequence similaritiesi

Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri348 – 37730RanBP2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG278522.
GeneTreeiENSGT00530000063620.
HOVERGENiHBG093954.
InParanoidiQ9H0F6.
OMAiHELQPPP.
PhylomeDBiQ9H0F6.
TreeFamiTF323486.

Family and domain databases

InterProiIPR026168. SHARPIN.
IPR029071. Ubiquitin-rel_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PANTHERiPTHR22770:SF31. PTHR22770:SF31. 1 hit.
PfamiPF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H0F6-1) [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
MAPPAGGAAA AASDLGSAAV LLAVHAAVRP LGAGPDAEAQ LRRLQLSADP
60 70 80 90 100
ERPGRFRLEL LGAGPGAVNL EWPLESVSYT IRGPTQHELQ PPPGGPGTLS
110 120 130 140 150
LHFLNPQEAQ RWAVLVRGAT VEGQNGSKSN SPPALGPEAC PVSLPSPPEA
160 170 180 190 200
STLKGPPPEA DLPRSPGNLT EREELAGSLA RAIAGGDEKG AAQVAAVLAQ
210 220 230 240 250
HRVALSVQLQ EACFPPGPIR LQVTLEDAAS AASAASSAHV ALQVHPHCTV
260 270 280 290 300
AALQEQVFSE LGFPPAVQRW VIGRCLCVPE RSLASYGVRQ DGDPAFLYLL
310 320 330 340 350
SAPREAPATG PSPQHPQKMD GELGRLFPPS LGLPPGPQPA ASSLPSPLQP
360 370 380
SWSCPSCTFI NAPDRPGCEM CSTQRPCTWD PLAAAST
Length:387
Mass (Da):39,949
Last modified:March 1, 2001 - v1
Checksum:i33EE4BF66936AB60
GO
Isoform 2 (identifier: Q9H0F6-2) [UniParc]FASTAAdd to Basket

Also known as: hSIPL1A

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

Show »
Length:326
Mass (Da):33,878
Checksum:iC92FE8845FD1EC3E
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381A → P in AAH02688. 1 PublicationCurated
Sequence conflicti243 – 2431Q → R in BAC11666. (PubMed:11230166)Curated
Sequence conflicti257 – 2571V → A in AAH02688. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti282 – 2821S → T.
Corresponds to variant rs11541804 [ dbSNP | Ensembl ].
VAR_047799
Natural varianti294 – 2941P → S.
Corresponds to variant rs34674752 [ dbSNP | Ensembl ].
VAR_047800
Natural varianti311 – 3111P → R.
Corresponds to variant rs35844464 [ dbSNP | Ensembl ].
VAR_047801

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei309 – 32618TGPSP…ELGRL → QLVLSFLHLHQCPRPPWL in isoform 2. 2 PublicationsVSP_023837Add
BLAST
Alternative sequencei327 – 38761Missing in isoform 2. 2 PublicationsVSP_023838Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43777.1. [Q9H0F6-1]
RefSeqiNP_112236.3. NM_030974.3. [Q9H0F6-1]
UniGeneiHs.529755.

Genome annotation databases

EnsembliENST00000359551; ENSP00000352551; ENSG00000179526. [Q9H0F6-2]
ENST00000398712; ENSP00000381698; ENSG00000179526. [Q9H0F6-1]
GeneIDi81858.
KEGGihsa:81858.
UCSCiuc003zba.3. human. [Q9H0F6-1]

Polymorphism databases

DMDMi74733523.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43777.1. [Q9H0F6-1 ]
RefSeqi NP_112236.3. NM_030974.3. [Q9H0F6-1 ]
UniGenei Hs.529755.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4EMO X-ray 2.00 A/B/C/D 1-127 [» ]
ProteinModelPortali Q9H0F6.
SMRi Q9H0F6. Positions 18-121, 219-302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123608. 21 interactions.
DIPi DIP-57842N.
IntActi Q9H0F6. 12 interactions.
MINTi MINT-7034570.
STRINGi 9606.ENSP00000381698.

PTM databases

PhosphoSitei Q9H0F6.

Polymorphism databases

DMDMi 74733523.

Proteomic databases

MaxQBi Q9H0F6.
PaxDbi Q9H0F6.
PRIDEi Q9H0F6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359551 ; ENSP00000352551 ; ENSG00000179526 . [Q9H0F6-2 ]
ENST00000398712 ; ENSP00000381698 ; ENSG00000179526 . [Q9H0F6-1 ]
GeneIDi 81858.
KEGGi hsa:81858.
UCSCi uc003zba.3. human. [Q9H0F6-1 ]

Organism-specific databases

CTDi 81858.
GeneCardsi GC08M145153.
H-InvDB HIX0017281.
HIX0124604.
HGNCi HGNC:25321. SHARPIN.
HPAi HPA044453.
MIMi 611885. gene.
neXtProti NX_Q9H0F6.
PharmGKBi PA142670925.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG278522.
GeneTreei ENSGT00530000063620.
HOVERGENi HBG093954.
InParanoidi Q9H0F6.
OMAi HELQPPP.
PhylomeDBi Q9H0F6.
TreeFami TF323486.

Miscellaneous databases

GenomeRNAii 81858.
NextBioi 72187.
PROi Q9H0F6.
SOURCEi Search...

Gene expression databases

Bgeei Q9H0F6.
CleanExi HS_SHARPIN.
ExpressionAtlasi Q9H0F6. baseline.
Genevestigatori Q9H0F6.

Family and domain databases

InterProi IPR026168. SHARPIN.
IPR029071. Ubiquitin-rel_dom.
IPR001876. Znf_RanBP2.
[Graphical view ]
PANTHERi PTHR22770:SF31. PTHR22770:SF31. 1 hit.
Pfami PF00641. zf-RanBP. 1 hit.
[Graphical view ]
SMARTi SM00547. ZnF_RBZ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. 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.
    , 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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiSHRPN_HUMAN
AccessioniPrimary (citable) accession number: Q9H0F6
Secondary accession number(s): A6NEG3
, C0L3L2, D3DWL3, Q8IXF5, Q8IXF6, Q8N2E7, Q8TB25, Q9BUE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 100 of the entry and version 1 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 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3