Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7Z6J0

- SH3R1_HUMAN

UniProt

Q7Z6J0 - SH3R1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

E3 ubiquitin-protein ligase SH3RF1

Gene

SH3RF1

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

Functioni

Acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9) (By similarity). May be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane.By similarity
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes such as UBE2D1 or UBE2N and then transfers it to substrates. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis.
Plays an essential role in the targeting of HIV-1 Gag to the plasma membrane, this function is dependent on it's RING domain, and hence it's E3 ligase activity.

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri12 – 5342RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of apoptotic process Source: UniProtKB
  2. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  3. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  4. protein ubiquitination Source: UniProtKB-UniPathway
  5. regulation of JNK cascade Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ7Z6J0.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase SH3RF1 (EC:6.3.2.-)
Alternative name(s):
Plenty of SH3s
Short name:
Protein POSH
RING finger protein 142
SH3 domain-containing RING finger protein 1
SH3 multiple domains protein 2
Gene namesi
Name:SH3RF1
Synonyms:KIAA1494, POSH, RNF142, SH3MD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:17650. SH3RF1.

Subcellular locationi

Cytoplasmperinuclear region By similarity. Cell projectionlamellipodium. Cytoplasm. Golgi apparatustrans-Golgi network
Note: Colocalizes, with AKT2, in lamellipodia (By similarity). Colocalizes, with HERP1, in trans-Golgi network.By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytosol Source: UniProtKB
  3. Golgi apparatus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141V → A: Loss of Ubl activity. 1 Publication
Mutagenesisi304 – 3041S → A: Decreased level of phosphorylation and no change in the ability to induce apoptosis. 1 Publication
Mutagenesisi304 – 3041S → D: Decreased level of phosphorylation and Rac-binding ability and important loss of the ability to induce apoptosis. 1 Publication
Mutagenesisi304 – 3041S → E: Decreased Rac-binding ability. 1 Publication

Organism-specific databases

PharmGKBiPA134915904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 888888E3 ubiquitin-protein ligase SH3RF1PRO_0000334151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated at Ser-304 by AKT1 and AKT2. When phosphorylated, it has reduced ability to bind Rac.2 Publications
Subject to ubiquitination and proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ7Z6J0.
PaxDbiQ7Z6J0.
PRIDEiQ7Z6J0.

PTM databases

PhosphoSiteiQ7Z6J0.

Expressioni

Gene expression databases

BgeeiQ7Z6J0.
CleanExiHS_SH3RF1.
ExpressionAtlasiQ7Z6J0. baseline and differential.
GenevestigatoriQ7Z6J0.

Interactioni

Subunit structurei

Interacts with Rac; in a GTP-dependent manner (By similarity). Interacts with MAP3K10 and MAP3K11. Interacts with MAPK8IP; this interaction leads to the PJAC complex (POSH-JIP or SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio. Interacts with SIAH1. Interacts with HERP1. Probably part of a signaling complex that may contain SH3RF1, MAPK8IP, DLK1, MAP2K4, MAP2K7, MAPK8, MAPK9, AKT1 and AKT2.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAC1P630002EBI-311339,EBI-413628
SIAH2O432552EBI-311339,EBI-948141

Protein-protein interaction databases

BioGridi121673. 16 interactions.
IntActiQ7Z6J0. 11 interactions.
MINTiMINT-2792302.
STRINGi9606.ENSP00000284637.

Structurei

3D structure databases

ProteinModelPortaliQ7Z6J0.
SMRiQ7Z6J0. Positions 5-78, 137-255, 450-505, 835-888.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 19360SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini196 – 25964SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini445 – 50662SH3 3PROSITE-ProRule annotationAdd
BLAST
Domaini829 – 88860SH3 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni440 – 543104Interaction with AKT2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi397 – 4037Poly-Pro
Compositional biasi417 – 4248Poly-Ala
Compositional biasi657 – 6626Poly-Ala

Domaini

The RING finger domain is responsible of ubiquitination and proteasomal degradation.

Sequence similaritiesi

Belongs to the SH3RF family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 4 SH3 domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri12 – 5342RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiNOG314495.
GeneTreeiENSGT00760000119190.
HOGENOMiHOG000045564.
HOVERGENiHBG069552.
InParanoidiQ7Z6J0.
KOiK12171.
OMAiPKHSDTK.
OrthoDBiEOG7HMS0X.
PhylomeDBiQ7Z6J0.
TreeFamiTF105571.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028502. POSH1.
IPR001452. SH3_domain.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR10661:SF8. PTHR10661:SF8. 1 hit.
PfamiPF14604. SH3_9. 4 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00184. RING. 1 hit.
SM00326. SH3. 4 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 4 hits.
PROSITEiPS50002. SH3. 4 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7Z6J0-1) [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
MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP
60 70 80 90 100
ECRTLVGSGV EELPSNILLV RLLDGIKQRP WKPGPGGGSG TNCTNALRSQ
110 120 130 140 150
SSTVANCSSK DLQSSQGGQQ PRVQSWSPPV RGIPQLPCAK ALYNYEGKEP
160 170 180 190 200
GDLKFSKGDI IILRRQVDEN WYHGEVNGIH GFFPTNFVQI IKPLPQPPPQ
210 220 230 240 250
CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG MLADKIGIFP
260 270 280 290 300
ISYVEFNSAA KQLIEWDKPP VPGVDAGECS SAAAQSSTAP KHSDTKKNTK
310 320 330 340 350
KRHSFTSLTM ANKSSQASQN RHSMEISPPV LISSSNPTAA ARISELSGLS
360 370 380 390 400
CSAPSQVHIS TTGLIVTPPP SSPVTTGPSF TFPSDVPYQA ALGTLNPPLP
410 420 430 440 450
PPPLLAATVL ASTPPGATAA AAAAGMGPRP MAGSTDQIAH LRPQTRPSVY
460 470 480 490 500
VAIYPYTPRK EDELELRKGE MFLVFERCQD GWFKGTSMHT SKIGVFPGNY
510 520 530 540 550
VAPVTRAVTN ASQAKVPMST AGQTSRGVTM VSPSTAGGPA QKLQGNGVAG
560 570 580 590 600
SPSVVPAAVV SAAHIQTSPQ AKVLLHMTGQ MTVNQARNAV RTVAAHNQER
610 620 630 640 650
PTAAVTPIQV QNAAGLSPAS VGLSHHSLAS PQPAPLMPGS ATHTAAISIS
660 670 680 690 700
RASAPLACAA AAPLTSPSIT SASLEAEPSG RIVTVLPGLP TSPDSASSAC
710 720 730 740 750
GNSSATKPDK DSKKEKKGLL KLLSGASTKR KPRVSPPASP TLEVELGSAE
760 770 780 790 800
LPLQGAVGPE LPPGGGHGRA GSCPVDGDGP VTTAVAGAAL AQDAFHRKAS
810 820 830 840 850
SLDSAVPIAP PPRQACSSLG PVLNESRPVV CERHRVVVSY PPQSEAELEL
860 870 880
KEGDIVFVHK KREDGWFKGT LQRNGKTGLF PGSFVENI
Length:888
Mass (Da):93,129
Last modified:July 22, 2008 - v2
Checksum:iB3018000F03D0CF1
GO
Isoform 2 (identifier: Q7Z6J0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     394-441: TLNPPLPPPP...AGSTDQIAHL → APPPLLLLLE...IHTLLGKRIN
     442-888: Missing.

Note: No experimental confirmation available.

Show »
Length:441
Mass (Da):48,108
Checksum:i567606B80C58414A
GO

Sequence cautioni

The sequence AAH33203.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH53671.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the middle of the protein.
The sequence AAH33203.1 differs from that shown. Reason: Frameshift at position 182.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti663 – 6631P → S.
Corresponds to variant rs3811813 [ dbSNP | Ensembl ].
VAR_043342

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei394 – 44148TLNPP…QIAHL → APPPLLLLLEWDRGPWQDPL TRLHIYGRRLAPVCMLLYIH TLLGKRIN in isoform 2. 1 PublicationVSP_033622Add
BLAST
Alternative sequencei442 – 888447Missing in isoform 2. 1 PublicationVSP_033623Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC033203 mRNA. Translation: AAH33203.1. Sequence problems.
BC041023 mRNA. Translation: AAH41023.1.
BC053671 mRNA. Translation: AAH53671.1. Sequence problems.
AK021429 mRNA. Translation: BAB13822.1.
AB040927 mRNA. Translation: BAA96018.1.
CCDSiCCDS34099.1. [Q7Z6J0-1]
RefSeqiNP_065921.2. NM_020870.3. [Q7Z6J0-1]
UniGeneiHs.301804.

Genome annotation databases

EnsembliENST00000284637; ENSP00000284637; ENSG00000154447. [Q7Z6J0-1]
GeneIDi57630.
KEGGihsa:57630.
UCSCiuc003isa.1. human. [Q7Z6J0-1]

Polymorphism databases

DMDMi205830834.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC033203 mRNA. Translation: AAH33203.1 . Sequence problems.
BC041023 mRNA. Translation: AAH41023.1 .
BC053671 mRNA. Translation: AAH53671.1 . Sequence problems.
AK021429 mRNA. Translation: BAB13822.1 .
AB040927 mRNA. Translation: BAA96018.1 .
CCDSi CCDS34099.1. [Q7Z6J0-1 ]
RefSeqi NP_065921.2. NM_020870.3. [Q7Z6J0-1 ]
UniGenei Hs.301804.

3D structure databases

ProteinModelPortali Q7Z6J0.
SMRi Q7Z6J0. Positions 5-78, 137-255, 450-505, 835-888.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121673. 16 interactions.
IntActi Q7Z6J0. 11 interactions.
MINTi MINT-2792302.
STRINGi 9606.ENSP00000284637.

PTM databases

PhosphoSitei Q7Z6J0.

Polymorphism databases

DMDMi 205830834.

Proteomic databases

MaxQBi Q7Z6J0.
PaxDbi Q7Z6J0.
PRIDEi Q7Z6J0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284637 ; ENSP00000284637 ; ENSG00000154447 . [Q7Z6J0-1 ]
GeneIDi 57630.
KEGGi hsa:57630.
UCSCi uc003isa.1. human. [Q7Z6J0-1 ]

Organism-specific databases

CTDi 57630.
GeneCardsi GC04M170015.
HGNCi HGNC:17650. SH3RF1.
neXtProti NX_Q7Z6J0.
PharmGKBi PA134915904.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG314495.
GeneTreei ENSGT00760000119190.
HOGENOMi HOG000045564.
HOVERGENi HBG069552.
InParanoidi Q7Z6J0.
KOi K12171.
OMAi PKHSDTK.
OrthoDBi EOG7HMS0X.
PhylomeDBi Q7Z6J0.
TreeFami TF105571.

Enzyme and pathway databases

UniPathwayi UPA00143 .
SignaLinki Q7Z6J0.

Miscellaneous databases

ChiTaRSi SH3RF1. human.
GeneWikii SH3RF1.
GenomeRNAii 57630.
NextBioi 64333.
PROi Q7Z6J0.

Gene expression databases

Bgeei Q7Z6J0.
CleanExi HS_SH3RF1.
ExpressionAtlasi Q7Z6J0. baseline and differential.
Genevestigatori Q7Z6J0.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR028502. POSH1.
IPR001452. SH3_domain.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
PANTHERi PTHR10661:SF8. PTHR10661:SF8. 1 hit.
Pfami PF14604. SH3_9. 4 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00184. RING. 1 hit.
SM00326. SH3. 4 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 4 hits.
PROSITEi PS50002. SH3. 4 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-888 (ISOFORM 2).
    Tissue: Eye and Ovary.
  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.
    , 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 1-712 (ISOFORM 1).
    Tissue: Embryo.
  3. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-888 (ISOFORM 1).
    Tissue: Brain.
  4. "POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis."
    Xu Z., Kukekov N.V., Greene L.A.
    EMBO J. 22:252-261(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K10; MAP3K11; DLK1; MAP2K4; MAP2K7; MAPK8 AND MAPK9.
  5. "Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex."
    Figueroa C., Tarras S., Taylor J., Vojtek A.B.
    J. Biol. Chem. 278:47922-47927(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKT1 AND AKT2.
  6. Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, FUNCTION IN HIV-1 PLASMA MEMBRANE TARGETING, SUBCELLULAR LOCATION, SELF-UBIQUITINATION.
  7. "Siah1 interacts with the scaffold protein POSH to promote JNK activation and apoptosis."
    Xu Z., Sproul A., Wang W., Kukekov N., Greene L.A.
    J. Biol. Chem. 281:303-312(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIAH1.
  8. "Direct interaction of the molecular scaffolds POSH and JIP is required for apoptotic activation of JNKs."
    Kukekov N.V., Xu Z., Greene L.A.
    J. Biol. Chem. 281:15517-15524(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK8IP.
  9. Cited for: INTERACTION WITH AKT1 AND AKT2, PHOSPHORYLATION AT SER-304, MUTAGENESIS OF SER-304, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "The ubiquitin E3 ligase POSH regulates calcium homeostasis through spatial control of Herp."
    Tuvia S., Taglicht D., Erez O., Alroy I., Alchanati I., Bicoviski V., Dori-Bachash M., Ben-Avraham D., Reiss Y.
    J. Cell Biol. 177:51-61(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERP1, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-14.
  11. "POSH stimulates the ubiquitination and the clathrin-independent endocytosis of ROMK1 channels."
    Lin D.H., Yue P., Pan C.Y., Sun P., Zhang X., Han Z., Roos M., Caplan M., Giebisch G., Wang W.H.
    J. Biol. Chem. 284:29614-29624(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE.
  12. "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-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiSH3R1_HUMAN
AccessioniPrimary (citable) accession number: Q7Z6J0
Secondary accession number(s): Q05BT2
, Q8IW46, Q9HAM2, Q9P234
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 22, 2008
Last modified: October 29, 2014
This is version 98 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 4
    Human chromosome 4: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3