| Tag | Content |
|---|
| CPLM ID | CPLM-008102 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Citron Rho-interacting kinase |
Protein Synonyms/Alias | CRIK; Rho-interacting, serine/threonine-protein kinase 21 |
Gene Name | Cit |
Gene Synonyms/Alias | Crik |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1669 | YIIKDLEKLLMIAGE | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Probable RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2 (By similarity). |
Sequence Annotation | DOMAIN 97 359 Protein kinase.
DOMAIN 360 430 AGC-kinase C-terminal.
DOMAIN 1469 1589 PH.
DOMAIN 1617 1907 CNH.
NP_BIND 103 111 ATP (By similarity).
ZN_FING 1388 1437 Phorbol-ester/DAG-type.
REGION 1132 1328 Interaction with Rho/Rac.
MOTIF 1979 1984 SH3-binding (Potential).
ACT_SITE 221 221 Proton acceptor (By similarity).
BINDING 126 126 ATP (By similarity).
MOD_RES 432 432 Phosphoserine (By similarity).
MOD_RES 439 439 Phosphoserine (By similarity).
MOD_RES 479 479 Phosphoserine.
MOD_RES 1237 1237 Phosphotyrosine.
MOD_RES 1504 1504 Phosphotyrosine.
MOD_RES 1608 1608 Phosphoserine.
MOD_RES 1747 1747 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Kinase; Metal-binding; Mitosis; Neurogenesis; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; SH3-binding; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2055 AA |
Protein Sequence | MLKFKYGVRN PPEASASEPI ASRASRLNLF FQGKPPLMTQ QQMSALSREG MLDALFALFE 60
ECSQPALMKM KHVSSFVQKY SDTIAELREL QPSARDFEVR SLVGCGHFAE VQVVREKATG 120
DVYAMKIMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNNL YLVMEYQPGG 180
DFLSLLNRYE DQLDESMIQF YLAELILAVH SVHQMGYVHR DIKPENILID RTGEIKLVDF 240
GSAAKMNSNK VDAKLPIGTP DYMAPEVLTV MNEDRRGTYG LDCDWWSVGV VAYEMVYGKT 300
PFTEGTSART FNNIMNFQRF LKFPDDPKVS SELLDLLQSL LCVQKERLKF EGLCCHPFFA 360
RTDWNNIRNS PPPFVPTLKS DDDTSNFDEP EKNSWVSSSV CQLSPSGFSG EELPFVGFSY 420
SKALGYLGRS ESVVSSLDSP AKVSSMEKKL LIKSKELQDS QDKCHKMEQE MTRLHRRVSE 480
VEAVLSQKEV ELKASETQRS LLEQDLATYI TECSSLKRSL EQARMEVSQE DDKALQLLHD 540
IREQSRKLQE IKEQEYQAQV EEMRLMMNQL EEDLVSARRR SDLYESELRE SRLAAEEFKR 600
KANECQHKLM KAKDQGKPEV GEYSKLEKIN AEQQLKIQEL QEKLEKAVKA STEATELLQN 660
IRQAKERAER ELEKLHNRED SSEGIKKKLV EAEERRHSLE NKVKRLETME RRENRLKDDI 720
QTKSEQIQQM ADKILELEEK HREAQVSAQH LEVHLKQKEQ HYEEKIKVLD NQIKKDLADK 780
ESLENMMQRH EEEAHEKGKI LSEQKAMINA MDSKIRSLEQ RIVELSEANK LAANSSLFTQ 840
RNMKAQEEMI SELRQQKFYL ETQAGKLEAQ NRKLEEQLEK ISHQDHSDKS RLLELETRLR 900
EVSLEHEEQK LELKRQLTEL QLSLQERESQ LTALQAARAA LESQLRQAKT ELEETTAEAE 960
EEIQALTAHR DEIQRKFDAL RNSCTVITDL EEQLNQLTED NAELNNQNFY LSKQLDEASG 1020
ANDEIVQLRS EVDHLRREIT EREMQLTSQK QTMEALKTTC TMLEEQVLDL EALNDELLEK 1080
ERQWEAWRSV LGDEKSQFEC RVRELQRMLD TEKQSRARAD QRITESRQVV ELAVKEHKAE 1140
ILALQQALKE QKLKAESLSD KLNDLEKKHA MLEMNARSLQ QKLETERELK QRLLEEQAKL 1200
QQQMDLQKNH IFRLTQGLQE ALDRADLLKT ERSDLEYQLE NIQVLYSHEK VKMEGTISQQ 1260
TKLIDFLQAK MDQPAKKKKV PLQYNELKLA LEKEKARCAE LEEALQKTRI ELRSAREEAA 1320
HRKATDHPHP STPATARQQI AMSAIVRSPE HQPSAMSLLA PPSSRRKESS TPEEFSRRLK 1380
ERMHHNIPHR FNVGLNMRAT KCAVCLDTVH FGRQASKCLE CQVMCHPKCS TCLPATCGLP 1440
AEYATHFTEA FCRDKMNSPG LQSKEPGSSL HLEGWMKVPR NNKRGQQGWD RKYIVLEGSK 1500
VLIYDNEARE AGQRPVEEFE LCLPDGDVSI HGAVGASELA NTAKADVPYI LKMESHPHTT 1560
CWPGRTLYLL APSFPDKQRW VTALESVVAG GRVSREKAEA DAKLLGNSLL KLEGDDRLDM 1620
NCTLPFSDQV VLVGTEEGLY ALNVLKNSLT HIPGIGAVFQ IYIIKDLEKL LMIAGEERAL 1680
CLVDVKKVKQ SLAQSHLPAQ PDVSPNIFEA VKGCHLFAAG KIENSLCICA AMPSKVVILR 1740
YNDNLSKYCI RKEIETSEPC SCIHFTNYSI LIGTNKFYEI DMKQYTLDEF LDKNDHSLAP 1800
AVFASSSNSF PVSIVQANSA GQREEYLLCF HEFGVFVDSY GRRSRTDDLK WSRLPLAFAY 1860
REPYLFVTHF NSLEVIEIQA RSSLGSPARA YLEIPNPRYL GPAISSGAIY LASSYQDKLR 1920
VICCKGNLVK ESGTEQHRVP STSRSSPNKR GPPTYNEHIT KRVASSPAPP EGPSHPREPS 1980
TPHRYRDREG RTELRRDKSP GRPLEREKSP GRMLSTRRER SPGRLFEDSS RGRLPAGAVR 2040
TPLSQVNKVW DQSSV 2055 |
Gene Ontology | GO:0015629; C:actin cytoskeleton; IDA:MGI. GO:0001726; C:ruffle; IDA:MGI. GO:0005773; C:vacuole; IDA:MGI. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0005543; F:phospholipid binding; IEA:InterPro. GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. GO:0005083; F:small GTPase regulator activity; IEA:InterPro. GO:0000910; P:cytokinesis; ISS:UniProtKB. GO:0016358; P:dendrite development; IMP:MGI. GO:0035556; P:intracellular signal transduction; IEA:InterPro. GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:MGI. GO:0000070; P:mitotic sister chromatid segregation; IMP:MGI. GO:0050774; P:negative regulation of dendrite morphogenesis; IDA:MGI. GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI. GO:0007283; P:spermatogenesis; IMP:MGI. |
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